P53538 (SSU72_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Short name=CTD phosphatase SSU72
EC=3.1.3.16

Alternative name(s):
Suppressor of SUA7 protein 2

Gene names

Name:	SSU72
Ordered Locus Names:	YNL222W
ORF Names:	N1279

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

General annotation (Comments)

Function	Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. SSU72 is required for 3'-end formation of snoRNAs. Ref.5 Ref.7 Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). Ref.5 Ref.7
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2. Ref.6
Subcellular location	Nucleus Ref.6.
Sequence similarities	Belongs to the SSU72 phosphatase family.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dephosphorylation of RNA polymerase II C-terminal domain Inferred from mutant phenotype Ref.7PubMed 22235117. Source: SGD mRNA 3'-end processing Inferred from mutant phenotype PubMed 12704082. Source: SGD mRNA cleavage Inferred from mutant phenotype PubMed 12704082. Source: SGD snoRNA transcription Inferred from mutant phenotype Ref.5. Source: SGD termination of RNA polymerase II transcription, exosome-dependent Inferred from mutant phenotype PubMed 12944462. Source: SGD termination of RNA polymerase II transcription, poly(A)-coupled Inferred from mutant phenotype PubMed 12944462. Source: SGD transcription antitermination Inferred from mutant phenotype PubMed 12453421. Source: SGD transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype PubMed 17101794. Source: SGD transcriptional start site selection at RNA polymerase II promoter Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	mRNA cleavage and polyadenylation specificity factor complex Inferred from direct assay Ref.6. Source: SGD
Molecular_function	CTD phosphatase activity Inferred from mutant phenotype Ref.7PubMed 22235117. Source: SGD protein tyrosine phosphatase activity Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-18134,EBI-18134
CDC55	Q00362	1	EBI-18134,EBI-1942

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 206	206	RNA polymerase II subunit A C-terminal domain phosphatase SSU72		PRO_0000072230
Amino acid modifications
	Modified residue	41	1	Phosphothreonine Ref.8
	Modified residue	43	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	199	1	S → P in AAS56747. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P53538 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 1AE1B29B87C82FE9	FASTA	206	23,469
	10 20 30 40 50 60 MPSHRNSNLK FCTVCASNNN RSMESHKVLQ EAGYNVSSYG TGSAVRLPGL SIDKPNVYSF 70 80 90 100 110 120 GTPYNDIYND LLSQSADRYK SNGLLQMLDR NRRLKKAPEK WQESTKVFDF VFTCEERCFD 130 140 150 160 170 180 AVCEDLMNRG GKLNKIVHVI NVDIKDDDEN AKIGSKAILE LADMLNDKIE QCEKDDIPFE 190 200 DCIMDILTEW QSSHSQLPSL YAPSYY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Synthetic enhancement of a TFIIB defect by a mutation in SSU72, an essential yeast gene encoding a novel protein that affects transcription start site selection in vivo." Sun Z.W., Hampsey M. Mol. Cell. Biol. 16:1557-1566(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Ssu72 is a phosphatase essential for transcription termination of snoRNAs and specific mRNAs in yeast." Ganem C., Devaux F., Torchet C., Jacq C., Quevillon-Cheruel S., Labesse G., Facca C., Faye G. EMBO J. 22:1588-1598(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SNORNA 3-END FORMATION.
[6]	"Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends." Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J. J. Biol. Chem. 278:33000-33010(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]	"Ssu72 Is an RNA polymerase II CTD phosphatase." Krishnamurthy S., He X., Reyes-Reyes M., Moore C., Hampsey M. Mol. Cell 14:387-394(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A PHOSPHATASE, FUNCTION IN SNORNA 3'-END FORMATION.
[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 THR-41 AND SER-43, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U20390 Genomic DNA. Translation: AAA86497.1. Z71498 Genomic DNA. Translation: CAA96125.1. AY558421 Genomic DNA. Translation: AAS56747.1. BK006947 Genomic DNA. Translation: DAA10334.1.
PIR	S63180.
RefSeq	NP_014177.1. NM_001183060.1.
3D structure databases
ProteinModelPortal	P53538.
SMR	P53538. Positions 9-191.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6700N.
IntAct	P53538. 16 interactions.
MINT	MINT-432815.
STRING	4932.YNL222W.
Proteomic databases
PaxDb	P53538.
PeptideAtlas	P53538.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL222W; YNL222W; YNL222W.
GeneID	855499.
KEGG	sce:YNL222W.
Organism-specific databases
CYGD	YNL222w.
SGD	S000005166. SSU72.
Phylogenomic databases
eggNOG	COG5211.
GeneTree	ENSGT00390000010165.
HOGENOM	HOG000183445.
KO	K15544.
OMA	SMEAHNF.
OrthoDB	EOG4DFSXT.
Gene expression databases
Genevestigator	P53538.
GermOnline	YNL222W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006811. RNA_pol_II_suA. [Graphical view]
PANTHER	PTHR20383. PTHR20383. 1 hit.
Pfam	PF04722. Ssu72. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979493.

Entry information

Entry name

SSU72_YEAST

Accession

Primary (citable) accession number: P53538
Secondary accession number(s): D6W0W8, Q6Q569

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program