(data stored in ACNUC22665 zone)

HOGENOM: HS1_PE3984

ID   HS1_PE3984                           STANDARD;      PRT;   351 AA.
AC   HS1_PE3984; P06729; Q96TE5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=T-cell surface antigen CD2;AltName: Full=Erythrocyte
DE   receptor;AltName: Full=LFA-2;AltName: Full=LFA-3 receptor;AltName:
DE   Full=Rosette receptor;AltName: Full=T-cell surface antigen
DE   T11/Leu-5;AltName: CD_antigen=CD2;Flags: Precursor; (HS1.PE3984).
GN   Name=CD2; Synonyms=SRBC;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS1.PE3984.
CC       Homo sapiens chromosome 1 GRCh37  sequence 1..249240621 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:CD2_HUMAN
CC   -!- FUNCTION: CD2 interacts with lymphocyte function-associated
CC       antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells
CC       and other cell types. CD2 is implicated in the triggering of T-
CC       cells, the cytoplasmic domain is implicated in the signaling
CC       function.
CC   -!- SUBUNIT: Interacts with CD2AP (By similarity). Interacts with
CC       PSTPIP1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=CD2 entry;
CC       URL="http://en.wikipedia.org/wiki/CD2";
CC   -!- GENE_FAMILY: HOG000276890 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000116824;ENST00000369478;ENSP00000358490.
DR   EMBL; AK223393; - ;
DR   EMBL; AK301154; - ;
DR   EMBL; AK313614; - ;
DR   EMBL; AL135798; - ;
DR   EMBL; BC033583; - ;
DR   EMBL; CH471122; - ;
DR   EMBL; M14362; - ;
DR   EMBL; M16336; - ;
DR   EMBL; M16445; - ;
DR   EMBL; M19798; - ;
DR   EMBL; M19800; - ;
DR   EMBL; M19802; - ;
DR   EMBL; M19804; - ;
DR   EMBL; M19806; - ;
DR   EMBL; X07871; - ;
DR   EMBL; X07872; - ;
DR   EMBL; X07873; - ;
DR   EMBL; X07874; - ;
DR   UniProtKB/Swiss-Prot; P06729; Q96TE5; -.
DR   EMBL; M19806; AAA53095.1; -; Genomic_DNA.
DR   EMBL; M19798; AAA53095.1; JOINED; Genomic_DNA.
DR   EMBL; M19800; AAA53095.1; JOINED; Genomic_DNA.
DR   EMBL; M19802; AAA53095.1; JOINED; Genomic_DNA.
DR   EMBL; M19804; AAA53095.1; JOINED; Genomic_DNA.
DR   EMBL; M16445; AAA51738.1; -; mRNA.
DR   EMBL; M14362; AAA35571.1; -; mRNA.
DR   EMBL; M16336; AAA51946.1; -; mRNA.
DR   EMBL; X07871; CAA30721.1; -; Genomic_DNA.
DR   EMBL; X07872; CAA30721.1; JOINED; Genomic_DNA.
DR   EMBL; X07873; CAA30721.1; JOINED; Genomic_DNA.
DR   EMBL; X07874; CAA30721.1; JOINED; Genomic_DNA.
DR   EMBL; AL135798; CAC14840.1; -; Genomic_DNA.
DR   EMBL; BC033583; AAH33583.1; -; mRNA.
DR   IPI; IPI00027484; -.
DR   PIR; A28967; RWHUC2.
DR   RefSeq; NP_001758.2; NM_001767.3.
DR   UniGene; Hs.523500; -.
DR   PDB; 1CDB; NMR; -; A=25-129.
DR   PDB; 1GYA; NMR; -; A=25-129.
DR   PDB; 1HNF; X-ray; 2.50 A; A=25-206.
DR   PDB; 1L2Z; NMR; -; B=294-304.
DR   PDB; 1QA9; X-ray; 3.20 A; A/C=28-129.
DR   PDB; 2J6O; X-ray; 2.22 A; C=324-333.
DR   PDB; 2J7I; X-ray; 2.90 A; C/D=324-333.
DR   PDBsum; 1CDB; -.
DR   PDBsum; 1GYA; -.
DR   PDBsum; 1HNF; -.
DR   PDBsum; 1L2Z; -.
DR   PDBsum; 1QA9; -.
DR   PDBsum; 2J6O; -.
DR   PDBsum; 2J7I; -.
DR   ProteinModelPortal; P06729; -.
DR   SMR; P06729; 28-206.
DR   MINT; MINT-99488; -.
DR   STRING; P06729; -.
DR   GlycoSuiteDB; P06729; -.
DR   PRIDE; P06729; -.
DR   Ensembl; ENST00000369478; ENSP00000358490; ENSG00000116824.
DR   GeneID; 914; -.
DR   KEGG; hsa:914; -.
DR   UCSC; uc001egu.2; human.
DR   CTD; 914; -.
DR   GeneCards; GC01P115156; -.
DR   H-InvDB; HIX0000931; -.
DR   HGNC; HGNC:1639; CD2.
DR   HPA; CAB002430; -.
DR   HPA; HPA003883; -.
DR   MIM; 186990; gene.
DR   neXtProt; NX_P06729; -.
DR   PharmGKB; PA26198; -.
DR   eggNOG; prNOG09760; -.
DR   InParanoid; P06729; -.
DR   OMA; HQQKGPP; -.
DR   OrthoDB; EOG4H9XMK; -.
DR   PhylomeDB; P06729; -.
DR   Reactome; REACT_604; Hemostasis.
DR   DrugBank; DB00092; Alefacept.
DR   NextBio; 3780; -.
DR   ArrayExpress; P06729; -.
DR   Bgee; P06729; -.
DR   CleanEx; HS_CD2; -.
DR   Genevestigator; P06729; -.
DR   GermOnline; ENSG00000116824; Homo sapiens.
DR   GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; NAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; TAS:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; NAS:UniProtKB.
DR   GO; GO:0006917; P:induction of apoptosis; TAS:UniProtKB.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0001766; P:membrane raft polarization; TAS:UniProtKB.
DR   GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB.
DR   GO; GO:0030887; P:positive regulation of myeloid dendritic cell activation; NAS:UniProtKB.
DR   GO; GO:0045580; P:regulation of T cell differentiation; NAS:UniProtKB.
DR   GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008424; Ig_C2-set.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR015631; Signal_lymphocyte_activ_molc.
DR   InterPro; IPR015632; T-cell_sdhesion_molc_CD2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   PANTHER; PTHR12080:SF10; CD2_pre; 1.
DR   PANTHER; PTHR12080; SLAM_related; 1.
DR   Pfam; PF05790; C2-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR01870; CD2ANTIGEN.
DR   PROSITE; PS50835; IG_LIKE; FALSE_NEG.
DR   HOGENOMDNA; HS1.PE3984; -.
KW   ENSG000001168241755old_1320000031; ENSP000003584907901old_1320000031;
KW   B4DVN2_HUMAN; Q53F96_HUMAN; AK223393; AK301154; AK313614; AL135798;
KW   CH471122; M14362; M16336; M16445; M19798; M19800; M19802; M19804; M19806;
KW   X07872; X07873; X07874;
KW   3D-structure; Cell adhesion; Complete proteome; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   351 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM SDDIDDIKWE
     KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD DQDIYKVSIY DTKGKNVLEK
     IFDLKIQERV SKPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHLKLSQR VITHKWTTSL
     SAKFKCTAGN KVSKESSVEP VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ
     RSRRNDEELE TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP
     GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS N
//

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