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Q64455

- PTPRJ_MOUSE

UniProt

Q64455 - PTPRJ_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase eta

Gene

Ptprj

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. May be involved in the mechanism of contact inhibition of cell growth. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling.7 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1106 – 11061SubstrateBy similarity
    Active sitei1140 – 11401Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1184 – 11841SubstrateBy similarity

    GO - Molecular functioni

    1. phosphatase activity Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: UniProtKB
    2. heart development Source: MGI
    3. negative regulation of cell growth Source: Ensembl
    4. negative regulation of cell migration Source: UniProtKB
    5. negative regulation of cell proliferation Source: UniProtKB
    6. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    7. negative regulation of MAP kinase activity Source: UniProtKB
    8. negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    9. negative regulation of protein kinase B signaling Source: UniProtKB
    10. negative regulation of receptor activity Source: UniProtKB
    11. negative regulation of T cell receptor signaling pathway Source: UniProtKB
    12. negative regulation of vascular permeability Source: Ensembl
    13. oligodendrocyte differentiation Source: MGI
    14. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    15. positive chemotaxis Source: Ensembl
    16. positive regulation of cell-matrix adhesion Source: UniProtKB
    17. positive regulation of focal adhesion assembly Source: UniProtKB
    18. positive regulation of macrophage chemotaxis Source: UniProtKB
    19. positive regulation of platelet activation Source: UniProtKB
    20. positive regulation of protein kinase B signaling Source: Ensembl
    21. vasculogenesis Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase eta (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase eta
    Short name:
    R-PTP-eta
    Alternative name(s):
    HPTP beta-like tyrosine phosphatase
    Protein-tyrosine phosphatase receptor type J
    Short name:
    R-PTP-J
    Susceptibility to colon cancer 1
    CD_antigen: CD148
    Gene namesi
    Name:Ptprj
    Synonyms:Byp, Scc1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:104574. Ptprj.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cell projectionruffle membrane. Cell junction
    Note: After T-cell stimulation, it is temporarily excluded from immunological synapses. Found at cell borders.

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cell surface Source: Ensembl
    3. immunological synapse Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: UniProtKB
    6. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1106 – 11061D → A: Substrate trapping with much higher affinity for substrate. 1 Publication
    Mutagenesisi1140 – 11401C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 12381210Receptor-type tyrosine-protein phosphatase etaPRO_0000025445Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi85 – 851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi145 – 1451N-linked (GlcNAc...)1 Publication
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi313 – 3131N-linked (GlcNAc...)1 Publication
    Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi488 – 4881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi538 – 5381N-linked (GlcNAc...)1 Publication
    Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi576 – 5761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi662 – 6621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi691 – 6911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi725 – 7251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi811 – 8111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi838 – 8381N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ64455.
    PaxDbiQ64455.
    PRIDEiQ64455.

    PTM databases

    PhosphoSiteiQ64455.

    Expressioni

    Tissue specificityi

    Expressed at high levels in brain, kidney, spleen and intestine, and at lower levels in liver, lung, thymus and heart. Expressed at a high level in the myeloid cell line FDC-P2, and at a lower level in the pre-B lymphoid cell line WEHI-231 and the T hybridoma cell line HB21.7.31. Not expressed in the fibroblast cell line NIH3T3 or the erythroid cell line F5-5. Expressed in macrophages.3 Publications

    Developmental stagei

    Expressed at 11.5 dpc in presumptive macrophages concentrated in the liver and scattered throughout the embryonic mesenchyme. Expressed at 11.5 and 12.5 dpc in the developing eye and in the ganglia and processes of cranial and spinal nerves constituting the PNS.1 Publication

    Gene expression databases

    ArrayExpressiQ64455.
    BgeeiQ64455.
    CleanExiMM_PTPRJ.
    GenevestigatoriQ64455.

