Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21926

- CD9_HUMAN

UniProt

P21926 - CD9_HUMAN

Protein

CD9 antigen

Gene

CD9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Required for sperm-egg fusion.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. brain development Source: Ensembl
    3. cell adhesion Source: UniProtKB
    4. cellular component movement Source: UniProtKB
    5. fusion of sperm to egg plasma membrane Source: UniProtKB
    6. multicellular organism reproduction Source: Reactome
    7. negative regulation of cell proliferation Source: Ensembl
    8. oligodendrocyte development Source: Ensembl
    9. paranodal junction assembly Source: UniProtKB
    10. platelet activation Source: UniProtKB
    11. platelet degranulation Source: Reactome
    12. response to water deprivation Source: Ensembl
    13. single fertilization Source: Reactome

    Keywords - Biological processi

    Cell adhesion, Fertilization

    Enzyme and pathway databases

    ReactomeiREACT_164006. Sperm:Oocyte Membrane Binding.

    Protein family/group databases

    TCDBi8.A.40.1.9. the tetraspanin (tetraspanin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CD9 antigen
    Alternative name(s):
    5H9 antigen
    Cell growth-inhibiting gene 2 protein
    Leukocyte antigen MIC3
    Motility-related protein
    Short name:
    MRP-1
    Tetraspanin-29
    Short name:
    Tspan-29
    p24
    CD_antigen: CD9
    Gene namesi
    Name:CD9
    Synonyms:MIC3, TSPAN29
    ORF Names:GIG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1709. CD9.

    Subcellular locationi

    Membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. external side of plasma membrane Source: Ensembl
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProtKB
    5. integral component of plasma membrane Source: UniProtKB
    6. plasma membrane Source: Reactome
    7. platelet alpha granule membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91C → A: Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219. 1 Publication
    Mutagenesisi78 – 781C → A: Loss of palmitoylation; when associated with A-9; A-79; A-87; A-218 and A-219. 1 Publication
    Mutagenesisi79 – 791C → A: Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. 1 Publication
    Mutagenesisi87 – 871C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219. 1 Publication
    Mutagenesisi218 – 2181C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219. 1 Publication
    Mutagenesisi219 – 2191C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218. 1 Publication

    Organism-specific databases

    PharmGKBiPA26247.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 228227CD9 antigenPRO_0000219205Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi9 – 91S-palmitoyl cysteine1 Publication
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Lipidationi78 – 781S-palmitoyl cysteine1 Publication
    Lipidationi79 – 791S-palmitoyl cysteine1 Publication
    Lipidationi87 – 871S-palmitoyl cysteine1 Publication
    Lipidationi218 – 2181S-palmitoyl cysteine1 Publication
    Lipidationi219 – 2191S-palmitoyl cysteine1 Publication

    Post-translational modificationi

    Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro). The protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiP21926.
    PaxDbiP21926.
    PRIDEiP21926.

    PTM databases

    PhosphoSiteiP21926.

    Expressioni

    Tissue specificityi

    Detected in platelets (at protein level). Expressed by a variety of hematopoietic and epithelial cells.1 Publication

    Gene expression databases

    ArrayExpressiP21926.
    BgeeiP21926.
    CleanExiHS_CD9.
    GenevestigatoriP21926.

    Organism-specific databases

    HPAiCAB002490.

    Interactioni

    Subunit structurei

    Forms both disulfide-linked homodimers and higher homooligomers as well as heterooligomers with other members of the tetraspanin family. Interacts with CD63. Identified in a complex with CD63 and ITGB3. Associates with CR2/CD21 and with PTGFRN/CD9P1. Interacts directly with IGSF8.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MMEP084736EBI-4280101,EBI-353759

    Protein-protein interaction databases

    BioGridi107366. 23 interactions.
    DIPiDIP-1122N.
    IntActiP21926. 24 interactions.
    MINTiMINT-1527350.
    STRINGi9606.ENSP00000009180.

    Structurei

    3D structure databases

    ProteinModelPortaliP21926.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 5522ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini77 – 8711CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini112 – 19584ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini222 – 2287CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei56 – 7621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei88 – 11124HelicalSequence AnalysisAdd
    BLAST
    Transmembranei196 – 22126HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tetraspanin (TM4SF) family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG242618.
    HOGENOMiHOG000230651.
    HOVERGENiHBG002324.
    InParanoidiP21926.
    KOiK06460.
    OMAiALNCCGI.
    OrthoDBiEOG7FBRJV.
    PhylomeDBiP21926.
    TreeFamiTF352895.

    Family and domain databases

    Gene3Di1.10.1450.10. 1 hit.
    InterProiIPR028977. CD81_LEL.
    IPR000301. Tetraspanin.
    IPR018499. Tetraspanin/Peripherin.
    IPR018503. Tetraspanin_CS.
    IPR008952. Tetraspanin_EC2.
    [Graphical view]
    PfamiPF00335. Tetraspannin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002419. Tetraspanin. 1 hit.
    PRINTSiPR00259. TMFOUR.
    SUPFAMiSSF48652. SSF48652. 1 hit.
    PROSITEiPS00421. TM4_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P21926-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQETN    50
    NNNSSFYTGV YILIGAGALM MLVGFLGCCG AVQESQCMLG LFFGFLLVIF 100
    AIEIAAAIWG YSHKDEVIKE VQEFYKDTYN KLKTKDEPQR ETLKAIHYAL 150
    NCCGLAGGVE QFISDICPKK DVLETFTVKS CPDAIKEVFD NKFHIIGAVG 200
    IGIAVVMIFG MIFSMILCCA IRRNREMV 228
    Length:228
    Mass (Da):25,416
    Last modified:January 23, 2007 - v4
    Checksum:iF68333E0C20611D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151M → T in AAH11988. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38690 mRNA. Translation: AAA80320.1.
    L34068 mRNA. Translation: AAA59982.1.
    X60111 mRNA. Translation: CAA42708.1.
    S60489
    , S60462, S60463, S60464, S60700, S60699, S60465, S60472 Genomic DNA. Translation: AAC60586.1.
    L08118 Genomic DNA. No translation available.
    L08119 Genomic DNA. Translation: AAA51954.1. Sequence problems.
    L08120 Genomic DNA. Translation: AAA51955.1. Sequence problems.
    L08121 Genomic DNA. Translation: AAA51956.1.
    L08122 Genomic DNA. Translation: AAA51957.1.
    L08123 Genomic DNA. Translation: AAA51958.1.
    L08124 Genomic DNA. Translation: AAA51959.1.
    L08125 Genomic DNA. No translation available.
    AB079244 mRNA. Translation: BAE71132.1.
    AY423720 mRNA. Translation: AAS00483.1.
    AY422198 Genomic DNA. Translation: AAQ87878.1.
    CH471116 Genomic DNA. Translation: EAW88812.1.
    CH471116 Genomic DNA. Translation: EAW88813.1.
    BC011988 mRNA. Translation: AAH11988.1.
    CCDSiCCDS8540.1.
    PIRiA46123. A40402.
    RefSeqiNP_001760.1. NM_001769.3.
    UniGeneiHs.114286.
    Hs.712104.

    Genome annotation databases

    EnsembliENST00000009180; ENSP00000009180; ENSG00000010278.
    ENST00000382518; ENSP00000371958; ENSG00000010278.
    GeneIDi928.
    KEGGihsa:928.
    UCSCiuc001qnq.2. human.

    Polymorphism databases

    DMDMi231724.

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38690 mRNA. Translation: AAA80320.1 .
    L34068 mRNA. Translation: AAA59982.1 .
    X60111 mRNA. Translation: CAA42708.1 .
    S60489
    , S60462 , S60463 , S60464 , S60700 , S60699 , S60465 , S60472 Genomic DNA. Translation: AAC60586.1 .
    L08118 Genomic DNA. No translation available.
    L08119 Genomic DNA. Translation: AAA51954.1 . Sequence problems.
    L08120 Genomic DNA. Translation: AAA51955.1 . Sequence problems.
    L08121 Genomic DNA. Translation: AAA51956.1 .
    L08122 Genomic DNA. Translation: AAA51957.1 .
    L08123 Genomic DNA. Translation: AAA51958.1 .
    L08124 Genomic DNA. Translation: AAA51959.1 .
    L08125 Genomic DNA. No translation available.
    AB079244 mRNA. Translation: BAE71132.1 .
    AY423720 mRNA. Translation: AAS00483.1 .
    AY422198 Genomic DNA. Translation: AAQ87878.1 .
    CH471116 Genomic DNA. Translation: EAW88812.1 .
    CH471116 Genomic DNA. Translation: EAW88813.1 .
    BC011988 mRNA. Translation: AAH11988.1 .
    CCDSi CCDS8540.1.
    PIRi A46123. A40402.
    RefSeqi NP_001760.1. NM_001769.3.
    UniGenei Hs.114286.
    Hs.712104.

    3D structure databases

    ProteinModelPortali P21926.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107366. 23 interactions.
    DIPi DIP-1122N.
    IntActi P21926. 24 interactions.
    MINTi MINT-1527350.
    STRINGi 9606.ENSP00000009180.

    Protein family/group databases

    TCDBi 8.A.40.1.9. the tetraspanin (tetraspanin) family.

    PTM databases

    PhosphoSitei P21926.

    Polymorphism databases

    DMDMi 231724.

    Proteomic databases

    MaxQBi P21926.
    PaxDbi P21926.
    PRIDEi P21926.

    Protocols and materials databases

    DNASUi 928.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000009180 ; ENSP00000009180 ; ENSG00000010278 .
    ENST00000382518 ; ENSP00000371958 ; ENSG00000010278 .
    GeneIDi 928.
    KEGGi hsa:928.
    UCSCi uc001qnq.2. human.

    Organism-specific databases

    CTDi 928.
    GeneCardsi GC12P006308.
    HGNCi HGNC:1709. CD9.
    HPAi CAB002490.
    MIMi 143030. gene.
    neXtProti NX_P21926.
    PharmGKBi PA26247.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242618.
    HOGENOMi HOG000230651.
    HOVERGENi HBG002324.
    InParanoidi P21926.
    KOi K06460.
    OMAi ALNCCGI.
    OrthoDBi EOG7FBRJV.
    PhylomeDBi P21926.
    TreeFami TF352895.

    Enzyme and pathway databases

    Reactomei REACT_164006. Sperm:Oocyte Membrane Binding.

    Miscellaneous databases

    ChiTaRSi CD9. human.
    GeneWikii CD9.
    GenomeRNAii 928.
    NextBioi 3846.
    PROi P21926.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21926.
    Bgeei P21926.
    CleanExi HS_CD9.
    Genevestigatori P21926.

    Family and domain databases

    Gene3Di 1.10.1450.10. 1 hit.
    InterProi IPR028977. CD81_LEL.
    IPR000301. Tetraspanin.
    IPR018499. Tetraspanin/Peripherin.
    IPR018503. Tetraspanin_CS.
    IPR008952. Tetraspanin_EC2.
    [Graphical view ]
    Pfami PF00335. Tetraspannin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002419. Tetraspanin. 1 hit.
    PRINTSi PR00259. TMFOUR.
    SUPFAMi SSF48652. SSF48652. 1 hit.
    PROSITEi PS00421. TM4_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the CD9 antigen. A new family of cell surface proteins."
      Boucheix C., Benoit P., Frachet P., Billard M., Worthington R.E., Gagnon J., Uzan G.
      J. Biol. Chem. 266:117-122(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-5.
    2. "cDNA cloning and expression of platelet p24/CD9. Evidence for a new family of multiple membrane-spanning proteins."
      Lanza F., Wolf D., Fox C.F., Kieffer N., Seyer J.M., Fried V.A., Coughlin S.R., Phillips D.R., Jennings L.K.
      J. Biol. Chem. 266:10638-10645(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    3. "Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility."
      Miyake M., Koyama M., Seno M., Ikeyama S.
      J. Exp. Med. 174:1347-1354(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leukocyte.
    5. "The tetraspanin CD9 is preferentially expressed on the human CD4(+)CD45RA+ naive T cell population and is involved in T cell activation."
      Kobayashi H., Hosono O., Iwata S., Kawasaki H., Kuwana M., Tanaka H., Dang N.H., Morimoto C.
      Clin. Exp. Immunol. 137:101-108(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Identification of a human growth inhibition gene 2 (GIG2)."
      Kim J.W.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. SeattleSNPs variation discovery resource
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Ovary.
    10. "Purification and partial characterization of CD9 antigen of human platelets."
      Higashihara M., Takahata K., Yatomi Y., Nakahara K., Kurokawa K.
      FEBS Lett. 264:270-274(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Tissue: Platelet.
    11. "Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA."
      Ikeyama S., Koyama M., Yamaoko M., Sasada R., Miyake M.
      J. Exp. Med. 177:1231-1237(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN CELL MOTILITY AND METASTASIS.
    12. "CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin."
      Masellis-Smith A., Shaw A.R.
      J. Immunol. 152:2768-2777(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN CELL ADHESION.
    13. "Structural requirements for the inhibitory action of the CD9 large extracellular domain in sperm/oocyte binding and fusion."
      Higginbottom A., Takahashi Y., Bolling L., Coonrod S.A., White J.M., Partridge L.J., Monk P.N.
      Biochem. Biophys. Res. Commun. 311:208-214(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN SPERM-EGG FUSION.
    14. "Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking."
      Kovalenko O.V., Yang X., Kolesnikova T.V., Hemler M.E.
      Biochem. J. 377:407-417(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    15. "Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation."
      Charrin S., Manie S., Oualid M., Billard M., Boucheix C., Rubinstein E.
      FEBS Lett. 516:139-144(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219, MUTAGENESIS OF CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219.
    16. "The major CD9 and CD81 molecular partner. Identification and characterization of the complexes."
      Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M., Boucheix C., Rubinstein E.
      J. Biol. Chem. 276:14329-14337(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTGFRN.
    17. "EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily."
      Stipp C.S., Kolesnikova T.V., Hemler M.E.
      J. Biol. Chem. 276:40545-40554(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGSF8.
    18. "Palmitoylation supports the association of tetraspanin CD63 with CD9 and integrin alphaIIbbeta3 in activated platelets."
      Israels S.J., McMillan-Ward E.M.
      Thromb. Res. 125:152-158(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMYTOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CD63, IDENTIFICATION IN A COMPLEX WITH ITGB3 AND CD63.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCD9_HUMAN
    AccessioniPrimary (citable) accession number: P21926
    Secondary accession number(s): D3DUQ9, Q5J7W6, Q96ES4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 4 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3