UBC7_YEAST
ID UBC7_YEAST Reviewed; 165 AA.
AC Q02159; D6VZJ6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 7;
DE EC=2.3.2.23 {ECO:0000269|PubMed:9172777};
DE AltName: Full=E2 ubiquitin-conjugating enzyme 7;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=UBC7; Synonyms=QRI8; OrderedLocusNames=YMR022W; ORFNames=YM9711.12;
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].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1327148; DOI=10.1016/0167-4781(92)90015-r;
RA Vassal A., Boulet A., Decoster E., Faye G.;
RT "QRI8, a novel ubiquitin-conjugating enzyme in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1132:211-213(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8381213; DOI=10.1038/361369a0;
RA Jungmann J., Reins H.-A., Schobert C., Jentsch S.;
RT "Resistance to cadmium mediated by ubiquitin-dependent proteolysis.";
RL Nature 361:369-371(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
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 [7]
RP CATALYTIC ACTIVITY.
RX PubMed=9172777; DOI=10.1006/prep.1996.0016;
RA Yamazaki R.K., Chau V.;
RT "Bacterial expression of the Saccharomyces cerevisiae ubiquitin-conjugating
RT enzyme Ubc7.";
RL Protein Expr. Purif. 7:122-127(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH CUE1.
RX PubMed=9388185; DOI=10.1126/science.278.5344.1806;
RA Biederer T., Volkwein C., Sommer T.;
RT "Role of Cue1p in ubiquitination and degradation at the ER surface.";
RL Science 278:1806-1809(1997).
RN [9]
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 [10]
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 [11]
RP FUNCTION.
RX PubMed=11390656; DOI=10.1128/mcb.21.13.4276-4291.2001;
RA Gardner R.G., Shearer A.G., Hampton R.Y.;
RT "In vivo action of the HRD ubiquitin ligase complex: mechanisms of
RT endoplasmic reticulum quality control and sterol regulation.";
RL Mol. Cell. Biol. 21:4276-4291(2001).
RN [12]
RP FUNCTION, AND INTERACTION WITH HDR1.
RX PubMed=11146622; DOI=10.1038/35050524;
RA Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.;
RT "Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-
RT associated degradation.";
RL Nat. Cell Biol. 3:24-29(2001).
RN [13]
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 [14]
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 [15]
RP FUNCTION, AND INTERACTION WITH SSM4.
RX PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA Carvalho P., Goder V., Rapoport T.A.;
RT "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT degradation of ER proteins.";
RL Cell 126:361-373(2006).
RN [16]
RP UBIQUITINATION AT CYS-89, INTERACTION WITH UFD4, AND MUTAGENESIS OF CYS-39;
RP CYS-89 AND CYS-141.
RX PubMed=17310239; DOI=10.1038/ncb1558;
RA Ravid T., Hochstrasser M.;
RT "Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its
RT catalytic residue.";
RL Nat. Cell Biol. 9:422-427(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.93 ANGSTROMS).
RX PubMed=9048545; DOI=10.1021/bi962639e;
RA Cook W.J., Martin P.D., Edwards B.F.P., Yamazaki R.K., Chau V.;
RT "Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from
RT Saccharomyces cerevisiae at 2.9-A resolution.";
RL Biochemistry 36:1621-1627(1997).
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). Involved in resistance to
CC cadmium poisoning. {ECO:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:11146622, ECO:0000269|PubMed:11390656,
CC ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:8393731, ECO:0000269|PubMed:9388185,
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, ECO:0000255|PROSITE-
CC ProRule:PRU10133, ECO:0000269|PubMed:9172777};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Forms a heterodimer with CUE1. Interacts with SSM4/DOA10 and
CC HDR1. Interacts with UFD4. {ECO:0000269|PubMed:11146622,
CC ECO:0000269|PubMed:16179953, ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:17310239, ECO:0000269|PubMed:9388185}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Anchored via the membrane
CC protein CUE1 to the endoplasmic reticulum membrane.
CC -!- INDUCTION: By cadmium.
CC -!- PTM: Autoubiquitinated at Cys-89; undergoes 'Lys-48'-linked
CC polyubiquitination, which leads to proteasome-dependent protein
CC degradation. Degradation is autoregulated when its levels exceed that
CC of its binding partner CUE1. {ECO:0000269|PubMed:17310239}.
CC -!- MISCELLANEOUS: Present with 2100 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; X66829; CAA47302.1; -; Genomic_DNA.
DR EMBL; X69100; CAA48846.1; -; Genomic_DNA.
DR EMBL; Z49211; CAA89125.1; -; Genomic_DNA.
DR EMBL; AY558116; AAS56442.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09920.1; -; Genomic_DNA.
DR PIR; S28951; S28951.
DR RefSeq; NP_013735.1; NM_001182518.1.
DR PDB; 2UCZ; X-ray; 2.93 A; A=1-165.
DR PDB; 4JQU; X-ray; 1.81 A; A=2-165.
DR PDBsum; 2UCZ; -.
DR PDBsum; 4JQU; -.
DR AlphaFoldDB; Q02159; -.
DR SMR; Q02159; -.
DR BioGRID; 35193; 250.
DR ComplexPortal; CPX-2948; CUE1-UBC7 ubiquitin-conjugating enzyme complex.
DR DIP; DIP-6583N; -.
DR IntAct; Q02159; 619.
DR STRING; 4932.YMR022W; -.
DR iPTMnet; Q02159; -.
DR MaxQB; Q02159; -.
DR PaxDb; Q02159; -.
DR PRIDE; Q02159; -.
DR EnsemblFungi; YMR022W_mRNA; YMR022W; YMR022W.
DR GeneID; 855036; -.
DR KEGG; sce:YMR022W; -.
DR SGD; S000004624; UBC7.
DR VEuPathDB; FungiDB:YMR022W; -.
DR eggNOG; KOG0426; Eukaryota.
DR GeneTree; ENSGT00940000158193; -.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; Q02159; -.
DR OMA; KMWRENR; -.
DR BioCyc; YEAST:G3O-32727-MON; -.
DR BRENDA; 2.3.2.23; 984.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q02159; -.
DR PRO; PR:Q02159; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02159; protein.
DR GO; GO:1990389; C:CUE1-UBC7 ubiquitin-conjugating enzyme complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
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:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:SGD.
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; Cadmium; Cadmium resistance;
KW Endoplasmic reticulum; Membrane; Nucleotide-binding; Reference proteome;
KW Thioester bond; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..165
FT /note="Ubiquitin-conjugating enzyme E2 7"
FT /id="PRO_0000082554"
FT DOMAIN 4..164
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 89
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT CROSSLNK 89
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17310239"
FT MUTAGEN 39
FT /note="C->S: No effect; when associated with S-141."
FT /evidence="ECO:0000269|PubMed:17310239"
FT MUTAGEN 81
FT /note="N->A: Impairs degradation of UBC7-substrates, but
FT does not prevent protein degradation."
FT MUTAGEN 89
FT /note="C->A,S: Prevents polyubiquitin chain attachment and
FT protein degradation."
FT /evidence="ECO:0000269|PubMed:17310239"
FT MUTAGEN 141
FT /note="C->S: No effect; when associated with S-39."
FT /evidence="ECO:0000269|PubMed:17310239"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:4JQU"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:4JQU"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:4JQU"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:4JQU"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4JQU"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4JQU"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:4JQU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4JQU"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2UCZ"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:2UCZ"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:4JQU"
SQ SEQUENCE 165 AA; 18520 MW; D3D297847DBB462D CRC64;
MSKTAQKRLL KELQQLIKDS PPGIVAGPKS ENNIFIWDCL IQGPPDTPYA DGVFNAKLEF
PKDYPLSPPK LTFTPSILHP NIYPNGEVCI SILHSPGDDP NMYELAEERW SPVQSVEKIL
LSVMSMLSEP NIESGANIDA CILWRDNRPE FERQVKLSIL KSLGF
