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Q92729

- PTPRU_HUMAN

UniProt

Q92729 - PTPRU_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase U

Gene

PTPRU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1053 – 10531SubstrateSequence Analysis
    Active sitei1085 – 10851Phosphocysteine intermediateBy similarity
    Binding sitei1129 – 11291SubstrateBy similarity
    Active sitei1380 – 13801Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB
    4. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: UniProtKB
    2. cell adhesion Source: UniProtKB
    3. cell differentiation Source: UniProtKB-KW
    4. homotypic cell-cell adhesion Source: Ensembl
    5. negative regulation of cell migration Source: UniProtKB
    6. negative regulation of cell proliferation Source: UniProtKB
    7. organ regeneration Source: Ensembl
    8. peptidyl-tyrosine dephosphorylation Source: GOC
    9. protein dephosphorylation Source: UniProtKB
    10. protein localization to cell surface Source: UniProtKB
    11. response to glucocorticoid Source: Ensembl
    12. single organismal cell-cell adhesion Source: UniProtKB
    13. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase, Receptor

    Keywords - Biological processi

    Cell adhesion, Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase U (EC:3.1.3.48)
    Short name:
    R-PTP-U
    Alternative name(s):
    Pancreatic carcinoma phosphatase 2
    Short name:
    PCP-2
    Protein-tyrosine phosphatase J
    Short name:
    PTP-J
    Short name:
    hPTP-J
    Protein-tyrosine phosphatase pi
    Short name:
    PTP pi
    Protein-tyrosine phosphatase receptor omicron
    Short name:
    PTP-RO
    Receptor-type protein-tyrosine phosphatase psi
    Short name:
    R-PTP-psi
    Gene namesi
    Name:PTPRU
    Synonyms:FMI, PCP2, PTPRO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9683. PTPRU.

    Subcellular locationi

    Cell junction 1 Publication. Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. integral component of plasma membrane Source: UniProtKB
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1085 – 10851C → S: Loss of phosphatase activity toward CTNNB1. Loss of the inhibitory effect on CTNNB1 transcriptional activity without effect on interaction with CTNNB1; when associated with S-1380. 2 Publications
    Mutagenesisi1380 – 13801C → S: No effect on phosphatase activity toward CTNNB1. Loss of the inhibitory effect on CTNNB1 transcriptional activity without effect on interaction with CTNNB1; when associated with S-1085. 2 Publications

    Organism-specific databases

    PharmGKBiPA34028.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 14461428Receptor-type tyrosine-protein phosphatase UPRO_0000371658Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi210 ↔ 264Sequence Analysis
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
    Modified residuei848 – 8481Phosphoserine2 Publications
    Modified residuei853 – 8531Phosphoserine2 Publications

    Post-translational modificationi

    The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain By similarity. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed.By similarity1 Publication
    N-glycosylated.1 Publication
    Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ92729.
    PRIDEiQ92729.

    Expressioni

    Tissue specificityi

    High levels in brain, pancreas, and skeletal muscle; less in colon, kidney, liver, stomach, and uterus; not expressed in placenta and spleen. Also detected in heart, prostate, lung, thymus, testis and ovary. Ubiquitously expressed in brain. Expressed by hematopoietic stem cells.4 Publications

    Developmental stagei

    Expressed in fetal brain, lung and kidney.1 Publication

    Inductioni

    Up-regulated upon cell contact (at protein level). Down-regulated by phorbol ester (at protein level) and calcium ionophore but up-regulated by phorbol ester in megakaryocytic cells (PubMed:10397721).4 Publications

    Gene expression databases

    ArrayExpressiQ92729.
    BgeeiQ92729.
    CleanExiHS_PCP2.
    HS_PTPRU.
    GenevestigatoriQ92729.

    Organism-specific databases

    HPAiCAB011476.
    HPA039832.

    Interactioni

    Subunit structurei

    Forms homooligomeric complexes which mediate cell homotypic adhesion Probable. Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT. May interact with AP3B1.4 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KITP107212EBI-7052301,EBI-1379503

    Protein-protein interaction databases

    BioGridi115386. 3 interactions.
    IntActiQ92729. 1 interaction.
    MINTiMINT-1349420.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92729.
    SMRiQ92729. Positions 22-591, 871-1440.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 749731ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini771 – 1446676CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei750 – 77021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 188164MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini190 – 27586Ig-like C2-typeAdd
    BLAST
    Domaini288 – 38396Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini386 – 48499Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini485 – 591107Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 67483Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini888 – 1144257Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1176 – 1439264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni771 – 887117Mediates interaction with CTNNB1By similarityAdd
    BLAST
    Regioni1085 – 10917Substrate 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.
    HOVERGENiHBG062785.
    KOiK16662.
    OMAiLTDSYTR.
    OrthoDBiEOG70KGNP.
    PhylomeDBiQ92729.
    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.
    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.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92729-1) [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

    MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ     50
    WEQVRIHPGT RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV 100
    QFSYFLYSRD GHSPGTLGVY VRVNGGPLGS AVWNMTGSHG RQWHQAELAV 150
    STFWPNEYQV LFEALISPDR RGYMGLDDIL LLSYPCAKAP HFSRLGDVEV 200
    NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI SHRRFLATFP 250
    LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 300
    YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD 350
    TEYEISVLLT RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL 400
    TLQWEPLGYN VTRCHTYTVS LCYHYTLGSS HNQTIRECVK TEQGVSRYTI 450
    KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ TDEDVPSGIA AESLTFTPLE 500
    DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR RTISKLRNET 550
    YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 600
    LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP 650
    LTFEAALARG LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK 700
    AYLIYFQAAS HLKGETRLNC IRIARKAACK ESKRPLEVSQ RSEEMGLILG 750
    ICAGGLAVLI LLLGAIIVII RKGRDHYAYS YYPKPVNMTK ATVNYRQEKT 800
    HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS GGVTEASSLL 850
    GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES 900
    FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID 950
    GYHRSNHFIA TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR 1000
    YWPEDSDTYG DIKIMLVKTE TLAEYVVRTF ALERRGYSAR HEVRQFHFTA 1050
    WPEHGVPYHA TGLLAFIRRV KASTPPDAGP IVIHCSAGTG RTGCYIVLDV 1100
    MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA ILEACLCGET 1150
    TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL 1200
    PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT 1250
    LHPLQSTTPD FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY 1300
    GLMEVEFMSG TADEDLVARV FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT 1350
    PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC LNGGGRSGTF CACATVLEMI 1400
    RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL EGLESR 1446
    Length:1,446
    Mass (Da):162,423
    Last modified:May 5, 2009 - v2
    Checksum:i76F9BD6EFABE8663
    GO
    Isoform 2 (identifier: Q92729-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         774-783: Missing.

    Show »
    Length:1,436
    Mass (Da):161,107
    Checksum:iF88BB75170BF3676
    GO
    Isoform 3 (identifier: Q92729-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         774-783: Missing.
         993-995: Missing.

    Show »
    Length:1,433
    Mass (Da):160,795
    Checksum:iBA085FF7C36BB2A8
    GO
    Isoform 4 (identifier: Q92729-4) [UniParc]FASTAAdd to Basket

    Also known as: PTPRO

    The sequence of this isoform differs from the canonical sequence as follows:
         774-783: Missing.
         950-950: D → DIRINRE
         1329-1330: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,440
    Mass (Da):161,648
    Checksum:iEDE5C3CF8C8C9DA0
    GO

    Sequence cautioni

    The sequence CAA65016.1 differs from that shown. Reason: Several sequencing problems.
    The sequence CAA65832.1 differs from that shown. Reason: Several sequencing problems.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti359 – 3602LT → S in AAC51938. (PubMed:9434160)Curated
    Sequence conflicti401 – 4011T → A in AAC51938. (PubMed:9434160)Curated
    Sequence conflicti715 – 7151E → D in AAB51343. (PubMed:9070223)Curated
    Sequence conflicti840 – 8412SG → GW in AAC51938. (PubMed:9434160)Curated
    Sequence conflicti1215 – 12151P → A in AAB07074. 1 PublicationCurated
    Sequence conflicti1245 – 12451A → R in AAC51938. (PubMed:9434160)Curated
    Sequence conflicti1399 – 13991M → I in AAC51938. (PubMed:9434160)Curated
    Sequence conflicti1436 – 14361A → V in AAB07074. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601T → N.
    Corresponds to variant rs35332573 [ dbSNP | Ensembl ].
    VAR_055075
    Natural varianti471 – 4711R → L.
    Corresponds to variant rs35745442 [ dbSNP | Ensembl ].
    VAR_055076
    Natural varianti830 – 8301H → Y in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035650
    Natural varianti835 – 8351R → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035651
    Natural varianti856 – 8561R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035652
    Natural varianti940 – 9401N → S.
    Corresponds to variant rs2235937 [ dbSNP | Ensembl ].
    VAR_055077

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei774 – 78310Missing in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_037082
    Alternative sequencei950 – 9501D → DIRINRE in isoform 4. 1 PublicationVSP_037083
    Alternative sequencei993 – 9953Missing in isoform 3. 1 PublicationVSP_037084
    Alternative sequencei1329 – 13302Missing in isoform 4. 1 PublicationVSP_037085

