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P04157

- PTPRC_RAT

UniProt

P04157 - PTPRC_RAT

Protein

Receptor-type tyrosine-protein phosphatase C

Gene

Ptprc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (12 Jun 2007)
      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 similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei790 – 7901SubstrateBy similarity
    Active sitei822 – 8221Phosphocysteine intermediateBy similarity
    Binding sitei866 – 8661SubstrateBy similarity
    Active sitei1137 – 11371Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. heparin binding Source: Ensembl
    2. protein binding Source: RGD
    3. protein kinase binding Source: UniProtKB
    4. protein kinase regulator activity Source: RGD
    5. protein tyrosine phosphatase activity Source: UniProtKB
    6. transmembrane receptor protein tyrosine phosphatase activity Source: RGD

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 13

    Organism-specific databases

    RGDi3451. Ptprc.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell surface Source: RGD
    2. cytoplasmic side of plasma membrane Source: RGD
    3. external side of plasma membrane Source: Ensembl
    4. focal adhesion Source: UniProtKB
    5. integral component of membrane Source: RGD
    6. integral component of plasma membrane Source: UniProtKB
    7. membrane raft Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 12731250Receptor-type tyrosine-protein phosphatase CPRO_0000025472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Modified residuei944 – 9441PhosphoserineBy similarity
    Modified residuei1266 – 12661PhosphoserineBy similarity

    Post-translational modificationi

    Heavily N- and O-glycosylated.
    The cytoplasmic domain contains potential phosphorylation sites.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP04157.
    PRIDEiP04157.

    PTM databases

    PhosphoSiteiP04157.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are found in thymocyte and lymph node. Isoform 4 and isoform 3 are found in the lymph nod.

    Gene expression databases

    ArrayExpressiP04157.
    GenevestigatoriP04157.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi246829. 1 interaction.
    IntActiP04157. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP04157.
    SMRiP04157. Positions 594-1198.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 546523ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini568 – 1273706CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei547 – 56721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini361 – 45292Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini453 – 54593Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini622 – 881260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini913 – 1196284Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni822 – 8287Substrate 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.
    HOGENOMiHOG000049064.
    HOVERGENiHBG000066.
    KOiK06478.
    OMAiKANTSIC.
    OrthoDBiEOG7XSTCW.
    PhylomeDBiP04157.
    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. 1 hit.
    PF12453. PTP_N. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P04157-1) [UniParc]FASTAAdd to Basket

    Also known as: L-CA variant 4

    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 SLALLGPEVF VTGQGTTDDG LDTTEIVLLP QTDPLPARTT     50
    EFTPPSISER GNGSSETTYL PGFSSTLMPH LTPQPDSQTP SARGADTQTL 100
    SSQADLTTLT AAPSGETDPP GVPEESTVPE TFPGGTPILA RNSTAPSPTH 150
    TSNVSTTDIS SGANLTTPAP STLGFASNTT TSTEIATPQT KPSCDEKFGN 200
    VTVRYIYDDS SKNFNANLEG DKKPKCEYTD CEKELKNLPE CSQKNVTLSN 250
    GSCTPDKIIN LDVPPGTHNF NLTNCTPDIE ANTSICLEWK IKNKFTCDIQ 300
    KISYNFRCTP EMKTFALDKH GTLWLHNLTV RTNYTCAAEV LYNNVILLKQ 350
    DRRVQTDFGT PEMLPHVQCK NSTNSTTLVS WAEPASKHHG YILCYKKTPS 400
    EKCENLANDV NSFEVKNLRP YTEYTVSLFA YVIGRVQRNG PAKDCNFRTK 450
    AARPGKVNGM KTSRASDNSI NVTCNSPYEI NGPEARYILE VKSGGSLVKT 500
    FNQSTCKFVV DNLYYSTDYE FLVYFYNGEY LGDPEIKPQS TSYNSKALII 550
    FLVFLIIVTS IALLVVLYKI YDLRKKRSSN LDEQQELVER DEEKQLINVD 600
    PIHSDLLLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD ARKSQNQNKN 650
    RYVDILPYDY NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE 700
    TVDDFWKMIW EQKATVIVMV TRCEEGNRNK CAEYWPCMEE GTRTFRDVVV 750
    TINDHKRCPD YIIQKLSIAH KKEKATGREV THIQFTSWPD HGVPEDPHLL 800
    LKLRRRVNAF SNFFSGPIVV HCSAGVGRTG TYIGIDAMLE SLEAEGKVDV 850
    YGYVVNLRRQ RCLMVQVEAQ YILIHQALVE YNQFGETEVN LSELHSCLQN 900
    LKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK NRSSNVVPYD 950
    FNRVPLKHEL EMSKESEAES DESSDEDSDS EETSKYINAS FVMSYWKPEM 1000
    MIAAQGPLKE TIGDFWQMIF QRKVKVIVML TELMSGDQEV CAQYWGEGKQ 1050
    TYGDMEVMLK DTNKSSAYIL RAFELRHSKR KEPRTVYQYQ CTTWKGEELP 1100
    AEPKDLVTLI QNIKQKLPKS GSEGMKYHKH ASILVHCRDG SQQTGLFCAL 1150
    FNLLESAETE DVVDVFQVVK SLRKARPGMV GSFEQYQFLY DIMASIYPTQ 1200
    NGQVKKANSQ DKIEFHNEVD GAKQDANCVQ PADPLNKAQE DSKEVGASEP 1250
    ASGSEEPEHS ANGPMSPALT PSS 1273
    Length:1,273
    Mass (Da):143,269
    Last modified:June 12, 2007 - v2
    Checksum:iEDFA48100ACF2CB2
    GO
    Isoform 2 (identifier: P04157-2) [UniParc]FASTAAdd to Basket

