Reviewed,
UniProtKB/Swiss-Prot Q05209 (PTN12_HUMAN)
Last modified
January 19, 2010.
Version 100.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Tyrosine-protein phosphatase non-receptor type 12 EC=3.1.3.48 Alternative name(s): Protein-tyrosine phosphatase G1 Short name=PTPG1 PTP-PEST | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| 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)
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. |
| Subunit structure | Interacts with TGFB1I1 By similarity. Interacts with PSTPIP1. Ref.9 |
| Subcellular location | |
| Involvement in disease | Defects in PTPN12 are found in some colon cancers. |
| Sequence similarities | Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily. Contains 1 tyrosine-protein phosphatase domain. |
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 |
| Gene Ontology (GO) | |
| Biological process | protein amino acid dephosphorylation Ref.2 Traceable author statement. Source: ProtInc |
| Cellular component | soluble fraction Ref.1 Traceable author statement. Source: ProtInc |
| Molecular function | SH3 domain binding Inferred from physical interaction. Source: UniProtKB non-membrane spanning protein tyrosine phosphatase activity Ref.2Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Binary interactions
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 | 345 – 438 | 94 | Interaction with TGFB1I1 By similarity | ||||||
Sites | |||||||||
| Active site | 231 | 1 | Phosphocysteine intermediate 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.14 | ||||||
| Modified residue | 435 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 468 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 514 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 519 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 569 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 571 | 1 | Phosphoserine Ref.14 Ref.12 | ||||||
| Modified residue | 588 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 596 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 598 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 603 | 1 | Phosphoserine Ref.10 Ref.14 Ref.12 | ||||||
| Modified residue | 606 | 1 | Phosphoserine Ref.10 Ref.14 Ref.12 | ||||||
| Modified residue | 608 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 613 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 673 | 1 | Phosphoserine Ref.12 Ref.11 | ||||||
| Modified residue | 689 | 1 | Phosphoserine Ref.14 Ref.13 | ||||||
| Modified residue | 693 | 1 | Phosphothreonine Ref.14 Ref.13 | ||||||
Natural variations | |||||||||
| Natural variant | 61 | 1 | K → R in colon cancer. Ref.8 | VAR_006385 | |||||
| Natural variant | 322 | 1 | I → V: dbSNP rs9640663. Ref.1 Ref.5 | VAR_019512 | |||||
| Natural variant | 573 | 1 | T → A: dbSNP rs3750050. | VAR_020297 | |||||
| Natural variant | 706 | 1 | E → K: dbSNP rs2230602. | VAR_057129 | |||||
Experimental info | |||||||||
| Sequence conflict | 121 | 1 | I → V Ref.1 | ||||||
| Sequence conflict | 121 | 1 | I → V Ref.8 | ||||||
Sequences
| ||||||||||||||||||
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 VAL-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]. 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], VARIANT VAL-322. |
| [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: Epithelium. |
| [11] | "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: Epithelium. |
| [12] | "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. |
| [13] | "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. |
| [14] | "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. |
| [15] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| + | 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. NP_001124481.1. NP_002826.3. |
| UniGene | Hs.61812 |
3D structure databases | |
| SMR | Q05209. Positions 3-300. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q05209. 18 interactions. |
| STRING | Q05209. |
PTM databases | |
| PhosphoSite | Q05209. |
Proteomic databases | |
| PRIDE | Q05209. |
Genome annotation databases | |
| Ensembl | ENST00000248594; ENSP00000248594; ENSG00000127947; Homo sapiens. [Genome view] |
| GeneID | 5782. |
| KEGG | hsa:5782. |
| UCSC | uc003ugh.1. human. |
Organism-specific databases | |
| CTD | 5782. |
| GeneCards | GC07P077004. |
| H-InvDB | HIX0033626. |
| HGNC | HGNC:9645. PTPN12. |
| HPA | HPA007097. |
| MIM | 600079. gene. |
| PharmGKB | PA33987. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | HBG714475. |
| HOVERGEN | Q05209. |
| InParanoid | Q05209. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.48. 247. |
Gene expression databases | |
| ArrayExpress | Q05209. |
| Bgee | Q05209. |
| CleanEx | HS_PTPN12. |
| Genevestigator | Q05209. |
| GermOnline | ENSG00000127947. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000387. Dual-sp/Tyr_phosphatase. IPR016130. Tyr_Pase_AS. IPR012266. Tyr_Pase_non-rcpt_typ-12. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view] |
| 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 Resources | |
| 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 project | HPI (Human Proteome Initiative) | ||||||||
| 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