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95712 mRNA. Translation: CAA65016.1. Sequence problems.
    X97198 mRNA. Translation: CAA65832.1. Sequence problems.
    U73727 mRNA. Translation: AAB51343.1.
    U71075 mRNA. Translation: AAC51938.1.
    U60289 Genomic DNA. Translation: AAB07074.1.
    AL645859, AL049570, AL590729 Genomic DNA. Translation: CAH72393.1.
    AL645859, AL049570, AL590729 Genomic DNA. Translation: CAH72394.1.
    AL590729, AL049570, AL645859 Genomic DNA. Translation: CAI14331.1.
    AL590729, AL049570, AL645859 Genomic DNA. Translation: CAI14332.1.
    AL049570, AL590729, AL645859 Genomic DNA. Translation: CAI20946.1.
    AL049570, AL590729, AL645859 Genomic DNA. Translation: CAI20947.1.
    CH471059 Genomic DNA. Translation: EAX07651.1.
    CH471059 Genomic DNA. Translation: EAX07652.1.
    BC146655 mRNA. Translation: AAI46656.1.
    AB208855 mRNA. Translation: BAD92092.1.
    CCDSiCCDS334.1. [Q92729-1]
    CCDS335.1. [Q92729-2]
    CCDS44098.2. [Q92729-4]
    CCDS53290.1. [Q92729-3]
    PIRiJC5290.
    S72441.
    RefSeqiNP_001181930.1. NM_001195001.1. [Q92729-3]
    NP_005695.3. NM_005704.4. [Q92729-1]
    NP_573438.3. NM_133177.3. [Q92729-4]
    NP_573439.2. NM_133178.3. [Q92729-2]
    UniGeneiHs.19718.

    Genome annotation databases

    EnsembliENST00000345512; ENSP00000334941; ENSG00000060656. [Q92729-1]
    ENST00000373779; ENSP00000362884; ENSG00000060656. [Q92729-2]
    ENST00000428026; ENSP00000392332; ENSG00000060656. [Q92729-3]
    ENST00000460170; ENSP00000432906; ENSG00000060656. [Q92729-4]
    GeneIDi10076.
    KEGGihsa:10076.
    UCSCiuc001bru.3. human. [Q92729-1]
    uc001brw.3. human. [Q92729-2]
    uc009vtq.3. human. [Q92729-4]
    uc009vtr.3. human. [Q92729-3]

    Polymorphism databases

    DMDMi229462800.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95712 mRNA. Translation: CAA65016.1 . Sequence problems.
    X97198 mRNA. Translation: CAA65832.1 . Sequence problems.
    U73727 mRNA. Translation: AAB51343.1 .
    U71075 mRNA. Translation: AAC51938.1 .
    U60289 Genomic DNA. Translation: AAB07074.1 .
    AL645859 , AL049570 , AL590729 Genomic DNA. Translation: CAH72393.1 .
    AL645859 , AL049570 , AL590729 Genomic DNA. Translation: CAH72394.1 .
    AL590729 , AL049570 , AL645859 Genomic DNA. Translation: CAI14331.1 .
    AL590729 , AL049570 , AL645859 Genomic DNA. Translation: CAI14332.1 .
    AL049570 , AL590729 , AL645859 Genomic DNA. Translation: CAI20946.1 .
    AL049570 , AL590729 , AL645859 Genomic DNA. Translation: CAI20947.1 .
    CH471059 Genomic DNA. Translation: EAX07651.1 .
    CH471059 Genomic DNA. Translation: EAX07652.1 .
    BC146655 mRNA. Translation: AAI46656.1 .
    AB208855 mRNA. Translation: BAD92092.1 .
    CCDSi CCDS334.1. [Q92729-1 ]
    CCDS335.1. [Q92729-2 ]
    CCDS44098.2. [Q92729-4 ]
    CCDS53290.1. [Q92729-3 ]
    PIRi JC5290.
    S72441.
    RefSeqi NP_001181930.1. NM_001195001.1. [Q92729-3 ]
    NP_005695.3. NM_005704.4. [Q92729-1 ]
    NP_573438.3. NM_133177.3. [Q92729-4 ]
    NP_573439.2. NM_133178.3. [Q92729-2 ]
    UniGenei Hs.19718.

    3D structure databases

    ProteinModelPortali Q92729.
    SMRi Q92729. Positions 22-591, 871-1440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115386. 3 interactions.
    IntActi Q92729. 1 interaction.
    MINTi MINT-1349420.

    Chemistry

    ChEMBLi CHEMBL1961785.

    Polymorphism databases

    DMDMi 229462800.

