UBC2_CANGA
ID UBC2_CANGA Reviewed; 167 AA.
AC Q6FR76;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=Ubiquitin carrier protein UBC2;
DE AltName: Full=Ubiquitin-protein ligase UBC2;
GN Name=UBC2; OrderedLocusNames=CAGL0I00352g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Plays a role in transcription regulation by catalyzing the
CC monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives
CC a specific tag for epigenetic transcriptional activation and is also a
CC prerequisite for H3K4me and H3K79me formation. Also involved in
CC postreplication repair of UV-damaged DNA, in N-end rule-dependent
CC protein degradation and in sporulation. {ECO:0000255|PROSITE-
CC ProRule:PRU00388}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVX9}. Nucleus
CC {ECO:0000250|UniProtKB:Q5VVX9}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; CR380955; CAG60205.1; -; Genomic_DNA.
DR RefSeq; XP_447268.1; XM_447268.1.
DR AlphaFoldDB; Q6FR76; -.
DR SMR; Q6FR76; -.
DR STRING; 5478.XP_447268.1; -.
DR EnsemblFungi; CAG60205; CAG60205; CAGL0I00352g.
DR GeneID; 2889314; -.
DR KEGG; cgr:CAGL0I00352g; -.
DR CGD; CAL0130017; CAGL0I00352g.
DR VEuPathDB; FungiDB:CAGL0I00352g; -.
DR eggNOG; KOG0419; Eukaryota.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; Q6FR76; -.
DR OMA; DHKSQYI; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033503; C:HULC complex; IEA:EnsemblFungi.
DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097505; C:Rad6-Rad18 complex; IEA:EnsemblFungi.
DR GO; GO:1990305; C:RAD6-UBR2 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:1990303; C:UBR1-RAD6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070628; F:proteasome binding; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0010390; P:histone monoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:EnsemblFungi.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0090089; P:regulation of dipeptide transport; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Nucleotide-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..167
FT /note="Ubiquitin-conjugating enzyme E2 2"
FT /id="PRO_0000082529"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 148..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
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 ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 167 AA; 19189 MW; A9EF7E08327079AE CRC64;
MSTPARRRLM RDFKRMKEDS PPGVSASPLP DNVMVWNAMI IGPADTPYED GTFRLLLEFD
EDYPNKPPHV KFLSEMFHPN VYANGEICLD ILQNRWTPTY DVASILTSIQ SLFNDPNPAS
PANVEAATLF KDHKSQYIKR VKETVEKSWE DNMDDMDDSD EDDEDDE
