Protein:CEACAM1 |
Protein Summary |
 Gene summary |
| Gene name: CEACAM1 | ASpdb.0 ID: 634 | Gene | Gene symbol | CEACAM1 | Gene ID | 634 |
| Gene name | CEA cell adhesion molecule 1 |
| Synonyms | BGP|BGP1|BGPI |
| Cytomap | 19q13.2 |
| Type of gene | protein-coding |
| Description | carcinoembryonic antigen-related cell adhesion molecule 1CD66a antigenantigen CD66carcinoembryonic antigen related cell adhesion molecule 1carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein) |
| Modification date | 20240310 |
| UniProtAcc | P13688 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CEACAM1 | GO:0001915 | negative regulation of T cell mediated cytotoxicity | 18424730 |
| Gene | CEACAM1 | GO:0005886 | plasma membrane | 17192268 |
| Gene | CEACAM1 | GO:0005911 | cell-cell junction | 16291724 |
| Gene | CEACAM1 | GO:0009986 | cell surface | 25363763 |
| Gene | CEACAM1 | GO:0016020 | membrane | 11994468 |
| Gene | CEACAM1 | GO:0016324 | apical plasma membrane | 10436421 |
| Gene | CEACAM1 | GO:0030054 | cell junction | 8018919 |
| Gene | CEACAM1 | GO:0030334 | regulation of cell migration | 16291724 |
| Gene | CEACAM1 | GO:0042101 | T cell receptor complex | 18424730 |
| Gene | CEACAM1 | GO:0042802 | identical protein binding | 26483485 |
| Gene | CEACAM1 | GO:0043318 | negative regulation of cytotoxic T cell degranulation | 18424730 |
| Gene | CEACAM1 | GO:0044319 | wound healing, spreading of cells | 16291724 |
| Gene | CEACAM1 | GO:0050860 | negative regulation of T cell receptor signaling pathway | 18424730 |
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 |
| P13688-1 | P13688-1_2gk2_A.pdb | 2GK2 | X-ray | 2.2 | A | 34 | 141 |
| 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 |
| P13688 | CEACAM1 | P13688-1 | P13688-10 | 526 | 468 | 460 | 468 | Substitution | ASDQRDLTE | TTPMTHLTR | 460 | 468 |
| P13688 | CEACAM1 | P13688-1 | P13688-10 | 526 | 468 | 469 | 526 | Deletion | none | none | 468 | 468 |
| P13688 | CEACAM1 | P13688-1 | P13688-11 | 526 | 368 | 320 | 416 | Substitution | ELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNY | D | 320 | 320 |
| P13688 | CEACAM1 | P13688-1 | P13688-11 | 526 | 368 | 459 | 464 | Substitution | RASDQR | SSGPLQ | 363 | 368 |
| P13688 | CEACAM1 | P13688-1 | P13688-11 | 526 | 368 | 465 | 526 | Deletion | none | none | 368 | 368 |
| P13688 | CEACAM1 | P13688-1 | P13688-2 | 526 | 417 | 416 | 417 | Substitution | YN | CK | 416 | 417 |
| P13688 | CEACAM1 | P13688-1 | P13688-2 | 526 | 417 | 418 | 526 | Deletion | none | none | 417 | 417 |
| P13688 | CEACAM1 | P13688-1 | P13688-3 | 526 | 321 | 320 | 321 | Substitution | EL | GK | 320 | 321 |
| P13688 | CEACAM1 | P13688-1 | P13688-3 | 526 | 321 | 322 | 526 | Deletion | none | none | 321 | 321 |
| P13688 | CEACAM1 | P13688-1 | P13688-4 | 526 | 351 | 321 | 351 | Substitution | LSPVVAKPQIKASKTTVTGDKDSVNLTCSTN | SPVLGEDEAVPGQHHPQHKPCQEGGCWDVLV | 321 | 351 |
| P13688 | CEACAM1 | P13688-1 | P13688-4 | 526 | 351 | 352 | 526 | Deletion | none | none | 351 | 351 |
| P13688 | CEACAM1 | P13688-1 | P13688-5 | 526 | 461 | 321 | 416 | Substitution | LSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNY | RQNLTMLPRLDSNSWAQAILPSVSQSAEITD | 321 | 351 |
| P13688 | CEACAM1 | P13688-1 | P13688-6 | 526 | 430 | 320 | 416 | Substitution | ELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNY | D | 320 | 320 |
| P13688 | CEACAM1 | P13688-1 | P13688-7 | 526 | 252 | 143 | 416 | Deletion | none | none | 142 | 142 |
| P13688 | CEACAM1 | P13688-1 | P13688-8 | 526 | 464 | 459 | 464 | Substitution | RASDQR | SSGPLQ | 459 | 464 |
| P13688 | CEACAM1 | P13688-1 | P13688-8 | 526 | 464 | 465 | 526 | Deletion | none | none | 464 | 464 |
| P13688 | CEACAM1 | P13688-1 | P13688-9 | 526 | 399 | 321 | 416 | Substitution | LSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNY | MAFHHVAKAGLKLLSSSNPPASTSQSAKITD | 321 | 351 |
| P13688 | CEACAM1 | P13688-1 | P13688-9 | 526 | 399 | 459 | 464 | Substitution | RASDQR | SSGPLQ | 394 | 399 |
| P13688 | CEACAM1 | P13688-1 | P13688-9 | 526 | 399 | 465 | 526 | Deletion | none | none | 399 | 399 |
| Multiple sequence alignment of our canonical and alternatively spliced CEACAM1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CEACAM1 |
| UniProt-id | ENSG | ENST | ENSP |
| P13688-1 | ENSG00000079385.23 | ENST00000161559.11 | ENSP00000161559.6 |
| P13688-11 | ENSG00000079385.23 | ENST00000403461.5 | ENSP00000384083.1 |
| P13688-5 | ENSG00000079385.23 | ENST00000358394.7 | ENSP00000351165.2 |
| P13688-6 | ENSG00000079385.23 | ENST00000352591.9 | ENSP00000244291.6 |
| P13688-8 | ENSG00000079385.23 | ENST00000403444.7 | ENSP00000384709.3 |
| P13688-9 | ENSG00000079385.23 | ENST00000599389.1 | ENSP00000471918.1 |
| UniProt-id | NM ID | NP ID |
| P13688-1 | NM_001712.4 | NP_001703.2 |
| P13688-10 | NM_001205344.1 | NP_001192273.1 |
| P13688-11 | NM_001184816.1 | NP_001171745.1 |
| P13688-4 | XM_011527206.1 | XP_011525508.1 |
| P13688-5 | NM_001184815.1 | NP_001171744.1 |
| P13688-6 | NM_001184813.1 | NP_001171742.1 |
| P13688-8 | NM_001024912.2 | NP_001020083.1 |
| Amino acid sequences of our canonical and alternatively spliced CEACAM1 |
| accession_id | Protein sequence |
| P13688-1 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF FKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALAC |
| P13688-10 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF FKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALAC |
| P13688-11 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTDNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGK |
| P13688-2 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF |
| P13688-3 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS |
| P13688-4 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS |
| P13688-5 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTERQNLTMLPRLDSNSWAQAILPSVSQSAEITDNALPQENGL SPGAIAGIVIGVVALVALIAVALACFLHFGKTGRASDQRDLTEHKPSVSNHTQDHSNDPPNKMNEVTYSTLNFEAQQPTQPTSASPSLTA |
| P13688-6 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTDNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGK |
| P13688-7 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHF |
| P13688-8 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF FKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALAC |
| P13688-9 | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQAT PGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYS WLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTEMAFHHVAKAGLKLLSSSNPPASTSQSAKITDNALPQENGL |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CEACAM1 (go to UniProt):P13688 |
| 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 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=320;End=416 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=416;End=417 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=418;End=526 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=320;End=321 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=322;End=526 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=321;End=351 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=352;End=526 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=321;End=416 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=320;End=416 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=143;End=416 |
| P13688 | Topological domain | 35 | 428 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=321;End=416 |
| P13688 | Transmembrane | 429 | 452 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=418;End=526 |
| P13688 | Transmembrane | 429 | 452 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=322;End=526 |
| P13688 | Transmembrane | 429 | 452 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=352;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=460;End=468 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=469;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=459;End=464 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=465;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=418;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=322;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=352;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=459;End=464 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=465;End=526 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=459;End=464 |
| P13688 | Topological domain | 453 | 526 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=465;End=526 |
| P13688 | Domain | 145 | 232 | Note=Ig-like C2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Deletion;Start=143;End=416 |
| P13688 | Domain | 237 | 317 | Note=Ig-like C2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Deletion;Start=143;End=416 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Substitution;Start=320;End=416 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Deletion;Start=322;End=526 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Substitution;Start=321;End=351 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Deletion;Start=352;End=526 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Substitution;Start=321;End=416 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Substitution;Start=320;End=416 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Deletion;Start=143;End=416 |
| P13688 | Domain | 323 | 413 | Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 | Type=Substitution;Start=321;End=416 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=460;End=468 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=460;End=468 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=460;End=468 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 461 | 513 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=460;End=468 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=469;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=459;End=464 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=418;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=322;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=352;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=459;End=464 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=459;End=464 |
| P13688 | Compositional bias | 461 | 476 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=469;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=418;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=322;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=352;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
| P13688 | Compositional bias | 477 | 513 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=465;End=526 |
Gene Isoform Structures and Expression Levels for CEACAM1 |
| Gene structures of our canonical and alternative spliced genes of CEACAM1 * 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 P13688-1 |
| 3D view using mol* of P13688-10 |
| 3D view using mol* of P13688-11 |
| 3D view using mol* of P13688-2 |
| 3D view using mol* of P13688-3 |
| 3D view using mol* of P13688-4 |
| 3D view using mol* of P13688-5 |
| 3D view using mol* of P13688-6 |
| 3D view using mol* of P13688-7 |
| 3D view using mol* of P13688-8 |
| 3D view using mol* of P13688-9 |
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 P13688-1 |
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| pLDDT distribution across the protein length of P13688-10 |
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| pLDDT distribution across the protein length of P13688-11 |
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| pLDDT distribution across the protein length of P13688-2 |
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| pLDDT distribution across the protein length of P13688-3 |
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| pLDDT distribution across the protein length of P13688-4 |
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| pLDDT distribution across the protein length of P13688-5 |
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| pLDDT distribution across the protein length of P13688-6 |
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| pLDDT distribution across the protein length of P13688-7 |
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| pLDDT distribution across the protein length of P13688-8 |
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| pLDDT distribution across the protein length of P13688-9 |
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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 P13688-1 |
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| Ramachandran plot of P13688-2 |
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| Ramachandran plot of P13688-3 |
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| Ramachandran plot of P13688-4 |
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| Ramachandran plot of P13688-5 |
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| Ramachandran plot of P13688-6 |
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| Ramachandran plot of P13688-9 |
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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 |
| P13688-1 | 0.738 | 39 | 0.73 | 83.692 | 0.661 | 0.622 | 0.84 | 1.239 | 0.708 | 1.751 | 0.683 | 176,177,178,184,185,187,188,191,192,193,197,200
|
| P13688-10 | 0.694 | 35 | 0.709 | 82.32 | 0.72 | 0.539 | 0.7 | 1.019 | 0.523 | 1.947 | 0.982 | 176,177,178,184,185,187,188,189,191,192,193,197,20 0 |
| P13688-11 | 0.599 | 26 | 0.584 | 66.199 | 0.803 | 0.518 | 0.679 | 0.669 | 0.631 | 1.06 | 0.825 | 177,178,184,185,186,187,188,191,193
|
| P13688-2 | 0.725 | 33 | 0.688 | 67.571 | 0.492 | 0.687 | 0.974 | 1.052 | 0.812 | 1.296 | 1.552 | 180,181,185,186,188,190,191,202,208,209,210,213
|
| P13688-3 | 0.613 | 21 | 0.562 | 72.03 | 0.72 | 0.632 | 0.749 | 0.857 | 0.76 | 1.128 | 0.979 | 180,181,186,188,190,191,202,208,209,210,211,213
|
