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P35822

- PTPRK_MOUSE

UniProt

P35822 - PTPRK_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase kappa

Gene

Ptprk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1068 – 10681SubstrateBy similarity
    Active sitei1100 – 11001Phosphocysteine intermediateBy similarity
    Binding sitei1144 – 11441SubstrateBy similarity
    Active sitei1394 – 13941Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: MGI

    GO - Biological processi

    1. cell migration Source: Ensembl
    2. cellular response to reactive oxygen species Source: Ensembl
    3. cellular response to UV Source: Ensembl
    4. focal adhesion assembly Source: Ensembl
    5. negative regulation of cell cycle Source: Ensembl
    6. negative regulation of cell migration Source: Ensembl
    7. negative regulation of keratinocyte proliferation Source: Ensembl
    8. negative regulation of transcription, DNA-templated Source: Ensembl
    9. neuron projection development Source: Ensembl
    10. peptidyl-tyrosine dephosphorylation Source: GOC
    11. protein dephosphorylation Source: MGI
    12. protein localization to cell surface Source: Ensembl
    13. transforming growth factor beta receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase, Receptor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase kappa (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase kappa
    Short name:
    R-PTP-kappa
    Gene namesi
    Name:Ptprk
    Synonyms:Ptpk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:103310. Ptprk.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: MGI
    2. cell-cell junction Source: Ensembl
    3. cell surface Source: Ensembl
    4. dendrite Source: MGI
    5. integral component of membrane Source: UniProtKB-KW
    6. leading edge membrane Source: Ensembl
    7. neuronal cell body Source: MGI
    8. photoreceptor outer segment Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 14571432Receptor-type tyrosine-protein phosphatase kappaPRO_0000025447Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi215 ↔ 269PROSITE-ProRule annotation
    Glycosylationi415 – 4151N-linked (GlcNAc...)1 Publication
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi461 – 4611N-linked (GlcNAc...)1 Publication
    Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi585 – 5851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi589 – 5891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi689 – 6891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    This protein undergoes proteolytic processing.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP35822.
    PaxDbiP35822.
    PRIDEiP35822.

    PTM databases

    PhosphoSiteiP35822.

    Miscellaneous databases

    PMAP-CutDBP35822.

    Expressioni

    Tissue specificityi

    High levels in liver and kidney. Lower levels in lung, brain and heart. Not seen in spleen and testis.

    Developmental stagei

    Developmentally regulated with highest expression found in developing areas or in areas capable of developmental plasticity.

    Gene expression databases

    ArrayExpressiP35822.
    BgeeiP35822.
    CleanExiMM_PTPRK.
    GenevestigatoriP35822.

    Interactioni

    Protein-protein interaction databases

    IntActiP35822. 1 interaction.
    MINTiMINT-4109163.

