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P06729

- CD2_HUMAN

UniProt

P06729 - CD2_HUMAN

Protein

T-cell surface antigen CD2

Gene

CD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 2 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor activity Source: UniProtKB
    3. receptor binding Source: UniProt

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. blood coagulation Source: Reactome
    3. cell surface receptor signaling pathway Source: UniProtKB
    4. heterotypic cell-cell adhesion Source: UniProt
    5. leukocyte migration Source: Reactome
    6. membrane raft polarization Source: UniProtKB
    7. natural killer cell activation Source: UniProtKB
    8. positive regulation of interferon-gamma secretion Source: UniProt
    9. positive regulation of interleukin-8 secretion Source: UniProt
    10. positive regulation of myeloid dendritic cell activation Source: UniProtKB
    11. positive regulation of tumor necrosis factor production Source: UniProt
    12. regulation of T cell differentiation Source: UniProtKB
    13. single organismal cell-cell adhesion Source: UniProtKB
    14. T cell activation Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    SignaLinkiP06729.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T-cell surface antigen CD2
    Alternative name(s):
    Erythrocyte receptor
    LFA-2
    LFA-3 receptor
    Rosette receptor
    T-cell surface antigen T11/Leu-5
    CD_antigen: CD2
    Gene namesi
    Name:CD2
    Synonyms:SRBC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1639. CD2.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of plasma membrane Source: Ensembl
    2. cell surface Source: UniProt
    3. cytoplasmic side of plasma membrane Source: Ensembl
    4. external side of plasma membrane Source: MGI
    5. extracellular region Source: Ensembl
    6. integral component of plasma membrane Source: UniProtKB
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671K → R: Loss of LFA-3 binding. 1 Publication
    Mutagenesisi70 – 701Q → K: Loss of LFA-3 binding. 1 Publication
    Mutagenesisi110 – 1101Y → D: Loss of LFA-3 and CD59 binding. 1 Publication
    Mutagenesisi111 – 1111D → H: Loss of LFA-3 and CD59 binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA26198.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 351327T-cell surface antigen CD2PRO_0000014600Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi89 – 891N-linked (GlcNAc...)
    Disulfide bondi139 ↔ 2031 Publication
    Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi146 ↔ 1861 Publication
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP06729.
    PaxDbiP06729.
    PRIDEiP06729.

    PTM databases

    PhosphoSiteiP06729.
    UniCarbKBiP06729.

    Expressioni

    Gene expression databases

    ArrayExpressiP06729.
    BgeeiP06729.
    CleanExiHS_CD2.
    GenevestigatoriP06729.

    Organism-specific databases

    HPAiCAB002430.
    HPA003883.

    Interactioni

    Subunit structurei

    Interacts with CD2AP By similarity. Interacts with PSTPIP1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CD2APQ9Y5K64EBI-3912464,EBI-298152
    CD2BP2O954003EBI-3912464,EBI-768015
    SH3KBP1Q96B973EBI-3912464,EBI-346595

    Protein-protein interaction databases

    BioGridi107352. 16 interactions.
    IntActiP06729. 7 interactions.
    MINTiMINT-99488.
    STRINGi9606.ENSP00000358490.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 366
    Beta strandi41 – 433
    Beta strandi52 – 6110
    Helixi62 – 643
    Beta strandi67 – 715
    Helixi73 – 753
    Beta strandi77 – 804
    Beta strandi84 – 863
    Turni88 – 903
    Beta strandi92 – 943
    Helixi99 – 1013
    Beta strandi103 – 1119
    Beta strandi116 – 12712
    Beta strandi134 – 1385
    Turni139 – 1424
    Beta strandi143 – 1475
    Beta strandi155 – 1628
    Beta strandi164 – 1707
    Beta strandi172 – 1754
    Beta strandi180 – 18910
    Beta strandi194 – 20310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CDBNMR-A25-129[»]
    1GYANMR-A25-129[»]
    1HNFX-ray2.50A25-206[»]
    1L2ZNMR-B294-304[»]
    1QA9X-ray3.20A/C28-129[»]
    2J6OX-ray2.22C324-333[»]
    2J7IX-ray2.90C/D324-333[»]
    ProteinModelPortaliP06729.
    SMRiP06729. Positions 28-206.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06729.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 209185ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini236 – 351116CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei210 – 23526HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 128104Ig-like V-typeAdd
    BLAST
    Domaini129 – 20981Ig-like C2-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni61 – 7515LFA-3 (CD58) binding region 1Add
    BLAST
    Regioni106 – 12015LFA-3 (CD58) binding region 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi282 – 33857Pro-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47564.
    HOGENOMiHOG000276890.
    HOVERGENiHBG000262.
    InParanoidiP06729.
    KOiK06449.
    OMAiGTQVHQQ.
    OrthoDBiEOG7KSX9X.
    PhylomeDBiP06729.
    TreeFamiTF335971.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR015632. CD2.
    IPR013783. Ig-like_fold.
    IPR008424. Ig_C2-set.
    IPR013106. Ig_V-set.
    IPR015631. SLAM_fam_rcpts.
    [Graphical view]
    PANTHERiPTHR12080. PTHR12080. 1 hit.
    PTHR12080:SF10. PTHR12080:SF10. 1 hit.
    PfamiPF05790. C2-set. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    PRINTSiPR01870. CD2ANTIGEN.

