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UniProtKB/Swiss-Prot entry P06104

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UBC2_YEAST
Primary accession number P06104
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 93)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 2
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase UBC2
Ubiquitin carrier protein UBC2
Radiation sensitivity protein 6
Gene name
Name: RAD6
Synonyms: UBC2
OrderedLocusNames: YGL058W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3881753 [NCBI, ExPASy, EBI, Israel, Japan]
Reynolds P., Weber S., Prakash L.;
"RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive aspartates.";
Proc. Natl. Acad. Sci. U.S.A. 82:168-172(1985).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(199707)13:9<861::AID-YEA125>3.3.CO;2-0; PubMed=9234674 [NCBI, ExPASy, EBI, Israel, Japan]
Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
Yeast 13:861-869(1997).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
 PROTEIN SEQUENCE OF 77-91, AND FUNCTION.
DOI=10.1038/329131a0; PubMed=3306404 [NCBI, ExPASy, EBI, Israel, Japan]
Jentsch S., McGrath J.P., Varshavsky A.;
"The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme.";
Nature 329:131-134(1987).
[5]
 FUNCTION.
DOI=10.1007/BF00352514; PubMed=7038392 [NCBI, ExPASy, EBI, Israel, Japan]
Montelone B.A., Prakash S., Prakash L.;
"Recombination and mutagenesis in rad6 mutants of Saccharomyces cerevisiae: evidence for multiple functions of the RAD6 gene.";
Mol. Gen. Genet. 184:410-415(1981).
[6]
 INDUCTION.
DOI=10.1093/nar/18.4.771; PubMed=2179869 [NCBI, ExPASy, EBI, Israel, Japan]
Madura K., Prakash S., Prakash L.;
"Expression of the Saccharomyces cerevisiae DNA repair gene RAD6 that encodes a ubiquitin conjugating enzyme, increases in response to DNA damage and in meiosis but remains constant during the mitotic cell cycle.";
Nucleic Acids Res. 18:771-778(1990).
[7]
 FUNCTION, AND MUTAGENESIS OF CYS-88.
PubMed=2157209 [NCBI, ExPASy, EBI, Israel, Japan]
Sung P., Prakash S., Prakash L.;
"Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitin-conjugating activity and its various biological functions.";
Proc. Natl. Acad. Sci. U.S.A. 87:2695-2699(1990).
[8]
 FUNCTION, AND INTERACTION WITH UBR1.
PubMed=1651502 [NCBI, ExPASy, EBI, Israel, Japan]
Dohmen R.J., Madura K., Bartel B., Varshavsky A.;
"The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 88:7351-7355(1991).
[9]
 FUNCTION.
PubMed=2065660 [NCBI, ExPASy, EBI, Israel, Japan]
Sung P., Berleth E., Pickart C.M., Prakash S., Prakash L.;
"Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme.";
EMBO J. 10:2187-2193(1991).
[10]
 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBR1, AND MUTAGENESIS OF 1-MET--LEU-9.
PubMed=8436296 [NCBI, ExPASy, EBI, Israel, Japan]
Watkins J.F., Sung P., Prakash S., Prakash L.;
"The extremely conserved amino terminus of RAD6 ubiquitin-conjugating enzyme is essential for amino-end rule-dependent protein degradation.";
Genes Dev. 7:250-261(1993).
[11]
 FUNCTION, AND INTERACTION WITH RAD18 AND UBR1.
PubMed=7926769 [NCBI, ExPASy, EBI, Israel, Japan]
Bailly V., Lamb J., Sung P., Prakash S., Prakash L.;
"Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites.";
Genes Dev. 8:811-820(1994).
[12]
 FUNCTION, AND INTERACTION WITH RAD18.
DOI=10.1074/jbc.272.37.23360; PubMed=9287349 [NCBI, ExPASy, EBI, Israel, Japan]
Bailly V., Lauder S., Prakash S., Prakash L.;
"Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities.";
J. Biol. Chem. 272:23360-23365(1997).
[13]
 FUNCTION.
PubMed=9343433 [NCBI, ExPASy, EBI, Israel, Japan]
Huang H., Kahana A., Gottschling D.E., Prakash L., Liebman S.W.;
"The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 17:6693-6699(1997).
[14]
 INTERACTION WITH UBR1 AND UBR2.
DOI=10.1093/emboj/18.23.6832; PubMed=10581257 [NCBI, ExPASy, EBI, Israel, Japan]
Xie Y., Varshavsky A.;
"The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain.";
EMBO J. 18:6832-6844(1999).
[15]
 FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/19.13.3388; PubMed=10880451 [NCBI, ExPASy, EBI, Israel, Japan]
Ulrich H.D., Jentsch S.;
"Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair.";
EMBO J. 19:3388-3397(2000).
[16]
 FUNCTION, AND MUTAGENESIS OF CYS-88 AND 1-MET--LEU-9.
DOI=10.1038/nature00883; PubMed=12077605 [NCBI, ExPASy, EBI, Israel, Japan]
Sun Z.-W., Allis C.D.;
"Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast.";
Nature 418:104-108(2002).
[17]
 FUNCTION.
DOI=10.1038/nature00991; PubMed=12226657 [NCBI, ExPASy, EBI, Israel, Japan]
Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
"RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO.";
Nature 419:135-141(2002).
[18]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[19]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[20]
 FUNCTION.
DOI=10.1101/gad.1149604; PubMed=14752010 [NCBI, ExPASy, EBI, Israel, Japan]
Kao C.-F., Hillyer C., Tsukuda T., Henry K.W., Berger S.L., Osley M.A.;
"Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B.";
Genes Dev. 18:184-195(2004).
[21]
 FUNCTION.
DOI=10.1093/nar/gkh831; PubMed=15388802 [NCBI, ExPASy, EBI, Israel, Japan]
de Padula M., Slezak G., Auffret van Der Kemp P., Boiteux S.;
"The post-replication repair RAD18 and RAD6 genes are involved in the prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine in Saccharomyces cerevisiae.";
Nucleic Acids Res. 32:5003-5010(2004).
[22]
 FUNCTION, AND PHOSPHORYLATION AT SER-120.
DOI=10.1016/j.molcel.2005.09.010; PubMed=16307922 [NCBI, ExPASy, EBI, Israel, Japan]
Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.;
"The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS.";
Mol. Cell 20:589-599(2005).
[23]
 FUNCTION, AND INTERACTION WITH RTF1; PAF1 AND THE RNA POLYMERASE II HYPERPHOSPHORYLATED FORM.
DOI=10.1128/MCB.25.2.637-651.2005; PubMed=15632065 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A., Strahl B.D.;
"Histone H2B ubiquitylation is associated with elongating RNA polymerase II.";
Mol. Cell. Biol. 25:637-651(2005).
[24]
 FUNCTION.
DOI=10.1073/pnas.0504586102; PubMed=16247017 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Lawrence C.W.;
"The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination.";
Proc. Natl. Acad. Sci. U.S.A. 102:15954-15959(2005).
[25]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[26]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1074/jbc.273.11.6271; PubMed=9497353 [NCBI, ExPASy, EBI, Israel, Japan]
Worthylake D.K., Prakash S., Prakash L., Hill C.P.;
"Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6-A resolution.";
J. Biol. Chem. 273:6271-6276(1998).
Comments
  • FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation.
  • CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
  • PATHWAY: Protein modification; protein ubiquitination.
  • SUBUNIT: Forms heterodimer complexes with the E3 enzymes BRE1, RAD18 and UBR1. Interacts also with UBR2, RTF1, PAF1 and the RNA polymerase II hyperphosphorylated form. The interaction with RNA polymerase II is BRE1- and PAF1-dependent.
  • INTERACTION:
    P10862:RAD18; NbExp=2; IntAct=EBI-19722, EBI-14659;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • INDUCTION: Up-regulated by UV radiations and during meiosis.
  • DOMAIN: The acidic-tail domain of UBC2 mediates interaction with UBR1 and UBR2, and thus is important for polyubiquitination of histones. This domain is also important for sporulation.
  • PTM: The N-terminus is blocked.
  • MISCELLANEOUS: Present with 2770 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02962; AAA34952.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72580; CAA96761.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A21906; A21906.
RefSeq NP_011457.1; -.
3D structure databases
PDB
1AYZ; X-ray; 2.60 A; A/B/C=1-166.[ExPASy / RCSB / EBI]
PDBsum 1AYZ; -.
ModBase P06104.
Protein-protein interaction databases
DIP DIP:1555N; -.
IntAct P06104; -.
Organism-specific databases
CYGD YGL058w; -.
SGD S000003026; RAD6.
Yeast-GFP YGL058W.
Gene expression databases
GermOnline YGL058W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0000502; Cellular component: proteasome complex (inferred from physical interaction from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from SGD).
GO:0016574; Biological process: histone ubiquitination (inferred from direct assay from SGD).
GO:0006301; Biological process: postreplication repair (inferred from mutant phenotype from SGD).
GO:0006513; Biological process: protein monoubiquitination (inferred from mutant phenotype from SGD).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P06104.
ProtoNet P06104.
Proteomic databases
PeptideAtlas P06104; -.
Genome annotation databases
Ensembl YGL058W; Saccharomyces cerevisiae. [Contig view]
GeneID 852822; -.
GenomeReviews Y13135_GR; YGL058W.
KEGG sce:YGL058W; -.
NMPDR fig|4932.3.peg.2563; -.
Phylogenomic databases
HOGENOM P06104; -.
Other
LinkHub P06104; -.
NextBio 972372; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Ligase; Nucleus; Phosphoprotein; Sporulation; Transcription; Transcription regulation; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   172  172     Ubiquitin-conjugating enzyme E2 2. PRO_0000082540
COMPBIAS   150   172  23     Asp/Glu-rich (acidic tail). 
ACT_SITE   88    88        Glycyl thioester intermediate. 
MOD_RES   120   120        Phosphoserine; by SGV1. 
MUTAGEN   1     9        Missing: Prevents H3K4me3 formation. 
MUTAGEN   88    88        C->A,V: Loss of activity. 
HELIX   4    18  15      
STRAND   24    29  6      
STRAND   32    41  10      
TURN   47    50  4      
STRAND   52    58  7      
TURN   61    65  5      
STRAND   69    74  6      
STRAND   85    87  3      
HELIX   90    92  3      
TURN   93    95  3      
HELIX   102   113  12      
HELIX   124   132  9      
HELIX   134   152  19      
Sequence information
Length: 172 AA [This is the length of the unprocessed precursor] Molecular weight: 19706 Da [This is the MW of the unprocessed precursor] CRC64: 5F568DC28ABBD60F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTPARRRLM RDFKRMKEDA PPGVSASPLP DNVMVWNAMI IGPADTPYED GTFRLLLEFD 

        70         80         90        100        110        120 
EEYPNKPPHV KFLSEMFHPN VYANGEICLD ILQNRWTPTY DVASILTSIQ SLFNDPNPAS 

       130        140        150        160        170 
PANVEAATLF KDHKSQYVKR VKETVEKSWE DDMDDMDDDD DDDDDDDDDE AD
P06104 in FASTA format

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