| P13688-4 | 0.613 | 29 | 0.59 | 71.687 | 0.785 | 0.534 | 0.721 | 0.613 | 0.725 | 0.845 | 1.262 | 176,177,178,184,185,186,187,188,191,192,193,197
|
| P13688-5 | 0.6 | 29 | 0.53 | 56.938 | 0.655 | 0.607 | 0.864 | 0.743 | 1.042 | 0.713 | 0.355 | 246,247,248,249,250,319,321,322,323,324
|
| P13688-6 | 0.529 | 21 | 0.371 | 71.001 | 0.756 | 0.588 | 0.784 | 0.041 | 1.266 | 0.033 | 0.631 | 157,158,207,235,236,237,306,308,310
|
| P13688-7 | 0.533 | 19 | 0.346 | 51.107 | 0.683 | 0.619 | 0.9 | 0 | 1.333 | 0 | 1.358 | 69,79,94,96,98,99,109,113,115,116,120
|
| P13688-8 | 0.708 | 27 | 0.658 | 64.827 | 0.509 | 0.719 | 1.072 | 1.399 | 0.803 | 1.743 | 0.773 | 180,181,185,186,188,190,191,202,208,209,210,211,21 3 |
| P13688-9 | 0.687 | 45 | 0.618 | 91.581 | 0.72 | 0.591 | 0.789 | 0.233 | 1.128 | 0.207 | 0.582 | 245,246,247,248,249,250,253,319,321,322,323,324,32 5 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
 |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P13688-1_P13688-1_2gk2_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 P13688-1_2gk2_A_P13688-10.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-11.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-2.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-3.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-4.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-5.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-6.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-7.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-8.pdb |
| 3D view using mol* of P13688-1_2gk2_A_P13688-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P13688-1_P13688-10.pdb |
| 3D view using mol* of P13688-1_P13688-11.pdb |
| 3D view using mol* of P13688-1_P13688-2.pdb |
| 3D view using mol* of P13688-1_P13688-3.pdb |
| 3D view using mol* of P13688-1_P13688-4.pdb |
| 3D view using mol* of P13688-1_P13688-5.pdb |
| 3D view using mol* of P13688-1_P13688-6.pdb |
| 3D view using mol* of P13688-1_P13688-7.pdb |
| 3D view using mol* of P13688-1_P13688-8.pdb |
| 3D view using mol* of P13688-1_P13688-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P13688-1_vs_P13688-10.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-11.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-2.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-3.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-4.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-5.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-6.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-7.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-8.png |
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| ./stats/secondary_structure/figure/P13688-1_vs_P13688-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P13688-1_vs_P13688-10.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-11.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-2.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-3.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-4.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-5.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-6.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-7.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-8.png |
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| ./stats/relative_asa/P13688-1_vs_P13688-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=460;End=468 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 450 | 462 | Note=Interaction with calmodulin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=460;End=468 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Substitution;Start=459;End=464 |
| P13688 | Region | 452 | 526 | Note=Interaction with FLNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16573 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 489 | 526 | Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=469;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=418;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=322;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=352;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| P13688 | Region | 520 | 523 | Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 | Type=Deletion;Start=465;End=526 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CEACAM1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P13688 | CEACAM1 | DB00113 | Technetium Tc-99m arcitumomab | experimental | other/unknown |
Related Diseases to CEACAM1 |
| Previous studies relating to the alternative splicing of CEACAM1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CEACAM1 | 8055923 | Transcriptional control of the human biliary glycoprotein gene, a CEA gene family member down-regulated in colorectal carcinomas. | Biliary glycoprotein (BGP) isoantigens are derived by alternative splicing from a single gene and are the human homologs of rat C-CAM and the mouse Bgp species. These glycoproteins represent a family of cell-adhesion molecules. The mouse Bgp isoforms also act as receptors for the hepatitis viral capsid-protein. BGP is a member of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin supergene family, yet it displays restricted expression patterns and unique functions. Since the loss or reduced expression of BGP is associated with human colorectal carcinomas, the elements in its upstream regulatory region were analyzed. A cluster of transcriptional initiation sites and the minimal promoter, located within 150 bp upstream of the major transcriptional start site, were active in human colon carcinoma and hepatoma cells. Unlike the CEA gene, BGP gene transcription was not modulated by a silencer region; repetitive elements in the BGP upstream region were not involved in activation or repression. Footprinting experiments identified two cis-acting elements and mobility-shift assays demonstrated that these elements bound several transcription factors, among them, USF, HNF-4 and an AP-2-like factor. In cotransfection experiments, both the USF and HNF-4 transcription factors transactivate the BGP gene promoter and compete for the same regulatory element. The Sp1 transcription factor, shown to be involved in CEA gene transcriptional regulation, does not bind to the BGP gene promoter. We, therefore, propose that the relative distributions and interactions of these transcription factors mediate distinct transcriptional regulation of the BGP gene in colon and liver; this regulation could be distorted during the oncogenic process. | D015179 | Colorectal Neoplasms |
| CEACAM1 | 10955775 | C-CAM1, a candidate tumor suppressor gene, is abnormally expressed in primary lung cancers. | Previous studies have shown that the expression of the cell-cell adhesion molecule (C-CAM1), located at chromosome 19, is down-regulated in several types of human cancers, including prostate and breast cancers. Two major isoforms of C-CAM1, the long or L-form C-CAM1 and the short or S-form C-CAM1, are derived from the C-CAM1 gene through alternative splicing. Tumor cells transfected with L-form C-CAM1, which contains a cytoplasmic domain, display significantly lower growth rates and less tumorigenicity in both in vitro and in vivo models compared with untransfected tumor cells, suggesting that L-form C-CAM1 may be a tumor suppressor. The transfection of the cytoplasmic domain of L-form C-CAM1 could also cause suppression of tumor growth, further supporting the role of L-form C-CAM1 in tumorigenesis. In contrast to reports of most of the tumor types tested, Ohwada et al. (Am. J. Respir. Cell Mol. Biol., 11: 214-220, 1994) reported that C-CAM1 was not down-regulated or even up-regulated in lung cancer. Because the cytoplasmic domain of L-form C-CAM1 is critical for the tumor suppressor function of C-CAM1, we hypothesized that switching of the isoform rather than down- regulation of C-CAM1 gene expression occurs during lung tumorigenesis. To test this hypothesis, we analyzed pairs of tumor tissue and corresponding normal-appearing lung tissue from 51 patients with non-small cell lung cancer (NSCLC) and 43 cell lines to determine expression profiles of L-form C-CAM1 and S-form C-CAM1 using reverse transcription-PCR. We found that L-form C-CAM1 was the predominant form (75%; 38 of 51) in normal-appearing lung tissue, whereas most (84%; 43 of 51) of the primary NSCLC tissue samples expressed predominantly S-form C-CAM1 (P < 0.0001). Similarly, 19 (79%) of the 24 NSCLC cell lines and 17 (85%) of the 20 small cell lung cancer cell lines expressed predominantly S-form C-CAM1. The frequent alteration of the C-CAM1 expression pattern suggests that C-CAM1 has an important role in lung tumorigenesis. | D002289 | Carcinoma, Non-Small-Cell Lung |
