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P06127

- CD5_HUMAN

UniProt

P06127 - CD5_HUMAN

Protein

T-cell surface glycoprotein CD5

Gene

CD5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    May act as a receptor in regulating T-cell proliferation.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor activity Source: UniProtKB
    3. scavenger receptor activity Source: InterPro
    4. transmembrane signaling receptor activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic signaling pathway Source: Ensembl
    2. cell proliferation Source: UniProtKB
    3. cell recognition Source: UniProtKB
    4. T cell costimulation Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T-cell surface glycoprotein CD5
    Alternative name(s):
    Lymphocyte antigen T1/Leu-1
    CD_antigen: CD5
    Gene namesi
    Name:CD5
    Synonyms:LEU1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1685. CD5.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. integral component of plasma membrane Source: UniProtKB
    3. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26224.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 495471T-cell surface glycoprotein CD5PRO_0000033222Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 861 PublicationPROSITE-ProRule annotation
    Disulfide bondi60 ↔ 1251 PublicationPROSITE-ProRule annotation
    Disulfide bondi81 ↔ 1321 PublicationPROSITE-ProRule annotation
    Disulfide bondi107 ↔ 1171 PublicationPROSITE-ProRule annotation
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi201 ↔ 267PROSITE-ProRule annotation
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi244 ↔ 250PROSITE-ProRule annotation
    Disulfide bondi285 ↔ 3211 PublicationPROSITE-ProRule annotation
    Disulfide bondi301 ↔ 3601 PublicationPROSITE-ProRule annotation
    Disulfide bondi316 ↔ 3671 PublicationPROSITE-ProRule annotation
    Disulfide bondi342 ↔ 3501 PublicationPROSITE-ProRule annotation
    Modified residuei439 – 4391Phosphoserine2 Publications
    Modified residuei453 – 4531Phosphotyrosine1 Publication
    Modified residuei460 – 4601Phosphoserine1 Publication
    Modified residuei483 – 4831Phosphoserine1 Publication
    Modified residuei485 – 4851Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues by LYN; this creates binding sites for PTPN6/SHP-1.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP06127.
    PaxDbiP06127.
    PRIDEiP06127.

    PTM databases

    PhosphoSiteiP06127.
    UniCarbKBiP06127.

    Expressioni

    Gene expression databases

    ArrayExpressiP06127.
    BgeeiP06127.
    CleanExiHS_CD5.
    GenevestigatoriP06127.

    Organism-specific databases

    HPAiCAB015392.
    CAB020308.

    Interactioni

    Subunit structurei

    Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107359. 14 interactions.
    DIPiDIP-21N.
    IntActiP06127. 3 interactions.
    MINTiMINT-4656212.
    STRINGi9606.ENSP00000342681.

    Structurei

    Secondary structure

    1
    495
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 373
    Beta strandi39 – 424
    Beta strandi45 – 528
    Beta strandi55 – 584
    Helixi75 – 773
    Helixi78 – 836
    Beta strandi86 – 883
    Beta strandi90 – 945
    Turni101 – 1033
    Beta strandi104 – 1107
    Beta strandi117 – 1193
    Beta strandi122 – 1243
    Beta strandi126 – 1327
    Beta strandi275 – 2806
    Beta strandi286 – 29510
    Beta strandi298 – 3014
    Helixi310 – 3189
    Beta strandi323 – 3319
    Beta strandi339 – 3413
    Beta strandi344 – 3463
    Helixi347 – 3493
    Beta strandi354 – 3563
    Beta strandi362 – 3676

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JA4X-ray2.21A270-369[»]
    2JOPNMR-A25-134[»]
    2JP0NMR-A25-134[»]
    2OTTX-ray2.50X/Y276-368[»]
    ProteinModelPortaliP06127.
    SMRiP06127. Positions 25-134, 269-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06127.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 372348ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini403 – 49593CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei373 – 40230HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 13399SRCR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 268110SRCR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini276 – 36893SRCR 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 SRCR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG86650.
    HOGENOMiHOG000111490.
    HOVERGENiHBG005286.
    InParanoidiP06127.
    KOiK06455.
    OMAiMSFHRNH.
    OrthoDBiEOG7TF792.
    PhylomeDBiP06127.
    TreeFamiTF329295.

    Family and domain databases

    Gene3Di3.10.250.10. 2 hits.
    InterProiIPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR003566. Tcell_CD5.
    [Graphical view]
    PfamiPF00530. SRCR. 2 hits.
    [Graphical view]
    PRINTSiPR00258. SPERACTRCPTR.
    PR01409. TCELLCD5.
    SMARTiSM00202. SR. 2 hits.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 2 hits.
    PROSITEiPS50287. SRCR_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06127-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMGSLQPLA TLYLLGMLVA SCLGRLSWYD PDFQARLTRS NSKCQGQLEV    50
    YLKDGWHMVC SQSWGRSSKQ WEDPSQASKV CQRLNCGVPL SLGPFLVTYT 100
    PQSSIICYGQ LGSFSNCSHS RNDMCHSLGL TCLEPQKTTP PTTRPPPTTT 150
    PEPTAPPRLQ LVAQSGGQHC AGVVEFYSGS LGGTISYEAQ DKTQDLENFL 200
    CNNLQCGSFL KHLPETEAGR AQDPGEPREH QPLPIQWKIQ NSSCTSLEHC 250
    FRKIKPQKSG RVLALLCSGF QPKVQSRLVG GSSICEGTVE VRQGAQWAAL 300
    CDSSSARSSL RWEEVCREQQ CGSVNSYRVL DAGDPTSRGL FCPHQKLSQC 350
    HELWERNSYC KKVFVTCQDP NPAGLAAGTV ASIILALVLL VVLLVVCGPL 400
    AYKKLVKKFR QKKQRQWIGP TGMNQNMSFH RNHTATVRSH AENPTASHVD 450
    NEYSQPPRNS HLSAYPALEG ALHRSSMQPD NSSDSDYDLH GAQRL 495
    Length:495
    Mass (Da):54,578
    Last modified:November 30, 2010 - v2
    Checksum:i9131AEC9683EE1D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti289 – 2891V → E in BAF85387. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241P → L.1 Publication
    Corresponds to variant rs2241002 [ dbSNP | Ensembl ].
    VAR_020411
    Natural varianti461 – 4611H → R.6 Publications
    Corresponds to variant rs637186 [ dbSNP | Ensembl ].
    VAR_024649
    Natural varianti471 – 4711A → V.4 Publications
    Corresponds to variant rs2229177 [ dbSNP | Ensembl ].
    VAR_058203

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04391 mRNA. Translation: CAA27979.1.
    X89405
    , AJ237927, AJ237928, AJ237929, AJ237930, AJ237931, AJ237932 Genomic DNA. Translation: CAA61584.2.
    EF064752 Genomic DNA. Translation: ABK41935.1.
    AK292698 mRNA. Translation: BAF85387.1.
    AP000437 Genomic DNA. No translation available.
    BC027901 mRNA. Translation: AAH27901.1.
    CCDSiCCDS8000.1.
    PIRiA26396.
    RefSeqiNP_055022.2. NM_014207.3.
    UniGeneiHs.58685.

    Genome annotation databases

    EnsembliENST00000347785; ENSP00000342681; ENSG00000110448.
    GeneIDi921.
    KEGGihsa:921.
    UCSCiuc009ynk.3. human.

    Polymorphism databases

    DMDMi313104090.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04391 mRNA. Translation: CAA27979.1 .
    X89405
    , AJ237927 , AJ237928 , AJ237929 , AJ237930 , AJ237931 , AJ237932 Genomic DNA. Translation: CAA61584.2 .
    EF064752 Genomic DNA. Translation: ABK41935.1 .
    AK292698 mRNA. Translation: BAF85387.1 .
    AP000437 Genomic DNA. No translation available.
    BC027901 mRNA. Translation: AAH27901.1 .
    CCDSi CCDS8000.1.
    PIRi A26396.
    RefSeqi NP_055022.2. NM_014207.3.
    UniGenei Hs.58685.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JA4 X-ray 2.21 A 270-369 [» ]
    2JOP NMR - A 25-134 [» ]
    2JP0 NMR - A 25-134 [» ]
    2OTT X-ray 2.50 X/Y 276-368 [» ]
    ProteinModelPortali P06127.
    SMRi P06127. Positions 25-134, 269-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107359. 14 interactions.
    DIPi DIP-21N.
    IntActi P06127. 3 interactions.
    MINTi MINT-4656212.
    STRINGi 9606.ENSP00000342681.

