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P20604 (PP11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-1

EC=3.1.3.16
Gene names
Name:SIT4
Synonyms:PPH1
Ordered Locus Names:YDL047W
ORF Names:D2693
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the dephosphorylation of the large subunit of RNA polymerase II. Is required in late G1 for normal G1 cyclin expression, bud initiation and expression of certain genes that are periodically expressed during late G1. Associates with the SAP proteins in a cell cycle-dependent manner.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex. Forms a ternary complex with RRD1-TAP42. Ref.5 Ref.6 Ref.8 Ref.9

Subcellular location

Cytoplasm.

Developmental stage

Functions in the late cell cycle G1 phase for progression into the S phase, possibly associated in two separate complexes with the phosphorylated forms of p155 and p190, two high MW proteins.

Miscellaneous

Present with 3970 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from mutant phenotype PubMed 15150670. Source: SGD

G1/S transition of mitotic cell cycle

Inferred from genetic interaction Ref.4. Source: SGD

TOR signaling

Inferred from mutant phenotype PubMed 15367655. Source: SGD

actin cytoskeleton organization

Inferred from mutant phenotype PubMed 12080055. Source: SGD

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 18357452. Source: SGD

dephosphorylation

Inferred from mutant phenotype PubMed 15367655. Source: SGD

fungal-type cell wall organization

Inferred from mutant phenotype PubMed 12080055. Source: SGD

intracellular signal transduction

Inferred from mutant phenotype PubMed 12080055. Source: SGD

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

replicative cell aging

Inferred from mutant phenotype PubMed 15843932. Source: SGD

tRNA wobble uridine modification

Inferred from mutant phenotype PubMed 18755837. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay Ref.4. Source: SGD

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11805826PubMed 15150670PubMed 16429126PubMed 16874307PubMed 18467557PubMed 19749176PubMed 20489023PubMed 21179020PubMed 23267104. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from mutant phenotype PubMed 23864707. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Serine/threonine-protein phosphatase PP1-1
PRO_0000058881

Sites

Active site1151Proton donor By similarity
Metal binding531Manganese 1 By similarity
Metal binding551Manganese 1 By similarity
Metal binding821Manganese 1 By similarity
Metal binding821Manganese 2 By similarity
Metal binding1141Manganese 2 By similarity
Metal binding1641Manganese 2 By similarity
Metal binding2381Manganese 2 By similarity

Experimental info

Mutagenesis351L → A: Reduced interaction with TAP42. Ref.5
Mutagenesis37 – 382EE → AA: Nearly no interaction with TAP42. Ref.5
Mutagenesis381E → A: Normal interaction with TAP42. Ref.5
Mutagenesis401N → A: Normal interaction with TAP42. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P20604 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: AF52BC65E4E715EC

FASTA31135,538
        10         20         30         40         50         60 
MVSRGPDEWL ETIKKCQALT ENEMKQLCEM VKELLMEESN IQPVQTPVTV CGDIHGQFHD 

        70         80         90        100        110        120 
LLELFRTAGG FPDDINYIFL GDYVDRGYYS LETFTLLMCL KVKYPAKITL VRGNHESRQI 

       130        140        150        160        170        180 
TQVYGFYEEC LNKYGSTTVW KYCCQVFDFL TLAAIIDGKI LCVHGGLSPE IRMLDQIRVL 

       190        200        210        220        230        240 
SRAQEVPHEG GFSDLLWSDP DNVEAWQVSP RGAGWLFGSK VAREFNHVNG LNLIARAHQL 

       250        260        270        280        290        300 
VMEGFKYHFP EKDVVTVWSA PNYCYRCGNV ASVMKVDEDL EPTFKIFSAV PDDYIRESTA 

       310 
NHNNQRAGYF L 

« Hide

References

« Hide 'large scale' references
[1]"A suppressor of a HIS4 transcriptional defect encodes a protein with homology to the catalytic subunit of protein phosphatases."
Arndt K.T., Styles C.A., Fink G.R.
Cell 56:527-537(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"The SIT4 protein phosphatase functions in late G1 for progression into S phase."
Sutton A., Immanuel D., Arndt K.T.
Mol. Cell. Biol. 11:2133-2148(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases."
Wang H., Wang X., Jiang Y.
Mol. Biol. Cell 14:4342-4351(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAP42, MUTAGENESIS OF LEU-35; 37-GLU-GLU-38; GLU-38 AND ASN-40.
[6]"Multiple roles of Tap42 in mediating rapamycin-induced transcriptional changes in yeast."
Duevel K., Santhanam A., Garrett S., Schneper L., Broach J.R.
Mol. Cell 11:1467-1478(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAP42.
[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]"Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2."
Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V., Goris J.
Biochem. J. 386:93-102(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPE1 AND RRD1.
[9]"The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes."
Zheng Y., Jiang Y.
Mol. Biol. Cell 16:2119-2127(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RRD1 AND TAP42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24395 Genomic DNA. Translation: AAA56864.1.
Z71781 Genomic DNA. Translation: CAA96442.1.
Z74095 Genomic DNA. Translation: CAA98609.1.
BK006938 Genomic DNA. Translation: DAA11808.1.
PIRPABY1. A31874.
RefSeqNP_010236.1. NM_001180106.1.

3D structure databases

ProteinModelPortalP20604.
SMRP20604. Positions 7-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32011. 169 interactions.
DIPDIP-5850N.
IntActP20604. 40 interactions.
MINTMINT-615434.
STRING4932.YDL047W.

Proteomic databases

MaxQBP20604.
PaxDbP20604.
PeptideAtlasP20604.
PRIDEP20604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL047W; YDL047W; YDL047W.
GeneID851513.
KEGGsce:YDL047W.

Organism-specific databases

CYGDYDL047w.
SGDS000002205. SIT4.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074961.
HOGENOMHOG000172696.
KOK15427.
OMAQKDSAYT.
OrthoDBEOG7FFN29.

Enzyme and pathway databases

BioCycYEAST:G3O-29466-MONOMER.

Gene expression databases

GenevestigatorP20604.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968878.
PROP20604.

Entry information

Entry namePP11_YEAST
AccessionPrimary (citable) accession number: P20604
Secondary accession number(s): D6VRU8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families