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P08575

- PTPRC_HUMAN

UniProt

P08575 - PTPRC_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase C

Gene

PTPRC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (19 Jul 2003)
      Previous versions | rss
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    Functioni

    Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity By similarity.By similarity

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei819 – 8191SubstrateBy similarity
    Active sitei851 – 8511Phosphocysteine intermediate
    Binding sitei895 – 8951SubstrateBy similarity
    Active sitei1167 – 11671Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB
    4. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. B cell proliferation Source: UniProtKB
    3. B cell receptor signaling pathway Source: UniProtKB
    4. bone marrow development Source: UniProtKB
    5. cell cycle phase transition Source: UniProtKB
    6. cell surface receptor signaling pathway Source: ProtInc
    7. defense response to virus Source: UniProtKB
    8. dephosphorylation Source: UniProtKB
    9. hematopoietic progenitor cell differentiation Source: UniProtKB
    10. immunoglobulin biosynthetic process Source: UniProtKB
    11. negative regulation of cell adhesion involved in substrate-bound cell migration Source: UniProtKB
    12. negative regulation of cytokine-mediated signaling pathway Source: UniProtKB
    13. negative regulation of protein kinase activity Source: UniProtKB
    14. negative regulation of T cell mediated cytotoxicity Source: UniProtKB
    15. peptidyl-tyrosine dephosphorylation Source: GOC
    16. positive regulation of antigen receptor-mediated signaling pathway Source: UniProtKB
    17. positive regulation of B cell proliferation Source: UniProtKB
    18. positive regulation of hematopoietic stem cell migration Source: UniProtKB
    19. positive regulation of protein kinase activity Source: UniProtKB
    20. positive regulation of stem cell proliferation Source: UniProtKB
    21. positive regulation of T cell proliferation Source: UniProtKB
    22. protein dephosphorylation Source: UniProtKB
    23. regulation of cell cycle Source: UniProtKB
    24. release of sequestered calcium ion into cytosol Source: UniProtKB
    25. stem cell development Source: UniProtKB
    26. T cell differentiation Source: UniProtKB
    27. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_19200. Other semaphorin interactions.
    SignaLinkiP08575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase C (EC:3.1.3.48)
    Alternative name(s):
    Leukocyte common antigen
    Short name:
    L-CA
    T200
    CD_antigen: CD45
    Gene namesi
    Name:PTPRC
    Synonyms:CD45
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9666. PTPRC.

    Subcellular locationi

    Membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Membrane raft 1 Publication
    Note: Colocalized with DPP4 in membrane rafts.

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. extracellular vesicular exosome Source: UniProt
    3. focal adhesion Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. membrane Source: UniProtKB
    6. membrane raft Source: UniProtKB-SubCell
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti362 – 3632Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication
    VAR_021205
    Multiple sclerosis (MS) [MIM:126200]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease.1 Publication
    Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi851 – 8511C → S: Loss of activity. Abolishes interaction with SKAP1. 2 Publications

    Keywords - Diseasei

    Disease mutation, SCID

    Organism-specific databases

    MIMi126200. phenotype.
    608971. phenotype.
    Orphaneti169157. T-B+ severe combined immunodeficiency due to CD45 deficiency.
    PharmGKBiPA34011.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 13041281Receptor-type tyrosine-protein phosphatase CPRO_0000025470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)2 Publications
    Glycosylationi240 – 2401N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi276 – 2761N-linked (GlcNAc...)1 Publication
    Glycosylationi284 – 2841N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi335 – 3351N-linked (GlcNAc...)2 Publications
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi419 – 4191N-linked (GlcNAc...)1 Publication
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi488 – 4881N-linked (GlcNAc...)1 Publication
    Glycosylationi497 – 4971N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence Analysis
    Modified residuei973 – 9731Phosphoserine2 Publications
    Modified residuei1297 – 12971Phosphoserine1 Publication

    Post-translational modificationi

    Heavily N- and O-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP08575.
    PaxDbiP08575.
    PRIDEiP08575.

    PTM databases

    PhosphoSiteiP08575.
    UniCarbKBiP08575.