    Sequencei

    Sequence statusi: Complete.

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

    P06729-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM    50
    SDDIDDIKWE KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD 100
    DQDIYKVSIY DTKGKNVLEK IFDLKIQERV SKPKISWTCI NTTLTCEVMN 150
    GTDPELNLYQ DGKHLKLSQR VITHKWTTSL SAKFKCTAGN KVSKESSVEP 200
    VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ RSRRNDEELE 250
    TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP 300
    GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS 350
    N 351
    Length:351
    Mass (Da):39,448
    Last modified:October 23, 2007 - v2
    Checksum:iA03D853C3B618917
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2871G → A(PubMed:3490670)Curated
    Sequence conflicti339 – 35113HGAAE…SPSSN → MGQQKTHCPLPLIKKDRNCL FQ in AAA51946. (PubMed:3490670)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti217 – 2171C → Y in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035504
    Natural varianti266 – 2661H → Q.3 Publications
    Corresponds to variant rs699738 [ dbSNP | Ensembl ].
    VAR_017104
    Natural varianti339 – 3391H → N.
    Corresponds to variant rs35880225 [ dbSNP | Ensembl ].
    VAR_033608

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19806
    , M19798, M19800, M19802, M19804 Genomic DNA. Translation: AAA53095.1.
    M16445 mRNA. Translation: AAA51738.1.
    M14362 mRNA. Translation: AAA35571.1.
    M16336 mRNA. Translation: AAA51946.1.
    X07871
    , X07872, X07873, X07874 Genomic DNA. Translation: CAA30721.1.
    AL135798 Genomic DNA. Translation: CAC14840.1.
    BC033583 mRNA. Translation: AAH33583.1.
    CCDSiCCDS889.1.
    PIRiA28967. RWHUC2.
    RefSeqiNP_001758.2. NM_001767.3.
    UniGeneiHs.523500.

    Genome annotation databases

    EnsembliENST00000369478; ENSP00000358490; ENSG00000116824.
    GeneIDi914.
    KEGGihsa:914.
    UCSCiuc001egu.4. human.

    Polymorphism databases

    DMDMi160370002.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    CD2 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19806
    , M19798 , M19800 , M19802 , M19804 Genomic DNA. Translation: AAA53095.1 .
    M16445 mRNA. Translation: AAA51738.1 .
    M14362 mRNA. Translation: AAA35571.1 .
    M16336 mRNA. Translation: AAA51946.1 .
    X07871
    , X07872 , X07873 , X07874 Genomic DNA. Translation: CAA30721.1 .
    AL135798 Genomic DNA. Translation: CAC14840.1 .
    BC033583 mRNA. Translation: AAH33583.1 .
    CCDSi CCDS889.1.
    PIRi A28967. RWHUC2.
    RefSeqi NP_001758.2. NM_001767.3.
    UniGenei Hs.523500.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CDB NMR - A 25-129 [» ]
    1GYA NMR - A 25-129 [» ]
    1HNF X-ray 2.50 A 25-206 [» ]
    1L2Z NMR - B 294-304 [» ]
    1QA9 X-ray 3.20 A/C 28-129 [» ]
    2J6O X-ray 2.22 C 324-333 [» ]
    2J7I X-ray 2.90 C/D 324-333 [» ]
    ProteinModelPortali P06729.
    SMRi P06729. Positions 28-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107352. 16 interactions.
    IntActi P06729. 7 interactions.
    MINTi MINT-99488.
    STRINGi 9606.ENSP00000358490.

    Chemistry

    ChEMBLi CHEMBL2040.
    DrugBanki DB00092. Alefacept.
    GuidetoPHARMACOLOGYi 2600.

    PTM databases

    PhosphoSitei P06729.
    UniCarbKBi P06729.

    Polymorphism databases

    DMDMi 160370002.

    Proteomic databases

    MaxQBi P06729.
    PaxDbi P06729.
    PRIDEi P06729.

    Protocols and materials databases

    DNASUi 914.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369478 ; ENSP00000358490 ; ENSG00000116824 .
    GeneIDi 914.
    KEGGi hsa:914.
    UCSCi uc001egu.4. human.

    Organism-specific databases

    CTDi 914.
    GeneCardsi GC01P117297.
    H-InvDB HIX0000931.
    HGNCi HGNC:1639. CD2.
    HPAi CAB002430.
    HPA003883.
    MIMi 186990. gene.
    neXtProti NX_P06729.
    PharmGKBi PA26198.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47564.
    HOGENOMi HOG000276890.
    HOVERGENi HBG000262.
    InParanoidi P06729.
    KOi K06449.
    OMAi GTQVHQQ.
    OrthoDBi EOG7KSX9X.
    PhylomeDBi P06729.
    TreeFami TF335971.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    SignaLinki P06729.

    Miscellaneous databases

    EvolutionaryTracei P06729.
    GeneWikii CD2.
    GenomeRNAii 914.
    NextBioi 3780.
    PROi P06729.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06729.
    Bgeei P06729.
    CleanExi HS_CD2.
    Genevestigatori P06729.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR015632. CD2.
    IPR013783. Ig-like_fold.
    IPR008424. Ig_C2-set.
    IPR013106. Ig_V-set.
    IPR015631. SLAM_fam_rcpts.
    [Graphical view ]
    PANTHERi PTHR12080. PTHR12080. 1 hit.
    PTHR12080:SF10. PTHR12080:SF10. 1 hit.
    Pfami PF05790. C2-set. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    PRINTSi PR01870. CD2ANTIGEN.
    ProtoNeti Search...

    Publicationsi

    1. "Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes."
      Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L.
      Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure."
      Seed B., Aruffo A.
      Proc. Natl. Acad. Sci. U.S.A. 84:3365-3369(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-266.
    3. "Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen."
      Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.
      Proc. Natl. Acad. Sci. U.S.A. 83:8718-8722(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Erratum
      Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.
      Proc. Natl. Acad. Sci. U.S.A. 84:7256-7256(1987)
      Cited for: SEQUENCE REVISION.
    5. "Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes."
      Sayre P.H., Chang H.-C., Hussey R.E., Brown N.R., Richardson N.E., Spagnoli G., Clayton L.K., Reinherz E.L.
      Proc. Natl. Acad. Sci. U.S.A. 84:2941-2945(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "The structure of the human CD2 gene and its expression in transgenic mice."
      Lang G., Wotton D., Owen M.J., Sewell W.A., Brown M.H., Mason D.Y., Crumpton M.J., Kioussis D.
      EMBO J. 7:1675-1682(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-266.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 GLN-266.
      Tissue: Pancreas and Spleen.
    9. "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)."
      Peterson A., Seed B.
      Nature 329:842-846(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    10. "Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59."
      Hahn W.C., Menu E., Bothwell A.L.M., Sims P.J., Bierer B.E.
      Science 256:1805-1807(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CD59-BINDING DATA.
    11. "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion."
      Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L.
      EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSTPIP1.
    12. "Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5-A resolution."
      Bodian D.L., Jones E.Y., Harlos K., Stuart D.I., Davis S.J.
      Structure 2:755-766(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-206, DISULFIDE BONDS.
    13. "Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2."
      Withka J.M., Wyss D.F., Wagner G., Arulanandam A.R.N., Reinherz E.L., Recny M.A.
      Structure 1:69-81(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 25-129.
    14. "Conformation and function of the N-linked glycan in the adhesion domain of human CD2."
      Wyss D.F., Choi J.S., Li J., Knoppers M.H., Willis K.J., Arulanandam A.R., Smolyar A., Reinherz E.L., Wagner G.
      Science 269:1273-1278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 25-129.
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-217.

    Entry informationi

    Entry nameiCD2_HUMAN
    AccessioniPrimary (citable) accession number: P06729
    Secondary accession number(s): Q96TE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 170 of the entry and version 2 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, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3