UBC2_DEBHA
ID UBC2_DEBHA Reviewed; 168 AA.
AC Q6BU36;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=DEHA2C13904g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG86361.1; -; Genomic_DNA.
DR RefSeq; XP_458283.1; XM_458283.1.
DR AlphaFoldDB; Q6BU36; -.
DR SMR; Q6BU36; -.
DR STRING; 4959.XP_458283.1; -.
DR EnsemblFungi; CAG86361; CAG86361; DEHA2C13904g.
DR GeneID; 2900043; -.
DR KEGG; dha:DEHA2C13904g; -.
DR VEuPathDB; FungiDB:DEHA2C13904g; -.
DR eggNOG; KOG0419; Eukaryota.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; Q6BU36; -.
DR OMA; DHKSQYI; -.
DR OrthoDB; 1292821at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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..168
FT /note="Ubiquitin-conjugating enzyme E2 2"
FT /id="PRO_0000082531"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 143..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..168
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 168 AA; 19187 MW; 94913C1294E08A62 CRC64;
MSTPAKRRLM RDFKRMQQDA PSGVSASPLP DNVMSWNAVI IGPADTPFED GTFRLILQFD
EQYPNKPPSV KFISEMFHPN VYASGELCLD ILQNRWSPTY DVSSILTSIQ SLLNDPNISS
PANVEAANLY KDHRSQYIKR VRETVENSWN EDDEDEDEDE DEDIDDAE
