Protein:CD44 |
Protein Summary |
 Gene summary |
| Gene name: CD44 | ASpdb.0 ID: 960 | Gene | Gene symbol | CD44 | Gene ID | 960 |
| Gene name | CD44 molecule (IN blood group) |
| Synonyms | CDW44|CSPG8|ECM-III|ECMR-III|H-CAM|HCELL|HUTCH-1|HUTCH-I|Hermes-1|IN|LHR|MC56|MDU2|MDU3|MIC4|Pgp1 |
| Cytomap | 11p13 |
| Type of gene | protein-coding |
| Description | CD44 antigenCD44 molecule (Indian blood group)GP90 lymphocyte homing/adhesion receptorHermes antigenIn(Lu) related-p80Indian blood group antigencell surface glycoprotein CD44chondroitin sulfate proteoglycan 8epicanextracellular matrix receptor II |
| Modification date | 20240407 |
| UniProtAcc | P16070 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CD44 | GO:0004896 | cytokine receptor activity | 17045821 |
| Gene | CD44 | GO:0005540 | hyaluronic acid binding | 17170110|17324121 |
| Gene | CD44 | GO:0005794 | Golgi apparatus | - |
| Gene | CD44 | GO:0005829 | cytosol | - |
| Gene | CD44 | GO:0005886 | plasma membrane | 20962267 |
| Gene | CD44 | GO:0007155 | cell adhesion | 19703720 |
| Gene | CD44 | GO:0009986 | cell surface | 16809613|17170110 |
| Gene | CD44 | GO:0016324 | apical plasma membrane | 20962267 |
| Gene | CD44 | GO:0016477 | cell migration | 22726066 |
| Gene | CD44 | GO:0030214 | hyaluronan catabolic process | 17170110 |
| Gene | CD44 | GO:0031258 | lamellipodium membrane | 20962267 |
| Gene | CD44 | GO:0033138 | positive regulation of peptidyl-serine phosphorylation | 17045821 |
| Gene | CD44 | GO:0035692 | macrophage migration inhibitory factor receptor complex | 17045821 |
| Gene | CD44 | GO:0042110 | T cell activation | 7528188 |
| Gene | CD44 | GO:0042995 | cell projection | 20962267 |
| Gene | CD44 | GO:0043518 | negative regulation of DNA damage response, signal transduction by p53 class mediator | 17045821 |
| Gene | CD44 | GO:0044344 | cellular response to fibroblast growth factor stimulus | 19577615 |
| Gene | CD44 | GO:0050731 | positive regulation of peptidyl-tyrosine phosphorylation | 17045821 |
| Gene | CD44 | GO:0070374 | positive regulation of ERK1 and ERK2 cascade | 17045821 |
| Gene | CD44 | GO:1902166 | negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator | 17045821 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P16070-1 | P16070-1_4pz4_A.pdb | 4PZ4 | X-ray | 1.6 | A | 18 | 171 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P16070 | CD44 | P16070-1 | P16070-10 | 742 | 493 | 223 | 223 | Substitution | T | N | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-10 | 742 | 493 | 224 | 472 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-11 | 742 | 429 | 223 | 535 | Deletion | none | none | 222 | 222 |
| P16070 | CD44 | P16070-1 | P16070-12 | 742 | 361 | 223 | 223 | Substitution | T | R | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-12 | 742 | 361 | 224 | 604 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-13 | 742 | 425 | 223 | 223 | Substitution | T | N | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-13 | 742 | 425 | 224 | 472 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-13 | 742 | 425 | 536 | 536 | Substitution | N | R | 287 | 287 |
| P16070 | CD44 | P16070-1 | P16070-13 | 742 | 425 | 537 | 604 | Deletion | none | none | 287 | 287 |
| P16070 | CD44 | P16070-1 | P16070-14 | 742 | 396 | 223 | 223 | Substitution | T | N | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-14 | 742 | 396 | 224 | 472 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-14 | 742 | 396 | 506 | 506 | Substitution | Q | R | 257 | 257 |
| P16070 | CD44 | P16070-1 | P16070-14 | 742 | 396 | 507 | 535 | Deletion | none | none | 257 | 257 |
| P16070 | CD44 | P16070-1 | P16070-14 | 742 | 396 | 536 | 536 | Substitution | N | R | 258 | 258 |
| P16070 | CD44 | P16070-1 | P16070-14 | 742 | 396 | 537 | 604 | Deletion | none | none | 258 | 258 |
| P16070 | CD44 | P16070-1 | P16070-15 | 742 | 294 | 223 | 223 | Substitution | T | R | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-15 | 742 | 294 | 224 | 604 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-15 | 742 | 294 | 675 | 675 | Substitution | R | S | 294 | 294 |
| P16070 | CD44 | P16070-1 | P16070-15 | 742 | 294 | 676 | 742 | Deletion | none | none | 294 | 294 |
| P16070 | CD44 | P16070-1 | P16070-16 | 742 | 668 | 192 | 192 | Substitution | G | A | 192 | 192 |
| P16070 | CD44 | P16070-1 | P16070-16 | 742 | 668 | 193 | 223 | Deletion | none | none | 192 | 192 |
| P16070 | CD44 | P16070-1 | P16070-16 | 742 | 668 | 385 | 385 | Substitution | I | T | 354 | 354 |
| P16070 | CD44 | P16070-1 | P16070-16 | 742 | 668 | 386 | 428 | Deletion | none | none | 354 | 354 |
| P16070 | CD44 | P16070-1 | P16070-17 | 742 | 691 | 266 | 273 | Deletion | none | none | 265 | 265 |
| P16070 | CD44 | P16070-1 | P16070-17 | 742 | 691 | 385 | 385 | Substitution | I | T | 377 | 377 |
| P16070 | CD44 | P16070-1 | P16070-17 | 742 | 691 | 386 | 428 | Deletion | none | none | 377 | 377 |
| P16070 | CD44 | P16070-1 | P16070-18 | 742 | 340 | 223 | 223 | Substitution | T | R | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-18 | 742 | 340 | 224 | 604 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-18 | 742 | 340 | 605 | 625 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-19 | 742 | 139 | 78 | 139 | Substitution | RYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAF | SLHCSQQSKKVWAEEKASDQQWQWSCGGQKAKWTQRRGQQVSGNGAFGEQGVVRNSRPVYDS | 78 | 139 |
| P16070 | CD44 | P16070-1 | P16070-19 | 742 | 139 | 140 | 742 | Deletion | none | none | 139 | 139 |
| P16070 | CD44 | P16070-1 | P16070-2 | 742 | 29 | 23 | 29 | Substitution | DLNITCR | GVGRRKS | 23 | 29 |
| P16070 | CD44 | P16070-1 | P16070-2 | 742 | 29 | 30 | 742 | Deletion | none | none | 29 | 29 |
| P16070 | CD44 | P16070-1 | P16070-3 | 742 | 711 | 192 | 192 | Substitution | G | A | 192 | 192 |
| P16070 | CD44 | P16070-1 | P16070-3 | 742 | 711 | 193 | 223 | Deletion | none | none | 192 | 192 |
| P16070 | CD44 | P16070-1 | P16070-4 | 742 | 699 | 223 | 223 | Substitution | T | S | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-4 | 742 | 699 | 224 | 266 | Deletion | none | none | 223 | 223 |
| P16070 | CD44 | P16070-1 | P16070-5 | 742 | 734 | 266 | 273 | Deletion | none | none | 265 | 265 |
| P16070 | CD44 | P16070-1 | P16070-6 | 742 | 699 | 385 | 385 | Substitution | I | T | 385 | 385 |
| P16070 | CD44 | P16070-1 | P16070-6 | 742 | 699 | 386 | 428 | Deletion | none | none | 385 | 385 |
| P16070 | CD44 | P16070-1 | P16070-7 | 742 | 713 | 506 | 506 | Substitution | Q | R | 506 | 506 |
| P16070 | CD44 | P16070-1 | P16070-7 | 742 | 713 | 507 | 535 | Deletion | none | none | 506 | 506 |
| P16070 | CD44 | P16070-1 | P16070-8 | 742 | 674 | 536 | 536 | Substitution | N | R | 536 | 536 |
| P16070 | CD44 | P16070-1 | P16070-8 | 742 | 674 | 537 | 604 | Deletion | none | none | 536 | 536 |
| P16070 | CD44 | P16070-1 | P16070-9 | 742 | 675 | 675 | 675 | Substitution | R | S | 675 | 675 |
| P16070 | CD44 | P16070-1 | P16070-9 | 742 | 675 | 676 | 742 | Deletion | none | none | 675 | 675 |
| Multiple sequence alignment of our canonical and alternatively spliced CD44 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CD44 |
| UniProt-id | ENSG | ENST | ENSP |
| P16070-1 | ENSG00000026508.21 | ENST00000428726.8 | ENSP00000398632.2 |
| P16070-10 | ENSG00000026508.21 | ENST00000433892.6 | ENSP00000392331.2 |
| P16070-11 | ENSG00000026508.21 | ENST00000434472.6 | ENSP00000404447.2 |
| P16070-12 | ENSG00000026508.21 | ENST00000263398.11 | ENSP00000263398.6 |
| P16070-18 | ENSG00000026508.21 | ENST00000352818.8 | ENSP00000309732.6 |
| P16070-19 | ENSG00000026508.21 | ENST00000278386.10 | ENSP00000278386.6 |
| P16070-4 | ENSG00000026508.21 | ENST00000415148.6 | ENSP00000389830.2 |
| UniProt-id | NM ID | NP ID |
| P16070-1 | NM_000610.3 | NP_000601.3 |
| P16070-10 | NM_001001390.1 | NP_001001390.1 |
| P16070-11 | NM_001202555.1 | NP_001189484.1 |
| P16070-12 | NM_001001391.1 | NP_001001391.1 |
| P16070-13 | XM_011520488.1 | XP_011518790.1 |
| P16070-15 | NM_001202557.1 | NP_001189486.1 |
| P16070-18 | NM_001202556.1 | NP_001189485.1 |
| P16070-19 | NM_001001392.1 | NP_001001392.1 |
| P16070-4 | NM_001001389.1 | NP_001001389.1 |
| Amino acid sequences of our canonical and alternatively spliced CD44 |
| accession_id | Protein sequence |
| P16070-1 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSN TISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWN PEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSW TDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDV TGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGS QEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSET |
| P16070-10 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATNMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEG LEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTF HPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGL |
| P16070-11 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGS FGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSR |
| P16070-12 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATRDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWL IILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIG |
| P16070-13 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATNMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEG LEEDKDHPTTSTLTSSRDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCG |
| P16070-14 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATNMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTRRDQDTFHPSGGSH TTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKS |
| P16070-15 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATRDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWL |
| P16070-16 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGALMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDE DFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTTASAHTS HPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDK DHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGG SHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEAS |
| P16070-17 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAAGWEP NEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLI HHEHHEEEETPHSTSTTASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPL SMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTV GDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKK |
| P16070-18 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATRHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNS |
| P16070-19 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCSLHCSQQSKKVWA |
| P16070-2 | |
| P16070-3 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGALMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDE DFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSS TTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITL QPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESR TFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALA |
| P16070-4 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATSTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPR AFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQW FGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVE DLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGS FGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSR |
| P16070-5 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAAGWEP NEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLI HHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPIS HPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPN HSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTT SGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTAD |
| P16070-6 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSN TISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWN PEAHPPLIHHEHHEEEETPHSTSTTASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVE DLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGS FGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSR |
| P16070-7 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSN TISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWN PEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSW TDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTRNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKE SRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLA |
| P16070-8 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSN TISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWN PEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSW TDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSRDQDT FHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSG |
| P16070-9 | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPR IHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSS GSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSN TISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWN PEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSW TDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDV TGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGS |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CD44 (go to UniProt):P16070 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=472 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=223;End=535 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=604 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=472 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=536;End=536 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=537;End=604 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=472 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=506;End=506 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=507;End=535 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=536;End=536 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=537;End=604 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=604 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=192;End=192 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=193;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=385;End=385 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=386;End=428 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=266;End=273 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=385;End=385 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=386;End=428 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=604 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=605;End=625 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=78;End=139 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=140;End=742 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=23;End=29 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=30;End=742 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=192;End=192 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=193;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=223;End=223 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=224;End=266 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=266;End=273 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=385;End=385 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=386;End=428 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=506;End=506 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=507;End=535 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=536;End=536 |
| P16070 | Topological domain | 21 | 649 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=537;End=604 |
| P16070 | Transmembrane | 650 | 670 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=140;End=742 |
| P16070 | Transmembrane | 650 | 670 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=30;End=742 |
| P16070 | Topological domain | 671 | 742 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=675;End=675 |
| P16070 | Topological domain | 671 | 742 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=676;End=742 |
| P16070 | Topological domain | 671 | 742 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=140;End=742 |
| P16070 | Topological domain | 671 | 742 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=30;End=742 |
| P16070 | Topological domain | 671 | 742 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=675;End=675 |
| P16070 | Topological domain | 671 | 742 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=676;End=742 |
| P16070 | Domain | 32 | 120 | Note=Link;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00323 | Type=Substitution;Start=78;End=139 |
| P16070 | Domain | 32 | 120 | Note=Link;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00323 | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 160 | 189 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 160 | 189 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=223;End=535 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=536;End=536 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=506;End=506 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=507;End=535 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=536;End=536 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=385;End=385 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=386;End=428 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=266;End=273 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=385;End=385 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=386;End=428 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=605;End=625 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=224;End=266 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=266;End=273 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=385;End=385 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=386;End=428 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=506;End=506 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=507;End=535 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Substitution;Start=536;End=536 |
| P16070 | Region | 224 | 649 | Note=Stem | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=266;End=273 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=266 |
| P16070 | Region | 261 | 285 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=266;End=273 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=536;End=536 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=506;End=506 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=507;End=535 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=536;End=536 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=385;End=385 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=385;End=385 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=385;End=385 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=506;End=506 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=507;End=535 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=536;End=536 |
| P16070 | Region | 372 | 558 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=605;End=625 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 590 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Substitution;Start=675;End=675 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=676;End=742 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Substitution;Start=675;End=675 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=676;End=742 |
| P16070 | Compositional bias | 167 | 189 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 167 | 189 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=266;End=273 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=266 |
| P16070 | Compositional bias | 261 | 277 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=266;End=273 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=385;End=385 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=385;End=385 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=385;End=385 |
| P16070 | Compositional bias | 381 | 403 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=472 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 418 | 455 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=386;End=428 |
| P16070 | Compositional bias | 473 | 491 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Compositional bias | 473 | 491 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 473 | 491 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 473 | 491 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 473 | 491 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 473 | 491 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=506;End=506 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=507;End=535 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=506;End=506 |
| P16070 | Compositional bias | 499 | 516 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=507;End=535 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=223;End=535 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=536;End=536 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=507;End=535 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=536;End=536 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=507;End=535 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=536;End=536 |
| P16070 | Compositional bias | 529 | 558 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=224;End=604 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=605;End=625 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
| P16070 | Compositional bias | 590 | 620 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=537;End=604 |
| P16070 | Compositional bias | 627 | 642 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=140;End=742 |
| P16070 | Compositional bias | 627 | 642 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=742 |
Gene Isoform Structures and Expression Levels for CD44 |
| Gene structures of our canonical and alternative spliced genes of CD44 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P16070-1 |
| 3D view using mol* of P16070-10 |
| 3D view using mol* of P16070-11 |
| 3D view using mol* of P16070-12 |
| 3D view using mol* of P16070-13 |
| 3D view using mol* of P16070-14 |
| 3D view using mol* of P16070-15 |
| 3D view using mol* of P16070-16 |
| 3D view using mol* of P16070-17 |
| 3D view using mol* of P16070-18 |
| 3D view using mol* of P16070-19 |
| 3D view using mol* of P16070-2 |
| 3D view using mol* of P16070-3 |
| 3D view using mol* of P16070-4 |
| 3D view using mol* of P16070-5 |
| 3D view using mol* of P16070-6 |
| 3D view using mol* of P16070-7 |
