FN1
entrez
2335
canonical
uniprot
P02751
canonical
ensembl
ENSG00000115414
resolver
ensp
ENSP00000323534
resolver
ensp
ENSP00000338200
resolver
ensp
ENSP00000346839
resolver
ensp
ENSP00000348285
resolver
ensp
ENSP00000350534
resolver
ensp
ENSP00000352696
resolver
ensp
ENSP00000394423
resolver
ensp
ENSP00000398907
resolver
ensp
ENSP00000399538
resolver
ensp
ENSP00000410422
resolver
ensp
ENSP00000415018
resolver
ensp
ENSP00000535143
resolver
genesymbol
FN1
resolver
genesymbol_syn
FN
resolver
hgnc
HGNC:3778
resolver
uniprot
B7ZLE5
resolver
uniprot
B7ZLF0
resolver
uniprot
E9PE77
resolver
uniprot
E9PG29
resolver
uniprot
O95609
resolver
uniprot
O95610
resolver
uniprot
Q14312
resolver
uniprot
Q14325
resolver
uniprot
Q14326
resolver
uniprot
Q17RV7
resolver
uniprot
Q53S27
resolver
uniprot
Q564H7
resolver
uniprot
Q585T2
resolver
uniprot
Q59EH1
resolver
uniprot
Q60FE4
resolver
uniprot
Q68DP8
resolver
uniprot
Q68DP9
resolver
uniprot
Q68DT4
resolver
uniprot
Q6LDP6
resolver
uniprot
Q6MZS0
resolver
uniprot
Q6MZU5
resolver
uniprot
Q6N025
resolver
uniprot
Q6N0A6
resolver
uniprot
Q7Z391
resolver
uniprot
Q86T27
resolver
uniprot
Q8IVI8
resolver
uniprot
Q96KP7
resolver
uniprot
Q96KP8
resolver
uniprot
Q96KP9
resolver
uniprot
Q9H1B8
resolver
uniprot
Q9HAP3
resolver
uniprot
Q9UMK2
resolver
uniprot
Q9UQS6
resolver
uniprot_entry
B7ZLE5_HUMAN
resolver
uniprot_entry
FINC_HUMAN
resolver
uniprot_entry
Q9UQS6_HUMAN
resolver
uniprot_sec
B7ZLF0
resolver
uniprot_sec
E9PE77
resolver
uniprot_sec
E9PG29
resolver
uniprot_sec
O95609
resolver
uniprot_sec
O95610
resolver
uniprot_sec
Q14312
resolver
uniprot_sec
Q14325
resolver
uniprot_sec
Q14326
resolver
uniprot_sec
Q17RV7
resolver
uniprot_sec
Q53S27
resolver
uniprot_sec
Q564H7
resolver
uniprot_sec
Q585T2
resolver
uniprot_sec
Q59EH1
resolver
uniprot_sec
Q60FE4
resolver
uniprot_sec
Q68DP8
resolver
uniprot_sec
Q68DP9
resolver
uniprot_sec
Q68DT4
resolver
uniprot_sec
Q6LDP6
resolver
uniprot_sec
Q6MZS0
resolver
uniprot_sec
Q6MZU5
resolver
uniprot_sec
Q6N025
resolver
uniprot_sec
Q6N0A6
resolver
uniprot_sec
Q7Z391
resolver
uniprot_sec
Q86T27
resolver
uniprot_sec
Q8IVI8
resolver
uniprot_sec
Q96KP7
resolver
uniprot_sec
Q96KP8
resolver
uniprot_sec
Q96KP9
resolver
uniprot_sec
Q9H1B8
resolver
uniprot_sec
Q9HAP3
resolver
uniprot_sec
Q9UMK2
resolver
amino_acid_sequence
MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE
uniprot
proteins
disease_involvement
DISEASE: Glomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life. {ECO:0000269|PubMed:18268355}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondylometaphyseal dysplasia, corner fracture type (SMDCF) [MIM:184255]: An autosomal dominant form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDCF is characterized by flake-like, triangular, or curvilinear ossification centers at the edges of irregular metaphyses that simulate fractures. These corner fractures involve the distal tibia, the ulnar aspect of the distal radius, the proximal humerus, and the proximal femur. They represent irregular ossification at the growth plates and secondary ossification centers. {ECO:0000269|PubMed:29100092}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated monocyte activation (PubMed:34089617). {ECO:0000250|UniProtKB:P11276, ECO:0000269|PubMed:3024962, ECO:0000269|PubMed:34089617, ECO:0000269|PubMed:3593230, ECO:0000269|PubMed:3900070, ECO:0000269|PubMed:7989369}.; FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. {ECO:0000269|PubMed:11209058, ECO:0000269|PubMed:15665290, ECO:0000269|PubMed:19379667, ECO:0000269|PubMed:8114919}.; FUNCTION: Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling. {ECO:0000250|UniProtKB:P11276}.
uniprot
proteins
mass_dalton
272320
uniprot
proteins
mutagenesis
MUTAGEN 641; /note="Y->A: Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 642; /note="I->A: Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 663; /note="L->A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 K but abolishes polymerization activity; when associated with A-666."; /evidence="ECO:0000269|PubMed:12946358, ECO:0000269|PubMed:19379667"; MUTAGEN 666; /note="Y->A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 kinase but abolishes polymerization activity; when associated with A-663."; /evidence="ECO:0000269|PubMed:12946358, ECO:0000269|PubMed:19379667"; MUTAGEN 681; /note="L->A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 682; /note="I->A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 683; /note="S->A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 684; /note="I->A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 691; /note="E->A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 692; /note="V->A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 694; /note="R->A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 695; /note="F->A: Loss of ability to form fibronectin aggregates; when associated with A-697."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 696; /note="D->A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694."; /evidence="ECO:0000269|PubMed:12946358"; MUTAGEN 697; /note="F->A: Loss of ability to form fibronectin aggregates; when associated with A-695."; /evidence="ECO:0000269|PubMed:12946358
uniprot
proteins
post_translational_modification
PTM: Sulfated. {ECO:0000269|PubMed:2414772}.; PTM: It is not known whether both or only one of Thr-2155 and Thr-2156 are/is glycosylated. {ECO:0000269|PubMed:11285216, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16037490, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17614963, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2012601, ECO:0000269|PubMed:3584091}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000250|UniProtKB:P11276}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000305|PubMed:8114919}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000250|UniProtKB:P11276}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250|UniProtKB:P07589}.
uniprot
proteins
pubmed
10075919
uniprot
proteins
pubmed
10196121
uniprot
proteins
pubmed
10647176
uniprot
proteins
pubmed
11209058
uniprot
proteins
pubmed
11285216
uniprot
proteins
pubmed
11580843
uniprot
proteins
pubmed
11737888
uniprot
proteins
pubmed
11773026
uniprot
proteins
pubmed
11775745
uniprot
proteins
pubmed
11956183
uniprot
proteins
pubmed
12127832
uniprot
proteins
pubmed
12225811
uniprot
proteins
pubmed
12736686
uniprot
proteins
pubmed
12946358
uniprot
proteins
pubmed
1311202
uniprot
proteins
pubmed
1400330
uniprot
proteins
pubmed
1423622
uniprot
proteins
pubmed
14657397
uniprot
proteins
pubmed
14760718
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15665290
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16037490
uniprot
proteins
pubmed
16106752
uniprot
proteins
pubmed
16322219
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16336961
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17368672
uniprot
proteins
pubmed
17464288
uniprot
proteins
pubmed
17614963
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18042364
uniprot
proteins
pubmed
18268355
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18713862
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19251642
uniprot
proteins
pubmed
19379667
uniprot
proteins
pubmed
2012601
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
2414772
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
27834729
uniprot
proteins
pubmed
2822387
uniprot
proteins
pubmed
29100092
uniprot
proteins
pubmed
29777959
uniprot
proteins
pubmed
2989004
uniprot
proteins
pubmed
2992573
uniprot
proteins
pubmed
2992939
uniprot
proteins
pubmed
3003095
uniprot
proteins
pubmed
3021206
uniprot
proteins
pubmed
3024962
uniprot
proteins
pubmed
3031656
uniprot
proteins
pubmed
3375063
uniprot
proteins
pubmed
34089617
uniprot
proteins
pubmed
3478690
uniprot
proteins
pubmed
3584091
uniprot
proteins
pubmed
3593230
uniprot
proteins
pubmed
3770189
uniprot
proteins
pubmed
3770201
uniprot
proteins
pubmed
3900070
uniprot
proteins
pubmed
4019516
uniprot
proteins
pubmed
6200322
uniprot
proteins
pubmed
6304699
uniprot
proteins
pubmed
6462919
uniprot
proteins
pubmed
6630202
uniprot
proteins
pubmed
6688418
uniprot
proteins
pubmed
7050098
uniprot
proteins
pubmed
7583666
uniprot
proteins
pubmed
7989369
uniprot
proteins
pubmed
8114919
uniprot
proteins
pubmed
8120888
uniprot
proteins
pubmed
8308892
uniprot
proteins
pubmed
8406884
uniprot
proteins
pubmed
8548820
uniprot
proteins
pubmed
9501082
uniprot
proteins
pubmed
9514732
uniprot
proteins
sequence_length
2477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:29100092}. Secreted {ECO:0000250|UniProtKB:P11276}.
uniprot
proteins