| CEACAM1 | 10955775 | C-CAM1, a candidate tumor suppressor gene, is abnormally expressed in primary lung cancers. | Previous studies have shown that the expression of the cell-cell adhesion molecule (C-CAM1), located at chromosome 19, is down-regulated in several types of human cancers, including prostate and breast cancers. Two major isoforms of C-CAM1, the long or L-form C-CAM1 and the short or S-form C-CAM1, are derived from the C-CAM1 gene through alternative splicing. Tumor cells transfected with L-form C-CAM1, which contains a cytoplasmic domain, display significantly lower growth rates and less tumorigenicity in both in vitro and in vivo models compared with untransfected tumor cells, suggesting that L-form C-CAM1 may be a tumor suppressor. The transfection of the cytoplasmic domain of L-form C-CAM1 could also cause suppression of tumor growth, further supporting the role of L-form C-CAM1 in tumorigenesis. In contrast to reports of most of the tumor types tested, Ohwada et al. (Am. J. Respir. Cell Mol. Biol., 11: 214-220, 1994) reported that C-CAM1 was not down-regulated or even up-regulated in lung cancer. Because the cytoplasmic domain of L-form C-CAM1 is critical for the tumor suppressor function of C-CAM1, we hypothesized that switching of the isoform rather than down- regulation of C-CAM1 gene expression occurs during lung tumorigenesis. To test this hypothesis, we analyzed pairs of tumor tissue and corresponding normal-appearing lung tissue from 51 patients with non-small cell lung cancer (NSCLC) and 43 cell lines to determine expression profiles of L-form C-CAM1 and S-form C-CAM1 using reverse transcription-PCR. We found that L-form C-CAM1 was the predominant form (75%; 38 of 51) in normal-appearing lung tissue, whereas most (84%; 43 of 51) of the primary NSCLC tissue samples expressed predominantly S-form C-CAM1 (P < 0.0001). Similarly, 19 (79%) of the 24 NSCLC cell lines and 17 (85%) of the 20 small cell lung cancer cell lines expressed predominantly S-form C-CAM1. The frequent alteration of the C-CAM1 expression pattern suggests that C-CAM1 has an important role in lung tumorigenesis. | D018288 | Carcinoma, Small Cell |
| CEACAM1 | 10955775 | C-CAM1, a candidate tumor suppressor gene, is abnormally expressed in primary lung cancers. | Previous studies have shown that the expression of the cell-cell adhesion molecule (C-CAM1), located at chromosome 19, is down-regulated in several types of human cancers, including prostate and breast cancers. Two major isoforms of C-CAM1, the long or L-form C-CAM1 and the short or S-form C-CAM1, are derived from the C-CAM1 gene through alternative splicing. Tumor cells transfected with L-form C-CAM1, which contains a cytoplasmic domain, display significantly lower growth rates and less tumorigenicity in both in vitro and in vivo models compared with untransfected tumor cells, suggesting that L-form C-CAM1 may be a tumor suppressor. The transfection of the cytoplasmic domain of L-form C-CAM1 could also cause suppression of tumor growth, further supporting the role of L-form C-CAM1 in tumorigenesis. In contrast to reports of most of the tumor types tested, Ohwada et al. (Am. J. Respir. Cell Mol. Biol., 11: 214-220, 1994) reported that C-CAM1 was not down-regulated or even up-regulated in lung cancer. Because the cytoplasmic domain of L-form C-CAM1 is critical for the tumor suppressor function of C-CAM1, we hypothesized that switching of the isoform rather than down- regulation of C-CAM1 gene expression occurs during lung tumorigenesis. To test this hypothesis, we analyzed pairs of tumor tissue and corresponding normal-appearing lung tissue from 51 patients with non-small cell lung cancer (NSCLC) and 43 cell lines to determine expression profiles of L-form C-CAM1 and S-form C-CAM1 using reverse transcription-PCR. We found that L-form C-CAM1 was the predominant form (75%; 38 of 51) in normal-appearing lung tissue, whereas most (84%; 43 of 51) of the primary NSCLC tissue samples expressed predominantly S-form C-CAM1 (P < 0.0001). Similarly, 19 (79%) of the 24 NSCLC cell lines and 17 (85%) of the 20 small cell lung cancer cell lines expressed predominantly S-form C-CAM1. The frequent alteration of the C-CAM1 expression pattern suggests that C-CAM1 has an important role in lung tumorigenesis. | D008175 | Lung Neoplasms |
| CEACAM1 | 18507857 | Altered splicing of CEACAM1 in breast cancer: identification of regulatory sequences that control splicing of CEACAM1 into long or short cytoplasmic domain isoforms. | Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1), a cell adhesion molecule expressed in a variety of cell types is a putative tumor suppressor gene. Alternative splicing of CEACAM1 generates 11 different splice variants, which include 1-4 ectodomains with either short or long cytoplasmic domain generated by the exclusion (CEACAM1-S) or inclusion (CEACAM1-L) of exon 7. Studies in rodents indicate that optimal ratios of CEACAM1 splice variants are required to inhibit colonic tumor cell growth. | D001943 | Breast Neoplasms |
Clinically important variants in CEACAM1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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