| 3D view using mol* of P16070-8 |
| 3D view using mol* of P16070-9 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P16070-1 |
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| pLDDT distribution across the protein length of P16070-10 |
 |
| pLDDT distribution across the protein length of P16070-11 |
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| pLDDT distribution across the protein length of P16070-12 |
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| pLDDT distribution across the protein length of P16070-13 |
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| pLDDT distribution across the protein length of P16070-14 |
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| pLDDT distribution across the protein length of P16070-15 |
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| pLDDT distribution across the protein length of P16070-16 |
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| pLDDT distribution across the protein length of P16070-17 |
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| pLDDT distribution across the protein length of P16070-18 |
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| pLDDT distribution across the protein length of P16070-19 |
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| pLDDT distribution across the protein length of P16070-3 |
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| pLDDT distribution across the protein length of P16070-4 |
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| pLDDT distribution across the protein length of P16070-5 |
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| pLDDT distribution across the protein length of P16070-6 |
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| pLDDT distribution across the protein length of P16070-7 |
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| pLDDT distribution across the protein length of P16070-8 |
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| pLDDT distribution across the protein length of P16070-9 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P16070-1 |
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| Ramachandran plot of P16070-10 |
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| Ramachandran plot of P16070-11 |
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| Ramachandran plot of P16070-15 |
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| Ramachandran plot of P16070-16 |
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| Ramachandran plot of P16070-18 |
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| Ramachandran plot of P16070-2 |
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| Ramachandran plot of P16070-4 |
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| Ramachandran plot of P16070-6 |
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| Ramachandran plot of P16070-9 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P16070-1 | 1.035 | 104 | 0.945 | 244.902 | 0.544 | 0.75 | 0.993 | 0.385 | 1.364 | 0.282 | 0.623 | 25,26,27,30,35,37,42,74,75,76,77,78,79,88,90,96,97 ,98,99,150,303,304,305,306,307 |
| P16070-10 | 1.011 | 132 | 1.056 | 389.648 | 0.563 | 0.666 | 0.871 | 0.525 | 0.871 | 0.603 | 0.837 | 38,39,41,42,43,44,45,48,79,107,109,111,112,113,114 ,162,166,167,168,170,171,172,173,174,175,176,177,1 78,179,180,181 |
| P16070-11 | 1.003 | 348 | 0.974 | 1050.952 | 0.53 | 0.703 | 0.917 | 0.252 | 1.189 | 0.212 | 0.831 | 25,26,27,28,30,35,37,38,39,40,41,42,43,45,48,73,74 ,75,76,77,78,79,88,90,92,94,96,97,98,99,107,109,11 1,112,113,114,127,148,149,150,152,154,162,166,167, 170,171,172,173,174,175,176,178,179,180,181,182,18 3,184,185,187,189,190,191,192,193,194,195,196,197, 198 |
| P16070-12 | 0.991 | 322 | 0.949 | 909.636 | 0.525 | 0.684 | 0.904 | 0.193 | 1.233 | 0.156 | 0.504 | 25,27,28,30,35,37,39,40,41,42,73,74,75,76,77,78,79 ,88,90,91,92,94,96,97,98,99,127,148,150,152,154,17 9,180,181,182,183,184,185,186,187,189,190,191,192, 193,194,195,196,197,198,200 |
| P16070-13 | 1.022 | 184 | 1.043 | 584.815 | 0.585 | 0.725 | 0.914 | 0.412 | 1.019 | 0.405 | 0.984 | 25,26,27,28,30,35,37,73,74,75,76,77,78,90,91,92,94 ,96,127,148,149,150,152,185,187,189,191,193,194,19 5,196,197,198,199,200 |
| P16070-14 | 1.009 | 251 | 0.984 | 806.736 | 0.534 | 0.711 | 0.919 | 0.309 | 1.174 | 0.263 | 0.55 | 25,26,27,28,30,35,37,40,41,42,73,74,75,76,77,78,79 ,88,90,91,92,93,94,96,97,98,99,127,148,149,150,152 ,154,179,180,181,182,183,193,194,195,196,197,198 |
| P16070-15 | 0.988 | 285 | 0.975 | 1025.913 | 0.566 | 0.681 | 0.905 | 0.221 | 1.144 | 0.193 | 0.644 | 25,26,27,28,30,35,37,38,40,41,42,43,44,45,48,73,74 ,75,76,77,78,90,92,94,96,111,112,113,127,148,149,1 50,152,154,162,166,167,170,171,172,173,174,176,177 ,178,179,181,182,183,195,196,197,198 |
| P16070-16 | 1.032 | 124 | 1.024 | 465.108 | 0.508 | 0.746 | 0.966 | 0.418 | 1.115 | 0.374 | 0.689 | 25,26,27,28,30,35,37,73,74,75,76,77,78,90,91,92,94 ,97,127,148,149,150,274,275,276,277,278,279 |
| P16070-17 | 0.986 | 280 | 1.018 | 843.78 | 0.617 | 0.658 | 0.843 | 0.289 | 0.972 | 0.297 | 0.893 | 25,26,27,28,30,35,37,38,41,42,43,45,46,47,48,73,74 ,75,76,77,78,79,88,90,91,92,95,96,97,98,99,107,111 ,112,113,114,127,148,149,150,162,166,167,168,170,1 73,174,176,177,178,179,180,181,182,184,296,297,298 ,299,300,301,302 |
| P16070-18 | 0.968 | 189 | 1.001 | 511.756 | 0.613 | 0.633 | 0.845 | 0.263 | 0.979 | 0.269 | 0.712 | 38,39,40,41,42,43,45,48,77,78,79,88,96,97,98,99,10 7,109,111,112,113,114,162,166,167,170,171,172,173, 174,176,177,178,179,180,181,182 |
| P16070-19 | 0.818 | 70 | 0.82 | 214.032 | 0.765 | 0.588 | 0.752 | 0.245 | 0.98 | 0.25 | 0.761 | 25,27,28,30,35,37,40,41,42,74,75,76,77,78,79,80,81 ,84,85,86,101,110,119,121,124 |
| P16070-3 | 0.991 | 150 | 1.019 | 476.77 | 0.591 | 0.669 | 0.882 | 0.321 | 0.989 | 0.325 | 0.61 | 25,26,27,28,30,35,37,73,74,75,76,77,78,90,91,92,94 ,96,127,148,149,150,271,272,273,274,275,276,277,27 8,279 |
| P16070-4 | 1.019 | 217 | 0.971 | 491.862 | 0.441 | 0.727 | 0.954 | 0.398 | 1.243 | 0.32 | 0.845 | 25,26,27,28,30,35,37,73,74,75,76,77,78,90,91,92,93 ,94,96,97,127,150,256,257,259,260,262,263,264,265 |
| P16070-5 | 1.005 | 156 | 1.007 | 375.928 | 0.548 | 0.705 | 0.949 | 0.449 | 1.093 | 0.411 | 0.869 | 25,26,27,28,30,35,37,72,73,74,75,76,77,78,90,91,92 ,94,96,127,148,149,150,152,154,295,296,297,298,299 ,300,301,302 |
| P16070-6 | 0.981 | 152 | 0.995 | 334.082 | 0.545 | 0.669 | 0.886 | 0.373 | 1.061 | 0.351 | 0.881 | 25,26,27,28,30,35,37,73,74,75,76,77,78,91,92,94,96 ,127,148,149,150,154,303,304,305,306,307,308,309,3 10 |
| P16070-7 | 1.038 | 113 | 0.975 | 310.415 | 0.498 | 0.754 | 1.049 | 0.446 | 1.281 | 0.348 | 0.511 | 25,26,27,28,30,35,37,74,75,76,77,78,90,92,94,96,97 ,148,149,150,152,303,304,305,306,307 |
| P16070-8 | 0.905 | 68 | 0.892 | 235.641 | 0.632 | 0.734 | 0.945 | 0.633 | 0.995 | 0.636 | 0.946 | 25,26,27,28,30,35,37,74,75,76,77,78,90,127,148,149 ,150,302,303,304,305,306,307 |
| P16070-9 | 1.007 | 127 | 1.008 | 483.63 | 0.66 | 0.709 | 0.93 | 0.274 | 1.097 | 0.25 | 0.914 | 23,25,26,27,28,29,30,34,35,37,39,73,74,75,76,77,78 ,90,91,92,127,129,130,131,132,148,149,150,151,152, 154,301,302,303,304,305,306,307,308,309,310 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P16070-1_P16070-1_4pz4_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P16070-1_4pz4_A_P16070-10.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-11.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-12.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-13.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-14.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-15.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-16.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-17.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-18.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-19.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-2.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-3.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-4.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-5.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-6.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-7.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-8.pdb |
| 3D view using mol* of P16070-1_4pz4_A_P16070-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P16070-1_P16070-10.pdb |
| 3D view using mol* of P16070-1_P16070-11.pdb |
| 3D view using mol* of P16070-1_P16070-12.pdb |
| 3D view using mol* of P16070-1_P16070-13.pdb |
| 3D view using mol* of P16070-1_P16070-14.pdb |
| 3D view using mol* of P16070-1_P16070-15.pdb |
| 3D view using mol* of P16070-1_P16070-16.pdb |
| 3D view using mol* of P16070-1_P16070-17.pdb |
| 3D view using mol* of P16070-1_P16070-18.pdb |
| 3D view using mol* of P16070-1_P16070-19.pdb |
| 3D view using mol* of P16070-1_P16070-2.pdb |
| 3D view using mol* of P16070-1_P16070-3.pdb |
| 3D view using mol* of P16070-1_P16070-4.pdb |
| 3D view using mol* of P16070-1_P16070-5.pdb |
| 3D view using mol* of P16070-1_P16070-6.pdb |
| 3D view using mol* of P16070-1_P16070-7.pdb |
| 3D view using mol* of P16070-1_P16070-8.pdb |
| 3D view using mol* of P16070-1_P16070-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P16070-1_vs_P16070-10.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-11.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-12.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-13.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-14.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-15.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-16.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-17.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-18.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-19.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-2.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-3.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-4.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-5.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-6.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-7.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-8.png |
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| ./stats/secondary_structure/figure/P16070-1_vs_P16070-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P16070-1_vs_P16070-10.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-11.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-12.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-13.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-14.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-15.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-16.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-17.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-18.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-19.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-2.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-3.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-4.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-5.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-6.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-7.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-8.png |
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| ./stats/relative_asa/P16070-1_vs_P16070-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Substitution;Start=675;End=675 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=676;End=742 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=140;End=742 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=30;End=742 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Substitution;Start=675;End=675 |
| P16070 | Region | 673 | 691 | Note=Required for interaction with EZR%2C MSN and RDX and for co-localization to microvilli;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15379 | Type=Deletion;Start=676;End=742 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CD44 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P16070 | CD44 | DB08818 | Hyaluronic acid | approved, vet_approved | binder |
| P16070 | CD44 | DB06550 | Bivatuzumab | investigational |
Related Diseases to CD44 |
| Previous studies relating to the alternative splicing of CD44 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CD44 | 8352881 | Novel variants of CD44 arising from alternative splicing: changes in the CD44 alternative splicing pattern of MCF-7 breast carcinoma cells treated with hyaluronidase. | CD44 is a cell-surface glycoprotein postulated to play a role in a variety of biological processes, including lymphocyte homing and tumor-cell metastasis. Several isoforms of CD44 have been identified in human cells, and the genesis of some of these isoforms has been attributed to alternative splicing. In the study presented here we amplified three novel transcript variants of CD44 from human cell lines using a reverse transcriptase-polymerase chain reaction strategy. Two of the novel isoforms differed from previously described CD44 isoforms as a result of alternative splicing that occurred at previously reported splice junctions. The third novel CD44 isoform was generated from a previously unreported alternative splice junction near the 5' end of the open reading frame. Southern blot analysis of genomic DNA revealed that these novel isoforms and all of the previously described CD44 isoforms arose from alternative splicing. The capability of cells to modify their CD44 alternative splicing pattern was demonstrated in MCF-7 cells, which altered their CD44-isoform expression pattern in response to treatment with hyaluronidase. A better understanding of mechanisms regulating CD44 alternative splicing may provide insights into diverse processes, including tumor-cell metastasis and lymphocyte homing. | D001943 | Breast Neoplasms |
| CD44 | 8640758 | Restricted patterns of CD44 variant exon expression in human papillary thyroid carcinoma. | CD44 is a polymorphic family of cell surface proteoglycans and glycoproteins implicated in cell-cell and cell-matrix adhesion interactions, cell migration, and tumor metastasis. CD44 exists as a standard form and as multiple isoforms arising from alternative splicing of variant exons (termed v1-v10) encoding parts of the extracellular domain. We demonstrated previously that papillary thyroid carcinomas exhibit aberrant patterns of alternative CD44 mRNA splicing (G. Ermak et al., Cancer Res., 55: 4594-4598, 1995). In the present report, we use reverse transcription-PCR using a new high-performance polymerase formulation (Ex Taq; TaKaRa Shuzo Co., Ltd., Otsu, Japan) , followed by Southern hybridization, and demonstrate that alternative exon usage in papillary thyroid carcinomas is restricted primarily to exons v6, v7, v8, v9, and v10, with weak expression of v3. Expression of v8 is tightly linked to v9 and closely related to v10 expression. Also, v6 and v7 expression are closely related. Papillary thyroid cancers exhibit a marked increase in specific mRNA species containing combinations of exons v6 to v10. Several isoforms found in papillary cancers are not detectable in histologically normal tissue derived from the corresponding contralateral thyroid lobes. Examples include a 750-bp v6- and v7-containing PCR product and a 650-bp v8- and v9- containing PCR product. Finally, a novel 530-bp PCR product was discovered and shown to contain a subsegment from exon 4 joined to a subsegment of exon 13 (v8), followed by the complete sequence of exons 14 (v9) and 15 (v10). This novel isoform was present in both the papillary cancers and contralateral tissues. In conclusion, papillary thyroid cancers exhibit specific patterns of aberrant alternative CD44 splicing, distinguishing them from histologically normal thyroid tissue. | D002291 | Carcinoma, Papillary |
| CD44 | 8640758 | Restricted patterns of CD44 variant exon expression in human papillary thyroid carcinoma. | CD44 is a polymorphic family of cell surface proteoglycans and glycoproteins implicated in cell-cell and cell-matrix adhesion interactions, cell migration, and tumor metastasis. CD44 exists as a standard form and as multiple isoforms arising from alternative splicing of variant exons (termed v1-v10) encoding parts of the extracellular domain. We demonstrated previously that papillary thyroid carcinomas exhibit aberrant patterns of alternative CD44 mRNA splicing (G. Ermak et al., Cancer Res., 55: 4594-4598, 1995). In the present report, we use reverse transcription-PCR using a new high-performance polymerase formulation (Ex Taq; TaKaRa Shuzo Co., Ltd., Otsu, Japan) , followed by Southern hybridization, and demonstrate that alternative exon usage in papillary thyroid carcinomas is restricted primarily to exons v6, v7, v8, v9, and v10, with weak expression of v3. Expression of v8 is tightly linked to v9 and closely related to v10 expression. Also, v6 and v7 expression are closely related. Papillary thyroid cancers exhibit a marked increase in specific mRNA species containing combinations of exons v6 to v10. Several isoforms found in papillary cancers are not detectable in histologically normal tissue derived from the corresponding contralateral thyroid lobes. Examples include a 750-bp v6- and v7-containing PCR product and a 650-bp v8- and v9- containing PCR product. Finally, a novel 530-bp PCR product was discovered and shown to contain a subsegment from exon 4 joined to a subsegment of exon 13 (v8), followed by the complete sequence of exons 14 (v9) and 15 (v10). This novel isoform was present in both the papillary cancers and contralateral tissues. In conclusion, papillary thyroid cancers exhibit specific patterns of aberrant alternative CD44 splicing, distinguishing them from histologically normal thyroid tissue. | D013964 | Thyroid Neoplasms |
| CD44 | 12779084 | SR protein expression and CD44 splicing pattern in human breast tumours. | Altered gene expression during breast tumour progression can occur through alternative splicing of mRNAs. The SR proteins have been identified as important factors in RNA splicing and in the incorporation of alternative exons in experimental systems. We have studied SR protein expression by western blot in human breast cell lines and in a cohort of 101 invasive breast tumours to examine the relationship with alternatively spliced isoforms of the CD44 gene. Multiple SR proteins (SR75, 55, 40, 30) were expressed in most cell lines and tumours, and their relative expression was independent of grade, size, or nodal status. Higher relative expression of SR55 protein was associated with an altered pattern of CD44 variants incorporating exon v7 (p = 0.047) as determined by reverse transcription-polymerase chain reaction (RT-PCR) and Southern blot analysis. Nevertheless, transient transfection of MCF7 and HBL100 breast cell lines with SR55 had no direct effect on the expression of CD44 v7 variant expression. We conclude that while SR proteins may be important and necessary factors in mRNA splicing, other factors are also necessary to influence the regulation of alternatively spliced isoforms of CD44. | D001943 | Breast Neoplasms |
| CD44 | 12883358 | CD44s adhesive function spontaneous and PMA-inducible CD44 cleavage are regulated at post-translational level in cells of melanocytic lineage. | Adhesion between the CD44s receptor and hyaluronic acid plays an important role in cell migration, tumour growth and progression. Although the alternative splicing of CD44 variant exons represents the principal regulatory mechanism of CD44-mediated functions, CD44v spliced variants are scantily expressed in melanoma cells. For this reason, we have investigated the possibility that post-translational modifications of the CD44 standard receptor could play a pivotal role in regulating CD44-mediated functions in melanoma. Using metabolic inhibitors of N- and O-glycosylation, as well as melanoma transfectants expressing CD44s O-glycosylation site-specific mutants, we performed structural and functional analysis of N- and O-deglycosylated CD44s molecules expressed in melanoma cells. We discovered that complete N- and O-glycosylation is not required by CD44s to be correctly expressed on the melanoma cell surface. Indeed, variably glycosylated and functionally different CD44s molecules were constitutively expressed in primary and metastatic lesions. Furthermore, we observed that changes in N- and O-glycosylation of CD44s could modulate its cleavage. In fact, spontaneous CD44s shedding was dependent on the presence of partial or complete O-glycosylation of four serine-glycine motifs localized in the membrane-proximal CD44 ectodomain. Mutation of these serine residues, as well as an extensive metabolic O-deglycosylation, strongly impaired spontaneous CD44 shedding. Furthermore, an O-glycosylation-independent mechanism of CD44 cleavage has been identified. This alternative mechanism of receptor cleavage is phorbol 12-myristate-13-acetate (PMA) inducible, mediated by metalloproteinase and requires the presence of N-linked sugar residues. Our findings demonstrate that the post-translational modification of CD44s represents the principal regulatory mechanism of CD44s-mediated functions in melanoma. | D008545 | Melanoma |
| CD44 | 12883358 | CD44s adhesive function spontaneous and PMA-inducible CD44 cleavage are regulated at post-translational level in cells of melanocytic lineage. | Adhesion between the CD44s receptor and hyaluronic acid plays an important role in cell migration, tumour growth and progression. Although the alternative splicing of CD44 variant exons represents the principal regulatory mechanism of CD44-mediated functions, CD44v spliced variants are scantily expressed in melanoma cells. For this reason, we have investigated the possibility that post-translational modifications of the CD44 standard receptor could play a pivotal role in regulating CD44-mediated functions in melanoma. Using metabolic inhibitors of N- and O-glycosylation, as well as melanoma transfectants expressing CD44s O-glycosylation site-specific mutants, we performed structural and functional analysis of N- and O-deglycosylated CD44s molecules expressed in melanoma cells. We discovered that complete N- and O-glycosylation is not required by CD44s to be correctly expressed on the melanoma cell surface. Indeed, variably glycosylated and functionally different CD44s molecules were constitutively expressed in primary and metastatic lesions. Furthermore, we observed that changes in N- and O-glycosylation of CD44s could modulate its cleavage. In fact, spontaneous CD44s shedding was dependent on the presence of partial or complete O-glycosylation of four serine-glycine motifs localized in the membrane-proximal CD44 ectodomain. Mutation of these serine residues, as well as an extensive metabolic O-deglycosylation, strongly impaired spontaneous CD44 shedding. Furthermore, an O-glycosylation-independent mechanism of CD44 cleavage has been identified. This alternative mechanism of receptor cleavage is phorbol 12-myristate-13-acetate (PMA) inducible, mediated by metalloproteinase and requires the presence of N-linked sugar residues. Our findings demonstrate that the post-translational modification of CD44s represents the principal regulatory mechanism of CD44s-mediated functions in melanoma. | D012878 | Skin Neoplasms |
| CD44 | 14534711 | Evaluation of CD44 variant 6 expression and clinicopathological factors in pulmonary metastases from colon carcinoma. | Although relatively little is known about the molecular mechanisms underlying tumor progression, recently CD44 glycoproteins and the c-Met receptor tyrosine kinase have been identified as potentially important components of the metastatic cascade. CD44 is a family of transmembrane receptors generated from a single gene by alternative splicing and differential glycosylation. Important biological processes involving CD44 glycoproteins include cell adhesion, lymphocyte homing, hematopoiesis, tumor progression and metastasis. The precise mechanism via which CD44 promotes tumorigenesis have not yet been elucidated. We evaluated the expression of adhesion molecule CD44 variant 6 in pulmonary metastases from colorectal carcinomas and its correlation with clinicopathological parameters. Twenty patients were randomly selected from the patients who had undergone a resection of pulmonary metastasis from colorectal cancer. Formalin-fixed, paraffin-embedded archival specimens of tumor tissues and adjacent normal mucosa from these patients were the subjects of the present study. Immunoreactivity for CD44 was quantified. Specimens were considered positive if almost 25% of the neoplastic cells were stained. CD44 v6 expression was related to the interval between colon resection and metastases diagnosis, the number of pulmonary metastases, and the survival after lung resection. No statistical correlation was found between CD44 v6 positivity and disease-free interval after colon resection, number of metastases or 2-year survival after lung resection. Probably CD44 v6 is necessary and sufficient to confer metastatic potential to carcinoma cells increasing the migration capacity and participating in invasion via changes in adhesion to the extracellular ligands, but is not necessary to modify the clinical history of the metastases. Therefore the evaluation of CD44 v6 expression in lung metastases does not influence the therapeutic scheme. | D003110 | Colonic Neoplasms |
| CD44 | 14534711 | Evaluation of CD44 variant 6 expression and clinicopathological factors in pulmonary metastases from colon carcinoma. | Although relatively little is known about the molecular mechanisms underlying tumor progression, recently CD44 glycoproteins and the c-Met receptor tyrosine kinase have been identified as potentially important components of the metastatic cascade. CD44 is a family of transmembrane receptors generated from a single gene by alternative splicing and differential glycosylation. Important biological processes involving CD44 glycoproteins include cell adhesion, lymphocyte homing, hematopoiesis, tumor progression and metastasis. The precise mechanism via which CD44 promotes tumorigenesis have not yet been elucidated. We evaluated the expression of adhesion molecule CD44 variant 6 in pulmonary metastases from colorectal carcinomas and its correlation with clinicopathological parameters. Twenty patients were randomly selected from the patients who had undergone a resection of pulmonary metastasis from colorectal cancer. Formalin-fixed, paraffin-embedded archival specimens of tumor tissues and adjacent normal mucosa from these patients were the subjects of the present study. Immunoreactivity for CD44 was quantified. Specimens were considered positive if almost 25% of the neoplastic cells were stained. CD44 v6 expression was related to the interval between colon resection and metastases diagnosis, the number of pulmonary metastases, and the survival after lung resection. No statistical correlation was found between CD44 v6 positivity and disease-free interval after colon resection, number of metastases or 2-year survival after lung resection. Probably CD44 v6 is necessary and sufficient to confer metastatic potential to carcinoma cells increasing the migration capacity and participating in invasion via changes in adhesion to the extracellular ligands, but is not necessary to modify the clinical history of the metastases. Therefore the evaluation of CD44 v6 expression in lung metastases does not influence the therapeutic scheme. | D018450 | Disease Progression |
| CD44 | 14534711 | Evaluation of CD44 variant 6 expression and clinicopathological factors in pulmonary metastases from colon carcinoma. | Although relatively little is known about the molecular mechanisms underlying tumor progression, recently CD44 glycoproteins and the c-Met receptor tyrosine kinase have been identified as potentially important components of the metastatic cascade. CD44 is a family of transmembrane receptors generated from a single gene by alternative splicing and differential glycosylation. Important biological processes involving CD44 glycoproteins include cell adhesion, lymphocyte homing, hematopoiesis, tumor progression and metastasis. The precise mechanism via which CD44 promotes tumorigenesis have not yet been elucidated. We evaluated the expression of adhesion molecule CD44 variant 6 in pulmonary metastases from colorectal carcinomas and its correlation with clinicopathological parameters. Twenty patients were randomly selected from the patients who had undergone a resection of pulmonary metastasis from colorectal cancer. Formalin-fixed, paraffin-embedded archival specimens of tumor tissues and adjacent normal mucosa from these patients were the subjects of the present study. Immunoreactivity for CD44 was quantified. Specimens were considered positive if almost 25% of the neoplastic cells were stained. CD44 v6 expression was related to the interval between colon resection and metastases diagnosis, the number of pulmonary metastases, and the survival after lung resection. No statistical correlation was found between CD44 v6 positivity and disease-free interval after colon resection, number of metastases or 2-year survival after lung resection. Probably CD44 v6 is necessary and sufficient to confer metastatic potential to carcinoma cells increasing the migration capacity and participating in invasion via changes in adhesion to the extracellular ligands, but is not necessary to modify the clinical history of the metastases. Therefore the evaluation of CD44 v6 expression in lung metastases does not influence the therapeutic scheme. | D008175 | Lung Neoplasms |
| CD44 | 14534711 | Evaluation of CD44 variant 6 expression and clinicopathological factors in pulmonary metastases from colon carcinoma. | Although relatively little is known about the molecular mechanisms underlying tumor progression, recently CD44 glycoproteins and the c-Met receptor tyrosine kinase have been identified as potentially important components of the metastatic cascade. CD44 is a family of transmembrane receptors generated from a single gene by alternative splicing and differential glycosylation. Important biological processes involving CD44 glycoproteins include cell adhesion, lymphocyte homing, hematopoiesis, tumor progression and metastasis. The precise mechanism via which CD44 promotes tumorigenesis have not yet been elucidated. We evaluated the expression of adhesion molecule CD44 variant 6 in pulmonary metastases from colorectal carcinomas and its correlation with clinicopathological parameters. Twenty patients were randomly selected from the patients who had undergone a resection of pulmonary metastasis from colorectal cancer. Formalin-fixed, paraffin-embedded archival specimens of tumor tissues and adjacent normal mucosa from these patients were the subjects of the present study. Immunoreactivity for CD44 was quantified. Specimens were considered positive if almost 25% of the neoplastic cells were stained. CD44 v6 expression was related to the interval between colon resection and metastases diagnosis, the number of pulmonary metastases, and the survival after lung resection. No statistical correlation was found between CD44 v6 positivity and disease-free interval after colon resection, number of metastases or 2-year survival after lung resection. Probably CD44 v6 is necessary and sufficient to confer metastatic potential to carcinoma cells increasing the migration capacity and participating in invasion via changes in adhesion to the extracellular ligands, but is not necessary to modify the clinical history of the metastases. Therefore the evaluation of CD44 v6 expression in lung metastases does not influence the therapeutic scheme. | D009362 | Neoplasm Metastasis |
| CD44 | 15783086 | Expression of CD44v6 correlates with cell proliferation and cellular atypia in urothelial carcinoma cell lines 5637 and HT1197. | CD44 comprises a family of membrane adhesion molecules encoded by a single gene and diversified by alternative splicing and extensive posttranslational modifications. Alterations of CD44 expression patterns are linked to tumour invasion and formation of metastases. However, CD44 expression and its relation to the biological properties of tumours vary depending on the tumour type and origin. In transitional cell carcinoma of the urinary bladder, low CD44 expression is linked to enhanced tumour aggressiveness. We studied CD44 expression in two urothelial cancer cell lines, HT1197 and 5637. CD44s and a v6 variable exon-containing splice variants were detected in both cell lines by reverse transcription-PCR and by commercially available monoclonal antibodies. In both cell lines, Western blot analysis detected immunoreactive proteins with approximate sizes 70-85 kD, 95-110 kD, and 120-140 kD with CD44v6 antibody and weak bands with size 70-98 kD with CD44s antibody. At the cellular level, the pattern of CD44 immunoreactivity correlated with a lower level of cell differentiation and a higher degree of cell proliferation. In HT1197 cells, the CD44v6 was detected predominantly in small proliferating cells and in large multinuclear atypical cells. CD44s and CD44v6 displayed low immunoreactivity in HT1197 cells with a higher degree of epithelial differentiation. The 5637 cells expressed CD44v6 strongly and CD44s weakly. We conclude that CD44v6 expression correlates with a higher proliferative activity and with a stem cell-like phenotype in both cell lines and with cellular atypia in HT1197 cells. | D002295 | Carcinoma, Transitional Cell |
| CD44 | 15783086 | Expression of CD44v6 correlates with cell proliferation and cellular atypia in urothelial carcinoma cell lines 5637 and HT1197. | CD44 comprises a family of membrane adhesion molecules encoded by a single gene and diversified by alternative splicing and extensive posttranslational modifications. Alterations of CD44 expression patterns are linked to tumour invasion and formation of metastases. However, CD44 expression and its relation to the biological properties of tumours vary depending on the tumour type and origin. In transitional cell carcinoma of the urinary bladder, low CD44 expression is linked to enhanced tumour aggressiveness. We studied CD44 expression in two urothelial cancer cell lines, HT1197 and 5637. CD44s and a v6 variable exon-containing splice variants were detected in both cell lines by reverse transcription-PCR and by commercially available monoclonal antibodies. In both cell lines, Western blot analysis detected immunoreactive proteins with approximate sizes 70-85 kD, 95-110 kD, and 120-140 kD with CD44v6 antibody and weak bands with size 70-98 kD with CD44s antibody. At the cellular level, the pattern of CD44 immunoreactivity correlated with a lower level of cell differentiation and a higher degree of cell proliferation. In HT1197 cells, the CD44v6 was detected predominantly in small proliferating cells and in large multinuclear atypical cells. CD44s and CD44v6 displayed low immunoreactivity in HT1197 cells with a higher degree of epithelial differentiation. The 5637 cells expressed CD44v6 strongly and CD44s weakly. We conclude that CD44v6 expression correlates with a higher proliferative activity and with a stem cell-like phenotype in both cell lines and with cellular atypia in HT1197 cells. | D002471 | Cell Transformation, Neoplastic |
| CD44 | 15783086 | Expression of CD44v6 correlates with cell proliferation and cellular atypia in urothelial carcinoma cell lines 5637 and HT1197. | CD44 comprises a family of membrane adhesion molecules encoded by a single gene and diversified by alternative splicing and extensive posttranslational modifications. Alterations of CD44 expression patterns are linked to tumour invasion and formation of metastases. However, CD44 expression and its relation to the biological properties of tumours vary depending on the tumour type and origin. In transitional cell carcinoma of the urinary bladder, low CD44 expression is linked to enhanced tumour aggressiveness. We studied CD44 expression in two urothelial cancer cell lines, HT1197 and 5637. CD44s and a v6 variable exon-containing splice variants were detected in both cell lines by reverse transcription-PCR and by commercially available monoclonal antibodies. In both cell lines, Western blot analysis detected immunoreactive proteins with approximate sizes 70-85 kD, 95-110 kD, and 120-140 kD with CD44v6 antibody and weak bands with size 70-98 kD with CD44s antibody. At the cellular level, the pattern of CD44 immunoreactivity correlated with a lower level of cell differentiation and a higher degree of cell proliferation. In HT1197 cells, the CD44v6 was detected predominantly in small proliferating cells and in large multinuclear atypical cells. CD44s and CD44v6 displayed low immunoreactivity in HT1197 cells with a higher degree of epithelial differentiation. The 5637 cells expressed CD44v6 strongly and CD44s weakly. We conclude that CD44v6 expression correlates with a higher proliferative activity and with a stem cell-like phenotype in both cell lines and with cellular atypia in HT1197 cells. | D009361 | Neoplasm Invasiveness |
| CD44 | 15783086 | Expression of CD44v6 correlates with cell proliferation and cellular atypia in urothelial carcinoma cell lines 5637 and HT1197. | CD44 comprises a family of membrane adhesion molecules encoded by a single gene and diversified by alternative splicing and extensive posttranslational modifications. Alterations of CD44 expression patterns are linked to tumour invasion and formation of metastases. However, CD44 expression and its relation to the biological properties of tumours vary depending on the tumour type and origin. In transitional cell carcinoma of the urinary bladder, low CD44 expression is linked to enhanced tumour aggressiveness. We studied CD44 expression in two urothelial cancer cell lines, HT1197 and 5637. CD44s and a v6 variable exon-containing splice variants were detected in both cell lines by reverse transcription-PCR and by commercially available monoclonal antibodies. In both cell lines, Western blot analysis detected immunoreactive proteins with approximate sizes 70-85 kD, 95-110 kD, and 120-140 kD with CD44v6 antibody and weak bands with size 70-98 kD with CD44s antibody. At the cellular level, the pattern of CD44 immunoreactivity correlated with a lower level of cell differentiation and a higher degree of cell proliferation. In HT1197 cells, the CD44v6 was detected predominantly in small proliferating cells and in large multinuclear atypical cells. CD44s and CD44v6 displayed low immunoreactivity in HT1197 cells with a higher degree of epithelial differentiation. The 5637 cells expressed CD44v6 strongly and CD44s weakly. We conclude that CD44v6 expression correlates with a higher proliferative activity and with a stem cell-like phenotype in both cell lines and with cellular atypia in HT1197 cells. | D001749 | Urinary Bladder Neoplasms |
| CD44 | 16354706 | Regulation of CD44 alternative splicing by SRm160 and its potential role in tumor cell invasion. | The multiple isoforms of the transmembrane glycoprotein CD44 are produced by alternative RNA splicing. Expression of CD44 isoforms containing variable 5 exon (v5) correlates with enhanced malignancy and invasiveness of some tumors. Here we demonstrate that SRm160, a splicing coactivator, regulates CD44 alternative splicing in a Ras-dependent manner. Overexpression of SRm160 stimulates inclusion of CD44 v5 when Ras is activated. Conversely, small interfering RNA (siRNA)-mediated silencing of SRm160 significantly reduces v5 inclusion. Immunoprecipitation shows association of SRm160 with Sam68, a protein that also stimulates v5 inclusion in a Ras-dependent manner, suggesting that these two proteins interact to regulate CD44 splicing. Importantly, siRNA-mediated depletion of CD44 v5 decreases tumor cell invasion. Reduction of SRm160 by siRNA transfection downregulates the endogenous levels of CD44 isoforms, including v5, and correlates with a decrease in tumor cell invasiveness. | D009361 | Neoplasm Invasiveness |
| CD44 | 17726647 | The CD44 standard/ezrin complex regulates Fas-mediated apoptosis in Jurkat cells. | "The transmembrane receptor CD44 conveys important signals from the extracellular microenvironment to the cytoplasm, a phenomena known as ""outside-in"" signaling. CD44 exists as several isoforms that result from alternative splicing, which differ only in the extracellular domain but yet exhibit different activities. CD44 is a binding partner for the membrane-cytoskeleton cross-linker protein ezrin. In this study, we demonstrate that only CD44 standard (CD44s) colocalizes and interacts with the actin cross-linkers ezrin and moesin using well-characterized cell lines engineered to express different CD44 isoforms. Importantly, we also show that the association CD44s-ezrin-actin is an important modulator of Fas-mediated apoptosis. The results highlight a mechanism by which signals from the extracellular milieu regulate intracellular signaling activities involved in programmed cell death." | D015458 | Leukemia, T-Cell |
| CD44 | 17911438 | CD44 involvement in autoimmune inflammations: the lesson to be learned from CD44-targeting by antibody or from knockout mice. | CD44 is a multistructural and multifunctional glycoprotein, the diversity of which is generated by alternative splicing. In this communication we review some aspects related to CD44 structure and function in experimental autoimmune inflammation, focusing on research performed in our own laboratory. We have found that CD44 targeting by antibody, passively injected into DBA/1 mice with collagen-induced arthritis (CIA) and NOD mice with type I diabetes or actively generated by CD44 cDNA vaccination of SJL/j mice with autoimmune encephalomyelitis, markedly reduced the pathological manifestations of these diseases by attenuating cell migration of the inflammatory cells and/or by their apoptotic killing. However, genetic deletion of CD44 by knockout technology enhanced the development of CIA because of molecular redundancy mediated by RHAMM (a receptor of hyaluronan-mediated motility). The mechanisms that stand behind these findings are discussed. | D001327 | Autoimmune Diseases |
| CD44 | 17911438 | CD44 involvement in autoimmune inflammations: the lesson to be learned from CD44-targeting by antibody or from knockout mice. | CD44 is a multistructural and multifunctional glycoprotein, the diversity of which is generated by alternative splicing. In this communication we review some aspects related to CD44 structure and function in experimental autoimmune inflammation, focusing on research performed in our own laboratory. We have found that CD44 targeting by antibody, passively injected into DBA/1 mice with collagen-induced arthritis (CIA) and NOD mice with type I diabetes or actively generated by CD44 cDNA vaccination of SJL/j mice with autoimmune encephalomyelitis, markedly reduced the pathological manifestations of these diseases by attenuating cell migration of the inflammatory cells and/or by their apoptotic killing. However, genetic deletion of CD44 by knockout technology enhanced the development of CIA because of molecular redundancy mediated by RHAMM (a receptor of hyaluronan-mediated motility). The mechanisms that stand behind these findings are discussed. | D004195 | Disease Models, Animal |
| CD44 | 17911438 | CD44 involvement in autoimmune inflammations: the lesson to be learned from CD44-targeting by antibody or from knockout mice. | CD44 is a multistructural and multifunctional glycoprotein, the diversity of which is generated by alternative splicing. In this communication we review some aspects related to CD44 structure and function in experimental autoimmune inflammation, focusing on research performed in our own laboratory. We have found that CD44 targeting by antibody, passively injected into DBA/1 mice with collagen-induced arthritis (CIA) and NOD mice with type I diabetes or actively generated by CD44 cDNA vaccination of SJL/j mice with autoimmune encephalomyelitis, markedly reduced the pathological manifestations of these diseases by attenuating cell migration of the inflammatory cells and/or by their apoptotic killing. However, genetic deletion of CD44 by knockout technology enhanced the development of CIA because of molecular redundancy mediated by RHAMM (a receptor of hyaluronan-mediated motility). The mechanisms that stand behind these findings are discussed. | D007249 | Inflammation |
