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 confidence score
0.38
Supporting publications (n)
3
Transmembrane count
1
Protein classification
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information8
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 (2)
  • Enzymes
  • ENZYME proteins:Hydrolases
Transmembrane
755..775; Helical
Transmembrane Count
1
Entrez Gene Symbol
Supporting publications (n)
3
EVMP confidence score
0.38
Fluorescence & Localization4
PTPRH fluorescence
Tissue SpecificliverCell SpecificHepatocytesSingle-Nuclei Brain Specificchoroid plexus epithelial cell
Function & Pathway5
Relations & Evidence45

Ligand-Receptor Signaling (41)

41 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorHPMRNoYesNoYesNo
receptorreceptorSurfaceomeNoYesNoYesNo
receptor_tyrosine_phosphatasereceptorAlmen2009NoYesNoYesNo
receptor_like_protein_tyrosine_phosphatases_rptpsreceptorHPMRNoYesNoYesNo
rptpetareceptorHPMRNoYesNoYesNo
receptortypephosphatasesreceptorSurfaceomeNoYesNoYesNo
receptorreceptorOmniPathNoYesNoYesNo
extracellularextracellularHPMRNoNoNoYesNo
extracellularextracellularOmniPathNoNoNoYesNo
intracellularintracellularComPPINoNoNoYesNo
Page 1 of 5Next

Regulatory Interaction Network (3)

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

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometryMass spectrometry [LTQ-FT Ultra]Mass spectrometry [QTOF]23502905932396726
Sequence, Structure & Domains13

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 (2)
  • Protein-tyrosine phosphatase family
  • Receptor class 3 subfamily
Sequence Similarities
Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.
Clinical Relevance3
Interaction Protein (2)
ENSG00000112964ENSG00000146648
Interaction Count
2
Interaction Dataset
intact_biogrid
Supporting Publications3
PMIDTitleAbstract
36982312Saliva and Saliva Extracellular Vesicles for Biomarker Candidate Identification-Assay Development and Pilot Study in Amyotrophic Lateral Sclerosis.No abstract available
37322475Comprehensive profiling of extracellular vesicles in uveitis and scleritis enables biomarker discovery and mechanism exploration.No abstract available
38207106Proteomic, Metabolomic, and Fatty Acid Profiling of Small Extracellular Vesicles from Glioblastoma Stem-Like Cells and Their Role in Tumor Heterogeneity.No abstract available