Protein detail

PTPRH

Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1) (Transmembrane-type protein-tyrosine phosphatase type H)

Entry name
PTPRH
UniProt ID
EVMP score
0.38
Frequency
3
Transmembrane count
1
Protein classification
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1) (Transmembrane-type protein-tyrosine phosphatase type H)
Protein Function
  • Enzymes
  • ENZYME proteins:Hydrolases
Transmembrane
755..775; Helical
Transmembrane Count
1
Entrez Gene Symbol
Frequency
3
EVMP Score
0.38
Fluorescence & Localization
PTPRH fluorescence
Tissue SpecificliverCell SpecificHepatocytesSingle-Nuclei Brain Specificchoroid plexus epithelial cell
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

41 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularGO_IntercellNoNoNoYesNo
intracellularintracellularUniProt_locationNoNoNoYesNo
intracellularintracellularOmniPathNoNoNoYesNo
cell_adhesioncell_adhesionZhong2015YesYesNoYesNo
icamcell_adhesionZhong2015YesYesNoYesNo
adhesionadhesionOmniPathYesYesNoYesNo
cell_adhesioncell_adhesionOmniPathYesYesNoYesNo
transmembranetransmembraneUniProt_locationNoNoNoYesNo
transmembranetransmembraneUniProt_topologyNoNoNoYesNo
transmembranetransmembraneUniProt_keywordNoNoNoYesNo
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Regulatory Interaction Network

3 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
PTPRHQ9HD43INSRP06213YesNoYesSIGNOR_ProtMapperSIGNORProtMapperProtMapper:10734133SIGNOR:10734133
PTPRHQ9HD43EGFRP00533YesNoYesSIGNORSIGNOR:28065597
PTPRHQ9HD43GHRP10912YesNoYesLit-BM-17SIGNORIntActLit-BM-17:12907755IntAct:12907755SIGNOR:12907755

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometryMass spectrometry [LTQ-FT Ultra]Mass spectrometry [QTOF]23502905932396726
Sequence, Structure & Domains

Sequences

Length
1,115
Mass
122,353
Sequence
MAGAGGGLGVWGNLVLLGLCSWTGARAPAPNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVWVEKDGVNSSVGTVTTATAPNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAGTRSTAHTNITVDGLEPGCLYAFSMWVGKNGINSSRETRNATTAHNPVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQCTGDGGRTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAGTRSTAHTNITVDRLEPGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTNTSVTAERLEPGTLYTFSVWAEKNGARGSRQNVSISTVPNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPRTQSTSGTDITLKELEAGSLYHLTVWAERNEVRGYNSTLTAATAPNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRGQDPQANWVNQTSRTNETWYKVEALEPGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWSCPQGGYEAFELEVGGQRGSQDRSSCGEAVSVLGLGPARSYPATITTIWDGMKVVSHSVVCHTESAGVIAGAFVGILLFLILVGLLIFFLKRRNKKKQQKPELRDLVFSSPGDIPAEDFADHVRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQQSAQAPAEKEVPYEDVENLIYENVAAIQAHKLEV
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9HD43-1; Sequence=Displayed; Name=2; IsoId=Q9HD43-2; Sequence=VSP_031318; Name=3; IsoId=Q9HD43-3; Sequence=VSP_054222
Alternative Sequence
84..261; Missing (in isoform 2); 126..303; Missing (in isoform 3)

3D Structural Models

Turn
828..833; 837..840; 857..859; 870..873; 968..971
Helix
802..804; 805..827; 842..847; 897..899; 900..910; 993..1007; 1025..1043; 1048..1058; 1066..1082
Beta Strand
876..880; 888..892; 914..917; 921..923; 940..942; 945..954; 956..967; 972..981; 1012..1014; 1017..1019; 1021..1024; 1044..1046
3D Structure
X-ray crystallography (1)

Domain & Motif Annotations

Domain (CC)
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.
Domain (FT)
32..121; Fibronectin type-III 1; 122..209; Fibronectin type-III 2; 210..299; Fibronectin type-III 3; 300..387; Fibronectin type-III 4; 388..477; Fibronectin type-III 5; 478..563; Fibronectin type-III 6; 564..666; Fibronectin type-III 7; 665..749; Fibronectin type-III 8; 820..1079; Tyrosine-protein phosphatase
Protein Families
  • Protein-tyrosine phosphatase family
  • Receptor class 3 subfamily
Sequence Similarities
Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.
Clinical Relevance
Interaction Protein
ENSG00000112964ENSG00000146648
Interaction Count
2
Interaction Dataset
intact_biogrid