    Structurei

    3D structure databases

    ProteinModelPortaliP35822.
    SMRiP35822. Positions 32-595, 876-1456.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 752727ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini775 – 1457683CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei753 – 77422HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 193164MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini195 – 28086Ig-like C2-typeAdd
    BLAST
    Domaini293 – 38896Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini391 – 48797Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini490 – 594105Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini595 – 68894Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini899 – 1159261Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1191 – 1453263Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1100 – 11067Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 MAM domain.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00640000091300.
    HOGENOMiHOG000049029.
    HOVERGENiHBG062785.
    InParanoidiP35822.
    KOiK06776.
    OMAiYRDGYQR.
    OrthoDBiEOG70KGNP.
    PhylomeDBiP35822.
    TreeFamiTF312900.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    3.90.190.10. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR000998. MAM_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF00629. MAM. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00020. MAMDOMAIN.
    PR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 3 hits.
    SM00409. IG. 1 hit.
    SM00137. MAM. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    SSF49899. SSF49899. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS50853. FN3. 3 hits.
    PS50835. IG_LIKE. 1 hit.
    PS00740. MAM_1. 1 hit.
    PS50060. MAM_2. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P35822-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVAAAALPA FVALWLLYPW PLLGSALGQF SAGGCTFDDG PGACDYHQDL     50
    YDDFEWVHVS AQEPHYLPPE MPQGSYMVVD SSNHDPGEKA RLQLPTMKEN 100
    DTHCIDFSYL LYSQKGLNPG TLNILVRVNK GPLANPIWNV TGFTGRDWLR 150
    AELAVSTFWP NEYQVIFEAE VSGGRSGYIA IDDIQVLSYP CDKSPHFLRL 200
    GDVEVNAGQN ATFQCIATGR DAVHNKLWLQ RRNGEDIPVA QTKNINHRRF 250
    AASFRLQEVT KTDQDLYRCV TQSERGSGVS NFAQLIVREP PRPIAPPQLL 300
    GVGPTYLLIQ LNANSIIGDG PIILKEVEYR MTSGSWTETH AVNAPTYKLW 350
    HLDPDTEYEI RVLLTRPGEG GTGLPGPPLI TRTKCAEPMR TPKTLKIAEI 400
    QARRIAVDWE SLGYNITRCH TFNVTICYHY FRGHNESRAD CLDMDPKAPQ 450
    HVVNHLPPYT NVSLKMILTN PEGRKESEET IIQTDEDVPG PVPVKSLQGT 500
    SFENKIFLNW KEPLEPNGII TQYEVSYSSI RSFDPAVPVA GPPQTVSNLW 550
    NSTHHVFMHL HPGTTYQFFI RASTVKGFGP ATAINVTTNI SAPSLPDYEG 600
    VDASLNETAT TITVLLRPAQ AKGAPISAYQ IVVEQLHPHR TKREAGAMEC 650
    YQVPVTYQNA LSGGAPYYFA AELPPGNLPE PAPFTVGDNR TYKGFWNPPL 700
    APRKGYNIYF QAMSSVEKET KTQCVRIATK AAATEEPEVI PDPAKQTDRV 750
    VKIAGISAGI LVFILLLLVV IVIVKKSKLA KKRKDAMGNT RQEMTHMVNA 800
    MDRSYADQST LHAEDPLSLT FMDQHNFSPR LPNDPLVPTA VLDENHSATA 850
    ESSRLLDVPR YLCEGTESPY QTGQLHPAIR VADLLQHINL MKTSDSYGFK 900
    EEYESFFEGQ SASWDVAKKD QNRAKNRYGN IIAYDHSRVI LQPVEDDPSS 950
    DYINANYIDI WLYRDGYQRP SHYIATQGPV HETVYDFWRM VWQEQSACIV 1000
    MVTNLVEVGR VKCYKYWPDD TEVYGDFKVT CVEMEPLAEY VVRTFTLERR 1050
    GYNEIREVKQ FHFTGWPDHG VPYHATGLLS FIRRVKLSNP PSAGPIVVHC 1100
    SAGAGRTGCY IVIDIMLDMA EREGVVDIYN CVKALRSRRI NMVQTEEQYI 1150
    FIHDAILEAC LCGETAIPVC EFKAAYFDMI RIDSQTNSSH LKDEFQTLNS 1200
    VTPRLQAEDC SIACLPRNHD KNRFMDMLPP DRCLPFLITI DGESSNYINA 1250
    ALMDSYRQPA AFIVTQYPLP NTVKDFWRLV YDYGCTSIVM LNEVDLSQGC 1300
    PQYWPEEGML RYGPIQVECM SCSMDCDVIN RIFRICNLTR PQEGYLMVQQ 1350
    FQYLGWASHR EVPGSKRSFL KLILQVEKWQ EECEEGEGRT IIHCLNGGGR 1400
    SGMFCAIGIV VEMVKRQNVV DVFHAVKTLR NSKPNMVEAP EQYRFCYDVA 1450
    LEYLESS 1457
    Length:1,457
    Mass (Da):164,186
    Last modified:June 1, 1994 - v1
    Checksum:i19D4B99B7ECE8605
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10106 mRNA. Translation: AAA40021.1.
    CCDSiCCDS35874.1.
    PIRiA48066.
    RefSeqiNP_033009.1. NM_008983.2.
    UniGeneiMm.332303.

    Genome annotation databases

    EnsembliENSMUST00000166468; ENSMUSP00000126279; ENSMUSG00000019889.
    GeneIDi19272.
    KEGGimmu:19272.
    UCSCiuc007esk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10106 mRNA. Translation: AAA40021.1 .
    CCDSi CCDS35874.1.
    PIRi A48066.
    RefSeqi NP_033009.1. NM_008983.2.
    UniGenei Mm.332303.

    3D structure databases

    ProteinModelPortali P35822.
    SMRi P35822. Positions 32-595, 876-1456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P35822. 1 interaction.
    MINTi MINT-4109163.

    PTM databases

    PhosphoSitei P35822.

    Proteomic databases

    MaxQBi P35822.
    PaxDbi P35822.
    PRIDEi P35822.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000166468 ; ENSMUSP00000126279 ; ENSMUSG00000019889 .
    GeneIDi 19272.
    KEGGi mmu:19272.
    UCSCi uc007esk.1. mouse.

    Organism-specific databases

    CTDi 5796.
    MGIi MGI:103310. Ptprk.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00640000091300.
    HOGENOMi HOG000049029.
    HOVERGENi HBG062785.
    InParanoidi P35822.
    KOi K06776.
    OMAi YRDGYQR.
    OrthoDBi EOG70KGNP.
    PhylomeDBi P35822.
    TreeFami TF312900.

    Miscellaneous databases

    ChiTaRSi PTPRK. mouse.
    NextBioi 296162.
    PMAP-CutDB P35822.
    PROi P35822.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35822.
    Bgeei P35822.
    CleanExi MM_PTPRK.
    Genevestigatori P35822.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    3.90.190.10. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR000998. MAM_dom.
    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. 2 hits.
    PF00629. MAM. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00020. MAMDOMAIN.
    PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 3 hits.
    SM00409. IG. 1 hit.
    SM00137. MAM. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    SSF49899. SSF49899. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS50853. FN3. 3 hits.
    PS50835. IG_LIKE. 1 hit.
    PS00740. MAM_1. 1 hit.
    PS50060. MAM_2. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region."
      Jiang Y.P., Wang H., D'Eustachio P., Musacchio J.M., Schlessinger J., Sap J.
      Mol. Cell. Biol. 13:2942-2951(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: RI.
      Tissue: Brain.
    2. "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-139; ASN-415 AND ASN-461.

    Entry informationi

    Entry nameiPTPRK_MOUSE
    AccessioniPrimary (citable) accession number: P35822
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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