Q05209 (PTN12_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 118.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tyrosine-protein phosphatase non-receptor type 12 EC=3.1.3.48 Alternative name(s): PTP-PEST Protein-tyrosine phosphatase G1 Short name=PTPG1 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 780 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2. Ref.13 |
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. |
| Subunit structure | Interacts with TGFB1I1 By similarity. Interacts with PSTPIP1. Interacts with PTK2B/PYK2. Ref.9 Ref.13 |
| Subcellular location | |
| Post-translational modification | Phosphorylated by STK24/MST3 and this results in inhibition of its activity. Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 |
| Sequence similarities | Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily. Contains 1 tyrosine-protein phosphatase domain. |
| Sequence caution | The sequence BAD92761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| Disease | Disease mutation |
| Molecular function | Hydrolase Protein phosphatase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | plasma membrane Inferred from direct assay. Source: HPA soluble fractionTraceable author statement. Source: ProtInc |
| Molecular function | SH3 domain binding Inferred from physical interaction. Source: UniProtKB non-membrane spanning protein tyrosine phosphatase activityTraceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ERBB2 | P04626 | 4 | EBI-2266035,EBI-641062 | |
| PDGFRB | P09619 | 2 | EBI-2266035,EBI-641237 | |
| TEK | Q02763 | 2 | EBI-2266035,EBI-2257090 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 780 | 780 | Tyrosine-protein phosphatase non-receptor type 12 | PRO_0000094771 | |||||
Regions | |||||||||
| Domain | 28 – 293 | 266 | Tyrosine-protein phosphatase | ||||||
| Region | 231 – 237 | 7 | Substrate binding By similarity | ||||||
| Region | 345 – 438 | 94 | Interaction with TGFB1I1 By similarity | ||||||
Sites | |||||||||
| Active site | 231 | 1 | Phosphocysteine intermediate By similarity | ||||||
| Binding site | 199 | 1 | Substrate By similarity | ||||||
| Binding site | 278 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.7 | ||||||
| Modified residue | 186 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 332 | 1 | Phosphoserine Ref.10 Ref.16 | ||||||
| Modified residue | 435 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 468 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 514 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 519 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 569 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 571 | 1 | Phosphoserine Ref.14 Ref.16 | ||||||
| Modified residue | 588 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 596 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 598 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 603 | 1 | Phosphoserine Ref.10 Ref.14 Ref.16 | ||||||
| Modified residue | 606 | 1 | Phosphoserine Ref.10 Ref.14 Ref.16 | ||||||
| Modified residue | 608 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 613 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 673 | 1 | Phosphoserine Ref.12 Ref.14 | ||||||
| Modified residue | 689 | 1 | Phosphoserine Ref.15 Ref.16 | ||||||
| Modified residue | 693 | 1 | Phosphothreonine Ref.15 Ref.16 | ||||||
Natural variations | |||||||||
| Natural variant | 61 | 1 | K → R in colon cancer. Ref.8 | VAR_006385 | |||||
| Natural variant | 322 | 1 | V → I. Ref.1 Ref.4 Corresponds to variant rs9640663 [ dbSNP | Ensembl ]. | VAR_019512 | |||||
| Natural variant | 573 | 1 | T → A. Corresponds to variant rs3750050 [ dbSNP | Ensembl ]. | VAR_020297 | |||||
| Natural variant | 706 | 1 | E → K. Corresponds to variant rs2230602 [ dbSNP | Ensembl ]. | VAR_057129 | |||||
Experimental info | |||||||||
| Sequence conflict | 121 | 1 | I → V in BAA02648. Ref.1 | ||||||
| Sequence conflict | 121 | 1 | I → V in AAB30047. Ref.8 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase." Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M., Adachi M., Imai K., Yachi A. Biochem. Biophys. Res. Commun. 189:1223-1230(1992) [PubMed: 1472029] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-322. Tissue: Colon. |
| [2] | "Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase." Yang Q., Co D., Sommercorn J., Tonks N.K. J. Biol. Chem. 268:6622-6628(1993) [PubMed: 8454633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | Erratum Yang Q., Co D., Sommercorn J., Tonks N.K. J. Biol. Chem. 268:17650-17650(1993) [PubMed: 8349645] [Abstract] Cited for: SEQUENCE REVISION TO 495-517 AND 526-780. |
| [4] | Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-322. Tissue: Brain. |
| [5] | "The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. Wilson R.K.Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
| [7] | "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8, ACETYLATION AT MET-1. Tissue: Platelet. |
| [8] | "Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells." Takekawa M., Itoh F., Hinoda Y., Adachi M., Ariyama T., Inazawa J., Imai K., Yachi A. FEBS Lett. 339:222-228(1994) [PubMed: 7509295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-136, VARIANT COLON CANCER ARG-61. |
| [9] | "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion." Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L. EMBO J. 17:7320-7336(1998) [PubMed: 9857189] [Abstract] Cited for: INTERACTION WITH PSTPIP1. |
| [10] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-603 AND SER-606, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST." Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D. J. Biol. Chem. 281:38405-38417(2006) [PubMed: 17046825] [Abstract] Cited for: PHOSPHORYLATION BY STK24. |
| [12] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells." Sahu S.N., Nunez S., Bai G., Gupta A. Am. J. Physiol. 292:C2288-C2296(2007) [PubMed: 17329398] [Abstract] Cited for: INTERACTION WITH PTK2B/PYK2, FUNCTION. |
| [14] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-569; SER-571; SER-603; SER-606 AND SER-673, MASS SPECTROMETRY. Tissue: Platelet. |
| [15] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND THR-693, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-435; SER-468; SER-514; THR-519; SER-571; SER-588; SER-603; SER-606; SER-608; SER-613; SER-689 AND THR-693, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D13380 mRNA. Translation: BAA02648.1. M93425 mRNA. Translation: AAA36529.1. AC006451 Genomic DNA. Translation: AAQ96881.1. AB209524 mRNA. Translation: BAD92761.1. Different initiation. BC050008 mRNA. Translation: AAH50008.2. S69184 mRNA. Translation: AAB30047.2. |
| IPI | IPI00289082. |
| PIR | JC1368. |
| RefSeq | NP_001124480.1. NM_001131008.1. NP_001124481.1. NM_001131009.1. NP_002826.3. NM_002835.3. |
| UniGene | Hs.61812. |
3D structure databases | |
| ProteinModelPortal | Q05209. |
| SMR | Q05209. Positions 3-298. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q05209. 22 interactions. |
| MINT | MINT-243699. |
| STRING | Q05209. |
PTM databases | |
| PhosphoSite | Q05209. |
Polymorphism databases | |
| DMDM | 50403764. |
Proteomic databases | |
| PRIDE | Q05209. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000248594; ENSP00000248594; ENSG00000127947. |
| GeneID | 5782. |
| KEGG | hsa:5782. |
| UCSC | uc003ugh.1. human. |
Organism-specific databases | |
| CTD | 5782. |
| GeneCards | GC07P077166. |
| H-InvDB | HIX0033626. |
| HGNC | HGNC:9645. PTPN12. |
| HPA | HPA007097. |
| MIM | 600079. gene. |
| neXtProt | NX_Q05209. |
| GenAtlas | Search... |
Phylogenomic databases | |
| GeneTree | ENSGT00600000084181. |
| HOGENOM | HBG714475. |
| HOVERGEN | HBG007666. |
| InParanoid | Q05209. |
| OMA | TVWQDND. |
| OrthoDB | EOG42BX89. |
| PhylomeDB | Q05209. |
Gene expression databases | |
| ArrayExpress | Q05209. |
| Bgee | Q05209. |
| CleanEx | HS_PTPN12. |
| Genevestigator | Q05209. |
| GermOnline | ENSG00000127947. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000387. Tyr/Dual-specificity_Pase. IPR016130. Tyr_Pase_AS. IPR012266. Tyr_Pase_non-rcpt_typ-12. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view] |
| KO | K01104. |
| Pfam | PF00102. Y_phosphatase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000932. Tyr-Ptase_nr12. 1 hit. |
| PRINTS | PR00700. PRTYPHPHTASE. |
| SMART | SM00194. PTPc. 1 hit. [Graphical view] |
| PROSITE | PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 22488. |
| SOURCE | Search... |
Entry information
| Entry name | PTN12_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q05209 Secondary accession number(s): Q16130 Q86XU4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with