HUMAN:FINC

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FN1 (synonyms: FN)
Protein Name(s)	Fibronectin FN Cold-insoluble globulin CIG Anastellin Ugl-Y1 Ugl-Y2 Ugl-Y3
External Links
UniProt	P02751
EMBL	AJ276395 AJ535086 AJ849445 AB191261 AB209840 AL832202 BX537590 BX538017 BX538018 BX538045 BX640608 BX640731 BX640875 BX640920 CR749281 CR749316 CR749317 AC012462 AC073284 CH471063 BC117176 BC143763 M15801 AF312399 X02761 U41850 U42404 U42592 U42593 U42594 U42455 U42456 U42458 U42457 X07718 X07717 M18179 M18177 M18178 M12549 M10905 M14059 AJ320525 AJ320526 AJ320527 M27589 X04530
CCDS	CCDS2399.1 CCDS2400.1 CCDS42813.1 CCDS42814.1 CCDS46510.1 CCDS46512.1
PIR	A26460 I52394 S00848
RefSeq	NP_002017.1 NP_473375.2 NP_997639.1 NP_997641.1 NP_997643.1 NP_997647.1 XP_005246457.1 XP_005246463.1 XP_005246470.1 XP_005246472.1 XP_005246474.1
UniGene	Hs.203717
PDB	1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2CG7 2CK2 2CKU 2EC3 2FN2 2FNB 2GEE 2H41 2H45 2HA1 2OCF 2RKY 2RKZ 2RL0 3CAL 3EJH 3GXE 3M7P 3MQL 3R8Q 3T1W 3ZRZ 4GH7 4JE4 4JEG 4LXO 4MMX 4MMY 4MMZ 4PZ5
PDBsum	1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2CG7 2CK2 2CKU 2EC3 2FN2 2FNB 2GEE 2H41 2H45 2HA1 2OCF 2RKY 2RKZ 2RL0 3CAL 3EJH 3GXE 3M7P 3MQL 3R8Q 3T1W 3ZRZ 4GH7 4JE4 4JEG 4LXO 4MMX 4MMY 4MMZ 4PZ5
ProteinModelPortal	P02751
SMR	P02751
BioGrid	108621
DIP	DIP-29547N
IntAct	P02751
MINT	MINT-1779779
ChEMBL	CHEMBL3810
DrugBank	DB08888
PhosphoSite	P02751
UniCarbKB	P02751
DMDM	300669710
DOSAC-COBS-2DPAGE	P02751
MaxQB	P02751
PaxDb	P02751
PRIDE	P02751
DNASU	2335
Ensembl	ENST00000323926 ENST00000336916 ENST00000354785 ENST00000356005 ENST00000357867 ENST00000359671 ENST00000421182 ENST00000426059 ENST00000432072 ENST00000443816 ENST00000446046
GeneID	2335
KEGG	hsa:2335
UCSC	uc002vfa.3 uc002vfb.3 uc002vfc.3 uc002vfe.3 uc002vfg.3 uc002vfh.3 uc002vfi.3 uc002vfj.3
CTD	2335
GeneCards	GC02M216225
HGNC	HGNC:3778
HPA	CAB000126 HPA027066
MIM	135600 601894
neXtProt	NX_P02751
Orphanet	84090
PharmGKB	PA28194
eggNOG	NOG12793
GeneTree	ENSGT00760000119000
HOVERGEN	HBG005731
InParanoid	P02751
KO	K05717
OMA	PGHLNSY
OrthoDB	EOG7X9G60
PhylomeDB	P02751
TreeFam	TF329915
Reactome	REACT_118572 REACT_118779 REACT_12051 REACT_13552 REACT_150331 REACT_15381 REACT_15523 REACT_160131 REACT_163874 REACT_163906 REACT_163942
ChiTaRS	FN1
EvolutionaryTrace	P02751
GeneWiki	Fibronectin
GenomeRNAi	2335
NextBio	35481280
PRO	PR:P02751
Proteomes	UP000005640
Bgee	P02751
ExpressionAtlas	P02751
Genevestigator	P02751
GO	GO:0016324 GO:0005605 GO:0072562 GO:0005793 GO:0031012 GO:0005576 GO:0005615 GO:0070062 GO:0005577 GO:0031093 GO:0005518 GO:0008201 GO:0005178 GO:0016504 GO:0002020 GO:0006953 GO:0001525 GO:0007596 GO:0007161 GO:0007155 GO:0007044 GO:0035987 GO:0022617 GO:0030198 GO:0033622 GO:0050900 GO:0018149 GO:0030168 GO:0002576 GO:0045773 GO:0008360 GO:0009611 GO:0034446
Gene3D	2.10.10.10 2.60.40.10
InterPro	IPR000083 IPR003961 IPR000562 IPR013783 IPR013806
Pfam	PF00039 PF00040 PF00041
SMART	SM00058 SM00059 SM00060
SUPFAM	SSF49265 SSF57440
PROSITE	PS00022 PS01253 PS51091 PS00023 PS51092 PS50853

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0005201	extracellular matrix structural constituent	PMID:25037231^[1]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0001155)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:28327460^[2]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(CL:0002540)\|occurs_in:(CL:0002570)\|occurs_in:(CL:0002551)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28327460^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002540)\|part_of:(CL:0002570)\|part_of:(CL:0002551)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:23979707^[3]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(CL:0002543)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:27559042^[4]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0006618) occurs_in:(UBERON:0002302)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28344315^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002371)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:28344315^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	occurs_in:(UBERON:0002371)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:20551380^[6]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0001496)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:F1SS24	F	occurs_in:(UBERON:0002084)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28675934^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0003688)\|part_of:(UBERON:0001911)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:28675934^[7]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0003688)\|occurs_in:(UBERON:0001911)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001155)	Seeded From UniProt	complete
enables	GO:0005201	extracellular matrix structural constituent	PMID:25037231^[1]	ECO:0007666	automatically integrated combinatorial computational and experimental evidence used in manual assertion		F	occurs_in:(UBERON:0002107)	Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:17849409^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P9WQP1	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:17849409^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P9WMJ9	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:17849409^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P9WN39	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:12167537^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9AIS0	F		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:15292204^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O50835	F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:15292204^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:27068509^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0007318)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:23979707^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002543)	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:12421310^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P75391	F		Seeded From UniProt	complete
involved_in	GO:0051702	interaction with symbiont	PMID:12167537^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051702	interaction with symbiont	PMID:12167537^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051702	interaction with symbiont	PMID:19429745^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:19429745^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:C1G9X3	F		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:27559042^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0006618) part_of:(UBERON:0002302)	Seeded From UniProt	complete
involved_in	GO:2001202	negative regulation of transforming growth factor-beta secretion	PMID:25834989^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002553)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:25834989^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P02751) has_regulation_target:(UniProtKB:P98160) causally_upstream_of:(GO:0030198)	Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:25834989^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	acts_on_population_of:(CL:0002600)	Seeded From UniProt	complete
involved_in	GO:0048146	positive regulation of fibroblast proliferation	PMID:25834989^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(UBERON:0002048)	Seeded From UniProt	complete
involved_in	GO:1904237	positive regulation of substrate-dependent cell migration, cell attachment to substrate	PMID:25834989^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	results_in_movement_of:(CL:0002600)\|results_in_movement_of:(CL:0002553)	Seeded From UniProt	complete
involved_in	GO:0051702	interaction with symbiont	PMID:12421310^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P75390) has_regulation_target:(UniProtKB:P23568)	Seeded From UniProt	complete
involved_in	GO:0001932	regulation of protein phosphorylation	PMID:11792823^[15]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(GO:0016459)	Seeded From UniProt	complete
involved_in	GO:0070372	regulation of ERK1 and ERK2 cascade	PMID:11792823^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005178	integrin binding	PMID:11792823^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05556	F		Seeded From UniProt	complete
involved_in	GO:0052047	interaction with other organism via secreted substance involved in symbiotic interaction	PMID:17849409^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034446	substrate adhesion-dependent cell spreading	PMID:24658351^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(GO:0034683)	Seeded From UniProt	complete
involved_in	GO:0033622	integrin activation	PMID:24658351^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(GO:0034683)\|has_direct_input:(GO:0034683)	Seeded From UniProt	complete
enables	GO:0005178	integrin binding	PMID:24658351^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(GO:0034683)\|has_direct_input:(GO:0034683)	Seeded From UniProt	complete
involved_in	GO:0035987	endodermal cell differentiation	PMID:23154389^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:23658023^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)\|part_of:(CL:0002322)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[19]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:16677310^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P9WK17	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21276792^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000351)	Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:22952693^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P43235	F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:22952693^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07711	F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:22952693^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25774	F		Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[23]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:16157329^[25]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002553)	Seeded From UniProt	complete
enables	GO:0005178	integrin binding	PMID:19738201^[26]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P08648) has_direct_input:(UniProtKB:P05556)	Seeded From UniProt	complete
involved_in	GO:0034446	substrate adhesion-dependent cell spreading	PMID:16236823^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:1632457^[28]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000650)	Seeded From UniProt	complete
colocalizes_with	GO:0062023	collagen-containing extracellular matrix	PMID:20551380^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001496)	Seeded From UniProt	complete
colocalizes_with	GO:0062023	collagen-containing extracellular matrix	PMID:22261194^[29]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:F1SS24	C	part_of:(UBERON:0002084)	Seeded From UniProt	complete
involved_in	GO:0018149	peptide cross-linking	PMID:3997886^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:20551380^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001496)	Seeded From UniProt	complete
part_of	GO:0005577	fibrinogen complex	PMID:3997886^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0009611	response to wounding	PMID:7989369^[31]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008201	heparin binding	PMID:10075919^[32]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	PMID:1423622^[33]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005793	endoplasmic reticulum-Golgi intermediate compartment	PMID:15308636^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:14718574^[35]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005518	collagen binding	PMID:3024962^[36]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1901166	neural crest cell migration involved in autonomic nervous system development	PMID:26571399^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043394	proteoglycan binding	PMID:29030641^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	PMID:26571399^[37]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20541508^[39]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19931242^[40]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19826086^[41]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18160478^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18042364^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17914904^[44]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
involved_in	GO:0010952	positive regulation of peptidase activity	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0016504	P		Seeded From UniProt	complete
involved_in	GO:0045773	positive regulation of axon extension	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	P		Seeded From UniProt	complete
part_of	GO:0031012	extracellular matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	C		Seeded From UniProt	complete
enables	GO:0016504	peptidase activator activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	F		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	C		Seeded From UniProt	complete
involved_in	GO:0007161	calcium-independent cell-matrix adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	P		Seeded From UniProt	complete
involved_in	GO:0007160	cell-matrix adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	P		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	P		Seeded From UniProt	complete
involved_in	GO:0007044	cell-substrate junction assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	P		Seeded From UniProt	complete
part_of	GO:0005604	basement membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P11276 ensembl:ENSMUSP00000054499	C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000083	C		Seeded From UniProt	complete
involved_in	GO:0050900	leukocyte migration	Reactome:R-HSA-202733	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043687	post-translational protein modification	Reactome:R-HSA-597592	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031093	platelet alpha granule lumen	Reactome:R-HSA-481007	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030198	extracellular matrix organization	Reactome:R-HSA-1474244	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019221	cytokine-mediated signaling pathway	Reactome:R-HSA-6785807	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	Reactome:R-HSA-8952289	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6785895 Reactome:R-HSA-481007 Reactome:R-HSA-429441 Reactome:R-HSA-429415 Reactome:R-HSA-3788061 Reactome:R-HSA-3785684 Reactome:R-HSA-377644 Reactome:R-HSA-377643 Reactome:R-HSA-377641 Reactome:R-HSA-377640 Reactome:R-HSA-372705 Reactome:R-HSA-372697 Reactome:R-HSA-372693 Reactome:R-HSA-354165 Reactome:R-HSA-354149 Reactome:R-HSA-354124 Reactome:R-HSA-354087 Reactome:R-HSA-354073 Reactome:R-HSA-354066 Reactome:R-HSA-349593 Reactome:R-HSA-2731141 Reactome:R-HSA-2681681 Reactome:R-HSA-2545196 Reactome:R-HSA-2537665 Reactome:R-HSA-2533950 Reactome:R-HSA-2396337 Reactome:R-HSA-2327746 Reactome:R-HSA-2327733 Reactome:R-HSA-216050 Reactome:R-HSA-202723 Reactome:R-HSA-1566981	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002576	platelet degranulation	Reactome:R-HSA-114608	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008201	heparin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0358	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964	C		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0130	P		Seeded From UniProt	complete
involved_in	GO:0006953	acute-phase response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0011	P		Seeded From UniProt	complete
involved_in	GO:0001525	angiogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0037	P		Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0133	P		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page
↑ ^2.0 ^2.1 Ragelle, H et al. (2017) Comprehensive proteomic characterization of stem cell-derived extracellular matrices. Biomaterials 128 147-159 PubMed GONUTS page
↑ ^3.0 ^3.1 Zanivan, S et al. (2013) SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers. Mol. Cell Proteomics 12 3599-611 PubMed GONUTS page
↑ ^4.0 ^4.1 Barallobre-Barreiro, J et al. (2016) Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. Circulation 134 817-32 PubMed GONUTS page
↑ ^5.0 ^5.1 Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page
↑ ^7.0 ^7.1 Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Xolalpa, W et al. (2007) Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis. Proteomics 7 3332-41 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Allignet, J et al. (2002) Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding. FEMS Microbiol. Lett. 213 193-7 PubMed GONUTS page
↑ ^10.0 ^10.1 Kim, JH et al. (2004) BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. J. Biol. Chem. 279 41706-14 PubMed GONUTS page
↑ Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page
↑ ^12.0 ^12.1 Dallo, SF et al. (2002) Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Mol. Microbiol. 46 1041-51 PubMed GONUTS page
↑ ^13.0 ^13.1 Donofrio, FC et al. (2009) Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein. J. Med. Microbiol. 58 706-13 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 Ge, Q et al. (2015) Fibulin1C peptide induces cell attachment and extracellular matrix deposition in lung fibroblasts. Sci Rep 5 9496 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Twal, WO et al. (2001) Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility. J. Cell. Sci. 114 4587-98 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Van Agthoven, JF et al. (2014) Structural basis for pure antagonism of integrin αVβ3 by a high-affinity form of fibronectin. Nat. Struct. Mol. Biol. 21 383-8 PubMed GONUTS page
↑ Brafman, DA et al. (2013) Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions. Cell Death Differ. 20 369-81 PubMed GONUTS page
↑ Soteriou, D et al. (2013) Comparative proteomic analysis of supportive and unsupportive extracellular matrix substrates for human embryonic stem cell maintenance. J. Biol. Chem. 288 18716-31 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kinhikar, AG et al. (2006) Mycobacterium tuberculosis malate synthase is a laminin-binding adhesin. Mol. Microbiol. 60 999-1013 PubMed GONUTS page
↑ Atay, S et al. (2011) Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells. Exp. Cell Res. 317 1192-202 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Sage, J et al. (2012) Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners. PLoS ONE 7 e43494 PubMed GONUTS page
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Koli, K et al. (2005) Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts. Exp. Cell Res. 310 370-82 PubMed GONUTS page
↑ Humphries, JD et al. (2009) Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Sci Signal 2 ra51 PubMed GONUTS page
↑ Vainionpää, N et al. (2006) Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells. Am. J. Physiol., Cell Physiol. 290 C764-75 PubMed GONUTS page
↑ Hagège, J et al. (1992) Plasminogen activator inhibitor-1 deposition in the extracellular matrix of cultured human mesangial cells. Am. J. Pathol. 141 117-28 PubMed GONUTS page
↑ Barallobre-Barreiro, J et al. (2012) Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury. Circulation 125 789-802 PubMed GONUTS page
↑ ^30.0 ^30.1 Bale, MD et al. (1985) Incorporation of thrombospondin into fibrin clots. J. Biol. Chem. 260 7502-8 PubMed GONUTS page
↑ Rostagno, A et al. (1994) Further characterization of the NH2-terminal fibrin-binding site on fibronectin. J. Biol. Chem. 269 31938-45 PubMed GONUTS page
↑ Sharma, A et al. (1999) Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 18 1468-79 PubMed GONUTS page
↑ Main, AL et al. (1992) The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71 671-8 PubMed GONUTS page
↑ Breuza, L et al. (2004) Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279 47242-53 PubMed GONUTS page
↑ Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page
↑ Owens, RJ & Baralle, FE (1986) Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli. EMBO J. 5 2825-30 PubMed GONUTS page
↑ ^37.0 ^37.1 Soret, R et al. (2015) A collagen VI-dependent pathogenic mechanism for Hirschsprung's disease. J. Clin. Invest. 125 4483-96 PubMed GONUTS page
↑ Flowers, SA et al. (2017) Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface. Sci Rep 7 13149 PubMed GONUTS page
↑ Graille, M et al. (2010) Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding. Structure 18 710-8 PubMed GONUTS page
↑ L'Heureux, DZ et al. (2010) The interaction of angiocidin with tissue transglutaminase. Exp. Mol. Pathol. 88 15-25 PubMed GONUTS page
↑ Klotzsch, E et al. (2009) Fibronectin forms the most extensible biological fibers displaying switchable force-exposed cryptic binding sites. Proc. Natl. Acad. Sci. U.S.A. 106 18267-72 PubMed GONUTS page
↑ Mullen, LM et al. (2008) Novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats. Infect. Immun. 76 1093-104 PubMed GONUTS page
↑ Kuznetsova, SA et al. (2008) TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. Matrix Biol. 27 201-10 PubMed GONUTS page
↑ Smith, ML et al. (2007) Force-induced unfolding of fibronectin in the extracellular matrix of living cells. PLoS Biol. 5 e268 PubMed GONUTS page

[PMID:25037231-1] 1.0 ^1.1 ^1.2 ^1.3 Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page

[PMID:28327460-2] 2.0 ^2.1 Ragelle, H et al. (2017) Comprehensive proteomic characterization of stem cell-derived extracellular matrices. Biomaterials 128 147-159 PubMed GONUTS page

[PMID:23979707-3] 3.0 ^3.1 Zanivan, S et al. (2013) SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers. Mol. Cell Proteomics 12 3599-611 PubMed GONUTS page

[PMID:27559042-4] 4.0 ^4.1 Barallobre-Barreiro, J et al. (2016) Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. Circulation 134 817-32 PubMed GONUTS page

[PMID:28344315-5] 5.0 ^5.1 Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page

[PMID:20551380-6] 6.0 ^6.1 ^6.2 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page

[PMID:28675934-7] 7.0 ^7.1 Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page

[PMID:17849409-8] 8.0 ^8.1 ^8.2 ^8.3 Xolalpa, W et al. (2007) Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis. Proteomics 7 3332-41 PubMed GONUTS page

[PMID:12167537-9] 9.0 ^9.1 ^9.2 Allignet, J et al. (2002) Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding. FEMS Microbiol. Lett. 213 193-7 PubMed GONUTS page

[PMID:15292204-10] 10.0 ^10.1 Kim, JH et al. (2004) BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. J. Biol. Chem. 279 41706-14 PubMed GONUTS page

[PMID:27068509-11] Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page

[PMID:12421310-12] 12.0 ^12.1 Dallo, SF et al. (2002) Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Mol. Microbiol. 46 1041-51 PubMed GONUTS page

[PMID:19429745-13] 13.0 ^13.1 Donofrio, FC et al. (2009) Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein. J. Med. Microbiol. 58 706-13 PubMed GONUTS page

[PMID:25834989-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 Ge, Q et al. (2015) Fibulin1C peptide induces cell attachment and extracellular matrix deposition in lung fibroblasts. Sci Rep 5 9496 PubMed GONUTS page

[PMID:11792823-15] 15.0 ^15.1 ^15.2 Twal, WO et al. (2001) Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility. J. Cell. Sci. 114 4587-98 PubMed GONUTS page

[PMID:24658351-16] 16.0 ^16.1 ^16.2 Van Agthoven, JF et al. (2014) Structural basis for pure antagonism of integrin αVβ3 by a high-affinity form of fibronectin. Nat. Struct. Mol. Biol. 21 383-8 PubMed GONUTS page

[PMID:23154389-17] Brafman, DA et al. (2013) Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions. Cell Death Differ. 20 369-81 PubMed GONUTS page

[PMID:23658023-18] Soteriou, D et al. (2013) Comparative proteomic analysis of supportive and unsupportive extracellular matrix substrates for human embryonic stem cell maintenance. J. Biol. Chem. 288 18716-31 PubMed GONUTS page

[PMID:23533145-19] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:16677310-20] Kinhikar, AG et al. (2006) Mycobacterium tuberculosis malate synthase is a laminin-binding adhesin. Mol. Microbiol. 60 999-1013 PubMed GONUTS page

[PMID:21276792-21] Atay, S et al. (2011) Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells. Exp. Cell Res. 317 1192-202 PubMed GONUTS page

[PMID:22952693-22] 22.0 ^22.1 ^22.2 Sage, J et al. (2012) Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners. PLoS ONE 7 e43494 PubMed GONUTS page

[PMID:22516433-23] Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page

[PMID:19056867-24] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:16157329-25] Koli, K et al. (2005) Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts. Exp. Cell Res. 310 370-82 PubMed GONUTS page

[PMID:19738201-26] Humphries, JD et al. (2009) Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Sci Signal 2 ra51 PubMed GONUTS page

[PMID:16236823-27] Vainionpää, N et al. (2006) Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells. Am. J. Physiol., Cell Physiol. 290 C764-75 PubMed GONUTS page

[PMID:1632457-28] Hagège, J et al. (1992) Plasminogen activator inhibitor-1 deposition in the extracellular matrix of cultured human mesangial cells. Am. J. Pathol. 141 117-28 PubMed GONUTS page

[PMID:22261194-29] Barallobre-Barreiro, J et al. (2012) Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury. Circulation 125 789-802 PubMed GONUTS page

[PMID:3997886-30] 30.0 ^30.1 Bale, MD et al. (1985) Incorporation of thrombospondin into fibrin clots. J. Biol. Chem. 260 7502-8 PubMed GONUTS page

[PMID:7989369-31] Rostagno, A et al. (1994) Further characterization of the NH2-terminal fibrin-binding site on fibronectin. J. Biol. Chem. 269 31938-45 PubMed GONUTS page

[PMID:10075919-32] Sharma, A et al. (1999) Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 18 1468-79 PubMed GONUTS page

[PMID:1423622-33] Main, AL et al. (1992) The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71 671-8 PubMed GONUTS page

[PMID:15308636-34] Breuza, L et al. (2004) Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279 47242-53 PubMed GONUTS page

[PMID:14718574-35] Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page

[PMID:3024962-36] Owens, RJ & Baralle, FE (1986) Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli. EMBO J. 5 2825-30 PubMed GONUTS page

[PMID:26571399-37] 37.0 ^37.1 Soret, R et al. (2015) A collagen VI-dependent pathogenic mechanism for Hirschsprung's disease. J. Clin. Invest. 125 4483-96 PubMed GONUTS page

[PMID:29030641-38] Flowers, SA et al. (2017) Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface. Sci Rep 7 13149 PubMed GONUTS page

[PMID:20541508-39] Graille, M et al. (2010) Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding. Structure 18 710-8 PubMed GONUTS page

[PMID:19931242-40] L'Heureux, DZ et al. (2010) The interaction of angiocidin with tissue transglutaminase. Exp. Mol. Pathol. 88 15-25 PubMed GONUTS page

[PMID:19826086-41] Klotzsch, E et al. (2009) Fibronectin forms the most extensible biological fibers displaying switchable force-exposed cryptic binding sites. Proc. Natl. Acad. Sci. U.S.A. 106 18267-72 PubMed GONUTS page

[PMID:18160478-42] Mullen, LM et al. (2008) Novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats. Infect. Immun. 76 1093-104 PubMed GONUTS page

[PMID:18042364-43] Kuznetsova, SA et al. (2008) TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. Matrix Biol. 27 201-10 PubMed GONUTS page

[PMID:17914904-44] Smith, ML et al. (2007) Force-induced unfolding of fibronectin in the extracellular matrix of living cells. PLoS Biol. 5 e268 PubMed GONUTS page

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