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P04004

- VTNC_HUMAN

UniProt

P04004 - VTNC_HUMAN

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Protein

Vitronectin

Gene

VTN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei398 – 3992Cleavage

GO - Molecular functioni

  1. extracellular matrix binding Source: Ensembl
  2. heparin binding Source: UniProtKB-KW
  3. integrin binding Source: UniProtKB
  4. polysaccharide binding Source: InterPro
  5. scavenger receptor activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. cell adhesion mediated by integrin Source: BHF-UCL
  3. cell-matrix adhesion Source: UniProtKB
  4. endodermal cell differentiation Source: UniProtKB
  5. extracellular matrix organization Source: Reactome
  6. immune response Source: ProtInc
  7. innate immune response Source: Reactome
  8. negative regulation of blood coagulation Source: BHF-UCL
  9. negative regulation of endopeptidase activity Source: BHF-UCL
  10. positive regulation of cell-substrate adhesion Source: Ensembl
  11. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  12. positive regulation of protein binding Source: BHF-UCL
  13. positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  14. positive regulation of smooth muscle cell migration Source: BHF-UCL
  15. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  16. positive regulation of wound healing Source: BHF-UCL
  17. regulation of complement activation Source: Reactome
  18. smooth muscle cell-matrix adhesion Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitronectin
Short name:
VN
Alternative name(s):
S-protein
Serum-spreading factor
V75
Cleaved into the following 3 chains:
Gene namesi
Name:VTN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:12724. VTN.

Subcellular locationi

GO - Cellular componenti

  1. alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
  2. blood microparticle Source: UniProt
  3. extracellular matrix Source: BHF-UCL
  4. extracellular region Source: UniProtKB
  5. extracellular space Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProtKB
  7. proteinaceous extracellular matrix Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691T → A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-76. 1 Publication
Mutagenesisi69 – 691T → E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-76. 1 Publication
Mutagenesisi76 – 761T → A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-69. 1 Publication
Mutagenesisi76 – 761T → E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-69. 1 Publication

Organism-specific databases

PharmGKBiPA37335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 478459VitronectinPRO_0000036394Add
BLAST
Chaini20 – 398379Vitronectin V65 subunitPRO_0000036395Add
BLAST
Peptidei20 – 6344Somatomedin-BPRO_0000036396Add
BLAST
Chaini399 – 47880Vitronectin V10 subunitPRO_0000036397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 40Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi24 ↔ 28Alternate; alternate1 PublicationPROSITE-ProRule annotation
Disulfide bondi28 ↔ 58Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 51Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 40Alternate; alternate1 PublicationPROSITE-ProRule annotation
Disulfide bondi44 ↔ 501 PublicationPROSITE-ProRule annotation
Disulfide bondi51 ↔ 58Alternate; alternate1 PublicationPROSITE-ProRule annotation
Modified residuei69 – 691Phosphothreonine; by CK2; in vitro1 Publication
Modified residuei75 – 751Sulfotyrosine1 Publication
Modified residuei76 – 761Phosphothreonine; by CK2; in vitro1 Publication
Modified residuei78 – 781Sulfotyrosine1 Publication
Glycosylationi86 – 861N-linked (GlcNAc...) (complex)5 Publications
Glycosylationi169 – 1691N-linked (GlcNAc...)3 Publications
Glycosylationi242 – 2421N-linked (GlcNAc...) (complex)4 Publications
Modified residuei282 – 2821SulfotyrosineSequence Analysis
Disulfide bondi293 ↔ 4301 PublicationPROSITE-ProRule annotation
Modified residuei312 – 3121Phosphoserine3 Publications
Modified residuei397 – 3971Phosphoserine; by PKA2 Publications
Modified residuei417 – 4171SulfotyrosineSequence Analysis
Modified residuei420 – 4201SulfotyrosineSequence Analysis

Post-translational modificationi

Sulfated on 2 tyrosine residues.2 Publications
N- and O-glycosylated.By similarity
Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.1 Publication
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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP04004.
PeptideAtlasiP04004.
PRIDEiP04004.

2D gel databases

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

PTM databases

PhosphoSiteiP04004.
UniCarbKBiP04004.

Miscellaneous databases

PMAP-CutDBP04004.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP04004.
CleanExiHS_VTN.
ExpressionAtlasiP04004. baseline and differential.
GenevestigatoriP04004.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C1QBPQ070218EBI-1036653,EBI-347528

Protein-protein interaction databases

BioGridi113287. 74 interactions.
DIPiDIP-36566N.
IntActiP04004. 22 interactions.
MINTiMINT-4999753.
STRINGi9606.ENSP00000226218.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243
Turni25 – 295
Beta strandi32 – 343
Beta strandi36 – 394
Helixi44 – 474
Turni51 – 533
Helixi54 – 574
Beta strandi65 – 684

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP04004.
SMRiP04004. Positions 21-60, 155-343.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04004.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 6344SMBPROSITE-ProRule annotationAdd
BLAST
Repeati158 – 20245Hemopexin 1Add
BLAST
Repeati203 – 25048Hemopexin 2Add
BLAST
Repeati251 – 30555Hemopexin 3Add
BLAST
Repeati419 – 47254Hemopexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni362 – 39534Heparin-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi64 – 663Cell attachment site

Domaini

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

Sequence similaritiesi

Contains 4 hemopexin repeats.Curated
Contains 1 SMB (somatomedin-B) domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00530000063751.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.
InParanoidiP04004.
KOiK06251.
OMAiLLQRDSW.
PhylomeDBiP04004.
TreeFamiTF332780.

Family and domain databases

Gene3Di2.110.10.10. 3 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 3 hits.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04004-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC
60 70 80 90 100
CTDYTAECKP QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS
110 120 130 140 150
DLQAQSKGNP EQTPVLKPEE EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP
160 170 180 190 200
AEEELCSGKP FDAFTDLKNG SLFAFRGQYC YELDEKAVRP GYPKLIRDVW
210 220 230 240 250
GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP RNISDGFDGI
260 270 280 290 300
PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA
310 320 330 340 350
VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM
360 370 380 390 400
AGRIYISGMA PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT
410 420 430 440 450
WLSLFSSEES NLGANNYDDY RMDWLVPATC EPIQSVFFFS GDKYYRVNLR
460 470
TRRVDTVDPP YPRSIAQYWL GCPAPGHL
Length:478
Mass (Da):54,306
Last modified:October 23, 1986 - v1
Checksum:i0D6DB5591CBFEF45
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501C → N AA sequence (PubMed:631332)Curated
Sequence conflicti225 – 2251S → N(PubMed:3004934)Curated
Sequence conflicti225 – 2251S → N(PubMed:2447940)Curated
Sequence conflicti366 – 3661A → T in CAA26933. (PubMed:3004934)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221A → S.1 Publication
Corresponds to variant rs2227741 [ dbSNP | Ensembl ].
VAR_012983
Natural varianti268 – 2681R → Q.1 Publication
Corresponds to variant rs2227723 [ dbSNP | Ensembl ].
VAR_012984
Natural varianti400 – 4001T → M.2 Publications
Corresponds to variant rs704 [ dbSNP | Ensembl ].
VAR_012985

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11229.1.
PIRiA29744. SGHU1V.
RefSeqiNP_000629.3. NM_000638.3.
UniGeneiHs.2257.

Genome annotation databases

EnsembliENST00000226218; ENSP00000226218; ENSG00000109072.
GeneIDi7448.
KEGGihsa:7448.
UCSCiuc002hbc.3. human.

Polymorphism databases

DMDMi139653.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11229.1.
PIRi A29744. SGHU1V.
RefSeqi NP_000629.3. NM_000638.3.
UniGenei Hs.2257.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OC0 X-ray 2.28 B 20-70 [» ]
1S4G NMR - A 20-70 [» ]
1SSU NMR - A 20-70 [» ]
2JQ8 NMR - A 20-66 [» ]
3BT1 X-ray 2.80 B 21-60 [» ]
3BT2 X-ray 2.50 B 21-60 [» ]
4K24 X-ray 4.50 B 21-60 [» ]
ProteinModelPortali P04004.
SMRi P04004. Positions 21-60, 155-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113287. 74 interactions.
DIPi DIP-36566N.
IntActi P04004. 22 interactions.
MINTi MINT-4999753.
STRINGi 9606.ENSP00000226218.

Chemistry

ChEMBLi CHEMBL1075314.
DrugBanki DB00054. Abciximab.

PTM databases

PhosphoSitei P04004.
UniCarbKBi P04004.

Polymorphism databases

DMDMi 139653.

2D gel databases

DOSAC-COBS-2DPAGE P04004.
SWISS-2DPAGE P04004.

Proteomic databases

MaxQBi P04004.
PeptideAtlasi P04004.
PRIDEi P04004.

Protocols and materials databases

DNASUi 7448.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000226218 ; ENSP00000226218 ; ENSG00000109072 .
GeneIDi 7448.
KEGGi hsa:7448.
UCSCi uc002hbc.3. human.

Organism-specific databases

CTDi 7448.
GeneCardsi GC17M027137.
HGNCi HGNC:12724. VTN.
MIMi 193190. gene.
neXtProti NX_P04004.
PharmGKBi PA37335.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00530000063751.
HOGENOMi HOG000133161.
HOVERGENi HBG002902.
InParanoidi P04004.
KOi K06251.
OMAi LLQRDSW.
PhylomeDBi P04004.
TreeFami TF332780.

Enzyme and pathway databases

Reactomei REACT_118707. Regulation of Complement cascade.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.

Miscellaneous databases

EvolutionaryTracei P04004.
GeneWikii Vitronectin.
GenomeRNAii 7448.
NextBioi 29166.
PMAP-CutDB P04004.
PROi P04004.
SOURCEi Search...

Gene expression databases

Bgeei P04004.
CleanExi HS_VTN.
ExpressionAtlasi P04004. baseline and differential.
Genevestigatori P04004.

Family and domain databases

Gene3Di 2.110.10.10. 3 hits.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view ]
Pfami PF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view ]
PRINTSi PR00022. SOMATOMEDINB.
SMARTi SM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view ]
SUPFAMi SSF50923. SSF50923. 3 hits.
PROSITEi PS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. Cited for: GLYCOSYLATION AT ASN-86 AND ASN-242.
  26. 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.

Entry informationi

Entry nameiVTNC_HUMAN
AccessioniPrimary (citable) accession number: P04004
Secondary accession number(s): B2R7G0, P01141, Q9BSH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: October 29, 2014
This is version 187 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3