Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P53538 (SSU72_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 123. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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 processmRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay 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

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.5. Source: GOC

snoRNA transcription

Inferred from mutant phenotype Ref.5. Source: SGD

termination of RNA polymerase II transcription

Inferred from mutant phenotype Ref.5PubMed 22235117. 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

transcription initiation from RNA polymerase II promoter

Inferred from genetic interaction PubMed 11046131. Source: SGD

transcriptional start site selection at RNA polymerase II promoter

Inferred from mutant phenotype Ref.1. Source: SGD

   Cellular_componentmRNA cleavage and polyadenylation specificity factor complex

Inferred from direct assay Ref.6. Source: SGD

nucleus

Inferred from genetic interaction PubMed 11046131. Source: SGD

   Molecular_functionCTD phosphatase activity

Inferred from direct assay Ref.7PubMed 22235117. Source: SGD

phosphoprotein phosphatase activity

Inferred from genetic interaction Ref.5. Source: SGD

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 22235117. Source: SGD

protein tyrosine phosphatase activity

Inferred from direct assay Ref.5. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206RNA polymerase II subunit A C-terminal domain phosphatase SSU72
PRO_0000072230

Experimental info

Sequence conflict1991S → P in AAS56747. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P53538 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1AE1B29B87C82FE9

FASTA20623,469
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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]"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]"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. expand/collapse author list , 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS63180.
RefSeqNP_014177.1. NM_001183060.1.

3D structure databases

ProteinModelPortalP53538.
SMRP53538. Positions 9-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35614. 134 interactions.
DIPDIP-6700N.
IntActP53538. 16 interactions.
MINTMINT-432815.
STRING4932.YNL222W.

Proteomic databases

MaxQBP53538.
PaxDbP53538.
PeptideAtlasP53538.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL222W; YNL222W; YNL222W.
GeneID855499.
KEGGsce:YNL222W.

Organism-specific databases

CYGDYNL222w.
SGDS000005166. SSU72.

Phylogenomic databases

eggNOGCOG5211.
GeneTreeENSGT00390000010165.
HOGENOMHOG000183445.
KOK15544.
OMAMAKSNDI.
OrthoDBEOG7GTTG0.

Enzyme and pathway databases

BioCycYEAST:G3O-33225-MONOMER.

Gene expression databases

GenevestigatorP53538.

Family and domain databases

InterProIPR006811. RNA_pol_II_suA.
[Graphical view]
PANTHERPTHR20383. PTHR20383. 1 hit.
PfamPF04722. Ssu72. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979493.
PROP53538.

Entry information

Entry nameSSU72_YEAST
AccessionPrimary (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 14, 2014
This is version 123 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 XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families