    Proteomic databases

    PaxDbi Q92729.
    PRIDEi Q92729.

    Protocols and materials databases

    DNASUi 10076.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345512 ; ENSP00000334941 ; ENSG00000060656 . [Q92729-1 ]
    ENST00000373779 ; ENSP00000362884 ; ENSG00000060656 . [Q92729-2 ]
    ENST00000428026 ; ENSP00000392332 ; ENSG00000060656 . [Q92729-3 ]
    ENST00000460170 ; ENSP00000432906 ; ENSG00000060656 . [Q92729-4 ]
    GeneIDi 10076.
    KEGGi hsa:10076.
    UCSCi uc001bru.3. human. [Q92729-1 ]
    uc001brw.3. human. [Q92729-2 ]
    uc009vtq.3. human. [Q92729-4 ]
    uc009vtr.3. human. [Q92729-3 ]

    Organism-specific databases

    CTDi 10076.
    GeneCardsi GC01P029569.
    H-InvDB HIX0000346.
    HGNCi HGNC:9683. PTPRU.
    HPAi CAB011476.
    HPA039832.
    MIMi 602454. gene.
    neXtProti NX_Q92729.
    PharmGKBi PA34028.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOVERGENi HBG062785.
    KOi K16662.
    OMAi LTDSYTR.
    OrthoDBi EOG70KGNP.
    PhylomeDBi Q92729.
    TreeFami TF312900.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.

    Miscellaneous databases

    ChiTaRSi PTPRU. human.
    GeneWikii PTPRU.
    GenomeRNAii 10076.
    NextBioi 38089.
    PROi Q92729.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92729.
    Bgeei Q92729.
    CleanExi HS_PCP2.
    HS_PTPRU.
    Genevestigatori Q92729.

    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.
    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.
    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. "Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase."
      Crossland S., Smith P.D., Crompton M.R.
      Biochem. J. 319:249-254(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Mammary gland.
    2. "Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family."
      Wang H.-Y., Lian Z., Lerch M.M., Chen Z., Xie W., Ullrich A.
      Oncogene 12:2555-2562(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Pancreas.
    3. "Molecular cloning and characterization of a novel human receptor protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene expression by PMA and calcium ionophore in Jurkat T lymphoma cells."
      Wang B., Kishihara K., Zhang D., Hara H., Nomoto K.
      Biochem. Biophys. Res. Commun. 231:77-81(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION.
      Tissue: Skeletal muscle.
    4. "Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells."
      Avraham S., London R., Tulloch G.A., Ellis M., Fu Y., Jiang S., White R.A., Painter C., Steinberger A.A., Avraham H.
      Gene 204:5-16(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Brain.
    5. "Cloning and expression of R-PTP-psi, a novel receptor protein tyrosine phosphatase related to the homophilic binding R-PTP-kappa and -mu."
      Banville D., Masson S., L'Abbe D., Stocco R., Shen S.-H.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1446 (ISOFORM 2).
      Tissue: Brain.
    10. "Transcriptional regulation of a receptor protein tyrosine phosphatase gene hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T lymphoma cells."
      Wang B., Kishihara K., Zhang D., Sakamoto T., Nomoto K.
      Biochim. Biophys. Acta 1450:331-340(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and is associated with the c-Kit receptor."
      Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H.
      Blood 94:539-549(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, PROTEOLYTIC PROCESSING, INDUCTION BY PHORBOL ESTER.
    12. "Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin."
      Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., Wang H.-Y.
      Biochemistry 41:15854-15860(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTNNB1, INDUCTION, MUTAGENESIS OF CYS-1085 AND CYS-1380.
    13. "Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and increases E-cadherin-dependent cell adhesion."
      Yan H.-X., Yang W., Zhang R., Chen L., Tang L., Zhai B., Liu S.-Q., Cao H.-F., Man X.-B., Wu H.-P., Wu M.-C., Wang H.-Y.
      J. Biol. Chem. 281:15423-15433(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF CYS-1085 AND CYS-1380.
    14. "Involvement of beta3A subunit of adaptor protein-3 in intracellular trafficking of receptor-like protein tyrosine phosphatase PCP-2."
      Dong H., Yuan H., Jin W., Shen Y., Xu X., Wang H.-Y.
      Acta Biochim. Biophys. Sin. 39:540-546(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP3B1.
    15. "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-848 AND SER-853, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-830; TRP-835 AND CYS-856.

    Entry informationi

    Entry nameiPTPRU_HUMAN
    AccessioniPrimary (citable) accession number: Q92729
    Secondary accession number(s): A6H8L1
    , O00197, P78399, Q59HA4, Q5SYU4, Q5SYU5, Q92735, Q92850
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 143 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3