P53965 (SIW14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase SIW14
EC=3.1.3.48

Gene names

Name:	SIW14
Ordered Locus Names:	YNL032W
ORF Names:	N2746

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	281 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in actin filament organization and endocytosis. Ref.5
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Cytoplasm Ref.3.
Miscellaneous	Present with 4070 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from mutant phenotype Ref.5. Source: SGD endocytosis Inferred from mutant phenotype Ref.5. Source: SGD response to stress Inferred from genetic interaction PubMed 10514564. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.3. Source: SGD
Molecular_function	protein tyrosine phosphatase activity Inferred from sequence or structural similarity PubMed 11967829. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
OCA1	P50946	5	EBI-28668,EBI-28814
OCA2	P53949	4	EBI-28668,EBI-28725

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 281	281	Tyrosine-protein phosphatase SIW14		PRO_0000094922
Sites
	Active site	214	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	94	1	Phosphoserine Ref.6 Ref.7 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P53965 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 88BD8AFC620B4570	FASTA	281	32,755
	10 20 30 40 50 60 MGLYQAKNDE GSDPKSSSKI DDLIENEAEI IRLIKEDGKL LIDNGDGRDI HNIIQEDKLL 70 80 90 100 110 120 SVEFNEVLKR FHGEEKSDIP RKEFDEDEDD GYDSNEHHQK TIEVMNTLNH VINKEVIPPE 130 140 150 160 170 180 NFSHVVGEIY RSSFPRQENF SFLHERLKLK SILVLIPEEY PQENLNFLKL TGIKLYQVGM 190 200 210 220 230 240 SGNKEPFVNI PSHLLTKALE IVLNPANQPI LIHCNRGKHR TGCLIGCIRK LQNWSLTMIF 250 260 270 280 DEYRRFAFPK ARALDQQFIE MYDDDEIKRI ASKNNWLPLQ W

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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].
[4]	"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].
[5]	"A synthetic lethal screen identifies a role for the cortical actin patch/endocytosis complex in the response to nutrient deprivation in Saccharomyces cerevisiae." Care A., Vousden K.A., Binley K.M., Radcliffe P., Trevethick J., Mannazzu I., Sudbery P.E. Genetics 166:707-719(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"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-94, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY.
[8]	"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-94, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71308 Genomic DNA. Translation: CAA95895.1. BK006947 Genomic DNA. Translation: DAA10513.1.
PIR	S62954.
RefSeq	NP_014366.3. NM_001182871.3.
3D structure databases
ProteinModelPortal	P53965.
SMR	P53965. Positions 116-263.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1990N.
IntAct	P53965. 22 interactions.
MINT	MINT-384829.
STRING	4932.YNL032W.
Proteomic databases
PaxDb	P53965.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL032W; YNL032W; YNL032W.
GeneID	855699.
KEGG	sce:YNL024C-A. sce:YNL032W.
Organism-specific databases
CYGD	YNL032w.
SGD	S000004977. SIW14.
Phylogenomic databases
eggNOG	COG2365.
GeneTree	ENSGT00530000066535.
HOGENOM	HOG000188365.
OMA	PPENFSH.
OrthoDB	EOG447K3D.
Gene expression databases
Genevestigator	P53965.
GermOnline	YNL032W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016130. Tyr_Pase_AS. IPR020428. Tyr_Pase_dualsp-Pase_euk. IPR004861. Tyr_Pase_SIW14-like. [Graphical view]
Pfam	PF03162. Y_phosphatase2. 1 hit. [Graphical view]
PRINTS	PR01911. PFDSPHPHTASE.
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	980028.

Entry information

Entry name

SIW14_YEAST

Accession

Primary (citable) accession number: P53965
Secondary accession number(s): D6W1E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program