    Expressioni

    Gene expression databases

    ArrayExpressiP08575.
    BgeeiP08575.
    CleanExiHS_PTPRC.
    GenevestigatoriP08575.

    Organism-specific databases

    HPAiCAB000052.
    CAB002800.
    CAB056154.
    HPA000440.

    Interactioni

    Subunit structurei

    Binds GANAB and PRKCSH By similarity. Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSKP412403EBI-1341,EBI-1380630
    CTNNB1P352222EBI-1341,EBI-491549
    ERBB2P046262EBI-1341,EBI-641062
    ITGALP207012EBI-1341,EBI-961214
    LCKP062397EBI-1341,EBI-1348
    LckP062402EBI-1341,EBI-1401From a different organism.
    LGALS1P093822EBI-1341,EBI-1048875
    TEKQ027633EBI-1341,EBI-2257090

    Protein-protein interaction databases

    BioGridi111752. 24 interactions.
    DIPiDIP-224N.
    IntActiP08575. 39 interactions.
    MINTiMINT-1130341.
    STRINGi9606.ENSP00000356346.

    Structurei

    Secondary structure

    1
    1304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni633 – 6353
    Helixi636 – 65621
    Beta strandi663 – 6653
    Turni668 – 6703
    Helixi673 – 6786
    Turni688 – 6903
    Beta strandi691 – 6933
    Beta strandi698 – 7003
    Turni701 – 7044
    Beta strandi705 – 7117
    Beta strandi714 – 7163
    Beta strandi720 – 7234
    Turni728 – 7303
    Helixi731 – 74010
    Beta strandi745 – 7484
    Beta strandi752 – 7543
    Beta strandi757 – 7593
    Turni767 – 7693
    Beta strandi771 – 7744
    Beta strandi777 – 78610
    Beta strandi788 – 80215
    Beta strandi807 – 8148
    Helixi826 – 83611
    Beta strandi847 – 8504
    Beta strandi852 – 8554
    Helixi856 – 86914
    Helixi871 – 8744
    Beta strandi875 – 8773
    Helixi879 – 8879
    Helixi897 – 91317
    Helixi920 – 9223
    Helixi923 – 9308
    Helixi941 – 9488
    Helixi960 – 9623
    Helixi966 – 9683
    Turni979 – 9813
    Beta strandi1018 – 10225
    Beta strandi1029 – 10346
    Turni1038 – 10403
    Helixi1041 – 105010
    Beta strandi1055 – 10584
    Beta strandi1062 – 10643
    Beta strandi1067 – 10704
    Beta strandi1088 – 10936
    Beta strandi1095 – 110511
    Beta strandi1113 – 11208
    Beta strandi1125 – 11273
    Helixi1132 – 114312
    Beta strandi1163 – 11719
    Helixi1174 – 118916
    Beta strandi1190 – 11923
    Helixi1195 – 120511
    Turni1207 – 12104
    Helixi1213 – 122513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YGRX-ray2.90A/B622-1231[»]
    1YGUX-ray2.90A/B622-1231[»]
    ProteinModelPortaliP08575.
    SMRiP08575. Positions 391-469, 498-562, 623-1228.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08575.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 575552ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini598 – 1304707CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei576 – 59722HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini389 – 48193Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini482 – 57493Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini651 – 910260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini942 – 1226285Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni851 – 8577Substrate bindingBy similarity

    Domaini

    The first PTPase domain interacts with SKAP1.

    Sequence similaritiesi

    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000049064.
    HOVERGENiHBG000066.
    InParanoidiP08575.
    KOiK06478.
    OMAiKANTSIC.
    PhylomeDBiP08575.
    TreeFamiTF351829.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    3.90.190.10. 2 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR016335. Leukocyte_common_ag.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR024739. PTP_recept_N.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF12567. CD45. 1 hit.
    PF00041. fn3. 2 hits.
    PF12453. PTP_N. 2 hits.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002004. Leukocyte_common_antigen. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 2 hits.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS50853. FN3. 2 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: At least 8 isoforms are produced.

