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P06104 (UBC2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 2

EC=6.3.2.19
Alternative name(s):
Radiation sensitivity protein 6
Ubiquitin carrier protein UBC2
Ubiquitin-protein ligase UBC2
Gene names
Name:RAD6
Synonyms:UBC2
Ordered Locus Names:YGL058W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Forms a 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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.24

Subcellular location

Cytoplasm. Nucleus Ref.11 Ref.16 Ref.19.

Induction

Up-regulated by UV radiations and during meiosis. Ref.7

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.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

Present with 2770 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Sporulation
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Ligase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.13. Source: GOC

DNA-templated transcription, termination

Inferred from mutant phenotype PubMed 23109428. Source: SGD

ER-associated ubiquitin-dependent protein catabolic process

Inferred from genetic interaction PubMed 23988329. Source: SGD

chromatin silencing at telomere

Inferred from mutant phenotype PubMed 12535539Ref.14. Source: SGD

double-strand break repair via homologous recombination

Inferred from genetic interaction PubMed 16783014. Source: SGD

error-free postreplication DNA repair

Inferred from genetic interaction PubMed 9576943. Source: SGD

error-free translesion synthesis

Inferred from genetic interaction PubMed 9409821. Source: SGD

error-prone translesion synthesis

Inferred from genetic interaction PubMed 770231. Source: SGD

histone monoubiquitination

Inferred from mutant phenotype PubMed 12535538PubMed 12535539. Source: SGD

meiotic DNA double-strand break formation

Inferred from mutant phenotype PubMed 15280549. Source: SGD

mitotic G1 DNA damage checkpoint

Inferred from mutant phenotype PubMed 15632126PubMed 16166626. Source: SGD

protein monoubiquitination

Inferred from mutant phenotype Ref.18. Source: SGD

protein polyubiquitination

Inferred from mutant phenotype Ref.9Ref.11. Source: SGD

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.11. Source: SGD

regulation of dipeptide transport

Inferred from mutant phenotype PubMed 9427760. Source: SGD

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

transcription from RNA polymerase II promoter

Inferred from physical interaction Ref.24. Source: SGD

ubiquitin-dependent protein catabolic process via the N-end rule pathway

Inferred from mutant phenotype Ref.9. Source: SGD

   Cellular_componentRad6-Rad18 complex

Inferred from direct assay Ref.13. Source: SGD

cytoplasm

Inferred from direct assay Ref.16. Source: SGD

nucleus

Inferred from direct assay Ref.16Ref.11. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from direct assay Ref.5Ref.13. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Ubiquitin-conjugating enzyme E2 2
PRO_0000082540

Regions

Compositional bias150 – 17223Asp/Glu-rich (acidic tail)

Sites

Active site881Glycyl thioester intermediate

Amino acid modifications

Modified residue1201Phosphoserine; by SGV1 Ref.23 Ref.26

Experimental info

Mutagenesis1 – 99Missing: Prevents H3K4me3 formation. Ref.11 Ref.17
Mutagenesis881C → A or V: Loss of activity. Ref.8 Ref.17

Secondary structure

.......................... 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06104 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 5F568DC28ABBD60F

FASTA17219,706
        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 

« Hide

References

« Hide 'large scale' references
[1]"RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive aspartates."
Reynolds P., Weber S., Prakash L.
Proc. Natl. Acad. Sci. U.S.A. 82:168-172(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
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. expand/collapse author list , 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.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme."
Jentsch S., McGrath J.P., Varshavsky A.
Nature 329:131-134(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 77-91, FUNCTION.
[6]"Recombination and mutagenesis in rad6 mutants of Saccharomyces cerevisiae: evidence for multiple functions of the RAD6 gene."
Montelone B.A., Prakash S., Prakash L.
Mol. Gen. Genet. 184:410-415(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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."
Madura K., Prakash S., Prakash L.
Nucleic Acids Res. 18:771-778(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitin-conjugating activity and its various biological functions."
Sung P., Prakash S., Prakash L.
Proc. Natl. Acad. Sci. U.S.A. 87:2695-2699(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-88.
[9]"The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme."
Dohmen R.J., Madura K., Bartel B., Varshavsky A.
Proc. Natl. Acad. Sci. U.S.A. 88:7351-7355(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBR1.
[10]"Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme."
Sung P., Berleth E., Pickart C.M., Prakash S., Prakash L.
EMBO J. 10:2187-2193(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The extremely conserved amino terminus of RAD6 ubiquitin-conjugating enzyme is essential for amino-end rule-dependent protein degradation."
Watkins J.F., Sung P., Prakash S., Prakash L.
Genes Dev. 7:250-261(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBR1, MUTAGENESIS OF 1-MET--LEU-9.
[12]"Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites."
Bailly V., Lamb J., Sung P., Prakash S., Prakash L.
Genes Dev. 8:811-820(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD18 AND UBR1.
[13]"Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities."
Bailly V., Lauder S., Prakash S., Prakash L.
J. Biol. Chem. 272:23360-23365(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD18.
[14]"The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in Saccharomyces cerevisiae."
Huang H., Kahana A., Gottschling D.E., Prakash L., Liebman S.W.
Mol. Cell. Biol. 17:6693-6699(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain."
Xie Y., Varshavsky A.
EMBO J. 18:6832-6844(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBR1 AND UBR2.
[16]"Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair."
Ulrich H.D., Jentsch S.
EMBO J. 19:3388-3397(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]"Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast."
Sun Z.-W., Allis C.D.
Nature 418:104-108(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-88 AND 1-MET--LEU-9.
[18]"RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO."
Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.
Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[20]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[21]"Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B."
Kao C.-F., Hillyer C., Tsukuda T., Henry K.W., Berger S.L., Osley M.A.
Genes Dev. 18:184-195(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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."
de Padula M., Slezak G., Auffret van Der Kemp P., Boiteux S.
Nucleic Acids Res. 32:5003-5010(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS."
Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.
Mol. Cell 20:589-599(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-120.
[24]"Histone H2B ubiquitylation is associated with elongating RNA polymerase II."
Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A., Strahl B.D.
Mol. Cell. Biol. 25:637-651(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RTF1; PAF1 AND THE RNA POLYMERASE II HYPERPHOSPHORYLATED FORM.
[25]"The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination."
Zhang H., Lawrence C.W.
Proc. Natl. Acad. Sci. U.S.A. 102:15954-15959(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[26]"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-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6-A resolution."
Worthylake D.K., Prakash S., Prakash L., Hill C.P.
J. Biol. Chem. 273:6271-6276(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02962 Genomic DNA. Translation: AAA34952.1.
Z72580 Genomic DNA. Translation: CAA96761.1.
BK006941 Genomic DNA. Translation: DAA08044.1.
PIRA21906.
RefSeqNP_011457.1. NM_001180923.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYZX-ray2.60A/B/C1-166[»]
ProteinModelPortalP06104.
SMRP06104. Positions 2-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33189. 363 interactions.
DIPDIP-1555N.
IntActP06104. 13 interactions.
MINTMINT-394584.
STRING4932.YGL058W.

Proteomic databases

PaxDbP06104.
PeptideAtlasP06104.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL058W; YGL058W; YGL058W.
GeneID852822.
KEGGsce:YGL058W.

Organism-specific databases

CYGDYGL058w.
SGDS000003026. RAD6.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110565.
HOGENOMHOG000233454.
KOK10573.
OMAETVENSW.
OrthoDBEOG7SBP18.

Enzyme and pathway databases

BioCycYEAST:G3O-30566-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP06104.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06104.
NextBio972372.
PROP06104.

Entry information

Entry nameUBC2_YEAST
AccessionPrimary (citable) accession number: P06104
Secondary accession number(s): D6VU83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways