P20604 (PP11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	311 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 cascade Inferred from mutant phenotype PubMed 15367655. Source: SGD actin cytoskeleton organization Inferred from mutant phenotype PubMed 12080055. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular response to oxidative stress Inferred from mutant phenotype PubMed 18357452. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype PubMed 12080055. Source: SGD intracellular protein kinase cascade Inferred from mutant phenotype PubMed 12080055. Source: SGD mitosis 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_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD nucleus Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Traceable author statement PubMed 9123967. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RRD1	P40454	4	EBI-13707,EBI-25278
SAP155	P43612	14	EBI-13707,EBI-16370
SAP185	P40856	11	EBI-13707,EBI-16384
SAP190	P36123	6	EBI-13707,EBI-16392
TAP42	Q04372	8	EBI-13707,EBI-18926

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 311	311	Serine/threonine-protein phosphatase PP1-1		PRO_0000058881
Sites
	Active site	115	1	Proton donor By similarity
	Metal binding	53	1	Iron By similarity
	Metal binding	55	1	Iron By similarity
	Metal binding	82	1	Iron By similarity
	Metal binding	82	1	Manganese By similarity
	Metal binding	114	1	Manganese By similarity
	Metal binding	164	1	Manganese By similarity
	Metal binding	238	1	Manganese By similarity
Experimental info
	Mutagenesis	35	1	L → A: Reduced interaction with TAP42. Ref.5
	Mutagenesis	37 – 38	2	EE → AA: Nearly no interaction with TAP42. Ref.5
	Mutagenesis	38	1	E → A: Normal interaction with TAP42. Ref.5
	Mutagenesis	40	1	N → A: Normal interaction with TAP42. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P20604 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: AF52BC65E4E715EC	FASTA	311	35,538
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	PABY1. A31874.
RefSeq	NP_010236.1. NM_001180106.1.
3D structure databases
ProteinModelPortal	P20604.
SMR	P20604. Positions 7-291.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5850N.
IntAct	P20604. 60 interactions.
MINT	MINT-615434.
STRING	4932.YDL047W.
Proteomic databases
PaxDb	P20604.
PeptideAtlas	P20604.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL047W; YDL047W; YDL047W.
GeneID	851513.
KEGG	sce:YDL047W.
Organism-specific databases
CYGD	YDL047w.
SGD	S000002205. SIT4.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00550000074961.
HOGENOM	HOG000172696.
KO	K15427.
OMA	KIFSAVP.
OrthoDB	EOG48KVKR.
Gene expression databases
Genevestigator	P20604.
GermOnline	YDL047W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968878.

Entry information

Entry name

PP11_YEAST

Accession

Primary (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:	April 3, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program