CDC73_YEAST
ID CDC73_YEAST Reviewed; 393 AA.
AC Q06697; D6VZ54;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cell division control protein 73;
DE AltName: Full=RNA polymerase-associated protein CDC73;
GN Name=CDC73; OrderedLocusNames=YLR418C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9032243; DOI=10.1128/mcb.17.3.1160;
RA Shi X., Chang M., Wolf A.J., Chang C.-H., Frazer-Abel A.A., Wade P.A.,
RA Burton Z.F., Jaehning J.A.;
RT "Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex
RT distinct from the Srbp-containing holoenzyme.";
RL Mol. Cell. Biol. 17:1160-1169(1997).
RN [4]
RP SUBUNIT.
RX PubMed=10219085; DOI=10.1093/nar/27.10.2126;
RA Koch C., Wollmann P., Dahl M., Lottspeich F.;
RT "A role for Ctr9p and Paf1p in the regulation of G1 cyclin expression in
RT yeast.";
RL Nucleic Acids Res. 27:2126-2134(1999).
RN [5]
RP IDENTIFICATION IN THE PAF1 COMPLEX.
RX PubMed=11884586; DOI=10.1128/mcb.22.7.1971-1980.2002;
RA Mueller C.L., Jaehning J.A.;
RT "Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II
RT complex.";
RL Mol. Cell. Biol. 22:1971-1980(2002).
RN [6]
RP INTERACTION WITH POB3 AND SPT16.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15643076; DOI=10.1128/ec.4.1.209-220.2005;
RA Porter S.E., Penheiter K.L., Jaehning J.A.;
RT "Separation of the Saccharomyces cerevisiae Paf1 complex from RNA
RT polymerase II results in changes in its subnuclear localization.";
RL Eukaryot. Cell 4:209-220(2005).
RN [8]
RP FUNCTION.
RX PubMed=16246725; DOI=10.1016/j.molcel.2005.08.026;
RA Sheldon K.E., Mauger D.M., Arndt K.M.;
RT "A requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3'
RT end formation.";
RL Mol. Cell 20:225-236(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-150, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: The PAF1 complex is a multifunctional complex. Involved in
CC transcription initiation via genetic interactions with TATA-binding
CC proteins. Involved in elongation. It regulates 3'-end formation of
CC snR47 by modulating the recruitment or stable association of NRD1 and
CC NAB3 with RNA polymerase II. Also has a role in transcription-coupled
CC histone modification. Required for activation of RAD6 ubiquitin
CC conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126'
CC histone H2B. Activates the SET1 histone methyltransferase complex for
CC methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of
CC histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.
CC {ECO:0000269|PubMed:15643076, ECO:0000269|PubMed:16246725,
CC ECO:0000269|PubMed:9032243}.
CC -!- SUBUNIT: Component of the PAF1 complex which consists of at least
CC CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with FACT subunits POB3 and
CC SPT16. {ECO:0000269|PubMed:10219085, ECO:0000269|PubMed:11884586,
CC ECO:0000269|PubMed:12242279, ECO:0000269|PubMed:9032243}.
CC -!- INTERACTION:
CC Q06697; P38351: PAF1; NbExp=8; IntAct=EBI-29913, EBI-12855;
CC Q06697; P04050: RPO21; NbExp=17; IntAct=EBI-29913, EBI-15760;
CC Q06697; P53064: RTF1; NbExp=9; IntAct=EBI-29913, EBI-16303;
CC Q06697; Q00772: SLT2; NbExp=2; IntAct=EBI-29913, EBI-17372;
CC Q06697; P27692: SPT5; NbExp=6; IntAct=EBI-29913, EBI-17937;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15643076, ECO:0000269|PubMed:9032243}.
CC -!- SIMILARITY: Belongs to the CDC73 family. {ECO:0000305}.
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DR EMBL; U20162; AAB67500.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09720.1; -; Genomic_DNA.
DR PIR; S59383; S59383.
DR RefSeq; NP_013522.1; NM_001182306.1.
DR PDB; 3V46; X-ray; 1.55 A; A=230-393.
DR PDB; 4DM4; X-ray; 2.19 A; A/B=235-393.
DR PDB; 7DKH; X-ray; 2.90 A; C/G/K=155-211.
DR PDBsum; 3V46; -.
DR PDBsum; 4DM4; -.
DR PDBsum; 7DKH; -.
DR AlphaFoldDB; Q06697; -.
DR SMR; Q06697; -.
DR BioGRID; 31676; 1016.
DR ComplexPortal; CPX-1726; PAF1 complex.
DR DIP; DIP-1148N; -.
DR IntAct; Q06697; 24.
DR MINT; Q06697; -.
DR STRING; 4932.YLR418C; -.
DR iPTMnet; Q06697; -.
DR MaxQB; Q06697; -.
DR PaxDb; Q06697; -.
DR PRIDE; Q06697; -.
DR EnsemblFungi; YLR418C_mRNA; YLR418C; YLR418C.
DR GeneID; 851136; -.
DR KEGG; sce:YLR418C; -.
DR SGD; S000004410; CDC73.
DR VEuPathDB; FungiDB:YLR418C; -.
DR eggNOG; KOG3786; Eukaryota.
DR GeneTree; ENSGT00390000001114; -.
DR HOGENOM; CLU_025849_2_0_1; -.
DR InParanoid; Q06697; -.
DR OMA; GHTWQFN; -.
DR BioCyc; YEAST:G3O-32479-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q06697; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06697; protein.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:SGD.
DR GO; GO:0000791; C:euchromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IDA:SGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0016571; P:histone methylation; IC:ComplexPortal.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IMP:SGD.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; IMP:SGD.
DR GO; GO:2001165; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues; IMP:SGD.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0034402; P:recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex; IMP:SGD.
DR GO; GO:2001173; P:regulation of histone H2B conserved C-terminal lysine ubiquitination; IDA:SGD.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IGI:SGD.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 3.40.50.11990; -; 1.
DR InterPro; IPR007852; Cdc73/Parafibromin.
DR InterPro; IPR031336; CDC73_C.
DR InterPro; IPR038103; CDC73_C_sf.
DR PANTHER; PTHR12466; PTHR12466; 1.
DR Pfam; PF05179; CDC73_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..393
FT /note="Cell division control protein 73"
FT /id="PRO_0000238580"
FT REGION 210..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:7DKH"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4DM4"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:3V46"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:3V46"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:4DM4"
FT HELIX 372..389
FT /evidence="ECO:0007829|PDB:3V46"
SQ SEQUENCE 393 AA; 44456 MW; 9580B53EEFB75345 CRC64;
MANSLDRLRE HLKNGDKLVL KNNEGQSTDD ITKATMVETL SSDGSTQDSF PLNEETEIEI
DGSLVQLRII VHCWMNKDSS AADYLADCQN KQLTNVSFLQ RTDLINWLSG NTESSQYLKA
PGQKGETSDK VDIENKTLAG ELSTVKSTTS ASLENDSEVS DPVVVETMKH ERILVDHNSA
LRGAKPINFG YLIKDAELKL VQSIKGSLRG SKLPPGHKGA HGRISKTNGS SGGPRKDPII
LIPSAASSIL TVANIKQFLL ESKYVNPRNL PSVPNGLVNI EKNFERISRP IRFIIVDNTR
MFTKPEYWDR VVAIFTTGHT WQFNNYQWNS PQELFQRCKG YYFHFAGDSV PQHVQQWNVE
KVELDKNKRF KDVEVVRYFW HSLEKELISR GYR
