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P06800

- PTPRC_MOUSE

UniProt

P06800 - PTPRC_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase C

Gene

Ptprc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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 By similarity. Dephosphorylates LYN, and thereby modulates LYN activity.By similarity1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei808 – 8081SubstrateBy similarity
    Active sitei840 – 8401Phosphocysteine intermediateBy similarity
    Binding sitei884 – 8841SubstrateBy similarity
    Active sitei1155 – 11551Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. heparan sulfate proteoglycan binding Source: MGI
    2. heparin binding Source: MGI
    3. protein binding Source: IntAct
    4. protein kinase binding Source: UniProtKB
    5. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: MGI
    2. B cell differentiation Source: MGI
    3. B cell proliferation Source: UniProtKB
    4. B cell receptor signaling pathway Source: UniProtKB
    5. defense response to virus Source: UniProtKB
    6. dephosphorylation Source: UniProtKB
    7. heterotypic cell-cell adhesion Source: MGI
    8. leukocyte cell-cell adhesion Source: MGI
    9. negative regulation of cytokine-mediated signaling pathway Source: UniProtKB
    10. negative regulation of peptidyl-tyrosine phosphorylation Source: MGI
    11. negative regulation of protein autophosphorylation Source: MGI
    12. negative regulation of protein kinase activity Source: UniProtKB
    13. negative regulation of T cell mediated cytotoxicity Source: UniProtKB
    14. negative thymic T cell selection Source: MGI
    15. peptidyl-tyrosine dephosphorylation Source: GOC
    16. positive regulation of alpha-beta T cell proliferation Source: MGI
    17. positive regulation of antigen receptor-mediated signaling pathway Source: UniProtKB
    18. positive regulation of B cell proliferation Source: MGI
    19. positive regulation of extrinsic apoptotic signaling pathway Source: MGI
    20. positive regulation of gamma-delta T cell differentiation Source: MGI
    21. positive regulation of humoral immune response mediated by circulating immunoglobulin Source: MGI
    22. positive regulation of isotype switching to IgG isotypes Source: MGI
    23. positive regulation of MAPK cascade Source: MGI
    24. positive regulation of T cell differentiation Source: MGI
    25. positive regulation of T cell mediated cytotoxicity Source: MGI
    26. positive regulation of T cell mediated immunity Source: MGI
    27. positive regulation of T cell proliferation Source: UniProtKB
    28. positive thymic T cell selection Source: MGI
    29. protein dephosphorylation Source: UniProtKB
    30. regulation of B cell differentiation Source: MGI
    31. regulation of B cell receptor signaling pathway Source: MGI
    32. regulation of cell cycle Source: UniProtKB
    33. regulation of extrinsic apoptotic signaling pathway Source: MGI
    34. regulation of humoral immune response mediated by circulating immunoglobulin Source: MGI
    35. release of sequestered calcium ion into cytosol Source: UniProtKB
    36. T cell differentiation Source: UniProtKB
    37. T cell proliferation Source: MGI
    38. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_216080. Phosphorylation of CD3 and TCR zeta chains.

    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
    Lymphocyte antigen 5
    Short name:
    Ly-5
    T200
    CD_antigen: CD45
    Gene namesi
    Name:Ptprc
    Synonyms:Ly-5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:97810. Ptprc.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell periphery Source: MGI
    2. external side of plasma membrane Source: MGI
    3. focal adhesion Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. membrane raft Source: UniProtKB-SubCell
    6. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 12911268Receptor-type tyrosine-protein phosphatase CPRO_0000025471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence Analysis
    Modified residuei962 – 9621Phosphoserine1 Publication
    Modified residuei1284 – 12841PhosphoserineBy similarity

    Post-translational modificationi

    Heavily N- and O-glycosylated.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP06800.
    PaxDbiP06800.
    PRIDEiP06800.

    PTM databases

    PhosphoSiteiP06800.

    Expressioni

    Developmental stagei

    Expression is restricted to the hematopoietic compartment of development.

    Gene expression databases

    ArrayExpressiP06800.
    BgeeiP06800.
    CleanExiMM_PTPRC.
    GenevestigatoriP06800.

    Interactioni

    Subunit structurei

    Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes By similarity. Binds GANAB and PRKCSH.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LckP062403EBI-1672,EBI-1401

    Protein-protein interaction databases

    BioGridi202493. 3 interactions.
    IntActiP06800. 8 interactions.
    MINTiMINT-188397.
    STRINGi10090.ENSMUSP00000074352.

    Structurei

    3D structure databases

    ProteinModelPortaliP06800.
    SMRiP06800. Positions 612-1216.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 564541ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini587 – 1291705CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei565 – 58622HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini374 – 47097Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini471 – 56696Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini640 – 899260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini931 – 1214284Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni840 – 8467Substrate bindingBy similarity

    Domaini

    The first PTPase domain interacts with SKAP1.By similarity

    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.
    GeneTreeiENSGT00680000099951.
    HOVERGENiHBG000066.
    OrthoDBiEOG7XSTCW.
    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.
    PF12453. PTP_N. 1 hit.
    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. 2 hits.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06800-1) [UniParc]FASTAAdd to Basket

    Also known as: B220

    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

    MGLWLKLLAF GFALLDTEVF VTGQTPTPSD ELSTTENALL LPQSDPLPAR     50
    TTESTPPSIS ERGNGSSETT YHPGVLSTLL PHLSPQPDSQ TPSAGGADTQ 100
    TFSSQADNPT LTPAPGGGTD PPGVPGERTV PGTIPADTAF PVDTPSLARN 150
    SSAASPTHTS NVSTTDISSG ASLTTLTPST LGLASTDPPS TTIATTTKQT 200
    CAAMFGNITV NYTYESSNQT FKADLKDVQN AKCGNEDCEN VLNNLEECSQ 250
    IKNISVSNDS CAPATTIDLY VPPGTDKFSL HDCTPKEKAN TSICLEWKTK 300
    NLDFRKCNSD NISYVLHCEP ENNTKCIRRN TFIPERCQLD NLRAQTNYTC 350
    VAEILYRGVK LVKNVINVQT DLGIPETPKP SCGDPAARKT LVSWPEPVSK 400
    PESASKPHGY VLCYKNNSEK CKSLPNNVTS FEVESLKPYK YYEVSLLAYV 450
    NGKIQRNGTA EKCNFHTKAD RPDKVNGMKT SRPTDNSINV TCGPPYETNG 500
    PKTFYILVVR SGGSFVTKYN KTNCQFYVDN LYYSTDYEFL VSFHNGVYEG 550
    DSVIRNESTN FNAKALIIFL VFLIIVTSIA LLVVLYKIYD LRKKRSSNLD 600
    EQQELVERDD EKQLMDVEPI HSDILLETYK RKIADEGRLF LAEFQSIPRV 650
    FSKFPIKDAR KPHNQNKNRY VDILPYDYNR VELSEINGDA GSTYINASYI 700
    DGFKEPRKYI AAQGPRDETV DDFWRMIWEQ KATVIVMVTR CEEGNRNKCA 750
    EYWPSMEEGT RAFKDIVVTI NDHKRCPDYI IQKLNVAHKK EKATGREVTH 800
    IQFTSWPDHG VPEDPHLLLK LRRRVNAFSN FFSGPIVVHC SAGVGRTGTY 850
    IGIDAMLEGL EAEGKVDVYG YVVKLRRQRC LMVQVEAQYI LIHQALVEYN 900
    QFGETEVNLS ELHSCLHNMK KRDPPSDPSP LEAEYQRLPS YRSWRTQHIG 950
    NQEENKKKNR NSNVVPYDFN RVPLKHELEM SKESEPESDE SSDDDSDSEE 1000
    TSKYINASFV MSYWKPEMMI AAQGPLKETI GDFWQMIFQR KVKVIVMLTE 1050
    LVNGDQEVCA QYWGEGKQTY GDMEVEMKDT NRASAYTLRT FELRHSKRKE 1100
    PRTVYQYQCT TWKGEELPAE PKDLVSMIQD LKQKLPKASP EGMKYHKHAS 1150
    ILVHCRDGSQ QTGLFCALFN LLESAETEDV VDVFQVVKSL RKARPGVVCS 1200
    YEQYQFLYDI IASIYPAQNG QVKKTNSQDK IEFHNEVDGG KQDANCVRPD 1250
    GPLNKAQEDS RGVGTPEPTN SAEEPEHAAN GSASPAPTQS S 1291
    Length:1,291
    Mass (Da):144,604
    Last modified:July 27, 2011 - v3
    Checksum:iED752FD195BA9643
    GO
    Isoform 2 (identifier: P06800-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-73: Missing.

    Show »
    Length:1,248
    Mass (Da):140,040
    Checksum:iD08281C0463EA174
    GO
    Isoform 3 (identifier: P06800-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-169: Missing.

    Show »
    Length:1,152
    Mass (Da):130,622
    Checksum:iF1AA6650E654CAAB
    GO

    Sequence cautioni

    The sequence AAA39462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti300 – 3001K → E in AAA39459. (PubMed:1822988)Curated
    Sequence conflicti398 – 3981V → A in AAA39459. (PubMed:1822988)Curated
    Sequence conflicti402 – 4032ES → DP in AAA39459. (PubMed:1822988)Curated
    Sequence conflicti476 – 4761N → T in AAA39459. (PubMed:1822988)Curated
    Sequence conflicti518 – 5203KYN → NTT in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti528 – 5281V → G in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti556 – 5561N → S in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti588 – 5881I → S in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti906 – 9061E → Q in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti931 – 9311L → R in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti953 – 9531E → G in AAA39458. (PubMed:2944116)Curated
    Sequence conflicti959 – 9591N → K in AAA39458. (PubMed:2944116)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei31 – 169139Missing in isoform 3. 2 PublicationsVSP_012442Add
    BLAST
    Alternative sequencei31 – 7343Missing in isoform 2. 1 PublicationVSP_012441Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14342 mRNA. Translation: AAA39458.1.
    M92933 mRNA. Translation: AAA39459.1.
    AC122903 Genomic DNA. No translation available.
    AC159278 Genomic DNA. No translation available.
    M17320 mRNA. Translation: AAA60449.1.
    M23354 Genomic DNA. Translation: AAA39462.1. Different initiation.
    M22456 Genomic DNA. Translation: AAB46374.1.
    M11934 mRNA. Translation: AAA39461.1.
    M23241 Genomic DNA. Translation: AAA39460.1.
    M15174 mRNA. Translation: AAA40161.1.
    PIRiA23329.
    A28334.
    A28335.
    I57644.
    UniGeneiMm.391573.

    Genome annotation databases

    EnsembliENSMUST00000027645; ENSMUSP00000027645; ENSMUSG00000026395. [P06800-1]
    ENSMUST00000112036; ENSMUSP00000107667; ENSMUSG00000026395. [P06800-3]
    UCSCiuc007cvf.2. mouse. [P06800-1]
    uc007cvh.2. mouse. [P06800-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14342 mRNA. Translation: AAA39458.1 .
    M92933 mRNA. Translation: AAA39459.1 .
    AC122903 Genomic DNA. No translation available.
    AC159278 Genomic DNA. No translation available.
    M17320 mRNA. Translation: AAA60449.1 .
    M23354 Genomic DNA. Translation: AAA39462.1 . Different initiation.
    M22456 Genomic DNA. Translation: AAB46374.1 .
    M11934 mRNA. Translation: AAA39461.1 .
    M23241 Genomic DNA. Translation: AAA39460.1 .
    M15174 mRNA. Translation: AAA40161.1 .
    PIRi A23329.
    A28334.
    A28335.
    I57644.
    UniGenei Mm.391573.

    3D structure databases

    ProteinModelPortali P06800.
    SMRi P06800. Positions 612-1216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202493. 3 interactions.
    IntActi P06800. 8 interactions.
    MINTi MINT-188397.
    STRINGi 10090.ENSMUSP00000074352.

    Chemistry

    GuidetoPHARMACOLOGYi 1852.

    PTM databases

    PhosphoSitei P06800.

    Proteomic databases

    MaxQBi P06800.
    PaxDbi P06800.
    PRIDEi P06800.

    Protocols and materials databases

    DNASUi 19264.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027645 ; ENSMUSP00000027645 ; ENSMUSG00000026395 . [P06800-1 ]
    ENSMUST00000112036 ; ENSMUSP00000107667 ; ENSMUSG00000026395 . [P06800-3 ]
    UCSCi uc007cvf.2. mouse. [P06800-1 ]
    uc007cvh.2. mouse. [P06800-3 ]

    Organism-specific databases

    MGIi MGI:97810. Ptprc.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00680000099951.
    HOVERGENi HBG000066.
    OrthoDBi EOG7XSTCW.
    TreeFami TF351829.

    Enzyme and pathway databases

    Reactomei REACT_216080. Phosphorylation of CD3 and TCR zeta chains.

    Miscellaneous databases

    NextBioi 296132.
    PROi P06800.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06800.
    Bgeei P06800.
    CleanExi MM_PTPRC.
    Genevestigatori P06800.

    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.
    PF12453. PTP_N. 1 hit.
    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. 2 hits.
    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. "Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA."
      Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. Erratum
      Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
      Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987)
      Cited for: SEQUENCE REVISION.
    3. "Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles."
      Zebedee S.L., Barritt D.S., Raschke W.C.
      Dev. Immunol. 1:243-254(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "Alternative use of 5' exons in the specification of Ly-5 isoforms distinguishing hematopoietic cell lineages."
      Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.
      Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-226 (ISOFORM 2).
    6. "Organization of the Ly-5 gene."
      Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.
      Mol. Cell. Biol. 8:4889-4895(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    7. "Sequence conservation in potential regulatory regions of the mouse and human leukocyte common antigen gene."
      Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.
      J. Biol. Chem. 264:6220-6229(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-263 (ISOFORM 3).
      Tissue: T-cell.
    9. "Structural features of Ly-5 glycoproteins of the mouse and counterparts in other mammals."
      Tung J.-S., Saga Y., Boyse E.A.
      Immunogenetics 28:271-277(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-73.
    10. "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
      Yi T., Cleveland J.L., Ihle J.N.
      Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 730-838.
    11. "Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within B- and T-lymphocyte lineages."
      Raschke W.C.
      Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 961-1291.
    12. "High sequence conservation between rat (T200) and mouse (Ly-5) leukocyte common antigens."
      Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.
      Immunogenetics 25:263-266(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    13. "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."
      Arendt C.W., Ostergaard H.L.
      J. Biol. Chem. 272:13117-13125(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GANAB AND PRKCSH.
    14. "CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells."
      Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H.
      J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPTPRC_MOUSE
    AccessioniPrimary (citable) accession number: P06800
    Secondary accession number(s): E9QLT5
    , Q61812, Q61813, Q61814, Q61815, Q78EF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3