ID   UBC2_YARLI              Reviewed;         151 AA.
AC   Q6C093;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 128.
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=YALI0F26697g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382132; CAG78731.1; -; Genomic_DNA.
DR   RefSeq; XP_505919.1; XM_505919.1.
DR   AlphaFoldDB; Q6C093; -.
DR   SMR; Q6C093; -.
DR   STRING; 284591.Q6C093; -.
DR   EnsemblFungi; CAG78731; CAG78731; YALI0_F26697g.
DR   GeneID; 2908858; -.
DR   KEGG; yli:YALI0F26697g; -.
DR   VEuPathDB; FungiDB:YALI0_F26697g; -.
DR   HOGENOM; CLU_030988_10_2_1; -.
DR   InParanoid; Q6C093; -.
DR   OMA; DHKSQYI; -.
DR   OrthoDB; 5478564at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001300; Chromosome F.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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: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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 formation; 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; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF254; UBIQUITIN-CONJUGATING ENZYME E2-17 KDA; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 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..151
FT                   /note="Ubiquitin-conjugating enzyme E2 2"
FT                   /id="PRO_0000082539"
FT   DOMAIN          4..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..26
FT                   /note="Disordered"
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   151 AA;  17198 MW;  C31B848BA8AC0BE1 CRC64;
     MSTTARRRLM RDFKRMQQDP PQGVSASPVA DNVLTWNAVI IGPAETPFED GTFRMVLQFD
     EQYPNKPPAV KFVSQMFHPN VYSSGELCLD ILQNRWSPTY DVAAILTSVQ SLLNDPNTSS
     PANVEASMLY KDHRQQYEKR VRDTVEASWT D
//