Fn1
entrez
14268
canonical
uniprot
P11276
canonical
ensembl
ENSMUSG00000026193
resolver
ensp
ENSMUSP00000054499
resolver
ensp
ENSMUSP00000139702
resolver
ensp
ENSMUSP00000140471
resolver
ensp
ENSMUSP00000140816
resolver
ensp
ENSMUSP00000140907
resolver
ensp
ENSMUSP00000140975
resolver
ensp
ENSMUSP00000141123
resolver
ensp
ENSMUSP00000212373
resolver
ensp
ENSMUSP00000212375
resolver
ensp
ENSMUSP00000212376
resolver
ensp
ENSMUSP00000212377
resolver
ensp
ENSMUSP00000212378
resolver
enst
ENSMUST00000055226
resolver
enst
ENSMUST00000186129
resolver
enst
ENSMUST00000187938
resolver
enst
ENSMUST00000188674
resolver
enst
ENSMUST00000188894
resolver
enst
ENSMUST00000189821
resolver
enst
ENSMUST00000190780
resolver
genesymbol
Fn1
resolver
uniprot
A0A087WPB0
resolver
uniprot
A0A087WR50
resolver
uniprot
A0A087WRY1
resolver
uniprot
A0A087WS56
resolver
uniprot
A0A087WSB4
resolver
uniprot
A0A087WSN6
resolver
uniprot
B7ZNJ1
resolver
uniprot
B9EHT6
resolver
uniprot
G5E8B8
resolver
uniprot
Q3TBB4
resolver
uniprot
Q3UGY5
resolver
uniprot
Q3UH17
resolver
uniprot
Q3UHL6
resolver
uniprot
Q3UHR1
resolver
uniprot
Q3UZF9
resolver
uniprot
Q61567
resolver
uniprot
Q61568
resolver
uniprot
Q61569
resolver
uniprot
Q64233
resolver
uniprot
Q80UI4
resolver
uniprot_entry
A0A087WPB0_MOUSE
resolver
uniprot_entry
A0A087WR50_MOUSE
resolver
uniprot_entry
A0A087WRY1_MOUSE
resolver
uniprot_entry
A0A087WS56_MOUSE
resolver
uniprot_entry
A0A087WSB4_MOUSE
resolver
uniprot_entry
A0A087WSN6_MOUSE
resolver
uniprot_entry
B7ZNJ1_MOUSE
resolver
uniprot_entry
B9EHT6_MOUSE
resolver
uniprot_entry
FINC_MOUSE
resolver
uniprot_entry
Q3TBB4_MOUSE
resolver
uniprot_entry
Q3UGY5_MOUSE
resolver
uniprot_entry
Q3UH17_MOUSE
resolver
uniprot_entry
Q3UHL6_MOUSE
resolver
uniprot_entry
Q3UHR1_MOUSE
resolver
uniprot_entry
Q3UZF9_MOUSE
resolver
uniprot_sec
G5E8B8
resolver
uniprot_sec
Q61567
resolver
uniprot_sec
Q61568
resolver
uniprot_sec
Q61569
resolver
uniprot_sec
Q64233
resolver
uniprot_sec
Q80UI4
resolver
amino_acid_sequence
MLRGPGPGRLLLLAVLCLGTSVRCTEAGKSKRQAQQIVQPQSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHALQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPYSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRSDNVPPPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSDIPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIPAPTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTENGIQLPGTTHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEGLNQPTDDSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYNQRTNTNVNCPIECFMPLDVQADRDDSRE
uniprot
proteins
function
FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (PubMed:21768292). Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292). Acts as a ligand for the Lilrb4a receptor, inhibiting Fcgr1/CD64-mediated monocyte activation (PubMed:34089617). {ECO:0000250|UniProtKB:P02751, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:34089617}.; 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:0000269|PubMed:36812915}.; 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:0000250|UniProtKB:P02751}.
uniprot
proteins
mass_dalton
272538
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="Q->A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48."; /evidence="ECO:0000269|PubMed:9312106"; MUTAGEN 35; /note="Q->L: 65% decrease in cross-linking efficiency; when associated with L-36."; /evidence="ECO:0000269|PubMed:9312106"; MUTAGEN 36; /note="Q->A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48."; /evidence="ECO:0000269|PubMed:9312106"; MUTAGEN 36; /note="Q->L: 65% decrease in cross-linking efficiency; when associated with L-35."; /evidence="ECO:0000269|PubMed:9312106"; MUTAGEN 48; /note="Q->A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36."; /evidence="ECO:0000269|PubMed:9312106
uniprot
proteins
post_translational_modification
PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; 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:0000269|PubMed:9312106}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02751}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250|UniProtKB:P02751}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000269|PubMed:26954549}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250|UniProtKB:P07589}.
uniprot
proteins
pubmed
11737251
uniprot
proteins
pubmed
1327855
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16944957
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17330941
uniprot
proteins
pubmed
17699513
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19656770
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21768292
uniprot
proteins
pubmed
2521606
uniprot
proteins
pubmed
26954549
uniprot
proteins
pubmed
29777959
uniprot
proteins
pubmed
3124113
uniprot
proteins
pubmed
34089617
uniprot
proteins
pubmed
36792666
uniprot
proteins
pubmed
36812915
uniprot
proteins
pubmed
7673336
uniprot
proteins
pubmed
8299972
uniprot
proteins
pubmed
9312106
uniprot
proteins
pubmed
9533887
uniprot
proteins
sequence_length
2477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:36812915}.
uniprot
proteins