    Also known as: L-CA variant 1

    The sequence of this isoform differs from the canonical sequence as follows:
         30-161: Missing.

    Show »
    Length:1,141
    Mass (Da):129,697
    Checksum:iD8CD289BA1873388
    GO
    Isoform 3 (identifier: P04157-3) [UniParc]FASTAAdd to Basket

    Also known as: L-CA variant 2

    The sequence of this isoform differs from the canonical sequence as follows:
         30-120: Missing.

    Show »
    Length:1,182
    Mass (Da):133,819
    Checksum:iEDF2153D0EBBF86E
    GO
    Isoform 4 (identifier: P04157-4) [UniParc]FASTAAdd to Basket

    Also known as: L-CA variant 3

    The sequence of this isoform differs from the canonical sequence as follows:
         30-71: Missing.
         121-161: Missing.

    Show »
    Length:1,190
    Mass (Da):134,662
    Checksum:i61CD4F787C7E695F
    GO
    Isoform 5 (identifier: P04157-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-161: Missing.

    Show »
    Length:1,183
    Mass (Da):134,182
    Checksum:i1076BD878F13B5CA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561S → R in AAA41518. 1 PublicationCurated
    Sequence conflicti56 – 561S → R in AAA41521. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei30 – 161132Missing in isoform 2. 1 PublicationVSP_005167Add
    BLAST
    Alternative sequencei30 – 12091Missing in isoform 3. 2 PublicationsVSP_005166Add
    BLAST
    Alternative sequencei30 – 7142Missing in isoform 4. 3 PublicationsVSP_005165Add
    BLAST
    Alternative sequencei72 – 16190Missing in isoform 5. 1 PublicationVSP_026163Add
    BLAST
    Alternative sequencei121 – 16141Missing in isoform 4. 3 PublicationsVSP_005168Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CB793707 mRNA. No translation available.
    Y00065 mRNA. Translation: CAA68272.1.
    Y00065 mRNA. Translation: CAA68273.1.
    Y00065 mRNA. Translation: CAA68274.1.
    Y00065 mRNA. Translation: CAA68275.1.
    M25820 mRNA. Translation: AAA41518.1.
    M25821 mRNA. Translation: AAA41519.1.
    M25822 mRNA. Translation: AAA41520.1.
    M25823 mRNA. Translation: AAA41521.1.
    PIRiA45854.
    RefSeqiNP_001103357.1. NM_001109887.1. [P04157-4]
    NP_001103358.1. NM_001109888.1. [P04157-5]
    NP_001103359.1. NM_001109889.1. [P04157-3]
    NP_001103360.1. NM_001109890.1. [P04157-2]
    NP_612516.2. NM_138507.2. [P04157-1]
    XP_006249972.1. XM_006249910.1. [P04157-1]
    UniGeneiRn.90166.

    Genome annotation databases

    EnsembliENSRNOT00000000814; ENSRNOP00000000814; ENSRNOG00000000655. [P04157-2]
    ENSRNOT00000029865; ENSRNOP00000029889; ENSRNOG00000000655. [P04157-5]
    ENSRNOT00000029878; ENSRNOP00000030503; ENSRNOG00000000655. [P04157-4]
    ENSRNOT00000060292; ENSRNOP00000057042; ENSRNOG00000000655. [P04157-3]
    ENSRNOT00000064785; ENSRNOP00000063859; ENSRNOG00000000655. [P04157-1]
    GeneIDi24699.
    KEGGirno:24699.
    UCSCiRGD:3451. rat. [P04157-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CB793707 mRNA. No translation available.
    Y00065 mRNA. Translation: CAA68272.1 .
    Y00065 mRNA. Translation: CAA68273.1 .
    Y00065 mRNA. Translation: CAA68274.1 .
    Y00065 mRNA. Translation: CAA68275.1 .
    M25820 mRNA. Translation: AAA41518.1 .
    M25821 mRNA. Translation: AAA41519.1 .
    M25822 mRNA. Translation: AAA41520.1 .
    M25823 mRNA. Translation: AAA41521.1 .
    PIRi A45854.
    RefSeqi NP_001103357.1. NM_001109887.1. [P04157-4 ]
    NP_001103358.1. NM_001109888.1. [P04157-5 ]
    NP_001103359.1. NM_001109889.1. [P04157-3 ]
    NP_001103360.1. NM_001109890.1. [P04157-2 ]
    NP_612516.2. NM_138507.2. [P04157-1 ]
    XP_006249972.1. XM_006249910.1. [P04157-1 ]
    UniGenei Rn.90166.

    3D structure databases

    ProteinModelPortali P04157.
    SMRi P04157. Positions 594-1198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246829. 1 interaction.
    IntActi P04157. 2 interactions.

    Chemistry

    GuidetoPHARMACOLOGYi 1852.

    PTM databases

    PhosphoSitei P04157.

    Proteomic databases

    PaxDbi P04157.
    PRIDEi P04157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000000814 ; ENSRNOP00000000814 ; ENSRNOG00000000655 . [P04157-2 ]
    ENSRNOT00000029865 ; ENSRNOP00000029889 ; ENSRNOG00000000655 . [P04157-5 ]
    ENSRNOT00000029878 ; ENSRNOP00000030503 ; ENSRNOG00000000655 . [P04157-4 ]
    ENSRNOT00000060292 ; ENSRNOP00000057042 ; ENSRNOG00000000655 . [P04157-3 ]
    ENSRNOT00000064785 ; ENSRNOP00000063859 ; ENSRNOG00000000655 . [P04157-1 ]
    GeneIDi 24699.
    KEGGi rno:24699.
    UCSCi RGD:3451. rat. [P04157-1 ]

    Organism-specific databases

    CTDi 5788.
    RGDi 3451. Ptprc.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00680000099951.
    HOGENOMi HOG000049064.
    HOVERGENi HBG000066.
    KOi K06478.
    OMAi KANTSIC.
    OrthoDBi EOG7XSTCW.
    PhylomeDBi P04157.
    TreeFami TF351829.

    Miscellaneous databases

    NextBioi 604155.
    PROi P04157.

    Gene expression databases

    ArrayExpressi P04157.
    Genevestigatori P04157.

    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. 1 hit.
    PF12453. PTP_N. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    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. "Amgen rat EST program."
      Amgen EST program
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-147 (ISOFORM 4).
    2. "Lymphocyte specific heterogeneity in the rat leucocyte common antigen (T200) is due to differences in polypeptide sequences near the NH2-terminus."
      Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.
      EMBO J. 6:1259-1264(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-218 (ISOFORMS 1; 2; 3 AND 4).
    3. Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.
      Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-1273 (ISOFORMS 1; 3; 4 AND 5).
    4. "Evidence from cDNA clones that the rat leukocyte-common antigen (T200) spans the lipid bilayer and contains a cytoplasmic domain of 80,000 Mr."
      Thomas M.L., Barclay A.N., Gagnon J., Williams A.F.
      Cell 41:83-93(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-1255 (ISOFORM 1).

    Entry informationi

    Entry nameiPTPRC_RAT
    AccessioniPrimary (citable) accession number: P04157
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3