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Q06697 (CDC73_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cell division control protein 73
Alternative name(s):
RNA polymerase-associated protein CDC73
Gene names
Name:CDC73
Ordered Locus Names:YLR418C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. Ref.3 Ref.7 Ref.8

Subunit structure

Component of the PAF1 complex which consists of at least CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with FACT subunits POB3 and SPT16. Ref.3 Ref.4 Ref.6

Subcellular location

Nucleusnucleoplasm Ref.3 Ref.7.

Sequence similarities

Belongs to the CDC73 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAF1P383516EBI-29913,EBI-12855
SLT2Q007722EBI-29913,EBI-17372

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Cell division control protein 73
PRO_0000238580

Amino acid modifications

Modified residue1141Phosphoserine Ref.9
Modified residue1431Phosphoserine Ref.9
Modified residue1491Phosphothreonine Ref.9
Modified residue1501Phosphoserine Ref.9
Modified residue1911Phosphotyrosine Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q06697 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9580B53EEFB75345

FASTA39344,456
        10         20         30         40         50         60 
MANSLDRLRE HLKNGDKLVL KNNEGQSTDD ITKATMVETL SSDGSTQDSF PLNEETEIEI 

        70         80         90        100        110        120 
DGSLVQLRII VHCWMNKDSS AADYLADCQN KQLTNVSFLQ RTDLINWLSG NTESSQYLKA 

       130        140        150        160        170        180 
PGQKGETSDK VDIENKTLAG ELSTVKSTTS ASLENDSEVS DPVVVETMKH ERILVDHNSA 

       190        200        210        220        230        240 
LRGAKPINFG YLIKDAELKL VQSIKGSLRG SKLPPGHKGA HGRISKTNGS SGGPRKDPII 

       250        260        270        280        290        300 
LIPSAASSIL TVANIKQFLL ESKYVNPRNL PSVPNGLVNI EKNFERISRP IRFIIVDNTR 

       310        320        330        340        350        360 
MFTKPEYWDR VVAIFTTGHT WQFNNYQWNS PQELFQRCKG YYFHFAGDSV PQHVQQWNVE 

       370        380        390 
KVELDKNKRF KDVEVVRYFW HSLEKELISR GYR 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme."
Shi X., Chang M., Wolf A.J., Chang C.-H., Frazer-Abel A.A., Wade P.A., Burton Z.F., Jaehning J.A.
Mol. Cell. Biol. 17:1160-1169(1997) [PubMed: 9032243] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[4]"A role for Ctr9p and Paf1p in the regulation of G1 cyclin expression in yeast."
Koch C., Wollmann P., Dahl M., Lottspeich F.
Nucleic Acids Res. 27:2126-2134(1999) [PubMed: 10219085] [Abstract]
Cited for: SUBUNIT.
[5]"Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex."
Mueller C.L., Jaehning J.A.
Mol. Cell. Biol. 22:1971-1980(2002) [PubMed: 11884586] [Abstract]
Cited for: IDENTIFICATION IN THE PAF1 COMPLEX.
[6]"RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach."
Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F.
Mol. Cell. Biol. 22:6979-6992(2002) [PubMed: 12242279] [Abstract]
Cited for: INTERACTION WITH POB3 AND SPT16.
[7]"Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization."
Porter S.E., Penheiter K.L., Jaehning J.A.
Eukaryot. Cell 4:209-220(2005) [PubMed: 15643076] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"A requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation."
Sheldon K.E., Mauger D.M., Arndt K.M.
Mol. Cell 20:225-236(2005) [PubMed: 16246725] [Abstract]
Cited for: FUNCTION.
[9]"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-114; SER-143; THR-149; SER-150 AND TYR-191, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20162 Genomic DNA. Translation: AAB67500.1.
BK006945 Genomic DNA. Translation: DAA09720.1.
PIRS59383.
RefSeqNP_013522.1. NM_001182306.1.

3D structure databases

ProteinModelPortalQ06697.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1148N.
IntActQ06697. 19 interactions.
MINTMINT-545984.
STRINGQ06697.

Proteomic databases

PeptideAtlasQ06697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR418C; YLR418C; YLR418C.
GeneID851136.
KEGGsce:YLR418C.
NMPDRfig|4932.3.peg.4552.

Organism-specific databases

CYGDYLR418c.
SGDS000004410. CDC73.

Phylogenomic databases

eggNOGfuNOG04767.
GeneTreeEFGT00050000001495.
HOGENOMHBG395398.
OMATRFILVD.
OrthoDBEOG4T1MWK.

Gene expression databases

ArrayExpressQ06697.
GenevestigatorQ06697.
GermOnlineYLR418C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR007852. RNA_pol_access_fac_Cdc73.
[Graphical view]
KOK15175.
PANTHERPTHR12466. Cdc73. 1 hit.
PfamPF05179. CDC73. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967887.

Entry information

Entry nameCDC73_YEAST
AccessionPrimary (citable) accession number: Q06697
Secondary accession number(s): D6VZ54
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 82 of the entry and version 1 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