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P25441 (RPC4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase III subunit RPC4
Short name=RNA polymerase III subunit C4
Alternative name(s):
C53
DNA-directed RNA polymerase III 47 kDa polypeptide
Gene names
Name:RPC53
Synonyms:RPC4
Ordered Locus Names:YDL150W
ORF Names:D1557
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for tRNA synthesis. The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator recognition and reinitiation. Ref.10

Subunit structure

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with RPC37/RPC5. RPC53/RPC4, RPC37/RPC5 and RPC11/RPC10 probably form a Pol III subcomplex. Ref.6

Subcellular location

Nucleus Ref.7.

Miscellaneous

Present with 998 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the eukaryotic RPC4/POLR3D RNA polymerase subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422DNA-directed RNA polymerase III subunit RPC4
PRO_0000073969

Regions

Motif25 – 295Nuclear localization signal Potential

Amino acid modifications

Modified residue1191Phosphoserine Ref.14
Modified residue1371Phosphoserine Ref.14
Modified residue1381Phosphoserine Ref.14
Modified residue1781Phosphoserine Ref.11
Modified residue1821Phosphoserine Ref.11
Modified residue2241Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
Modified residue2281Phosphothreonine Ref.11 Ref.12 Ref.13
Modified residue2321Phosphothreonine Ref.9 Ref.11 Ref.12 Ref.14

Experimental info

Sequence conflict421E → K in CAA45073. Ref.1
Sequence conflict2641L → LGL Ref.1
Sequence conflict284 – 2852NA → KR in CAA45073. Ref.1
Sequence conflict3921Q → H in CAA45073. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25441 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 206FBAC274BC72D5

FASTA42246,667
        10         20         30         40         50         60 
MSSNKGNGRL PSLKDSSSNG GGSAKPSLKF KPKAVARKSK EEREAAASKV KLEEESKRGN 

        70         80         90        100        110        120 
DKKHFNNKNK RVTGAGGQQR RMAKYLNNTH VISSGPLAAG NFVSEKGDLR RGFIKSEGSG 

       130        140        150        160        170        180 
SSLVQKGLET IDNGAESSEN EAEDDDNEGV ASKSKKKFNM GKEFEARNLI EDEDDGESEK 

       190        200        210        220        230        240 
SSDVDMDDEE WRSKRIEQLF PVRPVRVRHE DVETVKREIQ EALSEKPTRE PTPSVKTEPV 

       250        260        270        280        290        300 
GTGLQSYLEE RERQVNEKLA DLGLEKEFQS VDGKEAAAEL ELLNADHQHI LRKLKKMNNK 

       310        320        330        340        350        360 
PERFMVFQLP TRLPAFERPA VKEEKEDMET QASDPSKKKK NIKKKDTKDA LSTRELAGKV 

       370        380        390        400        410        420 
GSIRVHKSGK LSVKIGNVVM DIGKGAETTF LQDVIALSIA DDASSAELLG RVDGKIVVTP 


QI

« Hide

References

« Hide 'large scale' references
[1]"RPC53 encodes a subunit of Saccharomyces cerevisiae RNA polymerase C (III) whose inactivation leads to a predominantly G1 arrest."
Mann C., Micouin J.-Y., Chiannilkulchai N., Treich I., Buhler J.-M., Sentenac A.
Mol. Cell. Biol. 12:4314-4326(1992) [PubMed: 1406624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of a 23 kb region on the left arm of yeast chromosome IV."
Delaveau T.T.D., Blugeon C., Jacq C., Perea J.
Yeast 12:1587-1592(1996) [PubMed: 8972581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The yeast RNA polymerase III transcription machinery: a paradigm for eukaryotic gene activation."
Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O., Werner M., Carles C., Sentenac A.
Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998) [PubMed: 10384303] [Abstract]
Cited for: REVIEW ON THE RNA POL III COMPLEX.
[6]"A protein-protein interaction map of yeast RNA polymerase III."
Flores A., Briand J.-F., Gadal O., Andrau J.-C., Rubbi L., Van Mullem V., Boschiero C., Goussot M., Marck C., Carles C., Thuriaux P., Sentenac A., Werner M.
Proc. Natl. Acad. Sci. U.S.A. 96:7815-7820(1999) [PubMed: 10393904] [Abstract]
Cited for: INTERACTION WITH RPC4.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, MASS SPECTROMETRY.
Strain: YAL6B.
[10]"A subcomplex of RNA polymerase III subunits involved in transcription termination and reinitiation."
Landrieux E., Alic N., Ducrot C., Acker J., Riva M., Carles C.
EMBO J. 25:118-128(2006) [PubMed: 16362040] [Abstract]
Cited for: FUNCTION OF THE RPC53-RPC37 SUBCOMPLEX.
[11]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-182; SER-224; THR-228 AND THR-232, MASS SPECTROMETRY.
Strain: ADR376.
[12]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-228 AND THR-232, MASS SPECTROMETRY.
[13]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND THR-228, MASS SPECTROMETRY.
[14]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-137; SER-138; SER-224 AND THR-232, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X63501 Genomic DNA. Translation: CAA45073.1.
X97751 Genomic DNA. Translation: CAA66340.1.
Z74199 Genomic DNA. Translation: CAA98725.1.
BK006938 Genomic DNA. Translation: DAA11708.1.
PIRS67698.
RefSeqNP_010131.1. NM_001180210.1.

3D structure databases

ProteinModelPortalP25441.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1003N.
IntActP25441. 20 interactions.
MINTMINT-399225.
STRINGP25441.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL150W; YDL150W; YDL150W.
GeneID851404.
KEGGsce:YDL150W.
NMPDRfig|4932.3.peg.868.

Organism-specific databases

CYGDYDL150w.
SGDS000002309. RPC53.

Phylogenomic databases

eggNOGfuNOG08452.
GeneTreeEFGT00050000002638.
HOGENOMHBG203353.
OMAMSNRLES.
OrthoDBEOG48WGBB.

Enzyme and pathway databases

ReactomeREACT_87991. Transcription.

Gene expression databases

ArrayExpressP25441.
GenevestigatorP25441.
GermOnlineYDL150W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR007811. RNA_pol_III_Rpc4.
[Graphical view]
KOK03026.
PANTHERPTHR13408. RNA_pol_Rpc4. 1 hit.
PfamPF05132. RNA_pol_Rpc4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968576.

Entry information

Entry nameRPC4_YEAST
AccessionPrimary (citable) accession number: P25441
Secondary accession number(s): D6VRJ8, Q12073
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents