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P04004

- VTNC_HUMAN

UniProt

P04004 - VTNC_HUMAN

Protein

Vitronectin

Gene

VTN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 186 (01 Oct 2014)
      Sequence version 1 (23 Oct 1986)
      Previous versions | rss
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    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: BHF-UCL
    4. polysaccharide binding Source: InterPro
    5. protein binding Source: IntAct
    6. 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: BHF-UCL
    4. extracellular matrix organization Source: Reactome
    5. immune response Source: ProtInc
    6. innate immune response Source: Reactome
    7. negative regulation of blood coagulation Source: BHF-UCL
    8. negative regulation of endopeptidase activity Source: BHF-UCL
    9. positive regulation of cell-substrate adhesion Source: Ensembl
    10. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    11. positive regulation of protein binding Source: BHF-UCL
    12. positive regulation of receptor-mediated endocytosis Source: BHF-UCL
    13. positive regulation of smooth muscle cell migration Source: BHF-UCL
    14. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    15. positive regulation of wound healing Source: BHF-UCL
    16. regulation of complement activation Source: Reactome
    17. smooth muscle cell-matrix adhesion Source: BHF-UCL

    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: UniProt
    7. proteinaceous extracellular matrix Source: Ensembl

    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 – 751Sulfotyrosine2 Publications
    Modified residuei76 – 761Phosphothreonine; by CK2; in vitro1 Publication
    Modified residuei78 – 781Sulfotyrosine2 Publications
    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

    ArrayExpressiP04004.
    BgeeiP04004.
    CleanExiHS_VTN.
    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

    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

    MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC    50
    CTDYTAECKP QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS 100
    DLQAQSKGNP EQTPVLKPEE EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP 150
    AEEELCSGKP FDAFTDLKNG SLFAFRGQYC YELDEKAVRP GYPKLIRDVW 200
    GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP RNISDGFDGI 250
    PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA 300
    VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM 350
    AGRIYISGMA PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT 400
    WLSLFSSEES NLGANNYDDY RMDWLVPATC EPIQSVFFFS GDKYYRVNLR 450
    TRRVDTVDPP YPRSIAQYWL GCPAPGHL 478
    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 DB00013. Urokinase.

    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 GC17M026991.
    HGNCi HGNC:12724. VTN.
    MIMi 193190. gene.
    neXtProti NX_P04004.
    PharmGKBi PA37335.
    GenAtlasi Search...

    Phylogenomic databases

    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

    ArrayExpressi P04004.
    Bgeei P04004.
    CleanExi HS_VTN.
    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

    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 1, 2014
    This is version 186 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