ID UBC2_CRYNB Reviewed; 169 AA. AC P0CS17; Q55YQ1; Q5KN22; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 62. 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=CNBA7840; OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OS (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=283643; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). 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; AAEY01000005; EAL23017.1; -; Genomic_DNA. DR RefSeq; XP_777664.1; XM_772571.1. DR AlphaFoldDB; P0CS17; -. DR SMR; P0CS17; -. DR EnsemblFungi; AAW41362; AAW41362; CNA08010. DR GeneID; 4934050; -. DR KEGG; cnb:CNBA7840; -. DR VEuPathDB; FungiDB:CNBA7840; -. DR HOGENOM; CLU_030988_10_2_1; -. DR OrthoDB; 5478564at2759; -. DR UniPathway; UPA00143; -. 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: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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. 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; Sporulation; Transcription; KW Transcription regulation; Transferase; Ubl conjugation pathway. FT CHAIN 1..169 FT /note="Ubiquitin-conjugating enzyme E2 2" FT /id="PRO_0000410321" FT DOMAIN 4..150 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT ACT_SITE 88 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133" SQ SEQUENCE 169 AA; 18847 MW; DD23A363FAF849AE CRC64; MSTAAKRRLI RDFKRLTSDA PIGISGSPNP DNIMVWNAVI FGPPETPFED GSFRLTLTFT DAYPNKPPTV RFISKMFHPN IYANGELCLD ILQNRWSPTY DVAAILTSVQ SLLNDPNPAS PANVDAAQLF KENLKEYERR VKKTVELSWV DNADEIEAEV VEADEGSSS //