    Isoform 1 (identifier: P08575-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TGLTTAKMPS VPLSSDPLPT     50
    HTTAFSPAST FERENDFSET TTSLSPDNTS TQVSPDSLDN ASAFNTTGVS 100
    SVQTPHLPTH ADSQTPSAGT DTQTFSGSAA NAKLNPTPGS NAISDVPGER 150
    STASTFPTDP VSPLTTTLSL AHHSSAALPA RTSNTTITAN TSDAYLNASE 200
    TTTLSPSGSA VISTTTIATT PSKPTCDEKY ANITVDYLYN KETKLFTAKL 250
    NVNENVECGN NTCTNNEVHN LTECKNASVS ISHNSCTAPD KTLILDVPPG 300
    VEKFQLHDCT QVEKADTTIC LKWKNIETFT CDTQNITYRF QCGNMIFDNK 350
    EIKLENLEPE HEYKCDSEIL YNNHKFTNAS KIIKTDFGSP GEPQIIFCRS 400
    EAAHQGVITW NPPQRSFHNF TLCYIKETEK DCLNLDKNLI KYDLQNLKPY 450
    TKYVLSLHAY IIAKVQRNGS AAMCHFTTKS APPSQVWNMT VSMTSDNSMH 500
    VKCRPPRDRN GPHERYHLEV EAGNTLVRNE SHKNCDFRVK DLQYSTDYTF 550
    KAYFHNGDYP GEPFILHHST SYNSKALIAF LAFLIIVTSI ALLVVLYKIY 600
    DLHKKRSCNL DEQQELVERD DEKQLMNVEP IHADILLETY KRKIADEGRL 650
    FLAEFQSIPR VFSKFPIKEA RKPFNQNKNR YVDILPYDYN RVELSEINGD 700
    AGSNYINASY IDGFKEPRKY IAAQGPRDET VDDFWRMIWE QKATVIVMVT 750
    RCEEGNRNKC AEYWPSMEEG TRAFGDVVVK INQHKRCPDY IIQKLNIVNK 800
    KEKATGREVT HIQFTSWPDH GVPEDPHLLL KLRRRVNAFS NFFSGPIVVH 850
    CSAGVGRTGT YIGIDAMLEG LEAENKVDVY GYVVKLRRQR CLMVQVEAQY 900
    ILIHQALVEY NQFGETEVNL SELHPYLHNM KKRDPPSEPS PLEAEFQRLP 950
    SYRSWRTQHI GNQEENKSKN RNSNVIPYDY NRVPLKHELE MSKESEHDSD 1000
    ESSDDDSDSE EPSKYINASF IMSYWKPEVM IAAQGPLKET IGDFWQMIFQ 1050
    RKVKVIVMLT ELKHGDQEIC AQYWGEGKQT YGDIEVDLKD TDKSSTYTLR 1100
    VFELRHSKRK DSRTVYQYQY TNWSVEQLPA EPKELISMIQ VVKQKLPQKN 1150
    SSEGNKHHKS TPLLIHCRDG SQQTGIFCAL LNLLESAETE EVVDIFQVVK 1200
    ALRKARPGMV STFEQYQFLY DVIASTYPAQ NGQVKKNNHQ EDKIEFDNEV 1250
    DKVKQDANCV NPLGAPEKLP EAKEQAEGSE PTSGTEGPEH SVNGPASPAL 1300
    NQGS 1304
    Length:1,304
    Mass (Da):147,254
    Last modified:July 19, 2003 - v2
    Checksum:iA08FC22D6069BAF7
    GO
    Isoform 2 (identifier: P08575-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         32-192: Missing.

    Show »
    Length:1,143
    Mass (Da):130,898
    Checksum:iDB4B4400F3602B3C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti650 – 6501L → P in CAA68669. (PubMed:2824653)Curated
    Sequence conflicti1207 – 12071P → L in CAA68669. (PubMed:2824653)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti191 – 1911T → A.
    Corresponds to variant rs4915154 [ dbSNP | Ensembl ].
    VAR_036860
    Natural varianti228 – 2281E → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035653
    Natural varianti294 – 2941I → L.
    Corresponds to variant rs2230606 [ dbSNP | Ensembl ].
    VAR_051763
    Natural varianti362 – 3632Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression. 1 Publication
    VAR_021205
    Natural varianti421 – 4211T → I.
    Corresponds to variant rs6696162 [ dbSNP | Ensembl ].
    VAR_051764
    Natural varianti568 – 5681H → Q.
    Corresponds to variant rs12136658 [ dbSNP | Ensembl ].
    VAR_051765
    Natural varianti863 – 8631G → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035654
    Natural varianti1283 – 12831S → R.
    Corresponds to variant rs2298872 [ dbSNP | Ensembl ].
    VAR_020303

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei32 – 192161Missing in isoform 2. 2 PublicationsVSP_007780Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00638 mRNA. Translation: CAA68669.1.
    Y00062 mRNA. Translation: CAA68269.1.
    AK292131 mRNA. Translation: BAF84820.1.
    M23492
    , M23496, M23466, M23467, M23468, M23469, M23470, M23471, M23472, M23473, M23474, M23475, M23476, M23477, M23478, M23479, M23480, M23481, M23482, M23483, M23484, M23485, M23486, M23487, M23488, M23489, M23490, M23491 Genomic DNA. Translation: AAD15273.2.
    PIRiA46546.
    RefSeqiNP_002829.3. NM_002838.4.
    NP_563578.2. NM_080921.3.
    UniGeneiHs.654514.

    Genome annotation databases

    EnsembliENST00000367376; ENSP00000356346; ENSG00000081237. [P08575-1]
    ENST00000573477; ENSP00000461074; ENSG00000262418. [P08575-2]
    ENST00000573679; ENSP00000458322; ENSG00000262418. [P08575-1]
    ENST00000594404; ENSP00000471843; ENSG00000081237. [P08575-2]
    GeneIDi5788.
    KEGGihsa:5788.

    Polymorphism databases

    DMDMi33112650.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    PTPRCbase

    PTPRC mutation db

    Wikipedia

    CD45 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00638 mRNA. Translation: CAA68669.1 .
    Y00062 mRNA. Translation: CAA68269.1 .
    AK292131 mRNA. Translation: BAF84820.1 .
    M23492
    , M23496 , M23466 , M23467 , M23468 , M23469 , M23470 , M23471 , M23472 , M23473 , M23474 , M23475 , M23476 , M23477 , M23478 , M23479 , M23480 , M23481 , M23482 , M23483 , M23484 , M23485 , M23486 , M23487 , M23488 , M23489 , M23490 , M23491 Genomic DNA. Translation: AAD15273.2 .
    PIRi A46546.
    RefSeqi NP_002829.3. NM_002838.4.
    NP_563578.2. NM_080921.3.
    UniGenei Hs.654514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YGR X-ray 2.90 A/B 622-1231 [» ]
    1YGU X-ray 2.90 A/B 622-1231 [» ]
    ProteinModelPortali P08575.
    SMRi P08575. Positions 391-469, 498-562, 623-1228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111752. 24 interactions.
    DIPi DIP-224N.
    IntActi P08575. 39 interactions.
    MINTi MINT-1130341.
    STRINGi 9606.ENSP00000356346.

    Chemistry

    BindingDBi P08575.
    ChEMBLi CHEMBL3243.
    GuidetoPHARMACOLOGYi 1852.

    PTM databases

    PhosphoSitei P08575.
    UniCarbKBi P08575.

    Polymorphism databases

    DMDMi 33112650.

    Proteomic databases

    MaxQBi P08575.
    PaxDbi P08575.
    PRIDEi P08575.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367376 ; ENSP00000356346 ; ENSG00000081237 . [P08575-1 ]
    ENST00000573477 ; ENSP00000461074 ; ENSG00000262418 . [P08575-2 ]
    ENST00000573679 ; ENSP00000458322 ; ENSG00000262418 . [P08575-1 ]
    ENST00000594404 ; ENSP00000471843 ; ENSG00000081237 . [P08575-2 ]
    GeneIDi 5788.
    KEGGi hsa:5788.

    Organism-specific databases

    CTDi 5788.
    GeneCardsi GC01P198607.
    HGNCi HGNC:9666. PTPRC.
    HPAi CAB000052.
    CAB002800.
    CAB056154.
    HPA000440.
    MIMi 126200. phenotype.
    151460. gene.
    608971. phenotype.
    neXtProti NX_P08575.
    Orphaneti 169157. T-B+ severe combined immunodeficiency due to CD45 deficiency.
    PharmGKBi PA34011.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000049064.
    HOVERGENi HBG000066.
    InParanoidi P08575.
    KOi K06478.
    OMAi KANTSIC.
    PhylomeDBi P08575.
    TreeFami TF351829.

    Enzyme and pathway databases

    Reactomei REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_19200. Other semaphorin interactions.
    SignaLinki P08575.

    Miscellaneous databases

    ChiTaRSi PTPRC. human.
    EvolutionaryTracei P08575.
    GeneWikii PTPRC.
    GenomeRNAii 5788.
    NextBioi 22518.
    PROi P08575.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08575.
    Bgeei P08575.
    CleanExi HS_PTPRC.
    Genevestigatori P08575.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    3.90.190.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR016335. Leukocyte_common_ag.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR024739. PTP_recept_N.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF12567. CD45. 1 hit.
    PF00041. fn3. 2 hits.
    PF12453. PTP_N. 2 hits.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002004. Leukocyte_common_antigen. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 2 hits.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS50853. FN3. 2 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens."
      Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H.
      J. Exp. Med. 166:1548-1566(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Lymphocyte.
    2. "Structural variants of human T200 glycoprotein (leukocyte-common antigen)."
      Ralph S.J., Thomas M.L., Morton C.C., Trowbridge I.S.
      EMBO J. 6:1251-1257(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    3. "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] (ISOFORM 2).
      Tissue: Synovium.
    4. "Integrity of the exon 6 sequence is essential for tissue-specific alternative splicing of human leukocyte common antigen pre-mRNA."
      Tsai A.Y.M., Streuli M., Saito H.
      Mol. Cell. Biol. 9:4550-4555(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-192.
    5. "Complete exon-intron organization of the human leukocyte common antigen (CD45) gene."
      Hall L.R., Streuli M., Schlossman S.F., Saito H.
      J. Immunol. 141:2781-2787(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1304.
      Tissue: Placenta.
    6. "The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase."
      Charbonneau H., Tonks N.K., Walsh K.A., Fischer E.H.
      Proc. Natl. Acad. Sci. U.S.A. 85:7182-7186(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR."
      Streuli M., Krueger N.X., Thai T., Tang M., Saito H.
      EMBO J. 9:2399-2407(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    8. "SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription."
      Wu L., Fu J., Shen S.-H.
      Mol. Cell. Biol. 22:2673-2686(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1, MUTAGENESIS OF CYS-851, FUNCTION.
    9. "A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation."
      Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M.
      J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232 AND ASN-335.
      Tissue: Liver.
    12. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232; ASN-240; ASN-276; ASN-284; ASN-335; ASN-419; ASN-488 AND ASN-497.
      Tissue: Leukemic T-cell.
    13. "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 SER-973 AND SER-1297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45."
      Nam H.J., Poy F., Saito H., Frederick C.A.
      J. Exp. Med. 201:441-452(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 622-1231 ALONE AND IN COMPLEX WITH PHOSPHOPEPTIDE.
    16. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO MS.
    17. "A deletion in the gene encoding the CD45 antigen in a patient with SCID."
      Tchilian E.Z., Wallace D.L., Wells R.S., Flower D.R., Morgan G., Beverley P.C.L.
      J. Immunol. 166:1308-1313(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL, CHARACTERIZATION OF VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL.
    18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-228 AND ARG-863.

    Entry informationi

    Entry nameiPTPRC_HUMAN
    AccessioniPrimary (citable) accession number: P08575
    Secondary accession number(s): A8K7W6, Q16614, Q9H0Y6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 19, 2003
    Last modified: October 1, 2014
    This is version 175 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