    Interactioni

    Subunit structurei

    Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ64455.
    SMRiQ64455. Positions 44-108, 126-154, 217-605, 716-758, 919-1204.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 876848ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini898 – 1238341CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei877 – 89721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 12284Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini170 – 26697Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini270 – 35889Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini359 – 44385Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini444 – 52784Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 62194Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini622 – 71897Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini717 – 80387Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini942 – 1199258Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1140 – 11467Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000232054.
    HOVERGENiHBG053761.
    InParanoidiQ541R5.
    KOiK05698.

    Family and domain databases

    Gene3Di2.60.40.10. 7 hits.
    3.90.190.10. 1 hit.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 4 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 8 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 5 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS50853. FN3. 6 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q64455-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV     50
    SPTSVLLTWK HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY 100
    TFSIISVTTN ETLNKTITTE PWPVSDLHVT SVGVTQARLT WSNANGTASY 150
    RMLIEELTTH SSVNISGLKP GTNNSFAFPE SNETQADFAV AEEVPDANGT 200
    KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD TQYNATIYSQ 250
    AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV 300
    YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL 350
    QVYTSPDQVS DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS 400
    TGNQSYMVED LKPGTSYHFE IIPRGPDGTE GLSSTVNGST DPSAVTDIRV 450
    VNISTTEMQL EWQNTDDASG YTYHLVLESK SGSIIRTNSS QKWITVGSLT 500
    PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT TTTAAIRWKN 550
    EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT 600
    QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG 650
    FELGVRSDSW DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG 700
    KMALPAQNIC TTGITDPPTP DGSPNITSVS HNSVKVKFSG FEASHGPIKA 750
    YAVILTTGEA AQPSADVLKY TYEDFKRGAS DTYVTYLIRI EEKGQSQGLS 800
    EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT YNLQNDGLIN 850
    GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK 900
    RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK 950
    LIGISLPKYT AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY 1000
    MPGYHSKKDF IATQGPLPNT LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC 1050
    EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI RDFVVKNMQN SESHPLRQFH 1100
    FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC SAGVGRTGTF 1150
    IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII 1200
    RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA 1238
    Length:1,238
    Mass (Da):136,769
    Last modified:December 15, 2009 - v2
    Checksum:iE525D346A2C60335
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti175 – 1751S → T in BAA08146. (PubMed:8549806)Curated
    Sequence conflicti175 – 1751S → T in AAK96030. (PubMed:12089527)Curated
    Sequence conflicti175 – 1751S → T in AAK98640. (PubMed:12089527)Curated
    Sequence conflicti211 – 2111L → P in AAK98640. (PubMed:12089527)Curated
    Sequence conflicti217 – 2171V → A in AAK98640. (PubMed:12089527)Curated
    Sequence conflicti463 – 4631Q → H in BAE27842. (PubMed:16141072)Curated
    Sequence conflicti553 – 5531A → T in AAK98640. (PubMed:12089527)Curated
    Sequence conflicti622 – 6221P → S in AAK98640. (PubMed:12089527)Curated
    Sequence conflicti1061 – 10611D → E in AAK98640. (PubMed:12089527)Curated
    Sequence conflicti1126 – 11261Y → D in AAN11409. (PubMed:12089527)Curated
    Sequence conflicti1133 – 11331E → K in AAN11409. (PubMed:12089527)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D45212 mRNA. Translation: BAA08146.1.
    AY038877, AY038861 Genomic DNA. Translation: AAN11409.1.
    AY038891 mRNA. Translation: AAK96030.1.
    AY039232 mRNA. Translation: AAK98640.1.
    DQ133576 mRNA. Translation: ABA07808.1.
    AK147318 mRNA. Translation: BAE27842.1.
    AK147556 mRNA. Translation: BAE27993.1.
    PIRiS68700.
    RefSeqiNP_033008.3. NM_008982.5.
    UniGeneiMm.330393.

    Genome annotation databases

    GeneIDi19271.
    KEGGimmu:19271.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D45212 mRNA. Translation: BAA08146.1 .
    AY038877 , AY038861 Genomic DNA. Translation: AAN11409.1 .
    AY038891 mRNA. Translation: AAK96030.1 .
    AY039232 mRNA. Translation: AAK98640.1 .
    DQ133576 mRNA. Translation: ABA07808.1 .
    AK147318 mRNA. Translation: BAE27842.1 .
    AK147556 mRNA. Translation: BAE27993.1 .
    PIRi S68700.
    RefSeqi NP_033008.3. NM_008982.5.
    UniGenei Mm.330393.

    3D structure databases

    ProteinModelPortali Q64455.
    SMRi Q64455. Positions 44-108, 126-154, 217-605, 716-758, 919-1204.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q64455.

    Proteomic databases

    MaxQBi Q64455.
    PaxDbi Q64455.
    PRIDEi Q64455.

    Protocols and materials databases

    DNASUi 19271.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 19271.
    KEGGi mmu:19271.

    Organism-specific databases

    CTDi 5795.
    MGIi MGI:104574. Ptprj.

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000232054.
    HOVERGENi HBG053761.
    InParanoidi Q541R5.
    KOi K05698.

    Miscellaneous databases

    NextBioi 296158.
    PROi Q64455.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64455.
    Bgeei Q64455.
    CleanExi MM_PTPRJ.
    Genevestigatori Q64455.

    Family and domain databases

    Gene3Di 2.60.40.10. 7 hits.
    3.90.190.10. 1 hit.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00041. fn3. 4 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 8 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 5 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50853. FN3. 6 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1."
      Kuramochi S., Matsuda S., Matsuda Y., Saitoh T., Ohsugi M., Yamamoto T.
      FEBS Lett. 378:7-14(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: MRL-LPR/LPR.
      Tissue: Lymph node.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvSl and BALB/c.
    3. "Phenotypic consequences of the germ-line loss of the putative tumor suppressor Ptprj (Scc1)."
      Csikos T., Snoek M., de Boer T., Drenth T., Krimpenfort P., van Amerongen R., Zevenhoven J., van der Valk M., Hellberg C., Ostman A., Demant P., Berns A.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129P2.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6 and C57BL/6J.
      Tissue: Brain.
    5. "Identification of novel protein-tyrosine phosphatases in a human leukemia cell line, F-36P."
      Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.
      Leukemia 7:742-746(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed in macrophages and is regulated by CSF-1 and LPS."
      Osborne J.M., den Elzen N., Lichanska A.M., Costelloe E.O., Yamada T., Cassady A.I., Hume D.A.
      J. Leukoc. Biol. 64:692-701(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148."
      Grazia Lampugnani M., Zanetti A., Corada M., Takahashi T., Balconi G., Breviario F., Orsenigo F., Cattelino A., Kemler R., Daniel T.O., Dejana E.
      J. Cell Biol. 161:793-804(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-1106 AND CYS-1140.
    8. "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
      Lin J., Weiss A.
      J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. Cited for: FUNCTION.
    10. "The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion."
      Jandt E., Denner K., Kovalenko M., Ostman A., Bohmer F.D.
      Oncogene 22:4175-4185(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-1140.
    11. "Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling."
      Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., Weiss A.
      Immunity 28:183-196(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis."
      Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y., Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N., Zhu J.W., Weiss A., Watson S.P.
      Blood 113:4942-4954(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "CD148/DEP-1 association with areas of cytoskeletal organisation in macrophages."
      Dave R.K., Hume D.A., Elsegood C., Kellie S.
      Exp. Cell Res. 315:1734-1744(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "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-145; ASN-313; ASN-317 AND ASN-538.

    Entry informationi

    Entry nameiPTPRJ_MOUSE
    AccessioniPrimary (citable) accession number: Q64455
    Secondary accession number(s): Q3UH64
    , Q3UHL5, Q541R5, Q8CIW9, Q8K3Q2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 128 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. 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