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P04004 (VTNC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 181. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitronectin

Short name=VN
Alternative name(s):
S-protein
Serum-spreading factor
V75
Gene names
Name:VTN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.

Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.

Subunit structure

Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1, insulin and C1QBP. Ref.9 Ref.10 Ref.15 Ref.16

Subcellular location

Secretedextracellular space.

Tissue specificity

Plasma.

Domain

The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.

Post-translational modification

Sulfated on 2 tyrosine residues.

N- and O-glycosylated By similarity. Ref.22 Ref.25

Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.

It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Phosphorylation sites are present in the extracellular medium.

Sequence similarities

Contains 4 hemopexin repeats.

Contains 1 SMB (somatomedin-B) domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Traceable author statement PubMed 2418831. Source: ProtInc

cell adhesion mediated by integrin

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

cell-matrix adhesion

Inferred from direct assay PubMed 10022831. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

immune response

Traceable author statement PubMed 2418831. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

negative regulation of blood coagulation

Inferred by curator PubMed 1695900. Source: BHF-UCL

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 1695900. Source: BHF-UCL

positive regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10022831. Source: BHF-UCL

positive regulation of protein binding

Inferred from direct assay PubMed 1695900. Source: BHF-UCL

positive regulation of receptor-mediated endocytosis

Inferred from direct assay PubMed 8626514. Source: BHF-UCL

positive regulation of smooth muscle cell migration

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

positive regulation of vascular endothelial growth factor receptor signaling pathway

Traceable author statement PubMed 19267251. Source: BHF-UCL

positive regulation of wound healing

Inferred by curator PubMed 8837777. Source: BHF-UCL

regulation of complement activation

Traceable author statement. Source: Reactome

smooth muscle cell-matrix adhesion

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

   Cellular_componentalphav-beta3 integrin-vitronectin complex

Traceable author statement PubMed 19267251. Source: BHF-UCL

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular matrix

Inferred from direct assay PubMed 1632457. Source: BHF-UCL

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 1695900. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionextracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

integrin binding

Inferred from physical interaction PubMed 8837777. Source: BHF-UCL

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C1QBPQ070218EBI-1036653,EBI-347528

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.8 Ref.9
Chain20 – 478459Vitronectin
PRO_0000036394
Chain20 – 398379Vitronectin V65 subunit
PRO_0000036395
Peptide20 – 6344Somatomedin-B Ref.8
PRO_0000036396
Chain399 – 47880Vitronectin V10 subunit
PRO_0000036397

Regions

Domain20 – 6344SMB
Repeat158 – 20245Hemopexin 1
Repeat203 – 25048Hemopexin 2
Repeat251 – 30555Hemopexin 3
Repeat419 – 47254Hemopexin 4
Region362 – 39534Heparin-binding
Motif64 – 663Cell attachment site

Sites

Site398 – 3992Cleavage

Amino acid modifications

Modified residue691Phosphothreonine; by CK2; in vitro Ref.17
Modified residue751Sulfotyrosine Ref.22
Modified residue761Phosphothreonine; by CK2; in vitro Ref.17
Modified residue781Sulfotyrosine Ref.22
Modified residue2821Sulfotyrosine Potential
Modified residue3121Phosphoserine Ref.21 Ref.22 Ref.23
Modified residue3971Phosphoserine; by PKA Ref.11 Ref.14
Modified residue4171Sulfotyrosine Potential
Modified residue4201Sulfotyrosine Potential
Glycosylation861N-linked (GlcNAc...) (complex) Ref.19 Ref.20 Ref.22 Ref.24 Ref.25
Glycosylation1691N-linked (GlcNAc...) Ref.19 Ref.20 Ref.24
Glycosylation2421N-linked (GlcNAc...) (complex) Ref.19 Ref.20 Ref.24 Ref.25
Disulfide bond24 ↔ 40Alternate; alternate By similarity
Disulfide bond24 ↔ 28Alternate; alternate Ref.18
Disulfide bond28 ↔ 58Alternate; alternate By similarity
Disulfide bond38 ↔ 51Alternate; alternate By similarity
Disulfide bond38 ↔ 40Alternate; alternate Ref.18
Disulfide bond44 ↔ 50 Ref.18
Disulfide bond51 ↔ 58Alternate; alternate Ref.18
Disulfide bond293 ↔ 430 Ref.18

Natural variations

Natural variant1221A → S. Ref.6
Corresponds to variant rs2227741 [ dbSNP | Ensembl ].
VAR_012983
Natural variant2681R → Q. Ref.6
Corresponds to variant rs2227723 [ dbSNP | Ensembl ].
VAR_012984
Natural variant4001T → M. Ref.6 Ref.7
Corresponds to variant rs704 [ dbSNP | Ensembl ].
VAR_012985

Experimental info

Mutagenesis691T → A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-76. Ref.17
Mutagenesis691T → E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-76. Ref.17
Mutagenesis761T → A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-69. Ref.17
Mutagenesis761T → E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-69. Ref.17
Sequence conflict501C → N AA sequence Ref.8
Sequence conflict2251S → N Ref.3
Sequence conflict2251S → N Ref.4
Sequence conflict3661A → T in CAA26933. Ref.3

Secondary structure

............... 478
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04004 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: 0D6DB5591CBFEF45

FASTA47854,306
        10         20         30         40         50         60 
MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC CTDYTAECKP 

        70         80         90        100        110        120 
QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS DLQAQSKGNP EQTPVLKPEE 

       130        140        150        160        170        180 
EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP AEEELCSGKP FDAFTDLKNG SLFAFRGQYC 

       190        200        210        220        230        240 
YELDEKAVRP GYPKLIRDVW GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP 

       250        260        270        280        290        300 
RNISDGFDGI PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA 

       310        320        330        340        350        360 
VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM AGRIYISGMA 

       370        380        390        400        410        420 
PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT WLSLFSSEES NLGANNYDDY 

       430        440        450        460        470 
RMDWLVPATC EPIQSVFFFS GDKYYRVNLR TRRVDTVDPP YPRSIAQYWL GCPAPGHL 

« Hide

References

« Hide 'large scale' references
[1]"Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin."
Suzuki S., Oldberg A., Hayman E.G., Pierschbacher M.D., Ruoslahti E.
EMBO J. 4:2519-2524(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Suzuki S., Oldberg A., Hayman E.G., Pierschbacher M.D., Ruoslahti E.
Submitted (JUN-1986) to the PIR data bank
Cited for: SEQUENCE REVISION.
[3]"Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion."
Jenne D.E., Stanley K.K.
EMBO J. 4:3153-3157(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Nucleotide sequence and organization of the human S-protein gene: repeating peptide motifs in the 'pexin' family and a model for their evolution."
Jenne D.E., Stanley K.K.
Biochemistry 26:6735-6742(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[6]SeattleSNPs variation discovery resource
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-122; GLN-268 AND MET-400.
[7]"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], VARIANT MET-400.
Tissue: Lung.
[8]"Primary structure of somatomedin B: a growth hormone-dependent serum factor with protease inhibiting activity."
Fryklund L., Sievertsson H.
FEBS Lett. 87:55-60(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-63.
[9]"Identification of a PAI-1 binding site in vitronectin."
Sigurdardottir O., Wiman B.
Biochim. Biophys. Acta 1208:104-110(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-44, INTERACTION WITH SERPINE1/PAI1.
[10]"Insulin binds to type V collagen with retention of mitogenic activity."
Yaoi Y., Hashimoto K., Takahara K., Kato I.
Exp. Cell Res. 194:180-185(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 360-368, INTERACTION WITH INSULIN.
[11]"Phosphorylation of vitronectin by a protein kinase in human plasma. Identification of a unique phosphorylation site in the heparin-binding domain."
McGuire E.A., Peacock M.E., Inhorn R.C., Siegel N.R., Tollefsen D.M.
J. Biol. Chem. 263:1942-1945(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 393-400, PHOSPHORYLATION AT SER-397.
[12]Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Submitted (JUN-1992) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 399-413.
Tissue: Plasma.
[13]"Sulfation of two tyrosine-residues in human complement S-protein (vitronectin)."
Jenne D.E., Hille A., Stanley K.K., Huttner W.B.
Eur. J. Biochem. 185:391-395(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[14]"The phosphorylation of the two-chain form of vitronectin by protein kinase A is heparin dependent."
Chain D., Korc-Grodzicki B., Kreizman T., Shaltiel S.
FEBS Lett. 269:221-225(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-397.
[15]"Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin."
Seiffert D., Loskutoff D.J.
J. Biol. Chem. 266:2824-2830(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SERPINE1/PAI1.
[16]"The binding protein for globular heads of complement C1q, gC1qR. Functional expression and characterization as a novel vitronectin binding factor."
Lim B.L., Reid K.B., Ghebrehiwet B., Peerschke E.I., Leigh L.A., Preissner K.T.
J. Biol. Chem. 271:26739-26744(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1QBP.
[17]"Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading."
Seger D., Gechtman Z., Shaltiel S.
J. Biol. Chem. 273:24805-24813(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-69 AND THR-76, MUTAGENESIS OF THR-69 AND THR-76.
[18]"Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin."
Kamikubo Y., Okumura Y., Loskutoff D.J.
J. Biol. Chem. 277:27109-27119(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS IN SOMATOMEDIN-B.
[19]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242.
Tissue: Plasma.
[20]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242.
Tissue: Plasma.
[21]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[22]"Determination of the sites of tyrosine O-sulfation in peptides and proteins."
Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.
Nat. Methods 4:583-588(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-75 AND TYR-78, PHOSPHORYLATION AT SER-312, GLYCOSYLATION AT ASN-86, IDENTIFICATION BY MASS SPECTROMETRY.
[23]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[24]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242.
Tissue: Liver.
[25]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-86 AND ASN-242.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration."
Zhou A., Huntington J.A., Pannu N.S., Carrell R.W., Read R.J.
Nat. Struct. Biol. 10:541-544(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 22-58 IN COMPLEX WITH SERPINE1/PAI1.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03168 mRNA. Translation: CAA26933.1. Sequence problems.
X05006 Genomic DNA. Translation: CAA28659.1. Sequence problems.
AK312968 mRNA. Translation: BAG35807.1.
AF382388 Genomic DNA. Translation: AAK60270.1.
BC005046 mRNA. Translation: AAH05046.1.
PIRSGHU1V. A29744.
RefSeqNP_000629.3. NM_000638.3.
UniGeneHs.2257.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OC0X-ray2.28B20-70[»]
1S4GNMR-A20-70[»]
1SSUNMR-A20-70[»]
2JQ8NMR-A20-66[»]
3BT1X-ray2.80B21-60[»]
3BT2X-ray2.50B21-60[»]
4K24X-ray4.50B21-60[»]
ProteinModelPortalP04004.
SMRP04004. Positions 21-60, 65-344, 435-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113287. 73 interactions.
DIPDIP-36566N.
IntActP04004. 22 interactions.
MINTMINT-4999753.
STRING9606.ENSP00000226218.

Chemistry

ChEMBLCHEMBL1075314.
DrugBankDB00013. Urokinase.

PTM databases

PhosphoSiteP04004.
UniCarbKBP04004.

Polymorphism databases

DMDM139653.

2D gel databases

DOSAC-COBS-2DPAGEP04004.
SWISS-2DPAGEP04004.

Proteomic databases

PeptideAtlasP04004.
PRIDEP04004.

Protocols and materials databases

DNASU7448.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226218; ENSP00000226218; ENSG00000109072.
ENST00000573054; ENSP00000459404; ENSG00000262062.
GeneID7448.
KEGGhsa:7448.
UCSCuc002hbc.3. human.

Organism-specific databases

CTD7448.
GeneCardsGC17M026991.
HGNCHGNC:12724. VTN.
MIM193190. gene.
neXtProtNX_P04004.
PharmGKBPA37335.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000133161.
HOVERGENHBG002902.
InParanoidP04004.
KOK06251.
OMALLQRDSW.
PhylomeDBP04004.
TreeFamTF332780.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP04004.
BgeeP04004.
CleanExHS_VTN.
GenevestigatorP04004.

Family and domain databases

Gene3D2.110.10.10. 3 hits.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMSSF50923. SSF50923. 3 hits.
PROSITEPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04004.
GeneWikiVitronectin.
GenomeRNAi7448.
NextBio29166.
PMAP-CutDBP04004.
PROP04004.
SOURCESearch...

Entry information

Entry nameVTNC_HUMAN
AccessionPrimary (citable) accession number: P04004
Secondary accession number(s): B2R7G0, P01141, Q9BSH7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: April 16, 2014
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM