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P13501

- CCL5_HUMAN

UniProt

P13501 - CCL5_HUMAN

Protein

C-C motif chemokine 5

Gene

CCL5

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

    Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei25 – 262Cleavage; by DPP4
    Sitei90 – 901Susceptible to oxidation

    GO - Molecular functioni

    1. CCR1 chemokine receptor binding Source: UniProtKB
    2. CCR4 chemokine receptor binding Source: BHF-UCL
    3. CCR5 chemokine receptor binding Source: BHF-UCL
    4. chemoattractant activity Source: UniProtKB
    5. chemokine activity Source: UniProtKB
    6. chemokine receptor antagonist activity Source: BHF-UCL
    7. chemokine receptor binding Source: BHF-UCL
    8. phosphatidylinositol phospholipase C activity Source: UniProtKB
    9. phospholipase activator activity Source: UniProtKB
    10. protein binding Source: UniProtKB
    11. protein homodimerization activity Source: BHF-UCL
    12. protein kinase activity Source: UniProtKB
    13. protein self-association Source: BHF-UCL
    14. receptor signaling protein tyrosine kinase activator activity Source: BHF-UCL

    GO - Biological processi

    1. activation of phospholipase D activity Source: BHF-UCL
    2. calcium ion transport Source: UniProtKB
    3. cell-cell signaling Source: BHF-UCL
    4. cellular calcium ion homeostasis Source: UniProtKB
    5. cellular protein complex assembly Source: BHF-UCL
    6. cellular response to fibroblast growth factor stimulus Source: UniProtKB
    7. cellular response to interferon-gamma Source: UniProtKB
    8. cellular response to interleukin-1 Source: UniProtKB
    9. cellular response to organic cyclic compound Source: UniProtKB
    10. cellular response to tumor necrosis factor Source: UniProtKB
    11. chemokine-mediated signaling pathway Source: BHF-UCL
    12. chemotaxis Source: UniProtKB
    13. dendritic cell chemotaxis Source: BHF-UCL
    14. eosinophil chemotaxis Source: BHF-UCL
    15. exocytosis Source: UniProtKB
    16. inflammatory response Source: UniProtKB
    17. leukocyte cell-cell adhesion Source: BHF-UCL
    18. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    19. macrophage chemotaxis Source: BHF-UCL
    20. MAPK cascade Source: UniProtKB
    21. monocyte chemotaxis Source: UniProtKB
    22. negative regulation by host of viral transcription Source: UniProtKB
    23. negative regulation of chemokine-mediated signaling pathway Source: GOC
    24. negative regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    25. negative regulation of macrophage apoptotic process Source: Ensembl
    26. negative regulation of T cell apoptotic process Source: BHF-UCL
    27. negative regulation of viral genome replication Source: BHF-UCL
    28. neutrophil activation Source: BHF-UCL
    29. positive chemotaxis Source: GOC
    30. positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
    31. positive regulation of calcium ion transport Source: UniProtKB
    32. positive regulation of cell adhesion Source: BHF-UCL
    33. positive regulation of cell-cell adhesion mediated by integrin Source: BHF-UCL
    34. positive regulation of cell migration Source: UniProtKB
    35. positive regulation of cellular biosynthetic process Source: BHF-UCL
    36. positive regulation of epithelial cell proliferation Source: Ensembl
    37. positive regulation of homotypic cell-cell adhesion Source: BHF-UCL
    38. positive regulation of innate immune response Source: BHF-UCL
    39. positive regulation of JAK-STAT cascade Source: BHF-UCL
    40. positive regulation of macrophage chemotaxis Source: BHF-UCL
    41. positive regulation of monocyte chemotaxis Source: BHF-UCL
    42. positive regulation of natural killer cell chemotaxis Source: UniProtKB
    43. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    44. positive regulation of phosphorylation Source: BHF-UCL
    45. positive regulation of protein tyrosine kinase activity Source: GOC
    46. positive regulation of smooth muscle cell migration Source: BHF-UCL
    47. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
    48. positive regulation of T cell apoptotic process Source: BHF-UCL
    49. positive regulation of T cell chemotaxis Source: BHF-UCL
    50. positive regulation of T cell migration Source: MGI
    51. positive regulation of T cell proliferation Source: BHF-UCL
    52. positive regulation of translational initiation Source: BHF-UCL
    53. positive regulation of tyrosine phosphorylation of STAT protein Source: BHF-UCL
    54. positive regulation of viral genome replication Source: BHF-UCL
    55. protein kinase B signaling Source: UniProtKB
    56. protein phosphorylation Source: GOC
    57. protein tetramerization Source: BHF-UCL
    58. regulation of chronic inflammatory response Source: BHF-UCL
    59. regulation of T cell activation Source: BHF-UCL
    60. response to toxic substance Source: UniProtKB
    61. response to virus Source: BHF-UCL

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Chemotaxis, Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-C motif chemokine 5
    Alternative name(s):
    EoCP
    Eosinophil chemotactic cytokine
    SIS-delta
    Small-inducible cytokine A5
    T cell-specific protein P228
    Short name:
    TCP228
    T-cell-specific protein RANTES
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CCL5
    Synonyms:D17S136E, SCYA5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:10632. CCL5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProtKB-KW

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35564.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23232 PublicationsAdd
    BLAST
    Chaini24 – 9168C-C motif chemokine 5PRO_0000005175Add
    BLAST
    Chaini26 – 9166RANTES(3-68)PRO_0000005176Add
    BLAST
    Chaini27 – 9165RANTES(4-68)PRO_0000005177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi27 – 271O-linked (GalNAc...); partial1 Publication
    Glycosylationi28 – 281O-linked (GalNAc...); partial1 Publication
    Disulfide bondi33 ↔ 57
    Disulfide bondi34 ↔ 73

    Post-translational modificationi

    N-terminal processed form RANTES(3-68) is produced by proteolytic cleavage, probably by DPP4, after secretion from peripheral blood leukocytes and cultured sarcoma cells.1 Publication
    The identity of the O-linked saccharides at Ser-27 and Ser-28 are not reported in PubMed:1380064. They are assigned by similarity.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP13501.
    PeptideAtlasiP13501.
    PRIDEiP13501.

    PTM databases

    PhosphoSiteiP13501.

    Miscellaneous databases

    PMAP-CutDBP13501.

    Expressioni

    Tissue specificityi

    T-cell and macrophage specific.

    Inductioni

    By mitogens.

    Gene expression databases

    ArrayExpressiP13501.
    BgeeiP13501.
    CleanExiHS_CCL5.
    GenevestigatoriP13501.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCR5P516814EBI-2848366,EBI-489374

    Protein-protein interaction databases

    BioGridi112255. 16 interactions.
    DIPiDIP-31N.
    IntActiP13501. 13 interactions.
    MINTiMINT-103226.
    STRINGi9606.ENSP00000293272.

    Structurei

    Secondary structure

    1
    91
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 333
    Beta strandi35 – 406
    Helixi44 – 463
    Beta strandi47 – 526
    Beta strandi57 – 593
    Beta strandi62 – 665
    Beta strandi71 – 744
    Helixi79 – 8911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B3AX-ray1.60A/B25-91[»]
    1EQTX-ray1.60A/B26-91[»]
    1HRJNMR-A/B24-91[»]
    1RTNNMR-A/B24-91[»]
    1RTONMR-A/B24-91[»]
    1U4LX-ray2.00A/B24-91[»]
    1U4MX-ray2.00A/B24-91[»]
    1U4PX-ray1.70A/B24-91[»]
    1U4RX-ray2.20A/B/C/D24-91[»]
    2L9HOther-A/B/C/D24-91[»]
    2VXWX-ray1.70A/B/C/D33-91[»]
    ProteinModelPortaliP13501.
    SMRiP13501. Positions 25-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13501.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG38896.
    HOVERGENiHBG017871.
    InParanoidiP13501.
    KOiK12499.
    OrthoDBiEOG7CVQ1F.
    PhylomeDBiP13501.
    TreeFamiTF334888.

    Family and domain databases

    InterProiIPR000827. Chemokine_CC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    [Graphical view]
    PfamiPF00048. IL8. 1 hit.
    [Graphical view]
    SMARTiSM00199. SCY. 1 hit.
    [Graphical view]
    SUPFAMiSSF54117. SSF54117. 1 hit.
    PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13501-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVSAAALAV ILIATALCAP ASASPYSSDT TPCCFAYIAR PLPRAHIKEY   50
    FYTSGKCSNP AVVFVTRKNR QVCANPEKKW VREYINSLEM S 91
    Length:91
    Mass (Da):9,990
    Last modified:July 15, 1999 - v3
    Checksum:iFB0BFAF9A87C620F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71A → R in AAA36725. (PubMed:2456327)Curated
    Sequence conflicti7 – 71A → R in AAF73070. 1 PublicationCurated
    Sequence conflicti14 – 141A → V in AAF73070. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 7515±1 Da from positions 27 - 91. Determined by SELDI. 1 Publication
    Molecular mass is 7862.8±1.1 Da from positions 24 - 91. Determined by ESI. 1 Publication
    Molecular mass is 8355±10 Da from positions 24 - 91. Determined by ESI. O-glycosylated.1 Publication

    Polymorphismi

    The variant Phe-24 is an antagonist of the chemokine receptors CCR1 and CCR3.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241S → F.1 Publication
    VAR_043043

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21121 mRNA. Translation: AAA36725.1.
    AF088219 Genomic DNA. Translation: AAC63331.1.
    DQ230537 mRNA. Translation: ABB69929.1.
    AF043341 mRNA. Translation: AAC03541.1.
    AF266753 mRNA. Translation: AAF73070.1.
    DQ017060 Genomic DNA. Translation: AAY22177.1.
    BC008600 mRNA. Translation: AAH08600.1.
    CCDSiCCDS11300.1.
    PIRiA28815.
    RefSeqiNP_002976.2. NM_002985.2.
    UniGeneiHs.514821.

    Genome annotation databases

    EnsembliENST00000603197; ENSP00000474412; ENSG00000271503.
    ENST00000605140; ENSP00000475057; ENSG00000271503.
    GeneIDi6352.
    KEGGihsa:6352.
    UCSCiuc002hkf.3. human.

    Polymorphism databases

    DMDMi6175077.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    RANTES entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21121 mRNA. Translation: AAA36725.1 .
    AF088219 Genomic DNA. Translation: AAC63331.1 .
    DQ230537 mRNA. Translation: ABB69929.1 .
    AF043341 mRNA. Translation: AAC03541.1 .
    AF266753 mRNA. Translation: AAF73070.1 .
    DQ017060 Genomic DNA. Translation: AAY22177.1 .
    BC008600 mRNA. Translation: AAH08600.1 .
    CCDSi CCDS11300.1.
    PIRi A28815.
    RefSeqi NP_002976.2. NM_002985.2.
    UniGenei Hs.514821.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B3A X-ray 1.60 A/B 25-91 [» ]
    1EQT X-ray 1.60 A/B 26-91 [» ]
    1HRJ NMR - A/B 24-91 [» ]
    1RTN NMR - A/B 24-91 [» ]
    1RTO NMR - A/B 24-91 [» ]
    1U4L X-ray 2.00 A/B 24-91 [» ]
    1U4M X-ray 2.00 A/B 24-91 [» ]
    1U4P X-ray 1.70 A/B 24-91 [» ]
    1U4R X-ray 2.20 A/B/C/D 24-91 [» ]
    2L9H Other - A/B/C/D 24-91 [» ]
    2VXW X-ray 1.70 A/B/C/D 33-91 [» ]
    ProteinModelPortali P13501.
    SMRi P13501. Positions 25-91.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112255. 16 interactions.
    DIPi DIP-31N.
    IntActi P13501. 13 interactions.
    MINTi MINT-103226.
    STRINGi 9606.ENSP00000293272.

    Chemistry

    BindingDBi P13501.
    ChEMBLi CHEMBL1275217.

    PTM databases

    PhosphoSitei P13501.

    Polymorphism databases

    DMDMi 6175077.

    Proteomic databases

    PaxDbi P13501.
    PeptideAtlasi P13501.
    PRIDEi P13501.

    Protocols and materials databases

    DNASUi 6352.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000603197 ; ENSP00000474412 ; ENSG00000271503 .
    ENST00000605140 ; ENSP00000475057 ; ENSG00000271503 .
    GeneIDi 6352.
    KEGGi hsa:6352.
    UCSCi uc002hkf.3. human.

    Organism-specific databases

    CTDi 6352.
    GeneCardsi GC17M034198.
    HGNCi HGNC:10632. CCL5.
    MIMi 187011. gene.
    neXtProti NX_P13501.
    PharmGKBi PA35564.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG38896.
    HOVERGENi HBG017871.
    InParanoidi P13501.
    KOi K12499.
    OrthoDBi EOG7CVQ1F.
    PhylomeDBi P13501.
    TreeFami TF334888.

    Enzyme and pathway databases

    Reactomei REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P13501.
    GeneWikii CCL5.
    GenomeRNAii 6352.
    NextBioi 24676.
    PMAP-CutDB P13501.
    PROi P13501.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13501.
    Bgeei P13501.
    CleanExi HS_CCL5.
    Genevestigatori P13501.

    Family and domain databases

    InterProi IPR000827. Chemokine_CC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    [Graphical view ]
    Pfami PF00048. IL8. 1 hit.
    [Graphical view ]
    SMARTi SM00199. SCY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54117. SSF54117. 1 hit.
    PROSITEi PS00472. SMALL_CYTOKINES_CC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human T cell-specific molecule is a member of a new gene family."
      Schall T.J., Jongstra J., Dyer B.J., Jorgensen J., Clayberger C., Davis M.M., Krensky A.M.
      J. Immunol. 141:1018-1025(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Organization of the chemokine gene cluster on human chromosome 17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and RANTES."
      Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.
      J. Interferon Cytokine Res. 19:227-234(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT PHE-24.
      Tissue: Blood.
    4. Jang J.S., Kim B.E.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leukocyte.
    5. "The complete sequence of human beta-chemokine RANTES mRNA."
      Zeng Q.P., Yang R.Y., Fu L.C.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Tissue: Brain.
    8. "Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils."
      Kameyoshi Y., Doerschner A., Mallet A.I., Christophers E., Schroeder J.-M.
      J. Exp. Med. 176:587-592(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-55, FUNCTION, MASS SPECTROMETRY, GLYCOSYLATION AT SER-27 AND SER-28, OXIDATION AT MET-90.
    9. "Platelets secrete an eosinophil-chemotactic cytokine which is a member of the C-C-chemokine family."
      Schroeder J.-M., Kameyoshi Y., Christophers E.
      Adv. Exp. Med. Biol. 351:119-128(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-55.
    10. "Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells."
      Cocchi F., DeVico A.L., Garzino-Demo A., Arya S.K., Gallo R.C., Lusso P.
      Science 270:1811-1815(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-56; 71-79 AND 83-91, FUNCTION.
    11. "Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection."
      Proost P., De Meester I., Schols D., Struyf S., Lambeir A.-M., Wuyts A., Opdenakker G., De Clercq E., Scharpe S., Van Damme J.
      J. Biol. Chem. 273:7222-7227(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RANTES(3-68), PROTEOLYTIC PROCESSING OF N-TERMINUS, FUNCTION.
    12. "Multiple pathways of amino terminal processing produce two truncated variants of RANTES/CCL5."
      Lim J.K., Burns J.M., Lu W., DeVico A.L.
      J. Leukoc. Biol. 78:442-452(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RANTES(4-68), MASS SPECTROMETRY, FUNCTION.
    13. "Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type."
      Skelton N.J., Aspiras F., Ogez J., Schall T.J.
      Biochemistry 34:5329-5342(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    14. Cited for: STRUCTURE BY NMR.
    15. "Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES."
      Wilken J., Hoover D., Thompson D.A., Barlow P.N., McSparron H., Picard L., Wlodawer A., Lubkowski J., Kent S.B.
      Chem. Biol. 6:43-51(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHESIS, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    16. "The crystal structure of Met-RANTES: comparison with native RANTES and AOP-RANTES."
      Hoover D.M., Shaw J., Gryczynski Z., Proudfoot A.E.I., Wells T.N.C., Lubkowski J.
      Protein Pept. Lett. 7:73-82(2000)
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

    Entry informationi

    Entry nameiCCL5_HUMAN
    AccessioniPrimary (citable) accession number: P13501
    Secondary accession number(s): O43646
    , Q0QVW8, Q4ZGJ1, Q9NYA2, Q9UBG2, Q9UC99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 164 of the entry and version 3 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