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Protein

Tyrosine-protein phosphatase SIW14

Gene

SIW14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in actin filament organization and endocytosis.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei214 – 2141Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: SGD

GO - Biological processi

  1. actin filament organization Source: SGD
  2. endocytosis Source: SGD
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. protein dephosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciYEAST:G3O-33069-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase SIW14 (EC:3.1.3.48)
Gene namesi
Name:SIW14
Ordered Locus Names:YNL032W
ORF Names:N2746
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL032w.
SGDiS000004977. SIW14.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Tyrosine-protein phosphatase SIW14PRO_0000094922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53965.
PaxDbiP53965.

Expressioni

Gene expression databases

GenevestigatoriP53965.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
OCA1P509464EBI-28668,EBI-28814
OCA2P539494EBI-28668,EBI-28725

Protein-protein interaction databases

BioGridi35795. 118 interactions.
DIPiDIP-1990N.
IntActiP53965. 21 interactions.
MINTiMINT-384829.
STRINGi4932.YNL032W.

Structurei

3D structure databases

ProteinModelPortaliP53965.
SMRiP53965. Positions 116-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2365.
GeneTreeiENSGT00530000066535.
HOGENOMiHOG000188365.
InParanoidiP53965.
KOiK18045.
OMAiPPENFSH.
OrthoDBiEOG7Z0K6V.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR020428. Tyr_Pase_dualsp-Pase_euk.
IPR004861. Tyr_Pase_SIW14-like.
[Graphical view]
PfamiPF03162. Y_phosphatase2. 1 hit.
[Graphical view]
PRINTSiPR01911. PFDSPHPHTASE.
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLYQAKNDE GSDPKSSSKI DDLIENEAEI IRLIKEDGKL LIDNGDGRDI
60 70 80 90 100
HNIIQEDKLL SVEFNEVLKR FHGEEKSDIP RKEFDEDEDD GYDSNEHHQK
110 120 130 140 150
TIEVMNTLNH VINKEVIPPE NFSHVVGEIY RSSFPRQENF SFLHERLKLK
160 170 180 190 200
SILVLIPEEY PQENLNFLKL TGIKLYQVGM SGNKEPFVNI PSHLLTKALE
210 220 230 240 250
IVLNPANQPI LIHCNRGKHR TGCLIGCIRK LQNWSLTMIF DEYRRFAFPK
260 270 280
ARALDQQFIE MYDDDEIKRI ASKNNWLPLQ W
Length:281
Mass (Da):32,755
Last modified:October 1, 1996 - v1
Checksum:i88BD8AFC620B4570
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71308 Genomic DNA. Translation: CAA95895.1.
BK006947 Genomic DNA. Translation: DAA10513.1.
PIRiS62954.
RefSeqiNP_014366.3. NM_001182871.3.

Genome annotation databases

EnsemblFungiiYNL032W; YNL032W; YNL032W.
GeneIDi855699.
KEGGisce:YNL032W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71308 Genomic DNA. Translation: CAA95895.1.
BK006947 Genomic DNA. Translation: DAA10513.1.
PIRiS62954.
RefSeqiNP_014366.3. NM_001182871.3.

3D structure databases

ProteinModelPortaliP53965.
SMRiP53965. Positions 116-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35795. 118 interactions.
DIPiDIP-1990N.
IntActiP53965. 21 interactions.
MINTiMINT-384829.
STRINGi4932.YNL032W.

Proteomic databases

MaxQBiP53965.
PaxDbiP53965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL032W; YNL032W; YNL032W.
GeneIDi855699.
KEGGisce:YNL032W.

Organism-specific databases

CYGDiYNL032w.
SGDiS000004977. SIW14.

Phylogenomic databases

eggNOGiCOG2365.
GeneTreeiENSGT00530000066535.
HOGENOMiHOG000188365.
InParanoidiP53965.
KOiK18045.
OMAiPPENFSH.
OrthoDBiEOG7Z0K6V.

Enzyme and pathway databases

BioCyciYEAST:G3O-33069-MONOMER.

Miscellaneous databases

NextBioi980028.

Gene expression databases

GenevestigatoriP53965.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR020428. Tyr_Pase_dualsp-Pase_euk.
IPR004861. Tyr_Pase_SIW14-like.
[Graphical view]
PfamiPF03162. Y_phosphatase2. 1 hit.
[Graphical view]
PRINTSiPR01911. PFDSPHPHTASE.
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSIW14_YEAST
AccessioniPrimary (citable) accession number: P53965
Secondary accession number(s): D6W1E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4070 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.