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P11276 (FINC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibronectin

Short name=FN

Cleaved into the following chain:

  1. Anastellin
Gene names
Name:Fn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.20

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. Ref.20

Subunit structure

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. Ref.13

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

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.

Induction

Glucocorticoids suppressed mRNA expression and protein synthesis. Ref.11

Post-translational modification

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.

Sequence similarities

Contains 12 fibronectin type-I domains.

Contains 2 fibronectin type-II domains.

Contains 17 fibronectin type-III domains.

Ontologies

Keywords
   Biological processAcute phase
Angiogenesis
Cell adhesion
Cell shape
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Pyrrolidone carboxylic acid
Sulfation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-independent cell-matrix adhesion

Inferred from direct assay PubMed 19651211. Source: MGI

cell adhesion

Inferred from direct assay PubMed 12021259PubMed 9441684. Source: MGI

cell-matrix adhesion

Inferred from direct assay PubMed 15728191. Source: MGI

cell-substrate junction assembly

Inferred from direct assay PubMed 12867986. Source: MGI

peptide cross-linking

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from direct assay PubMed 12879062. Source: MGI

positive regulation of peptidase activity

Inferred from direct assay PubMed 16061471. Source: GOC

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from mutant phenotype PubMed 12847088. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 10742111. Source: MGI

basal lamina

Inferred from direct assay PubMed 24191021. Source: MGI

basement membrane

Inferred from direct assay PubMed 11511678PubMed 8984825. Source: MGI

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: Ensembl

extracellular matrix

Inferred from direct assay PubMed 11511678PubMed 15065125PubMed 18559979PubMed 2209468. Source: MGI

fibrinogen complex

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from direct assay PubMed 15728191PubMed 9421166. Source: MGI

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidase activator activity

Inferred from direct assay PubMed 16061471. Source: MGI

protein binding

Inferred from physical interaction PubMed 15102471. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Plcg2Q8CIH56EBI-641955,EBI-617954

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Chain33 – 24772445Fibronectin
PRO_0000019236
Chain627 – 70175Anastellin By similarity
PRO_0000390480

Regions

Domain51 – 9141Fibronectin type-I 1
Domain96 – 13944Fibronectin type-I 2
Domain140 – 18344Fibronectin type-I 3
Domain185 – 22945Fibronectin type-I 4
Domain230 – 27445Fibronectin type-I 5
Domain306 – 34338Fibronectin type-I 6
Domain355 – 40349Fibronectin type-II 1
Domain415 – 46349Fibronectin type-II 2
Domain468 – 51649Fibronectin type-I 7
Domain516 – 55843Fibronectin type-I 8
Domain559 – 60244Fibronectin type-I 9
Domain610 – 717108Fibronectin type-III 1
Domain721 – 81191Fibronectin type-III 2
Domain812 – 90392Fibronectin type-III 3
Domain908 – 99790Fibronectin type-III 4
Domain998 – 108790Fibronectin type-III 5
Domain1088 – 117487Fibronectin type-III 6
Domain1175 – 126995Fibronectin type-III 7
Domain1270 – 135889Fibronectin type-III 8; extra domain 1
Domain1359 – 145193Fibronectin type-III 9
Domain1452 – 153988Fibronectin type-III 10
Domain1540 – 163394Fibronectin type-III 11
Domain1634 – 172592Fibronectin type-III 12
Domain1726 – 181388Fibronectin type-III 13; extra domain 2
Domain1814 – 190794Fibronectin type-III 14
Domain1908 – 199487Fibronectin type-III 15
Domain1995 – 208591Fibronectin type-III 16
Domain2193 – 228795Fibronectin type-III 17
Domain2294 – 233845Fibronectin type-I 10
Domain2339 – 238143Fibronectin type-I 11
Domain2383 – 242644Fibronectin type-I 12
DNA binding906 – 1171266
Region53 – 273221Fibrin- and heparin-binding 1
Region308 – 608301Collagen-binding
Region1357 – 1630274Cell-attachment
Region1811 – 2081271Heparin-binding 2
Region2082 – 2201120Connecting strand 3 (CS-3) (V region)
Region2296 – 2427132Fibrin-binding 2
Motif1614 – 16163Cell attachment site
Motif2181 – 21833Cell attachment site

Amino acid modifications

Modified residue331Pyrrolidone carboxylic acid By similarity
Modified residue8751Sulfotyrosine Potential
Modified residue8801Sulfotyrosine Potential
Modified residue23921Sulfotyrosine Potential
Modified residue24751Phosphoserine Ref.15 Ref.16 Ref.18
Glycosylation4301N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Ref.14 Ref.17
Glycosylation5421N-linked (GlcNAc...) Potential
Glycosylation8761N-linked (GlcNAc...) Potential
Glycosylation10011N-linked (GlcNAc...); atypical Ref.17
Glycosylation10061N-linked (GlcNAc...) Ref.12 Ref.17 Ref.19
Glycosylation12431N-linked (GlcNAc...) Potential
Glycosylation12901N-linked (GlcNAc...) Ref.17 Ref.19
Glycosylation21981N-linked (GlcNAc...) Ref.17
Disulfide bond53 ↔ 79 By similarity
Disulfide bond77 ↔ 88 By similarity
Disulfide bond98 ↔ 126 By similarity
Disulfide bond124 ↔ 136 By similarity
Disulfide bond142 ↔ 170 By similarity
Disulfide bond168 ↔ 180 By similarity
Disulfide bond187 ↔ 216 By similarity
Disulfide bond214 ↔ 226 By similarity
Disulfide bond232 ↔ 261 By similarity
Disulfide bond259 ↔ 271 By similarity
Disulfide bond308 ↔ 335 By similarity
Disulfide bond333 ↔ 342 By similarity
Disulfide bond360 ↔ 386 By similarity
Disulfide bond374 ↔ 401 By similarity
Disulfide bond420 ↔ 446 By similarity
Disulfide bond434 ↔ 461 By similarity
Disulfide bond470 ↔ 498 By similarity
Disulfide bond496 ↔ 508 By similarity
Disulfide bond518 ↔ 545 By similarity
Disulfide bond543 ↔ 555 By similarity
Disulfide bond561 ↔ 589 By similarity
Disulfide bond587 ↔ 599 By similarity
Disulfide bond2296 ↔ 2325 By similarity
Disulfide bond2323 ↔ 2335 By similarity
Disulfide bond2341 ↔ 2368 By similarity
Disulfide bond2366 ↔ 2378 By similarity
Disulfide bond2385 ↔ 2411 By similarity
Disulfide bond2409 ↔ 2420 By similarity
Disulfide bond2458Interchain (with C-2462)
Disulfide bond2462Interchain (with C-2458)
Cross-link35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-link36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-link48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Experimental info

Mutagenesis351Q → A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. Ref.10
Mutagenesis351Q → L: 65% decrease in cross-linking efficiency; when associated with L-36. Ref.10
Mutagenesis361Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. Ref.10
Mutagenesis361Q → L: 65% decrease in cross-linking efficiency; when associated with L-35. Ref.10
Mutagenesis481Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. Ref.10
Sequence conflict10631V → A in CAA63654. Ref.6
Sequence conflict18201F → L in CAA63654. Ref.6
Sequence conflict24401T → N in AAA37636. Ref.7

Secondary structure

............................... 2477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2012. Version 4.
Checksum: 24A207BE67F85585

FASTA2,477272,538
        10         20         30         40         50         60 
MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK PGCFDNGKHY 

        70         80         90        100        110        120 
QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM 

       130        140        150        160        170        180 
IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC 

       190        200        210        220        230        240 
KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS 

       250        260        270        280        290        300 
YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP 

       310        320        330        340        350        360 
QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC 

       370        380        390        400        410        420 
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC 

       430        440        450        460        470        480 
HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI 

       490        500        510        520        530        540 
GDQWDKQHDL GHMMRCTCVG NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM 

       550        560        570        580        590        600 
LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ 

       610        620        630        640        650        660 
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP 

       670        680        690        700        710        720 
GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS ASTPVTSNTV TGETAPYSPV 

       730        740        750        760        770        780 
VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL 

       790        800        810        820        830        840 
PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY 

       850        860        870        880        890        900 
RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT 

       910        920        930        940        950        960 
PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG QRLPVNRNTF 

       970        980        990       1000       1010       1020 
AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR 

      1030       1040       1050       1060       1070       1080 
ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY PLRNLQPGSE YTVTLVAVKG NQQSPKATGV 

      1090       1100       1110       1120       1130       1140 
FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS 

      1150       1160       1170       1180       1190       1200 
GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP 

      1210       1220       1230       1240       1250       1260 
DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK DDKESAPISD 

      1270       1280       1290       1300       1310       1320 
TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG 

      1330       1340       1350       1360       1370       1380 
YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP 

      1390       1400       1410       1420       1430       1440 
PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL 

      1450       1460       1470       1480       1490       1500 
RGRQKTGLDS PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR 

      1510       1520       1530       1540       1550       1560 
NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST PTSLLISWEP 

      1570       1580       1590       1600       1610       1620 
PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS 

      1630       1640       1650       1660       1670       1680 
SKPVSINYKT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA 

      1690       1700       1710       1720       1730       1740 
SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI 

      1750       1760       1770       1780       1790       1800 
AWESPQGQVS RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME 

      1810       1820       1830       1840       1850       1860 
SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE KTGPMKEINL 

      1870       1880       1890       1900       1910       1920 
SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT LENVSPPRRA RVTDATETTI 

      1930       1940       1950       1960       1970       1980 
TISWRTKTET ITGFQVDAIP ANGQTPVQRS ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA 

      1990       2000       2010       2020       2030       2040 
RSSPVIIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR 

      2050       2060       2070       2080       2090       2100 
PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI 

      2110       2120       2130       2140       2150       2160 
LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT TPPTAATPVR 

      2170       2180       2190       2200       2210       2220 
LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS 

      2230       2240       2250       2260       2270       2280 
EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALQNQRR HKVREEVVTV 

      2290       2300       2310       2320       2330       2340 
GNAVSEGLNQ PTDDSCFDPY TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW 

      2350       2360       2370       2380       2390       2400 
CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK 

      2410       2420       2430       2440       2450       2460 
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ RTNTNVNCPI 

      2470 
ECFMPLDVQA DRDDSRE 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15031.1. [P11276-1]
PIRA49173.
I48349.
RefSeqNP_034363.1. NM_010233.2. [P11276-1]
UniGeneMm.193099.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFNNMR-A1447-1630[»]
2MFNNMR-A1447-1630[»]
ProteinModelPortalP11276.
SMRP11276. Positions 49-274, 297-606, 609-808, 1172-1630, 1721-2081, 2332-2389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11276. 3 interactions.
MINTMINT-202764.

PTM databases

PhosphoSiteP11276.

Proteomic databases

PaxDbP11276.
PRIDEP11276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193. [P11276-1]
GeneID14268.
KEGGmmu:14268.
UCSCuc007bju.1. mouse.

Organism-specific databases

CTD2335.
MGIMGI:95566. Fn1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00750000117415.
HOGENOMHOG000234344.
HOVERGENHBG005731.
InParanoidP11276.
KOK05717.
OMAIPGHLNS.
OrthoDBEOG7X9G60.
TreeFamTF329915.

Gene expression databases

ArrayExpressP11276.
CleanExMM_FN1.
GenevestigatorP11276.

Family and domain databases

Gene3D2.10.10.10. 2 hits.
2.60.40.10. 17 hits.
InterProIPR000083. Fibronectin_type1.
IPR003961. Fibronectin_type3.
IPR000562. FN_type2_col-bd.
IPR013783. Ig-like_fold.
IPR013806. Kringle-like.
[Graphical view]
PfamPF00039. fn1. 12 hits.
PF00040. fn2. 2 hits.
PF00041. fn3. 17 hits.
[Graphical view]
SMARTSM00058. FN1. 12 hits.
SM00059. FN2. 2 hits.
SM00060. FN3. 17 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 11 hits.
SSF57440. SSF57440. 2 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSFN1. mouse.
EvolutionaryTraceP11276.
NextBio285629.
PROP11276.
SOURCESearch...

Entry information

Entry nameFINC_MOUSE
AccessionPrimary (citable) accession number: P11276
Secondary accession number(s): G5E8B8 expand/collapse secondary AC list , Q61567, Q61568, Q61569, Q64233, Q80UI4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 160 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot