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Protein

CD9 antigen

Gene

CD9

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

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

  • integrin binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processCell adhesion, Fertilization

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-1300652 Sperm:Oocyte Membrane Binding
R-HSA-5336415 Uptake and function of diphtheria toxin

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000010278.11
HGNCiHGNC:1709 CD9
MIMi143030 gene
neXtProtiNX_P21926

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 12CytoplasmicSequence analysisAdd BLAST11
Transmembranei13 – 33HelicalSequence analysisAdd BLAST21
Topological domaini34 – 55ExtracellularSequence analysisAdd BLAST22
Transmembranei56 – 76HelicalSequence analysisAdd BLAST21
Topological domaini77 – 87CytoplasmicSequence analysisAdd BLAST11
Transmembranei88 – 111HelicalSequence analysisAdd BLAST24
Topological domaini112 – 195ExtracellularSequence analysisAdd BLAST84
Transmembranei196 – 221HelicalSequence analysisAdd BLAST26
Topological domaini222 – 228CytoplasmicSequence analysis7

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9C → A: Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219. 1 Publication1
Mutagenesisi78C → A: Loss of palmitoylation; when associated with A-9; A-79; A-87; A-218 and A-219. 1 Publication1
Mutagenesisi79C → A: Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. 1 Publication1
Mutagenesisi87C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219. 1 Publication1
Mutagenesisi218C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219. 1 Publication1
Mutagenesisi219C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218. 1 Publication1

Organism-specific databases

DisGeNETi928
OpenTargetsiENSG00000010278
PharmGKBiPA26247

Chemistry databases

DrugBankiDB05398 C31G

Polymorphism and mutation databases

BioMutaiCD9
DMDMi231724

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002192052 – 228CD9 antigenAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi9S-palmitoyl cysteine1 Publication1
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi78S-palmitoyl cysteine1 Publication1
Lipidationi79S-palmitoyl cysteine1 Publication1
Lipidationi87S-palmitoyl cysteine1 Publication1
Disulfide bondi152 ↔ 1811 Publication
Disulfide bondi153 ↔ 1671 Publication
Lipidationi218S-palmitoyl cysteine1 Publication1
Lipidationi219S-palmitoyl cysteine1 Publication1

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

EPDiP21926
MaxQBiP21926
PaxDbiP21926
PeptideAtlasiP21926
PRIDEiP21926

PTM databases

iPTMnetiP21926
PhosphoSitePlusiP21926
SwissPalmiP21926

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000010278
CleanExiHS_CD9
ExpressionAtlasiP21926 baseline and differential
GenevisibleiP21926 HS

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. Interacts with PDPN; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN (PubMed:18541721). Interacts (via the second extracellular domain) with integrin ITGAV:ITGB3 (PubMed:27993971).6 Publications

Binary interactionsi

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

GO - Molecular functioni

  • integrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107366, 23 interactors
CORUMiP21926
DIPiDIP-1122N
IntActiP21926, 24 interactors
MINTiP21926
STRINGi9606.ENSP00000009180

Structurei

3D structure databases

ProteinModelPortaliP21926
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tetraspanin (TM4SF) family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3882 Eukaryota
ENOG4111IRY LUCA
GeneTreeiENSGT00880000137858
HOGENOMiHOG000230651
HOVERGENiHBG002324
InParanoidiP21926
KOiK06460
OMAiEVFHNKF
OrthoDBiEOG091G0K9H
PhylomeDBiP21926
TreeFamiTF352895

Family and domain databases

Gene3Di1.10.1450.10, 1 hit
InterProiView protein in InterPro
IPR000301 Tetraspanin
IPR018499 Tetraspanin/Peripherin
IPR018503 Tetraspanin_CS
IPR008952 Tetraspanin_EC2_sf
PfamiView protein in Pfam
PF00335 Tetraspannin, 1 hit
PIRSFiPIRSF002419 Tetraspanin, 1 hit
PRINTSiPR00259 TMFOUR
SUPFAMiSSF48652 SSF48652, 1 hit
PROSITEiView protein in PROSITE
PS00421 TM4_1, 1 hit

Sequencei

Sequence statusi: Complete.

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

P21926-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQETN
60 70 80 90 100
NNNSSFYTGV YILIGAGALM MLVGFLGCCG AVQESQCMLG LFFGFLLVIF
110 120 130 140 150
AIEIAAAIWG YSHKDEVIKE VQEFYKDTYN KLKTKDEPQR ETLKAIHYAL
160 170 180 190 200
NCCGLAGGVE QFISDICPKK DVLETFTVKS CPDAIKEVFD NKFHIIGAVG
210 220
IGIAVVMIFG MIFSMILCCA IRRNREMV
Length:228
Mass (Da):25,416
Last modified:January 23, 2007 - v4
Checksum:iF68333E0C20611D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti215M → T in AAH11988 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001317241.1, NM_001330312.1
NP_001760.1, NM_001769.3
UniGeneiHs.114286
Hs.712104

Genome annotation databases

EnsembliENST00000009180; ENSP00000009180; ENSG00000010278
ENST00000382518; ENSP00000371958; ENSG00000010278
GeneIDi928
KEGGihsa:928
UCSCiuc001qnq.3 human

Similar proteinsi

Entry informationi

Entry nameiCD9_HUMAN
AccessioniPrimary (citable) accession number: P21926
Secondary accession number(s): D3DUQ9, Q5J7W6, Q96ES4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 184 of the entry and version 4 of the sequence. See 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

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