Tyrosine-protein phosphatase MSG5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38590 (MSG5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase MSG5
EC=3.1.3.48

Gene names

Name:	MSG5
Ordered Locus Names:	YNL053W
ORF Names:	N2480, YNL2480W

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity phosphatase that dephosphorylates MAP kinase FUS3 on both a Tyr and a Ser or Thr. Has a role in adaptation to pheromone.
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
Induction	By pheromone.
Miscellaneous	Present with 538 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Ontologies

Keywords
Biological process	Cell cycle
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Inferred from mutant phenotype PubMed 12556475 Ref.1. Source: SGD cell cycle Inferred from electronic annotation. Source: UniProtKB-KW inactivation of MAPK activity involved in cell wall biogenesis Inferred from mutant phenotype PubMed 10625705 PubMed 14703512. Source: SGD inactivation of MAPK activity involved in conjugation with cellular fusion Inferred from mutant phenotype Ref.1. Source: SGD peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC regulation of MAPK export from nucleus Inferred from mutant phenotype PubMed 12556475 PubMed 17963515. Source: SGD regulation of fungal-type cell wall organization Inferred from mutant phenotype PubMed 14703512. Source: SGD
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from direct assay PubMed 17952059 PubMed 17963515. Source: SGD
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 489

489

Tyrosine-protein phosphatase MSG5

PRO_0000094916

Sites

Active site

319

Phosphocysteine intermediate

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

151

Phosphoserine Ref.8 Ref.9

Modified residue

178

Phosphothreonine Ref.8

Modified residue

422

Phosphoserine Ref.9

Modified residue

437

Phosphothreonine Ref.9

Experimental info

Mutagenesis

319

C → A: Loss of activity.

Sequence conflict

347 – 348

NK → DE in BAA04485. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P38590 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 0D02380B62EA48DC
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FASTA

489

54,217

        10         20         30         40         50         60 
MQFHSDKQHL DSKTDIDFKP NSPRSLQNRN TKNLSLDIAA LHPLMEFSSP SQDVPGSVKF 

        70         80         90        100        110        120 
PSPTPLNLFM KPKPIVLEKC PPKVSPRPTP PSLSMRRSEA SIYTLPTSLK NRTVSPSVYT 

       130        140        150        160        170        180 
KSSTVSSISK LSSSSPLSSF SEKPHLNRVH SLSVKTKDLK LKGIRGRSQT ISGLETSTPI 

       190        200        210        220        230        240 
SSTREGTLDS TDVNRFSNQK NMQTTLIFPE EDSDLNIDMV HAEIYQRTVY LDGPLLVLPP 

       250        260        270        280        290        300 
NLYLYSEPKL EDILSFDLVI NVAKEIPNLE FLIPPEMAHK IKYYHIEWTH TSKIVKDLSR 

       310        320        330        340        350        360 
LTRIIHTAHS QGKKILVHCQ CGVSRSASLI VAYIMRYYGL SLNDAYNKLK GVAKDISPNM 

       370        380        390        400        410        420 
GLIFQLMEWG TMLSKNSPGE EGETVHMPEE DDIGNNEVSS TTKSYSSASF RSFPMVTNLS 

       430        440        450        460        470        480 
SSPNDSSVNS SEVTPRTPAT LTGARTALAT ERGEDDEHCK SLSQPADSLE ASVDNESIST 


APEQMMFLP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae." Doi K., Gartner A., Ammerer G., Errede B., Shinkawa H., Sugimoto K., Matsumoto K. EMBO J. 13:61-70(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The sequence of a 44 420 bp fragment located on the left arm of chromosome XIV from Saccharomyces cerevisiae." Bergez P., Doignon F., Crouzet M. Yeast 11:967-974(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / FY1676.
[3]	Erratum Bergez P., Doignon F., Crouzet M. Yeast 12:297-297(1996) [PubMed] [Europe PMC] [Abstract]
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S288c / FY1676.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Primary structure of a gene for subunit V of the cytochrome c oxidase from Saccharomyces cerevisiae." Seraphin B., Simon M., Faye G. Curr. Genet. 9:435-439(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 415-489.
[7]	"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].
[8]	"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-22; SER-151 AND THR-178, MASS SPECTROMETRY. Strain: ADR376.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-422 AND THR-437, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17548 Genomic DNA. Translation: BAA04485.1. U12141 Genomic DNA. Translation: AAA99659.1. Z71329 Genomic DNA. Translation: CAA95922.1. X02561 Genomic DNA. Translation: CAA26402.1. BK006947 Genomic DNA. Translation: DAA10492.1.
PIR	S58725.
RefSeq	NP_014345.3. NM_001182892.3.
3D structure databases
ProteinModelPortal	P38590.
SMR	P38590. Positions 229-374.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5538N.
IntAct	P38590. 11 interactions.
MINT	MINT-543826.
STRING	4932.YNL053W.
Proteomic databases
PaxDb	P38590.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL053W; YNL053W; YNL053W.
GeneID	855674.
KEGG	sce:YNL046W. sce:YNL053W.
Organism-specific databases
CYGD	YNL053w.
SGD	S000004998. MSG5.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00680000100889.
HOGENOM	HOG000066070.
KO	K11240.
OrthoDB	EOG45B4R5.
Gene expression databases
Genevestigator	P38590.
GermOnline	YNL053W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979960.

Entry information

Entry name

MSG5_YEAST

Accession

Primary (citable) accession number: P38590
Secondary accession number(s): D6W1C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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