P29461 (PTP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase 2
EC=3.1.3.48

Alternative name(s):
Protein-tyrosine phosphatase 2
Short name=PTPase 2

Gene names

Name:	PTP2
Ordered Locus Names:	YOR208W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	750 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major phosphatase responsible with PTP3 for tyrosine dephosphorylation of MAP kinase HOG1 to inactivate its activity. May also be involved in the regulation of MAP kinase FUS3. May be implicated in the ubiquitin-mediated protein degradation. Ref.6 Ref.7
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with HOG1. Ref.6 Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.8.
Miscellaneous	Present with 149 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inactivation of MAPK activity involved in cell wall organization or biogenesis Inferred from mutant phenotype PubMed 10523653. Source: SGD inactivation of MAPK activity involved in osmosensory signaling pathway Inferred from genetic interaction Ref.6. Source: SGD peptidyl-tyrosine dephosphorylation Inferred from direct assay PubMed 10523653. Source: GOC protein dephosphorylation Inferred from mutant phenotype Ref.6. Source: SGD regulation of protein localization Inferred from mutant phenotype PubMed 10817757. Source: SGD regulation of sporulation Inferred from genetic interaction PubMed 10679022. Source: SGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 10523653. Source: SGD
Molecular_function	protein tyrosine phosphatase activity Inferred from direct assay PubMed 10523653. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 750	750	Tyrosine-protein phosphatase 2		PRO_0000094856
Regions
	Domain	383 – 737	355	Tyrosine-protein phosphatase
Sites
	Active site	666	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	258	1	Phosphoserine Ref.10
	Modified residue	430	1	Phosphoserine Ref.10 Ref.12
Experimental info
	Sequence conflict	371	1	L → S in AAB59323. Ref.3
	Sequence conflict	474 – 475	2	KL → NV Ref.1
	Sequence conflict	660 – 661	2	SP → GA in AAB59323. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P29461 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 1033D2F0AA23BD35	FASTA	750	85,868
	10 20 30 40 50 60 MDRIAQQYRN GKRDNNGNRM ASSAISEKGH IQVNQTRTPG QMPVYRGETI NLSNLPQNQI 70 80 90 100 110 120 KPCKDLDDVN IRRNNSNRHS KILLLDLCAG PNTNSFLGNT NAKDITVLSL PLPSTLVKRS 130 140 150 160 170 180 NYPFENLLKN YLGSDEKYIE FTKIIKDYDI FIFSDSFSRI SSCLKTTFCL IEKFKKFICH 190 200 210 220 230 240 FFPSPYLKFF LLEGSLNDSK APSLGKNKKN CILPKLDLNL NVNLTSRSTL NLRINIPPPN 250 260 270 280 290 300 DSNKIFLQSL KKDLIHYSPN SLQKFFQFNM PADLAPNDTI LPNWLKFCSV KENEKVILKK 310 320 330 340 350 360 LFNNFETLEN FEMQRLEKCL KFKKKPLHQK QLSQKQRGPQ STDDSKLYSL TSLQRQYKSS 370 380 390 400 410 420 LKSNIQKNQK LKLIIPKNNT SSSPSPLSSD DTIMSPINDY ELTEGIQSFT KNRYSNILPY 430 440 450 460 470 480 EHSRVKLPHS PKPPAVSEAS TTETKTDKSY PMCPVDAKNH SCKPNDYINA NYLKLTQINP 490 500 510 520 530 540 DFKYIATQAP LPSTMDDFWK VITLNKVKVI ISLNSDDELN LRKWDIYWNN LSYSNHTIKL 550 560 570 580 590 600 QNTWENICNI NGCVLRVFQV KKTAPQNDNI SQDCDLPHNG DLTSITMAVS EPFIVYQLQY 610 620 630 640 650 660 KNWLDSCGVD MNDIIKLHKV KNSLLFNPQS FITSLEKDVC KPDLIDDNNS ELHLDTANSS 670 680 690 700 710 720 PLLVHCSAGC GRTGVFVTLD FLLSILSPTT NHSNKIDVWN MTQDLIFIIV NELRKQRISM 730 740 750 VQNLTQYIAC YEALLNYFAL QKQIKNALPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a second protein tyrosine phosphatase gene, PTP2, from Saccharomyces cerevisiae." Guan K., Deschenes R.J., Dixon J.E. J. Biol. Chem. 267:10024-10030(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A gene encoding a putative tyrosine phosphatase suppresses lethality of an N-end rule-dependent mutant." Ota I.M., Varshavsky A. Proc. Natl. Acad. Sci. U.S.A. 89:2355-2359(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Multiple protein tyrosine phosphatase-encoding genes in the yeast Saccharomyces cerevisiae." James P., Hall B.D., Whelen S., Craig E.A. Gene 122:101-110(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The reference genome sequence of Saccharomyces cerevisiae: Then and now." Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M. G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases." Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H. Mol. Cell. Biol. 17:1289-1297(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HOG1.
[7]	"Two protein-tyrosine phosphatases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1." Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M. J. Biol. Chem. 272:17749-17755(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HOG1.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: ADR376.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M85287 Genomic DNA. No translation available. M82872 Genomic DNA. Translation: AAA34922.1. M38723 Genomic DNA. Translation: AAB59323.1. Z75116 Genomic DNA. Translation: CAA99423.1. BK006948 Genomic DNA. Translation: DAA10980.1.
PIR	S67100.
RefSeq	NP_014851.3. NM_001183627.3.
3D structure databases
ProteinModelPortal	P29461.
SMR	P29461. Positions 375-738.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	34603. 48 interactions.
DIP	DIP-2369N.
IntAct	P29461. 3 interactions.
MINT	MINT-510066.
STRING	4932.YOR208W.
Proteomic databases
MaxQB	P29461.
PaxDb	P29461.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR208W; YOR208W; YOR208W.
GeneID	854383.
KEGG	sce:YOR208W.
Organism-specific databases
CYGD	YOR208w.
SGD	S000005734. PTP2.
Phylogenomic databases
eggNOG	COG5599.
GeneTree	ENSGT00690000103379.
HOGENOM	HOG000115780.
KO	K01104.
OrthoDB	EOG793BJ4.
Enzyme and pathway databases
BioCyc	YEAST:YOR208W-MONOMER.
Gene expression databases
Genevestigator	P29461.
Family and domain databases
Gene3D	3.90.190.10. 1 hit.
InterPro	IPR029021. Prot-tyrosine_phosphatase-like. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00102. Y_phosphatase. 1 hit. [Graphical view]
PRINTS	PR00700. PRTYPHPHTASE.
SMART	SM00194. PTPc. 1 hit. [Graphical view]
SUPFAM	SSF52799. SSF52799. 3 hits.
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	976526.

Entry information

Entry name

PTP2_YEAST

Accession

Primary (citable) accession number: P29461
Secondary accession number(s): D6W2R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 11, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program