UBC2_YEAST
ID UBC2_YEAST Reviewed; 172 AA.
AC P06104; D6VU83;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 2;
DE AltName: Full=Radiation sensitivity protein 6;
DE AltName: Full=Ubiquitin carrier protein UBC2;
DE AltName: Full=Ubiquitin-protein ligase UBC2;
GN Name=RAD6; Synonyms=UBC2; OrderedLocusNames=YGL058W;
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 [GENOMIC DNA].
RX PubMed=3881753; DOI=10.1073/pnas.82.1.168;
RA Reynolds P., Weber S., Prakash L.;
RT "RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract
RT of 13 consecutive aspartates.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:168-172(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 77-91, AND FUNCTION.
RX PubMed=3306404; DOI=10.1038/329131a0;
RA Jentsch S., McGrath J.P., Varshavsky A.;
RT "The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme.";
RL Nature 329:131-134(1987).
RN [6]
RP FUNCTION.
RX PubMed=7038392; DOI=10.1007/bf00352514;
RA Montelone B.A., Prakash S., Prakash L.;
RT "Recombination and mutagenesis in rad6 mutants of Saccharomyces cerevisiae:
RT evidence for multiple functions of the RAD6 gene.";
RL Mol. Gen. Genet. 184:410-415(1981).
RN [7]
RP INDUCTION.
RX PubMed=2179869; DOI=10.1093/nar/18.4.771;
RA Madura K., Prakash S., Prakash L.;
RT "Expression of the Saccharomyces cerevisiae DNA repair gene RAD6 that
RT encodes a ubiquitin conjugating enzyme, increases in response to DNA damage
RT and in meiosis but remains constant during the mitotic cell cycle.";
RL Nucleic Acids Res. 18:771-778(1990).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF CYS-88.
RX PubMed=2157209; DOI=10.1073/pnas.87.7.2695;
RA Sung P., Prakash S., Prakash L.;
RT "Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein
RT abolishes its ubiquitin-conjugating activity and its various biological
RT functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2695-2699(1990).
RN [9]
RP FUNCTION, AND INTERACTION WITH UBR1.
RX PubMed=1651502; DOI=10.1073/pnas.88.16.7351;
RA Dohmen R.J., Madura K., Bartel B., Varshavsky A.;
RT "The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7351-7355(1991).
RN [10]
RP FUNCTION.
RX PubMed=2065660; DOI=10.1002/j.1460-2075.1991.tb07754.x;
RA Sung P., Berleth E., Pickart C.M., Prakash S., Prakash L.;
RT "Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein
RT degradation dependent on the N-end-recognizing E3 enzyme.";
RL EMBO J. 10:2187-2193(1991).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBR1, AND MUTAGENESIS OF
RP 1-MET--LEU-9.
RX PubMed=8436296; DOI=10.1101/gad.7.2.250;
RA Watkins J.F., Sung P., Prakash S., Prakash L.;
RT "The extremely conserved amino terminus of RAD6 ubiquitin-conjugating
RT enzyme is essential for amino-end rule-dependent protein degradation.";
RL Genes Dev. 7:250-261(1993).
RN [12]
RP FUNCTION, AND INTERACTION WITH RAD18 AND UBR1.
RX PubMed=7926769; DOI=10.1101/gad.8.7.811;
RA Bailly V., Lamb J., Sung P., Prakash S., Prakash L.;
RT "Specific complex formation between yeast RAD6 and RAD18 proteins: a
RT potential mechanism for targeting RAD6 ubiquitin-conjugating activity to
RT DNA damage sites.";
RL Genes Dev. 8:811-820(1994).
RN [13]
RP FUNCTION, AND INTERACTION WITH RAD18.
RX PubMed=9287349; DOI=10.1074/jbc.272.37.23360;
RA Bailly V., Lauder S., Prakash S., Prakash L.;
RT "Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has
RT ubiquitin conjugating, DNA binding, and ATP hydrolytic activities.";
RL J. Biol. Chem. 272:23360-23365(1997).
RN [14]
RP FUNCTION.
RX PubMed=9343433; DOI=10.1128/mcb.17.11.6693;
RA Huang H., Kahana A., Gottschling D.E., Prakash L., Liebman S.W.;
RT "The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:6693-6699(1997).
RN [15]
RP INTERACTION WITH UBR1 AND UBR2.
RX PubMed=10581257; DOI=10.1093/emboj/18.23.6832;
RA Xie Y., Varshavsky A.;
RT "The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3
RT is required for the synthesis of multiubiquitin chain.";
RL EMBO J. 18:6832-6844(1999).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10880451; DOI=10.1093/emboj/19.13.3388;
RA Ulrich H.D., Jentsch S.;
RT "Two RING finger proteins mediate cooperation between ubiquitin-conjugating
RT enzymes in DNA repair.";
RL EMBO J. 19:3388-3397(2000).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF CYS-88 AND 1-MET--LEU-9.
RX PubMed=12077605; DOI=10.1038/nature00883;
RA Sun Z.-W., Allis C.D.;
RT "Ubiquitination of histone H2B regulates H3 methylation and gene silencing
RT in yeast.";
RL Nature 418:104-108(2002).
RN [18]
RP FUNCTION.
RX PubMed=12226657; DOI=10.1038/nature00991;
RA Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
RT "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin
RT and SUMO.";
RL Nature 419:135-141(2002).
RN [19]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [20]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [21]
RP FUNCTION.
RX PubMed=14752010; DOI=10.1101/gad.1149604;
RA Kao C.-F., Hillyer C., Tsukuda T., Henry K.W., Berger S.L., Osley M.A.;
RT "Rad6 plays a role in transcriptional activation through ubiquitylation of
RT histone H2B.";
RL Genes Dev. 18:184-195(2004).
RN [22]
RP FUNCTION.
RX PubMed=15388802; DOI=10.1093/nar/gkh831;
RA de Padula M., Slezak G., Auffret van Der Kemp P., Boiteux S.;
RT "The post-replication repair RAD18 and RAD6 genes are involved in the
RT prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 32:5003-5010(2004).
RN [23]
RP FUNCTION, AND PHOSPHORYLATION AT SER-120.
RX PubMed=16307922; DOI=10.1016/j.molcel.2005.09.010;
RA Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.;
RT "The Bur1/Bur2 complex is required for histone H2B monoubiquitination by
RT Rad6/Bre1 and histone methylation by COMPASS.";
RL Mol. Cell 20:589-599(2005).
RN [24]
RP FUNCTION, AND INTERACTION WITH RTF1; PAF1 AND THE RNA POLYMERASE II
RP HYPERPHOSPHORYLATED FORM.
RX PubMed=15632065; DOI=10.1128/mcb.25.2.637-651.2005;
RA Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A.,
RA Strahl B.D.;
RT "Histone H2B ubiquitylation is associated with elongating RNA polymerase
RT II.";
RL Mol. Cell. Biol. 25:637-651(2005).
RN [25]
RP FUNCTION.
RX PubMed=16247017; DOI=10.1073/pnas.0504586102;
RA Zhang H., Lawrence C.W.;
RT "The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of
RT budding yeast employs sister-strand recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15954-15959(2005).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP 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).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9497353; DOI=10.1074/jbc.273.11.6271;
RA Worthylake D.K., Prakash S., Prakash L., Hill C.P.;
RT "Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating
RT enzyme Rad6 at 2.6-A resolution.";
RL J. Biol. Chem. 273:6271-6276(1998).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a
CC role in transcription regulation by catalyzing the monoubiquitination
CC of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for
CC epigenetic transcriptional activation, elongation by RNA polymerase II,
CC telomeric silencing, and is also a prerequisite for H3K4me and H3K79me
CC formation. In association with the E3 enzyme RAD18, it catalyzes the
CC monoubiquitination of POL30 'Lys-164', involved in postreplication
CC repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved
CC in prevention of spontaneous mutations caused by 7,8-dihydro-8-
CC oxoguanine. In association with the E3 enzyme UBR1, is involved in N-
CC end rule-dependent protein degradation. Also involved in sporulation.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:10880451,
CC ECO:0000269|PubMed:12077605, ECO:0000269|PubMed:12226657,
CC ECO:0000269|PubMed:14752010, ECO:0000269|PubMed:15388802,
CC ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:16247017,
CC ECO:0000269|PubMed:16307922, ECO:0000269|PubMed:1651502,
CC ECO:0000269|PubMed:2065660, ECO:0000269|PubMed:2157209,
CC ECO:0000269|PubMed:3306404, ECO:0000269|PubMed:7038392,
CC ECO:0000269|PubMed:7926769, ECO:0000269|PubMed:8436296,
CC ECO:0000269|PubMed:9287349, ECO:0000269|PubMed:9343433}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Forms a heterodimer complexes with the E3 enzymes BRE1, RAD18
CC and UBR1. Interacts also with UBR2, RTF1, PAF1 and the RNA polymerase
CC II hyperphosphorylated form. The interaction with RNA polymerase II is
CC BRE1- and PAF1-dependent. {ECO:0000269|PubMed:10581257,
CC ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:1651502,
CC ECO:0000269|PubMed:7926769, ECO:0000269|PubMed:8436296,
CC ECO:0000269|PubMed:9287349}.
CC -!- INTERACTION:
CC P06104; Q07457: BRE1; NbExp=4; IntAct=EBI-19722, EBI-31563;
CC P06104; P10862: RAD18; NbExp=4; IntAct=EBI-19722, EBI-14659;
CC P06104; P19812: UBR1; NbExp=4; IntAct=EBI-19722, EBI-19909;
CC P06104; Q07963: UBR2; NbExp=6; IntAct=EBI-19722, EBI-34338;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10880451,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}. Nucleus
CC {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:8436296}.
CC -!- INDUCTION: Up-regulated by UV radiations and during meiosis.
CC {ECO:0000269|PubMed:2179869}.
CC -!- DOMAIN: The acidic-tail domain of UBC2 mediates interaction with UBR1
CC and UBR2, and thus is important for polyubiquitination of histones.
CC This domain is also important for sporulation.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 2770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; K02962; AAA34952.1; -; Genomic_DNA.
DR EMBL; Z72580; CAA96761.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08044.1; -; Genomic_DNA.
DR PIR; A21906; A21906.
DR RefSeq; NP_011457.1; NM_001180923.1.
DR PDB; 1AYZ; X-ray; 2.60 A; A/B/C=1-172.
DR PDB; 4R62; X-ray; 2.28 A; A=1-172.
DR PDB; 7MEX; EM; 3.35 A; B=3-152.
DR PDB; 7MEY; EM; 3.67 A; B=1-172.
DR PDBsum; 1AYZ; -.
DR PDBsum; 4R62; -.
DR PDBsum; 7MEX; -.
DR PDBsum; 7MEY; -.
DR AlphaFoldDB; P06104; -.
DR SMR; P06104; -.
DR BioGRID; 33189; 416.
DR ComplexPortal; CPX-2902; RAD6-RAD18 ubiquitin ligase complex.
DR ComplexPortal; CPX-2910; BRE1-RAD6 ubiquitin ligase complex.
DR ComplexPortal; CPX-2918; UBR1-RAD6 ubiquitin ligase complex.
DR ComplexPortal; CPX-2935; RAD6-UBR2 ubiquitin ligase complex.
DR ComplexPortal; CPX-2937; MUB1-RAD6-UBR2 ubiquitin ligase complex.
DR DIP; DIP-1555N; -.
DR IntAct; P06104; 13.
DR MINT; P06104; -.
DR STRING; 4932.YGL058W; -.
DR iPTMnet; P06104; -.
DR PaxDb; P06104; -.
DR PRIDE; P06104; -.
DR EnsemblFungi; YGL058W_mRNA; YGL058W; YGL058W.
DR GeneID; 852822; -.
DR KEGG; sce:YGL058W; -.
DR SGD; S000003026; RAD6.
DR VEuPathDB; FungiDB:YGL058W; -.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000174704; -.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P06104; -.
DR OMA; DHKSQYI; -.
DR BioCyc; YEAST:G3O-30566-MON; -.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P06104; -.
DR PRO; PR:P06104; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P06104; protein.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0097505; C:Rad6-Rad18 complex; IDA:SGD.
DR GO; GO:1990305; C:RAD6-UBR2 ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:1990303; C:UBR1-RAD6 ubiquitin ligase complex; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070628; F:proteasome binding; IDA:SGD.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IGI:SGD.
DR GO; GO:0070987; P:error-free translesion synthesis; IGI:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IGI:SGD.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:ComplexPortal.
DR GO; GO:0016574; P:histone ubiquitination; IDA:ComplexPortal.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:SGD.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:ComplexPortal.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR GO; GO:0090089; P:regulation of dipeptide transport; IMP:SGD.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IC:ComplexPortal.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IPI:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IGI:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IMP:SGD.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromatin regulator; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Sporulation; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway.
FT CHAIN 1..172
FT /note="Ubiquitin-conjugating enzyme E2 2"
FT /id="PRO_0000082540"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 145..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 120
FT /note="Phosphoserine; by SGV1"
FT /evidence="ECO:0000269|PubMed:16307922,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 1..9
FT /note="Missing: Prevents H3K4me3 formation."
FT /evidence="ECO:0000269|PubMed:12077605,
FT ECO:0000269|PubMed:8436296"
FT MUTAGEN 88
FT /note="C->A,V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12077605,
FT ECO:0000269|PubMed:2157209"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:4R62"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:4R62"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:4R62"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:4R62"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4R62"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:4R62"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4R62"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4R62"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4R62"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4R62"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:4R62"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:4R62"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:4R62"
SQ SEQUENCE 172 AA; 19706 MW; 5F568DC28ABBD60F CRC64;
MSTPARRRLM RDFKRMKEDA PPGVSASPLP DNVMVWNAMI IGPADTPYED GTFRLLLEFD
EEYPNKPPHV KFLSEMFHPN VYANGEICLD ILQNRWTPTY DVASILTSIQ SLFNDPNPAS
PANVEAATLF KDHKSQYVKR VKETVEKSWE DDMDDMDDDD DDDDDDDDDE AD
