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Q9HD43

- PTPRH_HUMAN

UniProt

Q9HD43 - PTPRH_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase H

Gene

PTPRH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    May contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion-associated substrates and thus negatively regulating integrin-promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of p130cas, focal adhesion kinase and c-Src. Reduces migratory activity of Jurkat cells.4 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Regulated by reversible dimerization. Dimerization reduces its catalytic activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1020 – 10201Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. peptidyl-tyrosine dephosphorylation Source: GOC
    3. protein dephosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase H (EC:3.1.3.48)
    Short name:
    R-PTP-H
    Alternative name(s):
    Stomach cancer-associated protein tyrosine phosphatase 1
    Short name:
    SAP-1
    Transmembrane-type protein-tyrosine phosphatase type H
    Gene namesi
    Name:PTPRH
    Synonyms:SAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9672. PTPRH.

    Subcellular locationi

    Membrane Curated; Single-pass type I membrane protein Curated. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi986 – 9861D → A: Loss of activity. Acts as a dominant negative mutant. 1 Publication
    Mutagenesisi1020 – 10201C → S: Loss of activity. No induction of apoptosis. 2 Publications

    Organism-specific databases

    PharmGKBiPA34017.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 11151088Receptor-type tyrosine-protein phosphatase HPRO_0000318950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9HD43.
    PRIDEiQ9HD43.

    PTM databases

    PhosphoSiteiQ9HD43.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the brain, spleen and liver and at lower levels in the heart and stomach. Expressed in pancreatic and colorectal cancer cells, but not in normal pancreas or colon. Expression in hepatocellular carcinoma is related to the differentiation status of the tumor and expression is inversely related to tumor aggressiveness.3 Publications

    Inductioni

    Induced at the early stage of hepatocellular carcinoma and is suppressed at later stages.1 Publication

    Gene expression databases

    ArrayExpressiQ9HD43.
    BgeeiQ9HD43.
    CleanExiHS_PTPRH.
    GenevestigatoriQ9HD43.

    Organism-specific databases

    HPAiHPA042300.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked Probable. Interacts with LCK.2 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GHRP109124EBI-1267176,EBI-286316

    Protein-protein interaction databases

    BioGridi111758. 4 interactions.
    IntActiQ9HD43. 5 interactions.
    MINTiMINT-1349530.
    STRINGi9606.ENSP00000365528.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HD43.
    SMRiQ9HD43. Positions 28-561, 569-651, 800-1081.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 754727ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini776 – 1115340CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei755 – 77521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 12190Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini122 – 20988Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini210 – 29990Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini300 – 38788Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini388 – 47790Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini478 – 56386Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 666103Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini665 – 74985Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini820 – 1079260Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The extracellular domain mediates homodimerization. One or more cysteines in the extracellular domain is essential for the formation of dimers probably by forming a disulfide bond.
    The cytoplasmic domain mediates the interaction with LCK.

    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.
    HOGENOMiHOG000170539.
    HOVERGENiHBG108307.
    InParanoidiQ9HD43.
    KOiK18034.
    OMAiFSVWAEK.
    OrthoDBiEOG7PCJFZ.
    PhylomeDBiQ9HD43.
    TreeFamiTF351926.

    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.
    IPR028855. R-PTP-H.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PANTHERiPTHR19134:SF254. PTHR19134:SF254. 1 hit.
    PfamiPF00041. fn3. 7 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 7 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 4 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS50853. FN3. 7 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HD43-1) [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

    MAGAGGGLGV WGNLVLLGLC SWTGARAPAP NPGRNLTVET QTTSSISLSW     50
    EVPDGLDSQN SNYWVQCTGD GGTTETRNTT ATNVTVDGLG PGSLYTCSVW 100
    VEKDGVNSSV GTVTTATAPN PVRNLRVEAQ TNSSIALTWE VPDGPDPQNS 150
    TYGVEYTGDG GRAGTRSTAH TNITVDGLEP GCLYAFSMWV GKNGINSSRE 200
    TRNATTAHNP VRNLRVEAQT TSSISLSWEV PDGTDPQNST YCVQCTGDGG 250
    RTETRNTTDT RVTVDGLGPG SLYTCSVWVE KDGVNSSVEI VTSATAPNPV 300
    RNLTVEAQTN SSIALTWEVP DGPDPQNSTY GVEYTGDGGR AGTRSTAHTN 350
    ITVDRLEPGC LYVFSVWVGK NGINSSRETR NATTAPNPVR NLHMETQTNS 400
    SIALCWEVPD GPYPQDYTYW VEYTGDGGGT ETRNTTNTSV TAERLEPGTL 450
    YTFSVWAEKN GARGSRQNVS ISTVPNAVTS LSKQDWTNST IALRWTAPQG 500
    PGQSSYSYWV SWVREGMTDP RTQSTSGTDI TLKELEAGSL YHLTVWAERN 550
    EVRGYNSTLT AATAPNEVTD LQNETQTKNS VMLWWKAPGD PHSQLYVYWV 600
    QWASKGHPRR GQDPQANWVN QTSRTNETWY KVEALEPGTL YNFTVWAERN 650
    DVASSTQSLC ASTYPDTVTI TSCVSTSAGY GVNLIWSCPQ GGYEAFELEV 700
    GGQRGSQDRS SCGEAVSVLG LGPARSYPAT ITTIWDGMKV VSHSVVCHTE 750
    SAGVIAGAFV GILLFLILVG LLIFFLKRRN KKKQQKPELR DLVFSSPGDI 800
    PAEDFADHVR KNERDSNCGF ADKYQQLSLV GHSQSQMVAS ASENNAKNRY 850
    RNVLPYDWSR VPLKPIHEEP GSDYINASFM PGLWSPQEFI ATQGPLPQTV 900
    GDFWRLVWEQ QSHTLVMLTN CMEAGRVKCE HYWPLDSQPC THGHLRVTLV 950
    GEEVMENWTV RELLLLQVEE QKTLSVRQFH YQAWPDHGVP SSPDTLLAFW 1000
    RMLRQWLDQT MEGGPPIVHC SAGVGRTGTL IALDVLLRQL QSEGLLGPFS 1050
    FVRKMRESRP LMVQTEAQYV FLHQCILRFL QQSAQAPAEK EVPYEDVENL 1100
    IYENVAAIQA HKLEV 1115
    Length:1,115
    Mass (Da):122,352
    Last modified:May 18, 2010 - v3
    Checksum:iA7A1AB24CFCD3846
    GO
    Isoform 2 (identifier: Q9HD43-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-261: Missing.

    Show »
    Length:937
    Mass (Da):103,483
    Checksum:i5E579E14580244FF
    GO
    Isoform 3 (identifier: Q9HD43-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         126-303: Missing.

    Show »
    Length:937
    Mass (Da):103,412
    Checksum:iA444EEE28EA7324C
    GO

    Sequence cautioni

    The sequence BAA03645.2 differs from that shown. Reason: Frameshift at positions 213, 244, 264, 287 and 291.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941A → T in BAA03645. (PubMed:8294459)Curated
    Sequence conflicti422 – 4221E → G in BAA03645. (PubMed:8294459)Curated
    Sequence conflicti951 – 9511G → D in AAI11716. (PubMed:15489334)Curated
    Sequence conflicti1109 – 11091Q → K in AAI11716. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti232 – 2321D → N.
    Corresponds to variant rs55870162 [ dbSNP | Ensembl ].
    VAR_061762
    Natural varianti243 – 2431V → I.
    Corresponds to variant rs45535035 [ dbSNP | Ensembl ].
    VAR_061763
    Natural varianti348 – 3481H → Y.1 Publication
    Corresponds to variant rs2288515 [ dbSNP | Ensembl ].
    VAR_038918
    Natural varianti543 – 5431L → F.
    Corresponds to variant rs16986309 [ dbSNP | Ensembl ].
    VAR_038919
    Natural varianti781 – 7811K → N.
    Corresponds to variant rs2288523 [ dbSNP | Ensembl ].
    VAR_038920
    Natural varianti823 – 8231K → E.2 Publications
    Corresponds to variant rs890870 [ dbSNP | Ensembl ].
    VAR_038921
    Natural varianti831 – 8311G → D.
    Corresponds to variant rs36092369 [ dbSNP | Ensembl ].
    VAR_061764
    Natural varianti1076 – 10761I → V.
    Corresponds to variant rs2288419 [ dbSNP | Ensembl ].
    VAR_038922

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei84 – 261178Missing in isoform 2. 1 PublicationVSP_031318Add
    BLAST
    Alternative sequencei126 – 303178Missing in isoform 3. CuratedVSP_054222Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D15049 mRNA. Translation: BAA03645.2. Frameshift.
    AF275150
    , AF275131, AF275132, AF275133, AF275134, AF275135, AF275136, AF275137, AF275138, AF275139, AF275140, AF275141, AF275142, AF275143, AF275144, AF275145, AF275146, AF275147, AF275148, AF275149 Genomic DNA. Translation: AAF91411.1.
    AC010327 Genomic DNA. No translation available.
    BC111715 mRNA. Translation: AAI11716.1.
    BC111716 mRNA. Translation: AAI11717.1.
    CCDSiCCDS33110.1. [Q9HD43-1]
    CCDS54321.1. [Q9HD43-3]
    PIRiA49724.
    UniGeneiHs.179770.

    Genome annotation databases

    EnsembliENST00000263434; ENSP00000263434; ENSG00000080031. [Q9HD43-3]
    ENST00000376350; ENSP00000365528; ENSG00000080031. [Q9HD43-1]
    KEGGihsa:5794.
    UCSCiuc002qjq.3. human. [Q9HD43-1]

    Polymorphism databases

    DMDMi296452983.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D15049 mRNA. Translation: BAA03645.2 . Frameshift.
    AF275150
    , AF275131 , AF275132 , AF275133 , AF275134 , AF275135 , AF275136 , AF275137 , AF275138 , AF275139 , AF275140 , AF275141 , AF275142 , AF275143 , AF275144 , AF275145 , AF275146 , AF275147 , AF275148 , AF275149 Genomic DNA. Translation: AAF91411.1 .
    AC010327 Genomic DNA. No translation available.
    BC111715 mRNA. Translation: AAI11716.1 .
    BC111716 mRNA. Translation: AAI11717.1 .
    CCDSi CCDS33110.1. [Q9HD43-1 ]
    CCDS54321.1. [Q9HD43-3 ]
    PIRi A49724.
    UniGenei Hs.179770.

    3D structure databases

    ProteinModelPortali Q9HD43.
    SMRi Q9HD43. Positions 28-561, 569-651, 800-1081.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111758. 4 interactions.
    IntActi Q9HD43. 5 interactions.
    MINTi MINT-1349530.
    STRINGi 9606.ENSP00000365528.

    PTM databases

    PhosphoSitei Q9HD43.

    Polymorphism databases

    DMDMi 296452983.

    Proteomic databases

    PaxDbi Q9HD43.
    PRIDEi Q9HD43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263434 ; ENSP00000263434 ; ENSG00000080031 . [Q9HD43-3 ]
    ENST00000376350 ; ENSP00000365528 ; ENSG00000080031 . [Q9HD43-1 ]
    KEGGi hsa:5794.
    UCSCi uc002qjq.3. human. [Q9HD43-1 ]

    Organism-specific databases

    CTDi 5794.
    GeneCardsi GC19M055692.
    HGNCi HGNC:9672. PTPRH.
    HPAi HPA042300.
    MIMi 602510. gene.
    neXtProti NX_Q9HD43.
    PharmGKBi PA34017.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000170539.
    HOVERGENi HBG108307.
    InParanoidi Q9HD43.
    KOi K18034.
    OMAi FSVWAEK.
    OrthoDBi EOG7PCJFZ.
    PhylomeDBi Q9HD43.
    TreeFami TF351926.

    Miscellaneous databases

    GenomeRNAii 5794.
    NextBioi 22560.
    PROi Q9HD43.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HD43.
    Bgeei Q9HD43.
    CleanExi HS_PTPRH.
    Genevestigatori Q9HD43.

    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.
    IPR028855. R-PTP-H.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    PANTHERi PTHR19134:SF254. PTHR19134:SF254. 1 hit.
    Pfami PF00041. fn3. 7 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 7 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 4 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50853. FN3. 7 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 of a human transmembrane-type protein tyrosine phosphatase and its expression in gastrointestinal cancers."
      Matozaki T., Suzuki T., Uchida T., Inazawa J., Ariyama T., Matsuda K., Horita K., Noguchi H., Mizuno H., Sakamoto C., Kasuga M.
      J. Biol. Chem. 269:2075-2081(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT GLU-823.
    2. "Gene for the human transmembrane-type protein tyrosine phosphatase H (PTPRH): genomic structure, fine-mapping and its exclusion as a candidate for Peutz-Jeghers syndrome."
      Marneros A.G., Mehenni H., Reichenberger E., Antonarakis S.E., Krieg T., Olsen B.R.
      Cytogenet. Cell Genet. 92:213-216(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2), VARIANTS TYR-348 AND GLU-823.
    5. "Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130cas."
      Noguchi T., Tsuda M., Takeda H., Takada T., Inagaki K., Yamao T., Fukunaga K., Matozaki T., Kasuga M.
      J. Biol. Chem. 276:15216-15224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-986 AND CYS-1020.
    6. "Induction of apoptosis by stomach cancer-associated protein-tyrosine phosphatase-1."
      Takada T., Noguchi T., Inagaki K., Hosooka T., Fukunaga K., Yamao T., Ogawa W., Matozaki T., Kasuga M.
      J. Biol. Chem. 277:34359-34366(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-1020.
    7. "Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase, with the tyrosine kinase Lck. Roles in regulation of T cell function."
      Ito T., Okazawa H., Maruyama K., Tomizawa K., Motegi S., Ohnishi H., Kuwano H., Kosugi A., Matozaki T.
      J. Biol. Chem. 278:34854-34863(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH LCK.
    8. "Downregulation of stomach cancer-associated protein tyrosine phosphatase-1 (SAP-1) in advanced human hepatocellular carcinoma."
      Nagano H., Noguchi T., Inagaki K., Yoon S., Matozaki T., Itoh H., Kasuga M., Hayashi Y.
      Oncogene 22:4656-4663(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
    9. Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION, DOMAIN.

    Entry informationi

    Entry nameiPTPRH_HUMAN
    AccessioniPrimary (citable) accession number: Q9HD43
    Secondary accession number(s): C9JCH2
    , Q15426, Q2NKN9, Q2NKP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 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 19
      Human chromosome 19: 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