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Protein

Cell division control protein 73

Gene

CDC73

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SET2.3 Publications

GO - Molecular functioni

  • chromatin binding Source: SGD
  • RNA polymerase II core binding Source: SGD
  • RNA polymerase II C-terminal domain phosphoserine binding Source: SGD
  • transcription factor activity, RNA polymerase II transcription factor binding Source: SGD
  • transcription factor activity, TFIIF-class transcription factor binding Source: SGD

GO - Biological processi

  • histone modification Source: InterPro
  • mRNA 3'-end processing Source: SGD
  • negative regulation of DNA recombination Source: SGD
  • positive regulation of histone H3-K36 trimethylation Source: SGD
  • positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription elongation from RNA polymerase I promoter Source: SGD
  • recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex Source: SGD
  • regulation of histone H2B conserved C-terminal lysine ubiquitination Source: SGD
  • regulation of transcription-coupled nucleotide-excision repair Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • transcription elongation from RNA polymerase I promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32479-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 73
Alternative name(s):
RNA polymerase-associated protein CDC73
Gene namesi
Name:CDC73
Ordered Locus Names:YLR418C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR418C.
SGDiS000004410. CDC73.

Subcellular locationi

GO - Cellular componenti

  • Cdc73/Paf1 complex Source: SGD
  • nucleus Source: SGD
  • transcriptionally active chromatin Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Cell division control protein 73PRO_0000238580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei150 – 1501PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06697.
PeptideAtlasiQ06697.

PTM databases

iPTMnetiQ06697.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
PAF1P383518EBI-29913,EBI-12855
RPO21P0405017EBI-29913,EBI-15760
RTF1P5306410EBI-29913,EBI-16303
SLT2Q007722EBI-29913,EBI-17372
SPT5P276926EBI-29913,EBI-17937

GO - Molecular functioni

  • RNA polymerase II core binding Source: SGD
  • RNA polymerase II C-terminal domain phosphoserine binding Source: SGD

Protein-protein interaction databases

BioGridi31676. 675 interactions.
DIPiDIP-1148N.
IntActiQ06697. 22 interactions.
MINTiMINT-545984.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi239 – 2413Combined sources
Beta strandi248 – 2503Combined sources
Turni252 – 2543Combined sources
Helixi255 – 2617Combined sources
Helixi267 – 2693Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi291 – 2999Combined sources
Helixi305 – 3106Combined sources
Beta strandi311 – 3155Combined sources
Helixi320 – 3234Combined sources
Beta strandi326 – 3283Combined sources
Helixi331 – 3377Combined sources
Beta strandi338 – 3458Combined sources
Helixi352 – 3565Combined sources
Beta strandi357 – 3648Combined sources
Helixi369 – 3713Combined sources
Helixi372 – 38918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V46X-ray1.55A230-393[»]
4DM4X-ray2.19A/B235-393[»]
ProteinModelPortaliQ06697.
SMRiQ06697. Positions 234-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC73 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000001114.
HOGENOMiHOG000163861.
InParanoidiQ06697.
KOiK15175.
OMAiEYWNRIV.
OrthoDBiEOG7MPRQ9.

Family and domain databases

InterProiIPR007852. Cdc73/Parafibromin.
IPR031336. CDC73_C.
[Graphical view]
PANTHERiPTHR12466. PTHR12466. 1 hit.
PfamiPF05179. CDC73_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSLDRLRE HLKNGDKLVL KNNEGQSTDD ITKATMVETL SSDGSTQDSF
60 70 80 90 100
PLNEETEIEI DGSLVQLRII VHCWMNKDSS AADYLADCQN KQLTNVSFLQ
110 120 130 140 150
RTDLINWLSG NTESSQYLKA PGQKGETSDK VDIENKTLAG ELSTVKSTTS
160 170 180 190 200
ASLENDSEVS DPVVVETMKH ERILVDHNSA LRGAKPINFG YLIKDAELKL
210 220 230 240 250
VQSIKGSLRG SKLPPGHKGA HGRISKTNGS SGGPRKDPII LIPSAASSIL
260 270 280 290 300
TVANIKQFLL ESKYVNPRNL PSVPNGLVNI EKNFERISRP IRFIIVDNTR
310 320 330 340 350
MFTKPEYWDR VVAIFTTGHT WQFNNYQWNS PQELFQRCKG YYFHFAGDSV
360 370 380 390
PQHVQQWNVE KVELDKNKRF KDVEVVRYFW HSLEKELISR GYR
Length:393
Mass (Da):44,456
Last modified:November 1, 1996 - v1
Checksum:i9580B53EEFB75345
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20162 Genomic DNA. Translation: AAB67500.1.
BK006945 Genomic DNA. Translation: DAA09720.1.
PIRiS59383.
RefSeqiNP_013522.1. NM_001182306.1.

Genome annotation databases

EnsemblFungiiYLR418C; YLR418C; YLR418C.
GeneIDi851136.
KEGGisce:YLR418C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20162 Genomic DNA. Translation: AAB67500.1.
BK006945 Genomic DNA. Translation: DAA09720.1.
PIRiS59383.
RefSeqiNP_013522.1. NM_001182306.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V46X-ray1.55A230-393[»]
4DM4X-ray2.19A/B235-393[»]
ProteinModelPortaliQ06697.
SMRiQ06697. Positions 234-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31676. 675 interactions.
DIPiDIP-1148N.
IntActiQ06697. 22 interactions.
MINTiMINT-545984.

PTM databases

iPTMnetiQ06697.

Proteomic databases

MaxQBiQ06697.
PeptideAtlasiQ06697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR418C; YLR418C; YLR418C.
GeneIDi851136.
KEGGisce:YLR418C.

Organism-specific databases

EuPathDBiFungiDB:YLR418C.
SGDiS000004410. CDC73.

Phylogenomic databases

GeneTreeiENSGT00390000001114.
HOGENOMiHOG000163861.
InParanoidiQ06697.
KOiK15175.
OMAiEYWNRIV.
OrthoDBiEOG7MPRQ9.

Enzyme and pathway databases

BioCyciYEAST:G3O-32479-MONOMER.

Miscellaneous databases

PROiQ06697.

Family and domain databases

InterProiIPR007852. Cdc73/Parafibromin.
IPR031336. CDC73_C.
[Graphical view]
PANTHERiPTHR12466. PTHR12466. 1 hit.
PfamiPF05179. CDC73_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC73_YEAST
AccessioniPrimary (citable) accession number: Q06697
Secondary accession number(s): D6VZ54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.