PTPRH_HUMAN » Receptor-type tyrosine-protein phosphatase H

PTPRH_HUMAN » Receptor-type tyrosine-protein phosphatase H
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
PTPRH_HUMAN » Receptor-type tyrosine-protein phosphatase H » R-PTP-H; Stomach cancer-associated protein tyrosine phosphatase 1;SAP-1; Transmembrane-type protein-tyrosine phosphatase type H;
Hydrophobic Thickness 34.8 ± 1.6 Å
Tilt Angle 1 ± 0°
ΔGtransfer -60.9 kcal/mol
ΔGfold -26.8 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 752-777 (749-782)
Pathways none
PDB none
OPM none
Complexes none
Interactions

GHR, Complex: GHR:PTPRH, PubMed

Domains

AA: 30-108, PDBID: 2DKM, Subunit A, Seq Identity:28%, Fibronectin type III domain

AA: 119-195, PDBID: 1TDQ, Subunit A, Seq Identity:27%, Fibronectin type III domain

AA: 209-287, PDBID: 1FNF, Subunit A, Seq Identity:30%, Fibronectin type III domain

AA: 297-377, PDBID: 3LPW, Subunit B, Seq Identity:27%, Fibronectin type III domain

AA: 386-467, PDBID: 1X5G, Subunit A, Seq Identity:30%, Fibronectin type III domain

AA: 566-656, PDBID: 2CUH, Subunit A, Seq Identity:28%, Fibronectin type III domain

AA: 844-1078, PDBID: 2G59, Subunit B, Seq Identity:62%, Protein-tyrosine phosphatase

UniProt annotation for PTPRH_HUMAN » Receptor-type tyrosine-protein phosphatase H
FUNCTION: 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.

CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

ENZYME REGULATION: Regulated by reversible dimerization. Dimerization reduces its catalytic activity.

SUBUNIT: Homodimer; disulfide-linked (Probable). Interacts with LCK.

TISSUE SPECIFICITY: 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.

INDUCTION: Induced at the early stage of hepatocellular carcinoma and is suppressed at later stages.

DOMAIN: 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.

DOMAIN: The cytoplasmic domain mediates the interaction with LCK.

UniProt features for PTPRH_HUMAN » Receptor-type tyrosine-protein phosphatase H
SIGNAL 1 27 Potential.
CHAIN 28 1115 Receptor-type tyrosine-protein phosphatase H.
DOMAIN 30 117 Fibronectin type-III 1.
DOMAIN 119 206 Fibronectin type-III 2.
DOMAIN 207 296 Fibronectin type-III 3.
DOMAIN 297 384 Fibronectin type-III 4.
DOMAIN 386 473 Fibronectin type-III 5.
DOMAIN 475 563 Fibronectin type-III 6.
DOMAIN 565 663 Fibronectin type-III 7.
DOMAIN 665 749 Fibronectin type-III 8.
DOMAIN 820 1079 Tyrosine-protein phosphatase.
ACT_SITE 1020 1020 Phosphocysteine intermediate (By similarity).
Amino Acid Sequence for PTPRH_HUMAN » Receptor-type tyrosine-protein phosphatase H
MAGAGGGLGV WGNLVLLGLC SWTGARAPAP NPGRNLTVET QTTSSISLSW EVPDGLDSQN SNYWVQCTGD GGTTETRNTT ATNVTVDGLG PGSLYTCSVW VEKDGVNSSV GTVTTATAPN PVRNLRVEAQ TNSSIALTWE VPDGPDPQNS TYGVEYTGDG GRAGTRSTAH TNITVDGLEP GCLYAFSMWV GKNGINSSRE TRNATTAHNP VRNLRVEAQT TSSISLSWEV PDGTDPQNST YCVQCTGDGG RTETRNTTDT RVTVDGLGPG SLYTCSVWVE KDGVNSSVEI VTSATAPNPV RNLTVEAQTN SSIALTWEVP DGPDPQNSTY GVEYTGDGGR AGTRSTAHTN ITVDRLEPGC LYVFSVWVGK NGINSSRETR NATTAPNPVR NLHMETQTNS SIALCWEVPD GPYPQDYTYW VEYTGDGGGT ETRNTTNTSV TAERLEPGTL YTFSVWAEKN GARGSRQNVS ISTVPNAVTS LSKQDWTNST IALRWTAPQG PGQSSYSYWV SWVREGMTDP RTQSTSGTDI TLKELEAGSL YHLTVWAERN EVRGYNSTLT AATAPNEVTD LQNETQTKNS VMLWWKAPGD PHSQLYVYWV QWASKGHPRR GQDPQANWVN QTSRTNETWY KVEALEPGTL YNFTVWAERN DVASSTQSLC ASTYPDTVTI TSCVSTSAGY GVNLIWSCPQ GGYEAFELEV GGQRGSQDRS SCGEAVSVLG LGPARSYPAT ITTIWDGMKV VSHSVVCHTE SAGVIAGAFV GILLFLILVG LLIFFLKRRN KKKQQKPELR DLVFSSPGDI PAEDFADHVR KNERDSNCGF ADEYQQLSLV GHSQSQMVAS ASENNAKNRY RNVLPYDWSR VPLKPIHEEP GSDYINASFM PGLWSPQEFI ATQGPLPQTV GDFWRLVWEQ QSHTLVMLTN CMEAGRVKCE HYWPLDSQPC THGHLRVTLV GEEVMENWTV RELLLLQVEE QKTLSVRQFH YQAWPDHGVP SSPDTLLAFW RMLRQWLDQT MEGGPPIVHC SAGVGRTGTL IALDVLLRQL QSEGLLGPFS FVRKMRESRP LMVQTEAQYV FLHQCILRFL QQSAQAPAEK EVPYEDVENL IYENVAAIQA HKLEV