    PTM databases

    PhosphoSitei P06127.
    UniCarbKBi P06127.

    Polymorphism databases

    DMDMi 313104090.

    Proteomic databases

    MaxQBi P06127.
    PaxDbi P06127.
    PRIDEi P06127.

    Protocols and materials databases

    DNASUi 921.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347785 ; ENSP00000342681 ; ENSG00000110448 .
    GeneIDi 921.
    KEGGi hsa:921.
    UCSCi uc009ynk.3. human.

    Organism-specific databases

    CTDi 921.
    GeneCardsi GC11P060869.
    H-InvDB HIX0009680.
    HGNCi HGNC:1685. CD5.
    HPAi CAB015392.
    CAB020308.
    MIMi 153340. gene.
    neXtProti NX_P06127.
    PharmGKBi PA26224.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86650.
    HOGENOMi HOG000111490.
    HOVERGENi HBG005286.
    InParanoidi P06127.
    KOi K06455.
    OMAi MSFHRNH.
    OrthoDBi EOG7TF792.
    PhylomeDBi P06127.
    TreeFami TF329295.

    Miscellaneous databases

    EvolutionaryTracei P06127.
    GeneWikii CD5_(protein).
    GenomeRNAii 921.
    NextBioi 3810.
    PROi P06127.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06127.
    Bgeei P06127.
    CleanExi HS_CD5.
    Genevestigatori P06127.

    Family and domain databases

    Gene3Di 3.10.250.10. 2 hits.
    InterProi IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR003566. Tcell_CD5.
    [Graphical view ]
    Pfami PF00530. SRCR. 2 hits.
    [Graphical view ]
    PRINTSi PR00258. SPERACTRCPTR.
    PR01409. TCELLCD5.
    SMARTi SM00202. SR. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56487. SSF56487. 2 hits.
    PROSITEi PS50287. SRCR_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1."
      Jones N.H., Clabby M.L., Dialynas D.P., Huag H.-J.S., Herzenberg L.A., Strominger J.L.
      Nature 323:346-349(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-461 AND VAL-471.
    2. "Evolutionarily conserved transcription regulatory elements within the 5'-flanking region of the human CD5 gene."
      Calvo J., Sole J., Simarro M., Vives J., Lozano F.
      Tissue Antigens 47:257-261(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-461 AND VAL-471.
      Tissue: Lymphocyte.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-461 AND VAL-471.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-224 AND ARG-461.
      Tissue: Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS ARG-461 AND VAL-471.
      Tissue: Pancreas.
    7. "The B-cell surface protein CD72/Lyb-2 is the ligand for CD5."
      van de Velde H., von Hoegen I., Luo W., Parnes J.R., Thielemans K.
      Nature 351:662-665(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD72/LYB-2.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-460, VARIANT [LARGE SCALE ANALYSIS] ARG-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453; SER-483 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Crystal structure of the third extracellular domain of CD5 reveals the fold of a group B scavenger cysteine-rich receptor domain."
      Rodamilans B., Munoz I.G., Bragado-Nilsson E., Sarrias M.R., Padilla O., Blanco F.J., Lozano F., Montoya G.
      J. Biol. Chem. 282:12669-12677(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 270-369.
    12. "Three-dimensional solution structure and conformational plasticity of the N-terminal scavenger receptor cysteine-rich domain of human CD5."
      Garza-Garcia A., Esposito D., Rieping W., Harris R., Briggs C., Brown M.H., Driscoll P.C.
      J. Mol. Biol. 378:129-144(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 25-134, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCD5_HUMAN
    AccessioniPrimary (citable) accession number: P06127
    Secondary accession number(s): A0N0P4, A8K9I3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 148 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 11
      Human chromosome 11: 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