UBC6_YEAST
ID UBC6_YEAST Reviewed; 250 AA.
AC P33296; D3DM07;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 6;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 6;
DE AltName: Full=Ubiquitin carrier protein UBC6;
DE AltName: Full=Ubiquitin-protein ligase UBC6;
GN Name=UBC6; Synonyms=DOA2; OrderedLocusNames=YER100W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=8396728; DOI=10.1038/365176a0;
RA Sommer T., Jentsch S.;
RT "A protein translocation defect linked to ubiquitin conjugation at the
RT endoplasmic reticulum.";
RL Nature 365:176-179(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=8393731; DOI=10.1016/0092-8674(93)90426-q;
RA Chen P., Johnson P., Sommer T., Jentsch S., Hochstrasser M.;
RT "Multiple ubiquitin-conjugating enzymes participate in the in vivo
RT degradation of the yeast MAT alpha 2 repressor.";
RL Cell 74:357-369(1993).
RN [6]
RP FUNCTION.
RX PubMed=9695950; DOI=10.1016/s0092-8674(00)81421-x;
RA Johnson P.R., Swanson R., Rakhilina L., Hochstrasser M.;
RT "Degradation signal masking by heterodimerization of MATalpha2 and MATa1
RT blocks their mutual destruction by the ubiquitin-proteasome pathway.";
RL Cell 94:217-227(1998).
RN [7]
RP FUNCTION.
RX PubMed=11641273; DOI=10.1101/gad.933301;
RA Swanson R., Locher M., Hochstrasser M.;
RT "A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum
RT that functions in both ER-associated and Matalpha2 repressor degradation.";
RL Genes Dev. 15:2660-2674(2001).
RN [8]
RP INTERACTION WITH SSM4.
RX PubMed=16179953; DOI=10.1038/ncb1298;
RA Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.;
RT "Ubx2 links the Cdc48 complex to ER-associated protein degradation.";
RL Nat. Cell Biol. 7:993-998(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(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. {ECO:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:8393731,
CC ECO:0000269|PubMed:9695950}.
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- INTERACTION:
CC P33296; P39940: RSP5; NbExp=2; IntAct=EBI-19745, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8396728}.
CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X73234; CAA51706.1; -; Genomic_DNA.
DR EMBL; U18839; AAB64655.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07761.1; -; Genomic_DNA.
DR PIR; S36769; S36769.
DR RefSeq; NP_011026.3; NM_001178991.3.
DR AlphaFoldDB; P33296; -.
DR SMR; P33296; -.
DR BioGRID; 36846; 166.
DR DIP; DIP-1713N; -.
DR IntAct; P33296; 27.
DR MINT; P33296; -.
DR STRING; 4932.YER100W; -.
DR iPTMnet; P33296; -.
DR MaxQB; P33296; -.
DR PaxDb; P33296; -.
DR PRIDE; P33296; -.
DR EnsemblFungi; YER100W_mRNA; YER100W; YER100W.
DR GeneID; 856837; -.
DR KEGG; sce:YER100W; -.
DR SGD; S000000902; UBC6.
DR VEuPathDB; FungiDB:YER100W; -.
DR eggNOG; KOG0894; Eukaryota.
DR GeneTree; ENSGT00940000156173; -.
DR HOGENOM; CLU_041481_1_0_1; -.
DR InParanoid; P33296; -.
DR OMA; DKMFCEL; -.
DR BioCyc; YEAST:G3O-30265-MON; -.
DR Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P33296; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P33296; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..250
FT /note="Ubiquitin-conjugating enzyme E2 6"
FT /id="PRO_0000082552"
FT TOPO_DOM 1..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..167
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 209..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 87
FT /note="C->S: Loss of activity."
SQ SEQUENCE 250 AA; 28383 MW; 6D80C35ECC9CF5AD CRC64;
MATKQAHKRL TKEYKLMVEN PPPYILARPN EDNILEWHYI ITGPADTPYK GGQYHGTLTF
PSDYPYKPPA IRMITPNGRF KPNTRLCLSM SDYHPDTWNP GWSVSTILNG LLSFMTSDEA
TTGSITTSDH QKKTLARNSI SYNTFQNVRF KLIFPEVVQE NVETLEKRKL DEGDAANTGD
ETEDPFTKAA KEKVISLEEI LDPEDRIRAE QALRQSENNS KKDGKEPNDS SSMVYIGIAI
FLFLVGLFMK
