SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11276

- FINC_MOUSE

UniProt

P11276 - FINC_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fibronectin

Gene
Fn1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.1 Publication
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 By similarity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi906 – 1171266Add
BLAST

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. peptidase activator activity Source: MGI
  3. protein binding Source: IntAct

GO - Biological processi

  1. acute-phase response Source: UniProtKB-KW
  2. angiogenesis Source: UniProtKB-KW
  3. calcium-independent cell-matrix adhesion Source: MGI
  4. cell adhesion Source: MGI
  5. cell-matrix adhesion Source: MGI
  6. cell-substrate junction assembly Source: MGI
  7. peptide cross-linking Source: Ensembl
  8. positive regulation of axon extension Source: MGI
  9. positive regulation of peptidase activity Source: GOC
  10. regulation of cell shape Source: UniProtKB-KW
  11. substrate adhesion-dependent cell spreading Source: Ensembl
  12. wound healing Source: MGI
Complete GO annotation...

Keywords - Biological processi

Acute phase, Angiogenesis, Cell adhesion, Cell shape

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198998. Molecules associated with elastic fibres.
REACT_199052. Degradation of the extracellular matrix.
REACT_204211. Fibronectin matrix formation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Cleaved into the following chain:
Gene namesi
Name:Fn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:95566. Fn1.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. basal lamina Source: MGI
  3. basement membrane Source: MGI
  4. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  5. extracellular matrix Source: MGI
  6. fibrinogen complex Source: Ensembl
  7. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351Q → A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. 1 Publication
Mutagenesisi35 – 351Q → L: 65% decrease in cross-linking efficiency; when associated with L-36. 1 Publication
Mutagenesisi36 – 361Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. 1 Publication
Mutagenesisi36 – 361Q → L: 65% decrease in cross-linking efficiency; when associated with L-35. 1 Publication
Mutagenesisi48 – 481Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 By similarityAdd
BLAST
Chaini33 – 24772445FibronectinPRO_0000019236Add
BLAST
Chaini627 – 70175Anastellin By similarityPRO_0000390480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Pyrrolidone carboxylic acid By similarity
Cross-linki35 – 35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-linki36 – 36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-linki48 – 48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Disulfide bondi53 ↔ 79 By similarity
Disulfide bondi77 ↔ 88 By similarity
Disulfide bondi98 ↔ 126 By similarity
Disulfide bondi124 ↔ 136 By similarity
Disulfide bondi142 ↔ 170 By similarity
Disulfide bondi168 ↔ 180 By similarity
Disulfide bondi187 ↔ 216 By similarity
Disulfide bondi214 ↔ 226 By similarity
Disulfide bondi232 ↔ 261 By similarity
Disulfide bondi259 ↔ 271 By similarity
Disulfide bondi308 ↔ 335 By similarity
Disulfide bondi333 ↔ 342 By similarity
Disulfide bondi360 ↔ 386 By similarity
Disulfide bondi374 ↔ 401 By similarity
Disulfide bondi420 ↔ 446 By similarity
Glycosylationi430 – 4301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi434 ↔ 461 By similarity
Disulfide bondi470 ↔ 498 By similarity
Disulfide bondi496 ↔ 508 By similarity
Disulfide bondi518 ↔ 545 By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...)2 Publications
Glycosylationi542 – 5421N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi543 ↔ 555 By similarity
Disulfide bondi561 ↔ 589 By similarity
Disulfide bondi587 ↔ 599 By similarity
Modified residuei875 – 8751Sulfotyrosine Reviewed prediction
Glycosylationi876 – 8761N-linked (GlcNAc...) Reviewed prediction
Modified residuei880 – 8801Sulfotyrosine Reviewed prediction
Glycosylationi1001 – 10011N-linked (GlcNAc...); atypical1 Publication
Glycosylationi1006 – 10061N-linked (GlcNAc...)3 Publications
Glycosylationi1243 – 12431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1290 – 12901N-linked (GlcNAc...)2 Publications
Glycosylationi2198 – 21981N-linked (GlcNAc...)1 Publication
Disulfide bondi2296 ↔ 2325 By similarity
Disulfide bondi2323 ↔ 2335 By similarity
Disulfide bondi2341 ↔ 2368 By similarity
Disulfide bondi2366 ↔ 2378 By similarity
Disulfide bondi2385 ↔ 2411 By similarity
Modified residuei2392 – 23921Sulfotyrosine Reviewed prediction
Disulfide bondi2409 ↔ 2420 By similarity
Disulfide bondi2458 – 2458Interchain (with C-2462)
Disulfide bondi2462 – 2462Interchain (with C-2458)
Modified residuei2475 – 24751Phosphoserine3 Publications

Post-translational modificationi

Sulfated By similarity.
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).
Phosphorylation sites are present in the extracellular medium By similarity.
Proteolytic processing produces the C-terminal NC1 peptide, anastellin By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiP11276.
PRIDEiP11276.

PTM databases

PhosphoSiteiP11276.

Expressioni

Tissue specificityi

Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix.

Inductioni

Glucocorticoids suppressed mRNA expression and protein synthesis.1 Publication

Gene expression databases

ArrayExpressiP11276.
CleanExiMM_FN1.
GenevestigatoriP11276.

Interactioni

Subunit structurei

Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, LGALS3BP and COL13A1 and COMP By similarity. Interacts with TNR; interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Plcg2Q8CIH56EBI-641955,EBI-617954

Protein-protein interaction databases

IntActiP11276. 3 interactions.
MINTiMINT-202764.

Structurei

Secondary structure

1
2477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1455 – 14595
Beta strandi1461 – 14677
Beta strandi1476 – 14849
Beta strandi1492 – 14965
Beta strandi1501 – 15077
Beta strandi1510 – 152112
Beta strandi1530 – 15367
Beta strandi1545 – 15506
Beta strandi1553 – 15575
Beta strandi1567 – 158014
Beta strandi1582 – 15865
Beta strandi1591 – 15944
Beta strandi1600 – 161213
Beta strandi1615 – 16173
Beta strandi1624 – 16307

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFNNMR-A1447-1630[»]
2MFNNMR-A1447-1630[»]
ProteinModelPortaliP11276.
SMRiP11276. Positions 49-274, 297-606, 609-808, 1172-1630, 1721-2081, 2332-2389.

Miscellaneous databases

EvolutionaryTraceiP11276.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 9141Fibronectin type-I 1Add
BLAST
Domaini96 – 13944Fibronectin type-I 2Add
BLAST
Domaini140 – 18344Fibronectin type-I 3Add
BLAST
Domaini185 – 22945Fibronectin type-I 4Add
BLAST
Domaini230 – 27445Fibronectin type-I 5Add
BLAST
Domaini306 – 34338Fibronectin type-I 6Add
BLAST
Domaini355 – 40349Fibronectin type-II 1Add
BLAST
Domaini415 – 46349Fibronectin type-II 2Add
BLAST
Domaini468 – 51649Fibronectin type-I 7Add
BLAST
Domaini516 – 55843Fibronectin type-I 8Add
BLAST
Domaini559 – 60244Fibronectin type-I 9Add
BLAST
Domaini610 – 717108Fibronectin type-III 1Add
BLAST
Domaini721 – 81191Fibronectin type-III 2Add
BLAST
Domaini812 – 90392Fibronectin type-III 3Add
BLAST
Domaini908 – 99790Fibronectin type-III 4Add
BLAST
Domaini998 – 108790Fibronectin type-III 5Add
BLAST
Domaini1088 – 117487Fibronectin type-III 6Add
BLAST
Domaini1175 – 126995Fibronectin type-III 7Add
BLAST
Domaini1270 – 135889Fibronectin type-III 8; extra domain 1Add
BLAST
Domaini1359 – 145193Fibronectin type-III 9Add
BLAST
Domaini1452 – 153988Fibronectin type-III 10Add
BLAST
Domaini1540 – 163394Fibronectin type-III 11Add
BLAST
Domaini1634 – 172592Fibronectin type-III 12Add
BLAST
Domaini1726 – 181388Fibronectin type-III 13; extra domain 2Add
BLAST
Domaini1814 – 190794Fibronectin type-III 14Add
BLAST
Domaini1908 – 199487Fibronectin type-III 15Add
BLAST
Domaini1995 – 208591Fibronectin type-III 16Add
BLAST
Domaini2193 – 228795Fibronectin type-III 17Add
BLAST
Domaini2294 – 233845Fibronectin type-I 10Add
BLAST
Domaini2339 – 238143Fibronectin type-I 11Add
BLAST
Domaini2383 – 242644Fibronectin type-I 12Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 273221Fibrin- and heparin-binding 1Add
BLAST
Regioni308 – 608301Collagen-bindingAdd
BLAST
Regioni1357 – 1630274Cell-attachmentAdd
BLAST
Regioni1811 – 2081271Heparin-binding 2Add
BLAST
Regioni2082 – 2201120Connecting strand 3 (CS-3) (V region)Add
BLAST
Regioni2296 – 2427132Fibrin-binding 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1614 – 16163Cell attachment site
Motifi2181 – 21833Cell attachment site

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00750000117415.
HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP11276.
KOiK05717.
OMAiIPGHLNS.
OrthoDBiEOG7X9G60.
TreeFamiTF329915.

Family and domain databases

Gene3Di2.10.10.10. 2 hits.
2.60.40.10. 17 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. Fibronectin_type3.
IPR000562. FN_type2_col-bd.
IPR013783. Ig-like_fold.
IPR013806. Kringle-like.
[Graphical view]
PfamiPF00039. fn1. 12 hits.
PF00040. fn2. 2 hits.
PF00041. fn3. 17 hits.
[Graphical view]
SMARTiSM00058. FN1. 12 hits.
SM00059. FN2. 2 hits.
SM00060. FN3. 17 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 11 hits.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. EGF_1. 2 hits.
PS01253. FN1_1. 12 hits.
PS51091. FN1_2. 12 hits.
PS00023. FN2_1. 2 hits.
PS51092. FN2_2. 2 hits.
PS50853. FN3. 17 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. Each of the "extra domain" and the connecting strand 3 are present in some forms of fibronectin and absent in others.

Isoform 1 (identifier: P11276-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK     50
PGCFDNGKHY QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD 100
KYTGNTYKVG DTYERPKDSM IWDCTCIGAG RGRISCTIAN RCHEGGQSYK 150
IGDKWRRPHE TGGYMLECLC LGNGKGEWTC KPIAEKCFDH AAGTSYVVGE 200
TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS YRIGDTWSKK 250
DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP 300
QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT 350
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF 400
CTDHAVLVQT RGGNSNGALC HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ 450
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDL GHMMRCTCVG 500
NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR 550
GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ 600
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS 650
TGRWKEATIP GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS 700
ASTPVTSNTV TGETAPYSPV VATSESVTEI TASSFVVSWV SASDTVSGFR 750
VEYELSEEGD EPQYLDLPST ATSVNIPDLL PGRKYIVNVY QISEEGKQSL 800
ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY RIVYSPSVEG 850
SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT 900
PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG 950
QRLPVNRNTF AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT 1000
NLQFVNETDR TVLVTWTPPR ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY 1050
PLRNLQPGSE YTVTLVAVKG NQQSPKATGV FTTLQPLRSI PPYNTEVTET 1100
TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS GLTPGVEYTY 1150
TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP 1200
DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK 1250
DDKESAPISD TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT 1300
VVAAGEGIPI FEDFVDSSVG YYTVTGLEPG IDYDISVITL INGGESAPTT 1350
LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP PSIELTNLLV RYSPVKNEED 1400
VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL RGRQKTGLDS 1450
PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR 1500
NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST 1550
PTSLLISWEP PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP 1600
GADYTITLYA VTGRGDSPAS SKPVSINYKT EIDKPSQMQV TDVQDNSISV 1650
RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA SPDQTEMTIE GLQPTVEYVV 1700
SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS 1750
RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME 1800
SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE 1850
KTGPMKEINL SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT 1900
LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAIP ANGQTPVQRS 1950
ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA RSSPVIIDAS TAIDAPSNLR 2000
FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR PRPGVTEATI 2050
TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI 2100
LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT 2150
TPPTAATPVR LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS 2200
TGQEALSQTT ISWTPFQESS EYIISCQPVG TDEEPLQFQV PGTSTSATLT 2250
GLTRGVTYNI IVEALQNQRR HKVREEVVTV GNAVSEGLNQ PTDDSCFDPY 2300
TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW CHDNGVNYKI 2350
GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK 2400
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ 2450
RTNTNVNCPI ECFMPLDVQA DRDDSRE 2477
Length:2,477
Mass (Da):272,538
Last modified:October 3, 2012 - v4
Checksum:i24A207BE67F85585
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1063 – 10631V → A in CAA63654. 1 Publication
Sequence conflicti1820 – 18201F → L in CAA63654. 1 Publication
Sequence conflicti2440 – 24401T → N in AAA37636. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC124821 Genomic DNA. No translation available.
CH466548 Genomic DNA. Translation: EDL00265.1.
BC051082 mRNA. No translation available.
Z22729 Genomic DNA. Translation: CAA80422.1.
X82402 mRNA. Translation: CAA57796.1.
X93167 mRNA. Translation: CAA63654.1.
M18194 mRNA. Translation: AAA37636.1.
S45680 mRNA. Translation: AAB23491.1.
CCDSiCCDS15031.1. [P11276-1]
PIRiA49173.
I48349.
RefSeqiNP_034363.1. NM_010233.2. [P11276-1]
UniGeneiMm.193099.

Genome annotation databases

EnsembliENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193. [P11276-1]
GeneIDi14268.
KEGGimmu:14268.
UCSCiuc007bju.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC124821 Genomic DNA. No translation available.
CH466548 Genomic DNA. Translation: EDL00265.1 .
BC051082 mRNA. No translation available.
Z22729 Genomic DNA. Translation: CAA80422.1 .
X82402 mRNA. Translation: CAA57796.1 .
X93167 mRNA. Translation: CAA63654.1 .
M18194 mRNA. Translation: AAA37636.1 .
S45680 mRNA. Translation: AAB23491.1 .
CCDSi CCDS15031.1. [P11276-1 ]
PIRi A49173.
I48349.
RefSeqi NP_034363.1. NM_010233.2. [P11276-1 ]
UniGenei Mm.193099.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MFN NMR - A 1447-1630 [» ]
2MFN NMR - A 1447-1630 [» ]
ProteinModelPortali P11276.
SMRi P11276. Positions 49-274, 297-606, 609-808, 1172-1630, 1721-2081, 2332-2389.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11276. 3 interactions.
MINTi MINT-202764.

PTM databases

PhosphoSitei P11276.

Proteomic databases

PaxDbi P11276.
PRIDEi P11276.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055226 ; ENSMUSP00000054499 ; ENSMUSG00000026193 . [P11276-1 ]
GeneIDi 14268.
KEGGi mmu:14268.
UCSCi uc007bju.1. mouse.

Organism-specific databases

CTDi 2335.
MGIi MGI:95566. Fn1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00750000117415.
HOGENOMi HOG000234344.
HOVERGENi HBG005731.
InParanoidi P11276.
KOi K05717.
OMAi IPGHLNS.
OrthoDBi EOG7X9G60.
TreeFami TF329915.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198998. Molecules associated with elastic fibres.
REACT_199052. Degradation of the extracellular matrix.
REACT_204211. Fibronectin matrix formation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSi FN1. mouse.
EvolutionaryTracei P11276.
NextBioi 285629.
PROi P11276.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11276.
CleanExi MM_FN1.
Genevestigatori P11276.

Family and domain databases

Gene3Di 2.10.10.10. 2 hits.
2.60.40.10. 17 hits.
InterProi IPR000083. Fibronectin_type1.
IPR003961. Fibronectin_type3.
IPR000562. FN_type2_col-bd.
IPR013783. Ig-like_fold.
IPR013806. Kringle-like.
[Graphical view ]
Pfami PF00039. fn1. 12 hits.
PF00040. fn2. 2 hits.
PF00041. fn3. 17 hits.
[Graphical view ]
SMARTi SM00058. FN1. 12 hits.
SM00059. FN2. 2 hits.
SM00060. FN3. 17 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 11 hits.
SSF57440. SSF57440. 2 hits.
PROSITEi PS00022. EGF_1. 2 hits.
PS01253. FN1_1. 12 hits.
PS51091. FN1_2. 12 hits.
PS00023. FN2_1. 2 hits.
PS51092. FN2_2. 2 hits.
PS50853. FN3. 17 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-920.
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  4. "Sequence of the mouse fibronectin-encoding gene promoter region."
    Polly P., Nicholson R.C.
    Gene 137:353-354(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
    Tissue: Liver.
  5. "Regulation of mesenchymal extracellular matrix protein synthesis by transforming growth factor-beta and glucocorticoids in tumor stroma."
    Talts J.F., Weller A., Timpl R., Ekblom M., Ekblom P.
    J. Cell Sci. 108:2153-2162(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 562-834.
    Strain: NMRI.
  6. Gorski G., Aros M., Norton P.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 899-2376.
  7. "Induction of fibronectin gene transcription and mRNA is a primary response to growth-factor stimulation of AKR-2B cells."
    Blatti S.P., Foster D.N., Ranganthan G., Moses H.L., Getz M.J.
    Proc. Natl. Acad. Sci. U.S.A. 85:1119-1123(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
  8. "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts."
    Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.
    Exp. Cell Res. 180:537-545(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
  9. "Fibronectin gene expression in proliferating, quiescent, and SV40-infected mouse kidney cells."
    Khandjian E.W., Salomon C., Leonard N., Tremblay S., Turler H.
    Exp. Cell Res. 202:464-470(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
    Tissue: Kidney.
  10. "Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix."
    Corbett S.A., Lee L., Wilson C.L., Schwarzbauer J.E.
    J. Biol. Chem. 272:24999-25005(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSGLUTAMINATION AT GLN-35; GLN-36 AND GLN-48, MUTAGENESIS OF GLN-35; GLN-36 AND GLN-48.
  11. "Glucocorticoids down-regulate the extracellular matrix proteins fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma."
    Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.
    Eur. J. Haematol. 67:176-184(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY GLUCOCORTICOIDS.
  12. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006.
    Strain: C57BL/6.
    Tissue: Plasma.
  13. "TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding."
    de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W., Fukumoto S., Yamada Y.
    J. Biol. Chem. 282:30878-30888(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBLN7.
  14. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528.
    Strain: C57BL/6.
    Tissue: Plasma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528; ASN-1001; ASN-1006; ASN-1290 AND ASN-2198.
    Tissue: Myoblast.
  18. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  19. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006 AND ASN-1290.
  20. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
    Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
    J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure."
    Copie V., Tomita Y., Akiyama S.K., Aota S., Yamada K.M., Venable R.M., Pastor R.W., Krueger S., Torchia D.A.
    J. Mol. Biol. 277:663-682(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1447-1630.

Entry informationi

Entry nameiFINC_MOUSE
AccessioniPrimary (citable) accession number: P11276
Secondary accession number(s): G5E8B8
, Q61567, Q61568, Q61569, Q64233, Q80UI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: September 3, 2014
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi