Protein:FGFR1 |
Protein Summary |
Gene summary |
| Gene name: FGFR1 | ASpdb.0 ID: 2260 | Gene | Gene symbol | FGFR1 | Gene ID | 2260 |
| Gene name | fibroblast growth factor receptor 1 |
| Synonyms | BFGFR|CD331|CEK|ECCL|FGFBR|FGFR-1|FLG|FLT-2|FLT2|HBGFR|HH2|HRTFDS|KAL2|N-SAM|OGD|bFGF-R-1 |
| Cytomap | 8p11.23 |
| Type of gene | protein-coding |
| Description | fibroblast growth factor receptor 1FGFR1/PLAG1 fusionFMS-like tyrosine kinase 2basic fibroblast growth factor receptor 1fms-related tyrosine kinase 2heparin-binding growth factor receptorhydroxyaryl-protein kinaseproto-oncogene c-Fgr |
| Modification date | 20240416 |
| UniProtAcc | P11362 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | FGFR1 | GO:0004713 | protein tyrosine kinase activity | 8622701 |
| Gene | FGFR1 | GO:0005007 | fibroblast growth factor receptor activity | 18480409|20133753 |
| Gene | FGFR1 | GO:0005886 | plasma membrane | 18480409 |
| Gene | FGFR1 | GO:0008201 | heparin binding | 18480409 |
| Gene | FGFR1 | GO:0008284 | positive regulation of cell population proliferation | 8663044 |
| Gene | FGFR1 | GO:0008543 | fibroblast growth factor receptor signaling pathway | 8663044|21885851 |
| Gene | FGFR1 | GO:0010863 | positive regulation of phospholipase C activity | 18480409 |
| Gene | FGFR1 | GO:0017134 | fibroblast growth factor binding | 8663044|18480409 |
| Gene | FGFR1 | GO:0018108 | peptidyl-tyrosine phosphorylation | 8622701|18480409 |
| Gene | FGFR1 | GO:0043235 | receptor complex | 23382219 |
| Gene | FGFR1 | GO:0043406 | positive regulation of MAP kinase activity | 8622701|18480409 |
| Gene | FGFR1 | GO:0044344 | cellular response to fibroblast growth factor stimulus | 21885851 |
| Gene | FGFR1 | GO:0046777 | protein autophosphorylation | 8622701 |
| Gene | FGFR1 | GO:0090722 | receptor-receptor interaction | 24157794 |
| Gene | FGFR1 | GO:2001028 | positive regulation of endothelial cell chemotaxis | 21885851 |
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 |
| P11362-1 | P11362-1_3gql_A.pdb | 3GQL | X-ray | 2.8 | A | 463 | 774 |
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 |
| P11362 | FGFR1 | P11362-1 | P11362-10 | 822 | 573 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-10 | 822 | 573 | 619 | 662 | Substitution | CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRL | VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHSPHRLL | 530 | 573 |
| P11362 | FGFR1 | P11362-1 | P11362-10 | 822 | 573 | 663 | 822 | Deletion | none | none | 573 | 573 |
| P11362 | FGFR1 | P11362-1 | P11362-11 | 822 | 571 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-11 | 822 | 571 | 428 | 429 | Deletion | none | none | 338 | 338 |
| P11362 | FGFR1 | P11362-1 | P11362-11 | 822 | 571 | 619 | 662 | Substitution | CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRL | VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHSPHRLL | 528 | 571 |
| P11362 | FGFR1 | P11362-1 | P11362-11 | 822 | 571 | 663 | 822 | Deletion | none | none | 571 | 571 |
| P11362 | FGFR1 | P11362-1 | P11362-12 | 822 | 502 | 1 | 160 | Deletion | none | none | 0 | 0 |
| P11362 | FGFR1 | P11362-1 | P11362-12 | 822 | 502 | 619 | 662 | Substitution | CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRL | VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHSPHRLL | 459 | 502 |
| P11362 | FGFR1 | P11362-1 | P11362-12 | 822 | 502 | 663 | 822 | Deletion | none | none | 502 | 502 |
| P11362 | FGFR1 | P11362-1 | P11362-13 | 822 | 500 | 1 | 160 | Deletion | none | none | 0 | 0 |
| P11362 | FGFR1 | P11362-1 | P11362-13 | 822 | 500 | 428 | 429 | Deletion | none | none | 267 | 267 |
| P11362 | FGFR1 | P11362-1 | P11362-13 | 822 | 500 | 619 | 662 | Substitution | CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRL | VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHSPHRLL | 457 | 500 |
| P11362 | FGFR1 | P11362-1 | P11362-13 | 822 | 500 | 663 | 822 | Deletion | none | none | 500 | 500 |
| P11362 | FGFR1 | P11362-1 | P11362-14 | 822 | 731 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-14 | 822 | 731 | 148 | 149 | Deletion | none | none | 58 | 58 |
| P11362 | FGFR1 | P11362-1 | P11362-15 | 822 | 150 | 120 | 150 | Substitution | DALPSSEDDDDDDDSSSEEKETDNTKPNRMP | ACPDLQEAKWCSASFHSITPLPFGLGTRLSD | 120 | 150 |
| P11362 | FGFR1 | P11362-1 | P11362-15 | 822 | 150 | 151 | 822 | Deletion | none | none | 150 | 150 |
| P11362 | FGFR1 | P11362-1 | P11362-16 | 822 | 302 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-16 | 822 | 302 | 313 | 391 | Substitution | TAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMV | VIMAPVFVGQSTGKETTVSGAQVPVGRLSCPRMGSFLTLQAHTLHLSRDLATSPRTSNRGHKVEVSWEQRAAGMGGAGL | 224 | 302 |
| P11362 | FGFR1 | P11362-1 | P11362-16 | 822 | 302 | 392 | 822 | Deletion | none | none | 302 | 302 |
| P11362 | FGFR1 | P11362-1 | P11362-17 | 822 | 61 | 32 | 61 | Substitution | QPWGAPVEVESFLVHPGDLLQLRCRLRDDV | CPDLQEAKSCSASFHSITPLPFGLGTRLSD | 32 | 61 |
| P11362 | FGFR1 | P11362-1 | P11362-17 | 822 | 61 | 62 | 822 | Deletion | none | none | 61 | 61 |
| P11362 | FGFR1 | P11362-1 | P11362-18 | 822 | 300 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-18 | 822 | 300 | 148 | 149 | Deletion | none | none | 58 | 58 |
| P11362 | FGFR1 | P11362-1 | P11362-18 | 822 | 300 | 313 | 391 | Substitution | TAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMV | VIMAPVFVGQSTGKETTVSGAQVPVGRLSCPRMGSFLTLQAHTLHLSRDLATSPRTSNRGHKVEVSWEQRAAGMGGAGL | 222 | 300 |
| P11362 | FGFR1 | P11362-1 | P11362-18 | 822 | 300 | 392 | 822 | Deletion | none | none | 300 | 300 |
| P11362 | FGFR1 | P11362-1 | P11362-19 | 822 | 822 | 119 | 119 | Substitution | S | SVPI | 119 | 122 |
| P11362 | FGFR1 | P11362-1 | P11362-19 | 822 | 822 | 148 | 149 | Deletion | none | none | 150 | 150 |
| P11362 | FGFR1 | P11362-1 | P11362-19 | 822 | 822 | 313 | 360 | Substitution | TAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLE | HSGINSSDAEVLTLFNVTEAQSGEYVCKVSNYIGEANQSAWLTVTRP | 314 | 360 |
| P11362 | FGFR1 | P11362-1 | P11362-2 | 822 | 820 | 428 | 429 | Deletion | none | none | 427 | 427 |
| P11362 | FGFR1 | P11362-1 | P11362-20 | 822 | 812 | 1 | 30 | Substitution | MWSWKCLLFWAVLVTATLCTARPSPTLPEQ | MAAVTRDFGEMLLHSGRVLPAE | 1 | 22 |
| P11362 | FGFR1 | P11362-1 | P11362-20 | 822 | 812 | 427 | 428 | Deletion | none | none | 418 | 418 |
| P11362 | FGFR1 | P11362-1 | P11362-21 | 822 | 853 | 1 | 1 | Substitution | M | MEARVSLKRRIELTVEYPWRCGALSPTSNCRTGM | 1 | 34 |
| P11362 | FGFR1 | P11362-1 | P11362-21 | 822 | 853 | 148 | 149 | Deletion | none | none | 180 | 180 |
| P11362 | FGFR1 | P11362-1 | P11362-3 | 822 | 733 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-4 | 822 | 731 | 31 | 119 | Deletion | none | none | 30 | 30 |
| P11362 | FGFR1 | P11362-1 | P11362-4 | 822 | 731 | 428 | 429 | Deletion | none | none | 338 | 338 |
| P11362 | FGFR1 | P11362-1 | P11362-5 | 822 | 662 | 1 | 160 | Deletion | none | none | 0 | 0 |
| P11362 | FGFR1 | P11362-1 | P11362-6 | 822 | 660 | 1 | 160 | Deletion | none | none | 0 | 0 |
| P11362 | FGFR1 | P11362-1 | P11362-6 | 822 | 660 | 428 | 429 | Deletion | none | none | 267 | 267 |
| P11362 | FGFR1 | P11362-1 | P11362-7 | 822 | 820 | 148 | 149 | Deletion | none | none | 147 | 147 |
| P11362 | FGFR1 | P11362-1 | P11362-8 | 822 | 662 | 619 | 662 | Substitution | CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRL | VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHSPHRLL | 619 | 662 |
| P11362 | FGFR1 | P11362-1 | P11362-8 | 822 | 662 | 663 | 822 | Deletion | none | none | 662 | 662 |
| P11362 | FGFR1 | P11362-1 | P11362-9 | 822 | 660 | 428 | 429 | Deletion | none | none | 427 | 427 |
| P11362 | FGFR1 | P11362-1 | P11362-9 | 822 | 660 | 619 | 662 | Substitution | CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRL | VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHSPHRLL | 617 | 660 |
| P11362 | FGFR1 | P11362-1 | P11362-9 | 822 | 660 | 663 | 822 | Deletion | none | none | 660 | 660 |
Multiple sequence alignment of our canonical and alternatively spliced FGFR1 |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of FGFR1 |
| UniProt-id | ENSG | ENST | ENSP |
| P11362-1 | ENSG00000077782.23 | ENST00000447712.7 | ENSP00000400162.2 |
| P11362-14 | ENSG00000077782.23 | ENST00000326324.10 | ENSP00000327229.6 |
| P11362-15 | ENSG00000077782.23 | ENST00000484370.5 | ENSP00000433163.1 |
| P11362-2 | ENSG00000077782.23 | ENST00000532791.5 | ENSP00000432972.1 |
| P11362-20 | ENSG00000077782.23 | ENST00000335922.9 | ENSP00000337247.5 |
| P11362-3 | ENSG00000077782.23 | ENST00000356207.9 | ENSP00000348537.5 |
| P11362-7 | ENSG00000077782.23 | ENST00000397091.9 | ENSP00000380280.5 |
| P11362-7 | ENSG00000077782.23 | ENST00000397108.8 | ENSP00000380297.4 |
| P11362-7 | ENSG00000077782.23 | ENST00000397113.6 | ENSP00000380302.2 |
| UniProt-id | NM ID | NP ID |
| P11362-1 | NM_023110.2 | NP_075598.2 |
| P11362-14 | NM_023106.2 | NP_075594.1 |
| P11362-2 | NM_001174063.1 | NP_001167534.1 |
| P11362-20 | NM_001174064.1 | NP_001167535.1 |
| P11362-21 | NM_001174067.1 | NP_001167538.1 |
| P11362-3 | NM_001174066.1 | NP_001167537.1 |
| P11362-3 | NM_023105.2 | NP_075593.1 |
| P11362-7 | NM_001174065.1 | NP_001167536.1 |
| P11362-7 | NM_015850.3 | NP_056934.2 |
Amino acid sequences of our canonical and alternatively spliced FGFR1 |
| accession_id | Protein sequence |
| P11362-1 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD SVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPS SGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALG SNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLE ALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLS SSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGK HKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVL VTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMD KPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRH |
| P11362-10 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCP SSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVAL GSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVL EALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRL SSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIG KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKVWNLKAPLVHT |
| P11362-11 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCP SSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVAL GSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVL EALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSADSSASMNSGVLLVRPSRLSS SGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKH KNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKVWNLKAPLVHTPR |
| P11362-12 | MEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVER SPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYT CLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVS ADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDA TEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARG |
| P11362-13 | MEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVER SPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYT CLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSAD SSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATE KDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGME |
| P11362-14 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSS GTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGS NVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEA LEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSS SGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKH KNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV TEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDK PSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHP |
| P11362-15 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD |
| P11362-16 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCP SSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVAL GSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKVIMAPVFVGQSTGKETTVSGAQVPVGRLSCPRMGSFLTLQAHTLHLS |
| P11362-17 | |
| P11362-18 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSS GTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGS NVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKVIMAPVFVGQSTGKETTVSGAQVPVGRLSCPRMGSFLTLQAHTLHLSRD |
| P11362-19 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD SVPADSGLYACVTSSPSGSDTTYFSVNVSVPIDALPSSEDDDDDDDSSSEEKETDNTKPNPVAPYWTSPEKMEKKLHAVPAAKTVKFKCP SSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVAL GSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKHSGINSSDAEVLTLFNVTEAQSGEYVCKVSNYIGEANQSAWLTVTRP ALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLS SSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGK HKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVL VTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMD KPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRH |
| P11362-2 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD SVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPS SGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALG SNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLE ALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSADSSASMNSGVLLVRPSRLSSS GTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHK NIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT EDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKP SNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPA |
| P11362-20 | MAAVTRDFGEMLLHSGRVLPAEAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGL YACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTL RWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCK VYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAV MTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSADSSASMNSGVLLVRPSRLSSSGTPMLAGV SEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGA CTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIA DFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELY MMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLK |
| P11362-21 | MEARVSLKRRIELTVEYPWRCGALSPTSNCRTGMWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRL RDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPN PVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSI NHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLR NVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAK SIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVT KVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKD LVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVL LWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPS |
| P11362-3 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCP SSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVAL GSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVL EALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRL SSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIG KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNV LVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRM DKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPR |
| P11362-4 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCP SSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVAL GSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVL EALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSADSSASMNSGVLLVRPSRLSS SGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKH KNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV TEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDK PSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHP |
| P11362-5 | MEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVER SPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYT CLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVS ADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDA TEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARG MEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSP YPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSS |
| P11362-6 | MEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVER SPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYT CLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSAD SSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATE KDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGME YLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYP GVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGE |
| P11362-7 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD SVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSG TPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSN VEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEAL EERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSS GTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHK NIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT EDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKP SNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPA |
| P11362-8 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD SVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPS SGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALG SNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLE ALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLS SSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGK HKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKVWNLKAPLVHTP |
| P11362-9 | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQD SVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPS SGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALG SNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLE ALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVSADSSASMNSGVLLVRPSRLSSS GTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHK NIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKVWNLKAPLVHTPRP |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| FGFR1 (go to UniProt):P11362 |
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 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=160 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=160 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=148;End=149 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=120;End=150 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=151;End=822 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=313;End=391 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=32;End=61 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=62;End=822 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=148;End=149 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=313;End=391 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=119;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=148;End=149 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=313;End=360 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=1;End=30 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=148;End=149 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=31;End=119 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=160 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=160 |
| P11362 | Topological domain | 22 | 376 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=148;End=149 |
| P11362 | Transmembrane | 377 | 397 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=151;End=822 |
| P11362 | Transmembrane | 377 | 397 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=313;End=391 |
| P11362 | Transmembrane | 377 | 397 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=392;End=822 |
| P11362 | Transmembrane | 377 | 397 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=62;End=822 |
| P11362 | Transmembrane | 377 | 397 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=313;End=391 |
| P11362 | Transmembrane | 377 | 397 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=392;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=619;End=662 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=663;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=429 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=619;End=662 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=663;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=619;End=662 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=663;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=429 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=619;End=662 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=663;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=151;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=392;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=62;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=392;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=429 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=427;End=428 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=429 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=429 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=619;End=662 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=663;End=822 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=429 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=619;End=662 |
| P11362 | Topological domain | 398 | 822 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=663;End=822 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Substitution;Start=32;End=61 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=62;End=822 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Substitution;Start=119;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Substitution;Start=1;End=30 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=31;End=119 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 25 | 119 | Note=Ig-like C2-type 1 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 158 | 246 | Note=Ig-like C2-type 2 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 158 | 246 | Note=Ig-like C2-type 2 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 158 | 246 | Note=Ig-like C2-type 2 | Type=Deletion;Start=151;End=822 |
| P11362 | Domain | 158 | 246 | Note=Ig-like C2-type 2 | Type=Deletion;Start=62;End=822 |
| P11362 | Domain | 158 | 246 | Note=Ig-like C2-type 2 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 158 | 246 | Note=Ig-like C2-type 2 | Type=Deletion;Start=1;End=160 |
| P11362 | Domain | 255 | 357 | Note=Ig-like C2-type 3 | Type=Deletion;Start=151;End=822 |
| P11362 | Domain | 255 | 357 | Note=Ig-like C2-type 3 | Type=Substitution;Start=313;End=391 |
| P11362 | Domain | 255 | 357 | Note=Ig-like C2-type 3 | Type=Deletion;Start=62;End=822 |
| P11362 | Domain | 255 | 357 | Note=Ig-like C2-type 3 | Type=Substitution;Start=313;End=391 |
| P11362 | Domain | 255 | 357 | Note=Ig-like C2-type 3 | Type=Substitution;Start=313;End=360 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=619;End=662 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=663;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=619;End=662 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=663;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=619;End=662 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=663;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=619;End=662 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=663;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=151;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=392;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=62;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=392;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=619;End=662 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=663;End=822 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=619;End=662 |
| P11362 | Domain | 478 | 767 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=663;End=822 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=148;End=149 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=120;End=150 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=151;End=822 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=62;End=822 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=148;End=149 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=148;End=149 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=148;End=149 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 120 | 154 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=148;End=149 |
| P11362 | Region | 160 | 177 | Note=Heparin-binding | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 160 | 177 | Note=Heparin-binding | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 160 | 177 | Note=Heparin-binding | Type=Deletion;Start=151;End=822 |
| P11362 | Region | 160 | 177 | Note=Heparin-binding | Type=Deletion;Start=62;End=822 |
| P11362 | Region | 160 | 177 | Note=Heparin-binding | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 160 | 177 | Note=Heparin-binding | Type=Deletion;Start=1;End=160 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=151;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=392;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=62;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=392;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Region | 778 | 822 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Compositional bias | 123 | 137 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Compositional bias | 123 | 137 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Compositional bias | 123 | 137 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=120;End=150 |
| P11362 | Compositional bias | 123 | 137 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=62;End=822 |
| P11362 | Compositional bias | 123 | 137 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Compositional bias | 123 | 137 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=160 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=151;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=392;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=62;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=392;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
| P11362 | Compositional bias | 778 | 794 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=663;End=822 |
Gene Isoform Structures and Expression Levels for FGFR1 |
Gene structures of our canonical and alternative spliced genes of FGFR1* 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. |
Expression levels of gene isoforms across TCGA. |
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 P11362-1 |
| 3D view using mol* of P11362-10 |
| 3D view using mol* of P11362-11 |
| 3D view using mol* of P11362-12 |
| 3D view using mol* of P11362-13 |
| 3D view using mol* of P11362-14 |
| 3D view using mol* of P11362-15 |
| 3D view using mol* of P11362-16 |
| 3D view using mol* of P11362-17 |
| 3D view using mol* of P11362-18 |
| 3D view using mol* of P11362-19 |
| 3D view using mol* of P11362-2 |
| 3D view using mol* of P11362-20 |
| 3D view using mol* of P11362-21 |
| 3D view using mol* of P11362-3 |
| 3D view using mol* of P11362-4 |
| 3D view using mol* of P11362-5 |
| 3D view using mol* of P11362-6 |
| 3D view using mol* of P11362-7 |
| 3D view using mol* of P11362-8 |
| 3D view using mol* of P11362-9 |
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. |
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. |
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 |
| P11362-1 | 1.069 | 227 | 1.077 | 673.652 | 0.454 | 0.801 | 1.038 | 0.952 | 1.054 | 0.903 | 0.623 | 484,485,487,488,489,490,492,512,514,515,516,523,52 4,527,528,530,531,535,545,559,561,562,563,564,567, 568,571,622,623,627,628,630,640,641,642,643,644,64 6,654,656,657,658,660,661,662,663 |
| P11362-10 | 1.072 | 80 | 1.162 | 184.191 | 0.548 | 0.718 | 0.895 | 3.003 | 0.334 | 8.987 | 0.183 | 4,7,8,10,11,14,15,18,480,481,484,485,488,494,511,5 14,515,518,519,522 |
| P11362-11 | 1.049 | 886 | 1.09 | 2757.377 | 0.564 | 0.72 | 0.885 | 0.912 | 0.863 | 1.057 | 0.971 | 1,2,4,6,7,8,10,11,14,18,84,103,111,112,113,114,115 ,116,117,118,127,128,129,130,132,133,134,135,159,1 60,161,162,164,165,166,167,168,170,191,192,193,260 ,261,262,263,372,374,375,376,377,380,381,393,394,3 95,396,397,398,399,401,421,423,426,428,429,430,431 ,432,433,434,435,436,437,438,439,440,441,442,443,4 44,445,446,451,452,453,454,456,459,461,468,470,471 ,472,473,476,477,478,479,480,481,482,483,492,494,5 09,510,512,513,514,515,516,517,520,521,524,525,527 ,528,529,530,531,532,533,534,535,536,562,563,564,5 65,566,567,568,569,570,571 |
| P11362-12 | 1.048 | 304 | 1.095 | 995.043 | 0.548 | 0.709 | 0.922 | 0.863 | 0.831 | 1.039 | 1.048 | 282,283,284,285,286,287,288,289,303,304,305,306,30 7,308,310,311,312,329,362,363,365,366,367,369,370, 371,372,373,374,376,377,390,392,457,459,460,462,46 3,464,465,466,467,469,470,471,472,491,494,496,497, 498,500,501 |
| P11362-13 | 1.023 | 405 | 1.029 | 1331.526 | 0.565 | 0.732 | 0.91 | 0.445 | 1.074 | 0.414 | 0.64 | 123,124,125,126,127,128,130,148,150,153,154,155,15 6,157,158,160,163,182,184,185,186,188,189,322,323, 324,325,326,327,330,350,352,355,383,399,400,401,40 2,403,405,406,407,408,409,411,412,413,414,415,416, 417,419,420,421,422,423,424,427,428,431,432,438,44 1,442,445,449,485,486,487,488,489,491,498,499,500 |
| P11362-14 | 1.019 | 429 | 1.047 | 1351.763 | 0.563 | 0.707 | 0.931 | 0.814 | 0.975 | 0.835 | 0.905 | 351,352,353,354,355,356,371,372,373,374,375,376,37 7,393,394,396,397,398,399,400,401,421,423,424,425, 431,432,433,434,435,436,437,438,439,440,441,442,44 3,444,445,446,447,454,461,462,470,471,472,473,474, 476,477,480,526,527,528,531,532,536,537,539,549,55 0,551,552,553,555,556,559,560,561,562,563,564,565, 566,567,568,569,570,571,572,576,584,586 |
| P11362-15 | 0.759 | 48 | 0.757 | 169.099 | 0.73 | 0.598 | 0.727 | 0.531 | 0.777 | 0.683 | 1.176 | 32,33,34,36,37,38,39,56,58,103,109,110,111,112,113 |
| P11362-16 | 1.02 | 360 | 1.049 | 824.915 | 0.494 | 0.706 | 0.947 | 0.971 | 0.965 | 1.006 | 0.727 | 161,162,164,165,166,167,168,173,180,184,188,190,19 2,193,194,195,196,197,198,199,200,201,202,203,204, 205,206,207,208,210,217,219,222,225,226,227,229,26 2,263,264,265,266,267,268,286,287,288,289,290,291, 292,293,294,295,296,297 |
| P11362-17 | 0.641 | 46 | 0.55 | 23.667 | 0.689 | 0.514 | 0.772 | 0.192 | 1.216 | 0.158 | 0.235 | 22,24,25,26,27,28,29,30,31,32,33,36
|
| P11362-18 | 1.018 | 158 | 1.077 | 410.228 | 0.644 | 0.647 | 0.785 | 0.795 | 0.772 | 1.03 | 0.712 | 200,201,202,203,208,215,217,218,219,220,221,222,24 2,243,244,245,246,248,249,250,251,254,255,256,257, 258,259,272,273,274,275,276,277,284,289,291 |
| P11362-19 | 1.065 | 144 | 1.06 | 602.651 | 0.581 | 0.795 | 0.936 | 0.517 | 1.096 | 0.472 | 0.575 | 200,201,203,204,205,206,219,220,222,223,224,225,56 8,570,571,574,623,625,626,627,657,658,659,660,661, 662,663,664,665,666,675,692,699,702,703,704,705,70 6,710 |
| P11362-2 | 1.036 | 854 | 1.064 | 2441.131 | 0.496 | 0.731 | 0.927 | 0.679 | 0.965 | 0.704 | 0.701 | 169,170,171,188,189,190,191,196,197,198,199,200,20 2,203,204,205,206,207,208,210,218,219,220,221,222, 223,249,250,252,282,482,483,485,486,487,488,489,49 0,510,512,513,514,521,522,525,526,529,533,543,559, 560,561,562,563,565,566,568,569,570,572,573,575,57 6,577,578,579,580,581,582,583,584,585,586,587,589, 621,625,626,628,638,639,640,641,656,657,658,659,66 0,661,662,663,664,689,692,693,694,696,697,698,699, 700,701,702,703,704,705,715,717,718,719,720,721,72 2,767,768,769,770,771,773,774,775,776 |
| P11362-20 | 1.032 | 590 | 1.065 | 1955.786 | 0.563 | 0.714 | 0.904 | 0.629 | 0.931 | 0.676 | 1.059 | 161,162,163,164,241,242,244,271,272,273,274,275,27 6,277,278,279,306,307,308,310,312,315,316,337,338, 472,473,474,475,477,478,479,480,481,482,502,504,50 5,506,511,513,514,517,518,520,521,523,524,525,527, 528,535,551,552,553,554,555,557,558,607,609,612,61 3,617,618,620,630,631,632,633,634,636,637,640,641, 642,643,644,645,646,647,648,649,650,651,652,653,65 7,662,663,664,665,667,695,696,697,698,700,701,704 |
| P11362-21 | 1.062 | 125 | 1.104 | 296.695 | 0.47 | 0.735 | 0.983 | 0.892 | 0.849 | 1.051 | 1.12 | 230,602,603,605,606,608,609,610,611,612,615,616,61 7,620,622 |
| P11362-3 | 1.059 | 130 | 1.133 | 230.153 | 0.49 | 0.673 | 0.889 | 1.015 | 0.648 | 1.567 | 1.58 | 477,482,483,485,486,487,488,489,490,491,492,493,49 5,496,497,500,502,503 |
| P11362-4 | 1.11 | 189 | 1.13 | 411.6 | 0.417 | 0.841 | 1.092 | 1.52 | 0.966 | 1.573 | 0.941 | 393,394,395,396,397,398,399,400,401,421,423,424,42 5,433,436,437,440,444,454,470,472,473,476,477,480, 532,536,537,539,549,550,551,552,554,555,556,557,56 2 |
| P11362-5 | 1.055 | 253 | 1.04 | 903.805 | 0.532 | 0.78 | 1.014 | 0.845 | 1.128 | 0.749 | 0.659 | 324,325,327,328,329,330,331,332,352,354,355,356,36 3,364,367,368,370,371,375,385,401,402,403,404,405, 407,408,411,461,462,463,467,468,470,480,481,482,48 3,484,485,486,490,491,492,493,495,496,497,498,499, 500,501,502,503,507,515,517,525 |
| P11362-6 | 1.055 | 267 | 1.069 | 916.839 | 0.479 | 0.777 | 1.031 | 1.062 | 1.034 | 1.026 | 0.653 | 322,323,325,326,327,328,329,330,350,352,353,354,36 1,362,365,366,369,373,383,399,400,401,402,403,405, 406,409,460,461,465,466,468,478,479,480,481,482,48 4,488,489,490,491,493,494,495,496,497,498,499,500, 501,505,513,515 |
| P11362-7 | 1.055 | 123 | 1.102 | 299.439 | 0.541 | 0.719 | 0.955 | 0.809 | 0.825 | 0.981 | 0.932 | 454,455,456,457,458,459,460,461,462,463,514,515,51 8,519,520,523,550,551,552,553,554,555 |
| P11362-8 | 1.069 | 423 | 1.119 | 1340.444 | 0.526 | 0.733 | 0.916 | 1.001 | 0.8 | 1.25 | 0.931 | 463,465,466,467,468,471,472,484,485,487,488,489,49 0,492,512,514,516,523,524,526,527,528,529,530,531, 532,533,534,535,536,537,538,543,544,545,550,552,55 9,561,562,563,564,566,567,568,569,570,571,572,603, 606,607,614,619,620,622,623,624,625,626,627,654,65 5,656,657,658,659,660,661,662 |
| P11362-9 | 1.06 | 521 | 1.106 | 1690.99 | 0.519 | 0.726 | 0.925 | 0.939 | 0.827 | 1.136 | 0.907 | 170,222,249,250,253,278,279,280,281,282,283,284,28 5,286,287,314,315,316,317,318,319,320,321,322,324, 342,344,345,346,347,348,349,461,462,464,483,485,48 6,487,488,489,490,512,513,514,519,521,522,524,525, 526,527,528,529,531,532,535,566,567,568,605,617,61 8,620,621,622,623,624,649,650,651,652,653,654,655, 656,657,658,660 |
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 P11362-1_P11362-1_3gql_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 P11362-1_3gql_A_P11362-10.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-11.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-12.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-13.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-14.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-15.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-16.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-17.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-18.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-19.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-2.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-20.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-21.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-3.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-4.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-5.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-6.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-7.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-8.pdb |
| 3D view using mol* of P11362-1_3gql_A_P11362-9.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P11362-1_P11362-10.pdb |
| 3D view using mol* of P11362-1_P11362-11.pdb |
| 3D view using mol* of P11362-1_P11362-12.pdb |
| 3D view using mol* of P11362-1_P11362-13.pdb |
| 3D view using mol* of P11362-1_P11362-14.pdb |
| 3D view using mol* of P11362-1_P11362-15.pdb |
| 3D view using mol* of P11362-1_P11362-16.pdb |
| 3D view using mol* of P11362-1_P11362-17.pdb |
| 3D view using mol* of P11362-1_P11362-18.pdb |
| 3D view using mol* of P11362-1_P11362-19.pdb |
| 3D view using mol* of P11362-1_P11362-2.pdb |
| 3D view using mol* of P11362-1_P11362-20.pdb |
| 3D view using mol* of P11362-1_P11362-21.pdb |
| 3D view using mol* of P11362-1_P11362-3.pdb |
| 3D view using mol* of P11362-1_P11362-4.pdb |
| 3D view using mol* of P11362-1_P11362-5.pdb |
| 3D view using mol* of P11362-1_P11362-6.pdb |
| 3D view using mol* of P11362-1_P11362-7.pdb |
| 3D view using mol* of P11362-1_P11362-8.pdb |
| 3D view using mol* of P11362-1_P11362-9.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to FGFR1 |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P11362 | FGFR1 | DB15149 | Futibatinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB09079 | Nintedanib | approved | inhibitor |
| P11362 | FGFR1 | DB12147 | Erdafitinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB15685 | Selpercatinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB12010 | Fostamatinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB00398 | Sorafenib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB01109 | Heparin | approved, investigational | |
| P11362 | FGFR1 | DB15102 | Pemigatinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB07840 | (E)-[4-(3,5-Difluorophenyl)-3H-pyrrolo[2,3-b]pyridin-3-ylidene](3-methoxyphenyl)methanol | experimental | |
| P11362 | FGFR1 | DB08896 | Regorafenib | approved | inhibitor |
| P11362 | FGFR1 | DB02058 | 3-[4-(1-formylpiperazin-4-yl)-benzylidenyl]-2-indolinone | experimental | |
| P11362 | FGFR1 | DB07525 | 3-(3-methoxybenzyl)-1H-pyrrolo[2,3-b]pyridine | experimental | |
| P11362 | FGFR1 | DB11800 | Tivozanib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB15822 | Pralsetinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB11886 | Infigratinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB08577 | 3-[(3-(2-CARBOXYETHYL)-4-METHYLPYRROL-2-YL)METHYLENE]-2-INDOLINONE | experimental | |
| P11362 | FGFR1 | DB09078 | Lenvatinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB00039 | Palifermin | approved | agonist |
| P11362 | FGFR1 | DB08901 | Ponatinib | approved, investigational | inhibitor |
| P11362 | FGFR1 | DB05014 | XL999 | investigational |
Related Diseases to FGFR1 |
Previous studies relating to the alternative splicing of FGFR1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| FGFR1 | 1652059 | The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain. | To determine the mechanisms by which multiple forms of fibroblast growth factor (FGF) receptors are generated, we have mapped the arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene (flg). We found three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor. One of these alternatives encodes a sequence that is part of a secreted form of FGFR 1. The other two encode sequences that are likely part of transmembrane forms of FGFR 1. One of these forms has not been previously reported in published cDNAs. Also, we have determined the structural organization of a portion of the human FGFR 2 gene (bek) and found a similar arrangement of alternative exons for the third Ig-like domain. The arrangement of these genes suggests that there are conserved mechanisms governing the expression of secreted FGF receptors as well as the expression of at least two distinct membrane-spanning forms of the FGF receptors. The diverse forms appear to be generated by alternative splicing of mRNA and selective use of polyadenylation signals. | D001254 | Astrocytoma |
| FGFR1 | 1652059 | The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain. | To determine the mechanisms by which multiple forms of fibroblast growth factor (FGF) receptors are generated, we have mapped the arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene (flg). We found three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor. One of these alternatives encodes a sequence that is part of a secreted form of FGFR 1. The other two encode sequences that are likely part of transmembrane forms of FGFR 1. One of these forms has not been previously reported in published cDNAs. Also, we have determined the structural organization of a portion of the human FGFR 2 gene (bek) and found a similar arrangement of alternative exons for the third Ig-like domain. The arrangement of these genes suggests that there are conserved mechanisms governing the expression of secreted FGF receptors as well as the expression of at least two distinct membrane-spanning forms of the FGF receptors. The diverse forms appear to be generated by alternative splicing of mRNA and selective use of polyadenylation signals. | D009447 | Neuroblastoma |
| FGFR1 | 1652059 | The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain. | To determine the mechanisms by which multiple forms of fibroblast growth factor (FGF) receptors are generated, we have mapped the arrangement of exons and introns in the human FGF receptor 1 (FGFR 1) gene (flg). We found three alternative exons encoding a portion of the third immunoglobulin (Ig)-like domain of the receptor. One of these alternatives encodes a sequence that is part of a secreted form of FGFR 1. The other two encode sequences that are likely part of transmembrane forms of FGFR 1. One of these forms has not been previously reported in published cDNAs. Also, we have determined the structural organization of a portion of the human FGFR 2 gene (bek) and found a similar arrangement of alternative exons for the third Ig-like domain. The arrangement of these genes suggests that there are conserved mechanisms governing the expression of secreted FGF receptors as well as the expression of at least two distinct membrane-spanning forms of the FGF receptors. The diverse forms appear to be generated by alternative splicing of mRNA and selective use of polyadenylation signals. | D012509 | Sarcoma |
| FGFR1 | 18593464 | Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis. | Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis. | D001172 | Arthritis, Rheumatoid |
| FGFR1 | 18593464 | Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis. | Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis. | D004195 | Disease Models, Animal |
Clinically important variants in FGFR1 |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
|
|