UBC2_SCHPO
ID UBC2_SCHPO Reviewed; 151 AA.
AC P23566;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 171.
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=RAD6 homolog;
DE AltName: Full=Ubiquitin carrier protein 2;
DE AltName: Full=Ubiquitin-protein ligase 2;
GN Name=rhp6; Synonyms=ubc2; ORFNames=SPAC18B11.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2184030; DOI=10.1002/j.1460-2075.1990.tb08258.x;
RA Reynolds P., Koken M.H.M., Hoeijmakers J.H.J., Prakash S., Prakash L.;
RT "The rhp6+ gene of Schizosaccharomyces pombe: a structural and functional
RT homolog of the RAD6 gene from the distantly related yeast Saccharomyces
RT cerevisiae.";
RL EMBO J. 9:1423-1430(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=9710635; DOI=10.1128/mcb.18.9.5511;
RA Singh J., Goel V., Klar A.J.S.;
RT "A novel function of the DNA repair gene rhp6 in mating-type silencing by
RT chromatin remodeling in fission yeast.";
RL Mol. Cell. Biol. 18:5511-5522(1998).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF CYS-88.
RX PubMed=12456009; DOI=10.1128/ec.1.4.613-625.2002;
RA Nielsen I.S., Nielsen O., Murray J.M., Thon G.;
RT "The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6
RT affect transcriptional silencing of the mating-type region.";
RL Eukaryot. Cell 1:613-625(2002).
RN [5]
RP FUNCTION.
RX PubMed=12417737; DOI=10.1128/mcb.22.23.8366-8374.2002;
RA Choi E.S., Kim H.S., Jang Y.K., Hong S.H., Park S.D.;
RT "Two ubiquitin-conjugating enzymes, Rhp6 and UbcX, regulate heterochromatin
RT silencing in Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 22:8366-8374(2002).
RN [6]
RP FUNCTION.
RX PubMed=12511578; DOI=10.1074/jbc.m212732200;
RA Naresh A., Saini S., Singh J.;
RT "Identification of Uhp1, a ubiquitinated histone-like protein, as a
RT target/mediator of Rhp6 in mating-type silencing in fission yeast.";
RL J. Biol. Chem. 278:9185-9194(2003).
RN [7]
RP FUNCTION.
RX PubMed=16096059; DOI=10.1016/j.cell.2005.05.023;
RA Takeda K., Yanagida M.;
RT "Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and
RT destruction of the sensor and anchor Cut8.";
RL Cell 122:393-405(2005).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [9]
RP IDENTIFICATION IN THE HULC COMPLEX, FUNCTION OF THE HULC COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17363370; DOI=10.1074/jbc.m700292200;
RA Zofall M., Grewal S.I.S.;
RT "HULC, a histone H2B ubiquitinating complex, modulates heterochromatin
RT independent of histone methylation in fission yeast.";
RL J. Biol. Chem. 282:14065-14072(2007).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Component of the histone H2B ubiquitin ligase complex (HULC)
CC which 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 (By similarity). Required for
CC obr1 ubiquitination, which regulates mating-type silencing. With cut8,
CC regulates the nuclear accumulation of the proteasome.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12417737,
CC ECO:0000269|PubMed:12456009, ECO:0000269|PubMed:12511578,
CC ECO:0000269|PubMed:16096059, ECO:0000269|PubMed:17363370,
CC ECO:0000269|PubMed:9710635}.
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: Component of the histone H2B ubiquitin ligase complex (HULC)
CC composed of at least brl1, brl2, rhp6 and shf1.
CC {ECO:0000269|PubMed:17363370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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; X53252; CAA37340.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA90592.1; -; Genomic_DNA.
DR PIR; S12529; S12529.
DR PIR; T45220; T45220.
DR RefSeq; NP_592876.1; NM_001018276.2.
DR AlphaFoldDB; P23566; -.
DR SMR; P23566; -.
DR BioGRID; 279076; 17.
DR IntAct; P23566; 4.
DR STRING; 4896.SPAC18B11.07c.1; -.
DR MaxQB; P23566; -.
DR PaxDb; P23566; -.
DR EnsemblFungi; SPAC18B11.07c.1; SPAC18B11.07c.1:pep; SPAC18B11.07c.
DR GeneID; 2542622; -.
DR KEGG; spo:SPAC18B11.07c; -.
DR PomBase; SPAC18B11.07c; rhp6.
DR VEuPathDB; FungiDB:SPAC18B11.07c; -.
DR eggNOG; KOG0419; Eukaryota.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P23566; -.
DR OMA; DHKSQYI; -.
DR PhylomeDB; P23566; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P23566; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0033503; C:HULC complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; TAS:PomBase.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:PomBase.
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 1: Evidence at protein level;
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_0000082536"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..25
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 MUTAGEN 88
FT /note="C->A: No derepression of transcription."
FT /evidence="ECO:0000269|PubMed:12456009"
FT MUTAGEN 88
FT /note="C->S: No derepression of transcription."
FT /evidence="ECO:0000269|PubMed:12456009"
FT CONFLICT 111
FT /note="S -> R (in Ref. 1; CAA37340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 17097 MW; E4A88A40ECF35709 CRC64;
MSTTARRRLM RDFKRMQQDP PAGVSASPVS DNVMLWNAVI IGPADTPFED GTFKLVLSFD
EQYPNKPPLV KFVSTMFHPN VYANGELCLD ILQNRWSPTY DVAAILTSIQ SLLNDPNNAS
PANAEAAQLH RENKKEYVRR VRKTVEDSWE S
