UBC7_SCHPO
ID UBC7_SCHPO Reviewed; 166 AA.
AC O00102; Q9HDP3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 7;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=ubc7; Synonyms=ubcp3; ORFNames=SPBP16F5.04;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9154838; DOI=10.1128/mcb.17.6.3388;
RA Osaka F., Seino H., Seno T., Yamao F.;
RT "A ubiquitin-conjugating enzyme in fission yeast that is essential for the
RT onset of anaphase in mitosis.";
RL Mol. Cell. Biol. 17:3388-3397(1997).
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=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 [4]
RP FUNCTION.
RX PubMed=19520858; DOI=10.1074/jbc.m109.002436;
RA Hughes B.T., Nwosu C.C., Espenshade P.J.;
RT "Degradation of sterol regulatory element-binding protein precursor
RT requires the endoplasmic reticulum-associated degradation components Ubc7
RT and Hrd1 in fission yeast.";
RL J. Biol. Chem. 284:20512-20521(2009).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Functions in degradation of misfolded or regulated proteins
CC localized in the endoplasmic reticulum (ER) lumen or membrane via the
CC ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the
CC doa10 ubiquitin ligase complex, which is part of the ERAD-C pathway
CC responsible for the rapid degradation of membrane proteins with
CC misfolded cytoplasmic domains, and of the hrd1 ubiquitin ligase
CC complex, which is part of the ERAD-L and ERAD-M pathways responsible
CC for the rapid degradation of soluble lumenal and membrane proteins with
CC misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
CC misfolded transmembrane domains (ERAD-M) (By similarity). Together with
CC hrd1, required for the degradation of the transcription factor sre1
CC precursor in the absence of its binding partner scp1. Has a role in the
CC formation of chromatin structures that influence the localization of
CC transcriptional silencing factors. {ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000269|PubMed:12456009,
CC ECO:0000269|PubMed:19520858}.
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 -!- PTM: Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked
CC polyubiquitination, which leads to proteasome-dependent protein
CC degradation. {ECO:0000250|UniProtKB:Q02159}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; D85544; BAA20373.1; -; mRNA.
DR EMBL; CU329671; CAC08543.1; -; Genomic_DNA.
DR PIR; T43235; T43235.
DR RefSeq; NP_595778.1; NM_001021678.2.
DR PDB; 6OP8; X-ray; 1.70 A; A=1-166.
DR PDBsum; 6OP8; -.
DR AlphaFoldDB; O00102; -.
DR SMR; O00102; -.
DR BioGRID; 277766; 2.
DR STRING; 4896.SPBP16F5.04.1; -.
DR MaxQB; O00102; -.
DR PaxDb; O00102; -.
DR PRIDE; O00102; -.
DR EnsemblFungi; SPBP16F5.04.1; SPBP16F5.04.1:pep; SPBP16F5.04.
DR GeneID; 2541252; -.
DR KEGG; spo:SPBP16F5.04; -.
DR PomBase; SPBP16F5.04; ubc7.
DR VEuPathDB; FungiDB:SPBP16F5.04; -.
DR eggNOG; KOG0426; Eukaryota.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; O00102; -.
DR OMA; KMWRENR; -.
DR PhylomeDB; O00102; -.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O00102; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; ISO: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:0010620; P:negative regulation of transcription by transcription factor catabolism; 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:0030433; P:ubiquitin-dependent ERAD pathway; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW Thioester bond; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..166
FT /note="Ubiquitin-conjugating enzyme E2-18 kDa"
FT /id="PRO_0000082553"
FT DOMAIN 5..165
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 90
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CROSSLNK 90
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q02159"
FT CONFLICT 6
FT /note="A -> P (in Ref. 1; BAA20373)"
FT /evidence="ECO:0000305"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:6OP8"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6OP8"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6OP8"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6OP8"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6OP8"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6OP8"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:6OP8"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6OP8"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6OP8"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6OP8"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6OP8"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:6OP8"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:6OP8"
FT HELIX 149..166
FT /evidence="ECO:0007829|PDB:6OP8"
SQ SEQUENCE 166 AA; 18720 MW; C376ACE52EF444EE CRC64;
MSKAMALRRL MKEYKELTEN GPDGITAGPS NEDDFFTWDC LIQGPDGTPF EGGLYPATLK
FPSDYPLGPP TLKFECEFFH PNVYKDGTVC ISILHAPGDD PNMYESSSER WSPVQSVEKI
LLSVMSMLAE PNDESGANID ACKMWREDRE EYCRVVRRLA RKTLGL