| CD44 | 19167378 | Role of CD44s and CD44v6 on human breast cancer cell adhesion, migration, and invasion. | The interaction between the transmembrane receptor CD44 on epithelial tumor cells and its ligand hyaluronan in the surrounding extracellular matrix is important in tumor progression and metastasis. CD44 is encoded by a single 20-exon gene and expressed in standard form (CD44s), as well as a myriad of CD44 variants (CD44v) generated by alternative splicing of the CD44 mRNA. Previously, we demonstrated that hyaluronan (HA) production is increased at tumor-stroma interface in invasive and metastatic human breast cancers when compared with benign or premalignant lesions. We hypothesize that CD44 expression on breast cancer cells is a major contributing factor to cell adhesion, migration and invasion. To evaluate this hypothesis we examined the effects of 3 distinct anti-CD44s and 2 anti-CD44v6 monoclonal antibodies on breast cancer cell lines that expressed high and low CD44s and CD44v6. Using these antibodies we assessed the role of CD44 in cell adhesion, cell motility, and cell invasion using immobilized HA-coated wells, wound healing assays, and modified Boyden chamber respectively. Our results showed that anti-CD44s could inhibit breast cancer cell adhesion, motility and invasion, while anti-CD44v6 inhibits cell motility. In conclusion, our data suggests that CD44s is involved in breast cancer cell adhesion, motility and invasion through interaction with HA but CD44v6 is involved only in cell motility. Furthermore we concluded that antibodies against different epitopes on CD44 mediate distinct functional effects on breast cancer cells. | D001943 | Breast Neoplasms |
| CD44 | 19167378 | Role of CD44s and CD44v6 on human breast cancer cell adhesion, migration, and invasion. | The interaction between the transmembrane receptor CD44 on epithelial tumor cells and its ligand hyaluronan in the surrounding extracellular matrix is important in tumor progression and metastasis. CD44 is encoded by a single 20-exon gene and expressed in standard form (CD44s), as well as a myriad of CD44 variants (CD44v) generated by alternative splicing of the CD44 mRNA. Previously, we demonstrated that hyaluronan (HA) production is increased at tumor-stroma interface in invasive and metastatic human breast cancers when compared with benign or premalignant lesions. We hypothesize that CD44 expression on breast cancer cells is a major contributing factor to cell adhesion, migration and invasion. To evaluate this hypothesis we examined the effects of 3 distinct anti-CD44s and 2 anti-CD44v6 monoclonal antibodies on breast cancer cell lines that expressed high and low CD44s and CD44v6. Using these antibodies we assessed the role of CD44 in cell adhesion, cell motility, and cell invasion using immobilized HA-coated wells, wound healing assays, and modified Boyden chamber respectively. Our results showed that anti-CD44s could inhibit breast cancer cell adhesion, motility and invasion, while anti-CD44v6 inhibits cell motility. In conclusion, our data suggests that CD44s is involved in breast cancer cell adhesion, motility and invasion through interaction with HA but CD44v6 is involved only in cell motility. Furthermore we concluded that antibodies against different epitopes on CD44 mediate distinct functional effects on breast cancer cells. | D009361 | Neoplasm Invasiveness |
| CD44 | 19350388 | CD44 is overexpressed in basal-like breast cancers but is not a driver of 11p13 amplification. | Overexpression and alternative splicing of CD44 have been implicated in tumour progression. Here we describe the identification of a high level amplification of human 11p13, encompassing the CD44 gene, in primary breast cancers and cell lines and test whether CD44 acts as the driver of this amplicon. aCGH analysis revealed 11p13 amplification in 3% (3/100) of primary breast carcinomas and in two cell lines. The minimal region of amplification was 34.38-37.62 Mb. Amplification was confirmed by dual-colour FISH in these cell lines and further validated by CISH in an independent tumour cohort. CD44 expression in primary breast cancers was significantly associated with features of basal-like breast cancer. Detection of CD44 expression in breast cancer cell lines confirmed moderate to high expression in basal-like cell lines and minimal expression in luminal cell lines. In both, primary breast cancers and cell lines, 11p13 amplification was associated with high levels of CD44 mRNA expression. CD44 alternative splicing was detected in four of nine cell lines and in tumour samples, irrespective of the amplification status. RNAi mediated knock down of CD44 failed to reveal an increased dependence on CD44 expression for proliferation or survival in amplified cell lines. Given that expression of CD44 is not an absolute requirement for the survival of cells harbouring CD44 gene amplification, CD44 is unlikely to be a driver of the 11p13 amplicon. | D001943 | Breast Neoplasms |
| CD44 | 19582779 | Characterization of the expression of variant and standard CD44 in prostate cancer cells: identification of the possible molecular mechanism of CD44/MMP9 complex formation on the cell surface. | CD44 is a glycosylated adhesion molecule and osteopontin is one of its ligand. CD44 undergoes alternative splicing to produce variant isoforms. Our recent studies have shown an increase in the surface expression of CD44 isoforms (sCD44 and v4-v10 variant CD44) in prostate cancer cells over-expressing osteopontin (PC3/OPN). Formation of CD44/MMP9 complex on the cell surface is indispensable for MMP9 activity. In this study, we have characterized the expression of variant CD44 using RT-PCR, surface labeling with NHS-biotin, and immunoblotting. Expression of variant CD44 encompassing v4-v10 and sCD44 at mRNA and protein levels are of the same levels in PC3 and PC3/OPN cells. However, an increase in the surface expression of v6, v10, and sCD44 in PC3/OPN cells suggest that OPN may be a ligand for these isoforms. We then proceeded to determine the role of sCD44 in MMP9 activation. Based on our previous studies in osteoclasts, we hypothesized that phosphorylation of CD44 has a role on its surface expression and subsequent activation of MMP9. We have prepared TAT-fused CD44 peptides comprising unphosphorylated and constitutively phosphorylated serine residues at positions Ser323 and Ser325. Transduction of phosphopeptides at Ser323 and Ser323/325 into PC3 cells reduced the surface levels of CD44, MMP9 activity, and cell migration; but had no effect on the membrane localization of MMP9. However, MMP9 knock-down PC3 cells showed reduced CD44 at cellular and surface levels. Thus we conclude that surface expression of CD44 and activation of MMP9 on the cell surface are interdependent. | D011471 | Prostatic Neoplasms |
| CD44 | 20361869 | PCBP-1 regulates alternative splicing of the CD44 gene and inhibits invasion in human hepatoma cell line HepG2 cells. | PCBP1 (or alpha CP1 or hnRNP E1), a member of the PCBP family, is widely expressed in many human tissues and involved in regulation of transcription, transportation process, and function of RNA molecules. However, the role of PCBP1 in CD44 variants splicing still remains elusive. | D006528 | Carcinoma, Hepatocellular |
| CD44 | 20361869 | PCBP-1 regulates alternative splicing of the CD44 gene and inhibits invasion in human hepatoma cell line HepG2 cells. | PCBP1 (or alpha CP1 or hnRNP E1), a member of the PCBP family, is widely expressed in many human tissues and involved in regulation of transcription, transportation process, and function of RNA molecules. However, the role of PCBP1 in CD44 variants splicing still remains elusive. | D008113 | Liver Neoplasms |
| CD44 | 20361869 | PCBP-1 regulates alternative splicing of the CD44 gene and inhibits invasion in human hepatoma cell line HepG2 cells. | PCBP1 (or alpha CP1 or hnRNP E1), a member of the PCBP family, is widely expressed in many human tissues and involved in regulation of transcription, transportation process, and function of RNA molecules. However, the role of PCBP1 in CD44 variants splicing still remains elusive. | D009361 | Neoplasm Invasiveness |
| CD44 | 20856229 | De novo expression of CD44 variants in sporadic and hereditary gastric cancer. | CD44 is the major ubiquitously expressed cell surface receptor for hyaluronate. The CD44 gene encodes several protein isoforms due to extensive alternative splicing and post-translational modifications. Some of these CD44 variable isoforms have been foreseen as key players in malignant transformation and their expression is highly restricted and highly specific, unlike the canonical CD44 standard isoform. In this study, we aimed at dissecting the mRNA splicing pattern of CD44 in normal stomach and gastric cancer (GC) cell lines (n=9) using cloning and quantitative mRNA amplification assays. Moreover, we assessed the RNA levels and protein expression pattern of relevant splicing forms in distinct premalignant and malignant gastric lesions (sporadic (n=43) and hereditary (n=3) forms) using real-time RT-PCR and immunohistochemistry. We also explored the association of CD44 and E-cadherin expression by immunohistochemistry, as E-cadherin has a pivotal functional role in GC. We established the pattern of CD44 variant forms in normal stomach and gastric malignancy. We observed that although exon v6-containing isoforms were rarely expressed in normal gastric mucosa, they became increasingly expressed both in gastric premalignant (hyperplastic polyps, complete and incomplete intestinal metaplasia, low- and high-grade dysplasia) and malignant lesions (cell lines derived from GCs, primary sporadic GCs and hereditary diffuse GCs (HDGCs)). Moreover, we verified that whenever E-cadherin expression was absent, exon v6-containing CD44 isoforms were overexpressed. The lack of expression of CD44 isoforms containing exon v6 in the surface and foveolar epithelia of normal stomach and, its de novo expression in premalignant, as well as in sporadic and hereditary malignant lesions of the stomach, pinpoint CD44 v6-containing isoforms as potential biomarkers for early transformation of the gastric mucosa. Further, our results raise the hypothesis of using CD44v6 as a marker of early invasive intramucosal carcinoma in HDGC CDH1 mutation carriers that lack CDH1 expression in their tumors. | D009362 | Neoplasm Metastasis |
| CD44 | 20856229 | De novo expression of CD44 variants in sporadic and hereditary gastric cancer. | CD44 is the major ubiquitously expressed cell surface receptor for hyaluronate. The CD44 gene encodes several protein isoforms due to extensive alternative splicing and post-translational modifications. Some of these CD44 variable isoforms have been foreseen as key players in malignant transformation and their expression is highly restricted and highly specific, unlike the canonical CD44 standard isoform. In this study, we aimed at dissecting the mRNA splicing pattern of CD44 in normal stomach and gastric cancer (GC) cell lines (n=9) using cloning and quantitative mRNA amplification assays. Moreover, we assessed the RNA levels and protein expression pattern of relevant splicing forms in distinct premalignant and malignant gastric lesions (sporadic (n=43) and hereditary (n=3) forms) using real-time RT-PCR and immunohistochemistry. We also explored the association of CD44 and E-cadherin expression by immunohistochemistry, as E-cadherin has a pivotal functional role in GC. We established the pattern of CD44 variant forms in normal stomach and gastric malignancy. We observed that although exon v6-containing isoforms were rarely expressed in normal gastric mucosa, they became increasingly expressed both in gastric premalignant (hyperplastic polyps, complete and incomplete intestinal metaplasia, low- and high-grade dysplasia) and malignant lesions (cell lines derived from GCs, primary sporadic GCs and hereditary diffuse GCs (HDGCs)). Moreover, we verified that whenever E-cadherin expression was absent, exon v6-containing CD44 isoforms were overexpressed. The lack of expression of CD44 isoforms containing exon v6 in the surface and foveolar epithelia of normal stomach and, its de novo expression in premalignant, as well as in sporadic and hereditary malignant lesions of the stomach, pinpoint CD44 v6-containing isoforms as potential biomarkers for early transformation of the gastric mucosa. Further, our results raise the hypothesis of using CD44v6 as a marker of early invasive intramucosal carcinoma in HDGC CDH1 mutation carriers that lack CDH1 expression in their tumors. | D013274 | Stomach Neoplasms |
| CD44 | 21258793 | CD44 in hematological neoplasias. | The CD44 protein family spans a large group of transmembrane glycoproteins acquired by alternative splicing and post-translational modifications. The great heterogeneity in molecular structure is reflected in its various important functions: CD44 mediates (1) interaction between cell and extracellular matrix, (2) signal submission, e.g., by acting as co-receptor for membrane-spanning receptor tyrosine kinases or by association with intracellular molecules initiating several signaling pathways, and (3) anchor function connecting to the cytoskeleton via the ezrin-radixin-moesin protein family. The expression pattern of the different CD44 isoforms display strong variations dependent on cell type, state of activation, and differentiation stage. In hematopoietic cells, CD44 mediates interaction of progenitor cells and bone marrow stroma during hematopoiesis, regulates maturation, and activation-induced cell death in T cells, influences neutrophil and macrophage migration as well as cytokine production, and participates in lymphocyte extravasation and migration. CD44 is involved in development and progress of hematological neoplasias by enhancement of apoptotic resistance, invasiveness, as well as regulation of bone marrow homing, and mobilization of leukemia-initiating cells into the peripheral blood. Thereby altered CD44 expression functions as marker for worse prognosis in most hematological malignancies. Additionally, CD44 expression levels can be used to distinguish between different hematological neoplasias and subtypes. Concerning new treatment strategies, CD44 displays promising potential either by direct targeting of CD44 expressed on the malignant cells or reversing an acquired resistance to primary treatment mediated through altered CD44 expression. The former can be achieved by antibody or hyaluronan-based immunotherapy. | D019337 | Hematologic Neoplasms |
| CD44 | 21393860 | CD44 splice isoform switching in human and mouse epithelium is essential for epithelial-mesenchymal transition and breast cancer progression. | Epithelial-mesenchymal transition (EMT) is a tightly regulated process that is critical for embryogenesis but is abnormally activated during cancer metastasis and recurrence. Here we show that a switch in CD44 alternative splicing is required for EMT. Using both in vitro and in vivo systems, we have demonstrated a shift in CD44 expression from variant isoforms (CD44v) to the standard isoform (CD44s) during EMT. This isoform switch to CD44s was essential for cells to undergo EMT and was required for the formation of breast tumors that display EMT characteristics in mice. Mechanistically, the splicing factor epithelial splicing regulatory protein 1 (ESRP1) controlled the CD44 isoform switch and was critical for regulating the EMT phenotype. Additionally, the CD44s isoform activated Akt signaling, providing a mechanistic link to a key pathway that drives EMT. Finally, CD44s expression was upregulated in high-grade human breast tumors and was correlated with the level of the mesenchymal marker N-cadherin in these tumors. Together, our data suggest that regulation of CD44 alternative splicing causally contributes to EMT and breast cancer progression. | D001943 | Breast Neoplasms |
| CD44 | 21393860 | CD44 splice isoform switching in human and mouse epithelium is essential for epithelial-mesenchymal transition and breast cancer progression. | Epithelial-mesenchymal transition (EMT) is a tightly regulated process that is critical for embryogenesis but is abnormally activated during cancer metastasis and recurrence. Here we show that a switch in CD44 alternative splicing is required for EMT. Using both in vitro and in vivo systems, we have demonstrated a shift in CD44 expression from variant isoforms (CD44v) to the standard isoform (CD44s) during EMT. This isoform switch to CD44s was essential for cells to undergo EMT and was required for the formation of breast tumors that display EMT characteristics in mice. Mechanistically, the splicing factor epithelial splicing regulatory protein 1 (ESRP1) controlled the CD44 isoform switch and was critical for regulating the EMT phenotype. Additionally, the CD44s isoform activated Akt signaling, providing a mechanistic link to a key pathway that drives EMT. Finally, CD44s expression was upregulated in high-grade human breast tumors and was correlated with the level of the mesenchymal marker N-cadherin in these tumors. Together, our data suggest that regulation of CD44 alternative splicing causally contributes to EMT and breast cancer progression. | D018450 | Disease Progression |
| CD44 | 21393860 | CD44 splice isoform switching in human and mouse epithelium is essential for epithelial-mesenchymal transition and breast cancer progression. | Epithelial-mesenchymal transition (EMT) is a tightly regulated process that is critical for embryogenesis but is abnormally activated during cancer metastasis and recurrence. Here we show that a switch in CD44 alternative splicing is required for EMT. Using both in vitro and in vivo systems, we have demonstrated a shift in CD44 expression from variant isoforms (CD44v) to the standard isoform (CD44s) during EMT. This isoform switch to CD44s was essential for cells to undergo EMT and was required for the formation of breast tumors that display EMT characteristics in mice. Mechanistically, the splicing factor epithelial splicing regulatory protein 1 (ESRP1) controlled the CD44 isoform switch and was critical for regulating the EMT phenotype. Additionally, the CD44s isoform activated Akt signaling, providing a mechanistic link to a key pathway that drives EMT. Finally, CD44s expression was upregulated in high-grade human breast tumors and was correlated with the level of the mesenchymal marker N-cadherin in these tumors. Together, our data suggest that regulation of CD44 alternative splicing causally contributes to EMT and breast cancer progression. | D015674 | Mammary Neoplasms, Animal |
| CD44 | 23342032 | Demonstration of a melanoma-specific CD44 alternative splicing pattern that remains qualitatively stable, but shows quantitative changes during tumour progression. | The role of CD44 in the progression of human melanoma has mostly been characterised by qualitative changes in expression of its individual variable exons. These exons however, may be expressed to form a number of molecules, the alternative splice variants of CD44, which may be structurally and functionally different. Using real-time PCR measurements with variable exon specific primers we have determined that all are expressed in human melanoma. To permit comparison between different tumours we identified a stable CD44 variable exon (CD44v) expression pattern, or CD44 'fingerprint'. This was found to remain unchanged in melanoma cell lines cultured in different matrix environments. To evaluate evolution of this fingerprint during tumour progression we established a scid mouse model, in which the pure expression pattern of metastatic primary tumours, circulating cells and metastases, non-metastatic primary tumours and lung colonies could be studied. Our analyses demonstrated, that although the melanoma CD44 fingerprint is qualitatively stable, quantitative changes are observed suggesting a possible role in tumour progression. | D002471 | Cell Transformation, Neoplastic |
| CD44 | 23342032 | Demonstration of a melanoma-specific CD44 alternative splicing pattern that remains qualitatively stable, but shows quantitative changes during tumour progression. | The role of CD44 in the progression of human melanoma has mostly been characterised by qualitative changes in expression of its individual variable exons. These exons however, may be expressed to form a number of molecules, the alternative splice variants of CD44, which may be structurally and functionally different. Using real-time PCR measurements with variable exon specific primers we have determined that all are expressed in human melanoma. To permit comparison between different tumours we identified a stable CD44 variable exon (CD44v) expression pattern, or CD44 'fingerprint'. This was found to remain unchanged in melanoma cell lines cultured in different matrix environments. To evaluate evolution of this fingerprint during tumour progression we established a scid mouse model, in which the pure expression pattern of metastatic primary tumours, circulating cells and metastases, non-metastatic primary tumours and lung colonies could be studied. Our analyses demonstrated, that although the melanoma CD44 fingerprint is qualitatively stable, quantitative changes are observed suggesting a possible role in tumour progression. | D018450 | Disease Progression |
| CD44 | 23342032 | Demonstration of a melanoma-specific CD44 alternative splicing pattern that remains qualitatively stable, but shows quantitative changes during tumour progression. | The role of CD44 in the progression of human melanoma has mostly been characterised by qualitative changes in expression of its individual variable exons. These exons however, may be expressed to form a number of molecules, the alternative splice variants of CD44, which may be structurally and functionally different. Using real-time PCR measurements with variable exon specific primers we have determined that all are expressed in human melanoma. To permit comparison between different tumours we identified a stable CD44 variable exon (CD44v) expression pattern, or CD44 'fingerprint'. This was found to remain unchanged in melanoma cell lines cultured in different matrix environments. To evaluate evolution of this fingerprint during tumour progression we established a scid mouse model, in which the pure expression pattern of metastatic primary tumours, circulating cells and metastases, non-metastatic primary tumours and lung colonies could be studied. Our analyses demonstrated, that although the melanoma CD44 fingerprint is qualitatively stable, quantitative changes are observed suggesting a possible role in tumour progression. | D008545 | Melanoma |
Clinically important variants in CD44 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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