Tyrosine-protein phosphatase non-receptor type 12

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Q05209 (PTN12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names 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

Name:

PTPN12

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	Cytoplasm.
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 fraction Traceable author statement. Source: ProtInc
Molecular function	SH3 domain binding Inferred from physical interaction. Source: UniProtKB non-membrane spanning protein tyrosine phosphatase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
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

Substrate binding By similarity

Region

345 – 438

Interaction with TGFB1I1 By similarity

Sites

Active site

231

Phosphocysteine intermediate By similarity

Binding site

199

Substrate By similarity

Binding site

278

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylmethionine Ref.7

Modified residue

186

Phosphoserine By similarity

Modified residue

332

Phosphoserine Ref.10 Ref.16

Modified residue

435

Phosphoserine Ref.16

Modified residue

468

Phosphoserine Ref.16

Modified residue

514

Phosphoserine Ref.16

Modified residue

519

Phosphothreonine Ref.16

Modified residue

569

Phosphothreonine Ref.14

Modified residue

571

Phosphoserine Ref.14 Ref.16

Modified residue

588

Phosphoserine Ref.16

Modified residue

596

Phosphoserine By similarity

Modified residue

598

Phosphothreonine By similarity

Modified residue

603

Phosphoserine Ref.10 Ref.14 Ref.16

Modified residue

606

Phosphoserine Ref.10 Ref.14 Ref.16

Modified residue

608

Phosphoserine Ref.16

Modified residue

613

Phosphoserine Ref.16

Modified residue

673

Phosphoserine Ref.12 Ref.14

Modified residue

689

Phosphoserine Ref.15 Ref.16

Modified residue

693

Phosphothreonine Ref.15 Ref.16

Natural variations

Natural variant

K → R in colon cancer. Ref.8

VAR_006385

Natural variant

322

V → I. Ref.1 Ref.4
Corresponds to variant rs9640663 [ dbSNP | Ensembl ].

VAR_019512

Natural variant

573

T → A.
Corresponds to variant rs3750050 [ dbSNP | Ensembl ].

VAR_020297

Natural variant

706

E → K.
Corresponds to variant rs2230602 [ dbSNP | Ensembl ].

VAR_057129

Experimental info

Sequence conflict

121

I → V in BAA02648. Ref.1

Sequence conflict

121

I → V in AAB30047. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

Q05209 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 663DB3E5176FD7FD
Show »

FASTA

780

88,106

        10         20         30         40         50         60 
MEQVEILRKF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK 

        70         80         90        100        110        120 
KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM 

       130        140        150        160        170        180 
IWEYNVVIIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCEDEQAR TDYFIRTLLL 

       190        200        210        220        230        240 
EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA 

       250        260        270        280        290        300 
ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL 

       310        320        330        340        350        360 
YEIHGAQKIA DGVNEINTEN MVSSIEPEKQ DSPPPKPPRT RSCLVEGDAK EEILQPPEPH 

       370        380        390        400        410        420 
PVPPILTPSP PSAFPTVTTV WQDNDRYHPK PVLHMVSSEQ HSADLNRNYS KSTELPGKNE 

       430        440        450        460        470        480 
STIEQIDKKL ERNLSFEIKK VPLQEGPKSF DGNTLLNRGH AIKIKSASPC IADKISKPQE 

       490        500        510        520        530        540 
LSSDLNVGDT SQNSCVDCSV TQSNKVSVTP PEESQNSDTP PRPDRLPLDE KGHVTWSFHG 

       550        560        570        580        590        600 
PENAIPIPDL SEGNSSDINY QTRKTVSLTP SPTTQVETPD LVDHDNTSPL FRTPLSFTNP 

       610        620        630        640        650        660 
LHSDDSDSDE RNSDGAVTQN KTNISTASAT VSAATSTESI STRKVLPMSI ARHNIAGTTH 

       670        680        690        700        710        720 
SGAEKDVDVS EDSPPPLPER TPESFVLASE HNTPVRSEWS ELQSQERSEQ KKSEGLITSE 

       730        740        750        760        770        780 
NEKCDHPAGG IHYEMCIECP PTFSDKREQI SENPTEATDI GFGNRCGKPK GPRDPPSEWT

« Hide

References

	« Hide 'large scale' referencesShow '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

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 118 of the entry and version 3 of the sequence. [Complete 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents