Protein detail

PTN12

Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1)

Entry name
PTN12
UniProt ID
EVMP confidence score
0.60
Supporting publications (n)
12
Transmembrane count
Protein classification
EnzymesPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1)
Protein Class (2)
EnzymesPredicted intracellular proteins
Protein Function (3)
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Hydrolases
Entrez Gene Symbol
Gene Synonym (2)
PTP-PESTPTPG1
Gene Description
Protein tyrosine phosphatase non-receptor type 12
Chromosome
7
Position
77537295-77640069
Supporting publications (n)
12
EVMP confidence score
0.60
Function & Pathway6
Relations & Evidence49

Enzyme-Mediated Modification (24)

24 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
PTPN12PRKYO43930S39phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKYO43930S435phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCBP05771S39phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPKEAKEA:17570479
PTPN12PRKCBP05771S435phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCGP05129S39phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCGP05129S435phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCDQ05655S39phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCDQ05655S435phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCEQ02156S39phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
PTPN12PRKCEQ02156S435phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
Page 2 of 3PreviousNext

Ligand-Receptor Signaling (5)

5 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network (18)

18 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
PTN12Q05209FAK1Q05397YesNoYesSPIKEAdhesomeSIGNORProtMapperDEPODHPRDSIGNOR_ProtMapperREACH_ProtMapperHPRD-phosSPIKE_LCAdhesome:9497381HPRD-phos:10400703SIGNOR:11432829ProtMapper:19595712HPRD:11314030Adhesome:10400703SPIKE:21876001HPRD:9497381HPRD-phos:11314030SIGNOR:19595712SPIKE_LC:21876001HPRD:10400703Adhesome:11314030DEPOD:19595712
PTN12Q05209WASPP42768YesNoYesSPIKEWangNetPathSIGNORProtMapperDEPODHPRDHINTIntActSIGNOR_ProtMapperHPRD-phosSPIKE_LCNetPath:14707117DEPOD:14707117IntAct:19167335SIGNOR:11711533ProtMapper:14707117SPIKE_LC:19167335SPIKE:19167335SPIKE_LC:14707117HPRD:15588985HPRD:11711533IntAct:14707117HPRD-phos:11711533HPRD:14707117SPIKE:14707117HINT:14707117SIGNOR:14707117
PTN12Q05209JAK2O60674YesNoYesWangNetPathSIGNORProtMapperHPRDCancerCellMapSIGNOR_ProtMapperSPIKESPIKE_LCSPIKE_LC:11731619CancerCellMap:11731619NetPath:11731619SPIKE:11731619SIGNOR:11731619ProtMapper:11731619HPRD:11731619
PTN12Q05209PPIP1O43586YesNoYesSPIKEWangNetPathSIGNORProtMapperDEPODHPRDHINTHuRIIntActSIGNOR_ProtMapperHPRD-phosSPIKE_LCIntAct:32296183SPIKE_LC:14707117HPRD:11711533HINT:35152348HPRD-phos:11711533HINT:9422760IntAct:35152348HPRD:9422760SIGNOR:11711533HPRD:11971877SPIKE:14707117DEPOD:11711533NetPath:14707117HINT:14707117HINT:11711533HINT:11971877IntAct:14707117HPRD-phos:11971877IntAct:11971877ProtMapper:11711533
PTN12Q05209INSRP06213YesNoYesAdhesomeSIGNORProtMapperHPRDSIGNOR_ProtMapperAdhesome:19167335Adhesome:8454633SIGNOR:8454633ProtMapper:10734133ProtMapper:8454633SIGNOR:10734133HPRD:8454633
PTN12Q05209GIT2Q14161YesNoYesSIGNOR_ProtMapperSIGNORProtMapperProtMapper:16317044SIGNOR:16317044
STK24Q9Y6E0PTN12Q05209YesNoYesSIGNORSIGNOR:26910843
PTN12Q05209BCAR1P56945YesNoYesDOMINOWangAdhesomeSIGNORDEPODHPRDHINTBioGRIDIntActSPIKE_LCBioGRID:12714323SIGNOR:11432829HPRD:12714323DEPOD:9748319DOMINO:9285683SPIKE_LC:9285683HPRD:9285683HINT:9748319HPRD:9920935Adhesome:9285683Adhesome:11432829DEPOD:8887669Adhesome:8887669HINT:9285683IntAct:9285683HINT:8887669DEPOD:9920935DEPOD:9285683HPRD:8887669HPRD:9748319DEPOD:12714323
PTN12Q05209GDIR1P52565YesYesNoSIGNORSIGNOR:25666508
KPCAP17252PTN12Q05209YesYesYesHPRD_MIMPSIGNORProtMapperPhosphoSite_KEAphosphoELM_KEAPhosphoNetworksHPRDKinexus_KEAWangPhosphoSite_ProtMapperBEL-Large-Corpus_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPiPTMnetPhosphoPointKEAHPRD_KEAphosphoELMSIGNOR_ProtMapperAdhesomeHPRD-phosHPRD-phos:18669648SIGNOR:7520867KEA:7520867KEA:94349924HPRD-phos:18767875HPRD-phos:7520867ProtMapper:15212693ProtMapper:7520867KEA:7909431HPRD-phos:20068231Adhesome:7909431HPRD:7520867Adhesome:94349924ProtMapper:18767875Adhesome:7520867ProtMapper:19651622phosphoELM:7909431ProtMapper:20068231ProtMapper:18669648phosphoELM:7520867HPRD-phos:19651622
Page 1 of 2Next

Protein Complex Composition (1)

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
PTPN12Q052094PDBPDB:5j8r

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometryMass spectrometry [MALDI TOF]140326690
Sequence, Structure & Domains14

Sequences

Length
780
Mass
88,106
Sequence
MEQVEILRKFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKIADGVNEINTENMVSSIEPEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDNDRYHPKPVLHMVSSEQHSADLNRNYSKSTELPGKNESTIEQIDKKLERNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASPCIADKISKPQELSSDLNVGDTSQNSCVDCSVTQSNKVSVTPPEESQNSDTPPRPDRLPLDEKGHVTWSFHGPENAIPIPDLSEGNSSDINYQTRKTVSLTPSPTTQVETPDLVDHDNTSPLFRTPLSFTNPLHSDDSDSDERNSDGAVTQNKTNISTASATVSAATSTESISTRKVLPMSIARHNIAGTTHSGAEKDVDVSEDSPPPLPERTPESFVLASEHNTPVRSEWSELQSQERSEQKKSEGLITSENEKCDHPAGGIHYEMCIECPPTFSDKREQISENPTEATDIGFGNRCGKPKGPRDPPSEWT
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q05209-1; Sequence=Displayed; Name=2; IsoId=Q05209-2; Sequence=VSP_046274; Name=3; IsoId=Q05209-3; Sequence=VSP_054168
Alternative Sequence
1..130; Missing (in isoform 2); 1..119; Missing (in isoform 3)

3D Structural Models

Turn
43..46; 111..113; 270..272
Helix
3..17; 27..42; 51..54; 56..61; 71..73; 114..123; 207..219; 236..252; 262..269; 280..298
Beta Strand
74..76; 90..94; 102..106; 128..131; 135..137; 155..157; 160..170; 173..182; 185..194; 222..225; 227..230; 232..235
3D Structure
NMR spectroscopy (1); X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
502..519; Polar residues; 521..533; Basic and acidic residues; 552..577; Polar residues; 587..601; Polar residues; 602..613; Basic and acidic residues; 622..639; Low complexity; 690..703; Polar residues; 704..725; Basic and acidic residues; 771..780; Basic and acidic residues
Domain (FT)
28..293; Tyrosine-protein phosphatase
Region
345..438; Interaction with TGFB1I1; 502..639; Disordered; 657..725; Disordered; 744..780; Disordered
Protein Families (2)
  • Protein-tyrosine phosphatase family
  • Non-receptor class 4 subfamily
Sequence Similarities
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily.
Clinical Relevance5
Interaction Protein (6)
ENSG00000050820ENSG00000089159ENSG00000111679ENSG00000140368ENSG00000146648ENSG00000160691
Interaction Count
6
Interaction Dataset (2)
intact_biogridintact_biogrid_opencell
Supporting Publications12
PMIDTitleAbstract
32854315Proteomic Profiling of Extracellular Vesicles Derived from Cerebrospinal Fluid of Alzheimer's Disease Patients: A Pilot Study.Recent studies have highlighted the importance of Aβ and tau-containing extracellular vesicles (EVs) in AD.
33441949Utility of Claudin-3 in extracellular vesicles from human bile as biomarkers of cholangiocarcinoma.No abstract available
34815502The von Willebrand factor stamps plasmatic extracellular vesicles from glioblastoma patients.No abstract available
36064647Systemic proteomics and miRNA profile analysis of exosomes derived from human pluripotent stem cells.No abstract available
36736734Extracellular vesicle proteomics and phosphoproteomics identify pathways for increased risk in patients hospitalized with COVID-19 and type 2 diabetes mellitus.No abstract available
37322475Comprehensive profiling of extracellular vesicles in uveitis and scleritis enables biomarker discovery and mechanism exploration.No abstract available
38113368In-Depth Proteome Profiling of Small Extracellular Vesicles Isolated from Cancer Cell Lines and Patient Serum.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
40189497Small extracellular vesicle-based one-step high-throughput microfluidic platform for epithelial ovarian cancer diagnosis.No abstract available
40465195Extracellular vesicle proteomics uncovers energy metabolism, complement system, and endoplasmic reticulum stress response dysregulation postexercise in males with myalgic encephalomyelitis/chronic fatigue syndrome.No abstract available
Page 1 of 2Next