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Ubiquitin-conjugating enzyme E2 7 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 7) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-18 kDa) (Ubiquitin-protein ligase)

 UBC7_YEAST              Reviewed;         165 AA.
Q02159; D6VZJ6;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 170.
RecName: Full=Ubiquitin-conjugating enzyme E2 7;
EC=2.3.2.23 {ECO:0000269|PubMed:9172777};
AltName: Full=E2 ubiquitin-conjugating enzyme 7;
AltName: Full=Ubiquitin carrier protein;
AltName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
AltName: Full=Ubiquitin-protein ligase;
Name=UBC7; Synonyms=QRI8; OrderedLocusNames=YMR022W;
ORFNames=YM9711.12;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204510 / AB320;
PubMed=1327148; DOI=10.1016/0167-4781(92)90015-R;
Vassal A., Boulet A., Decoster E., Faye G.;
"QRI8, a novel ubiquitin-conjugating enzyme in Saccharomyces
cerevisiae.";
Biochim. Biophys. Acta 1132:211-213(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8381213; DOI=10.1038/361369a0;
Jungmann J., Reins H.-A., Schobert C., Jentsch S.;
"Resistance to cadmium mediated by ubiquitin-dependent proteolysis.";
Nature 361:369-371(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
FUNCTION.
PubMed=8393731; DOI=10.1016/0092-8674(93)90426-Q;
Chen P., Johnson P., Sommer T., Jentsch S., Hochstrasser M.;
"Multiple ubiquitin-conjugating enzymes participate in the in vivo
degradation of the yeast MAT alpha 2 repressor.";
Cell 74:357-369(1993).
[7]
CATALYTIC ACTIVITY.
PubMed=9172777; DOI=10.1006/prep.1996.0016;
Yamazaki R.K., Chau V.;
"Bacterial expression of the Saccharomyces cerevisiae ubiquitin-
conjugating enzyme Ubc7.";
Protein Expr. Purif. 7:122-127(1996).
[8]
FUNCTION, AND INTERACTION WITH CUE1.
PubMed=9388185; DOI=10.1126/science.278.5344.1806;
Biederer T., Volkwein C., Sommer T.;
"Role of Cue1p in ubiquitination and degradation at the ER surface.";
Science 278:1806-1809(1997).
[9]
FUNCTION.
PubMed=9695950; DOI=10.1016/S0092-8674(00)81421-X;
Johnson P.R., Swanson R., Rakhilina L., Hochstrasser M.;
"Degradation signal masking by heterodimerization of MATalpha2 and
MATa1 blocks their mutual destruction by the ubiquitin-proteasome
pathway.";
Cell 94:217-227(1998).
[10]
FUNCTION.
PubMed=11641273; DOI=10.1101/gad.933301;
Swanson R., Locher M., Hochstrasser M.;
"A conserved ubiquitin ligase of the nuclear envelope/endoplasmic
reticulum that functions in both ER-associated and Matalpha2 repressor
degradation.";
Genes Dev. 15:2660-2674(2001).
[11]
FUNCTION.
PubMed=11390656; DOI=10.1128/MCB.21.13.4276-4291.2001;
Gardner R.G., Shearer A.G., Hampton R.Y.;
"In vivo action of the HRD ubiquitin ligase complex: mechanisms of
endoplasmic reticulum quality control and sterol regulation.";
Mol. Cell. Biol. 21:4276-4291(2001).
[12]
FUNCTION, AND INTERACTION WITH HDR1.
PubMed=11146622; DOI=10.1038/35050524;
Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.;
"Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-
associated degradation.";
Nat. Cell Biol. 3:24-29(2001).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
INTERACTION WITH SSM4.
PubMed=16179953; DOI=10.1038/ncb1298;
Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.;
"Ubx2 links the Cdc48 complex to ER-associated protein degradation.";
Nat. Cell Biol. 7:993-998(2005).
[15]
FUNCTION, AND INTERACTION WITH SSM4.
PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
Carvalho P., Goder V., Rapoport T.A.;
"Distinct ubiquitin-ligase complexes define convergent pathways for
the degradation of ER proteins.";
Cell 126:361-373(2006).
[16]
UBIQUITINATION AT CYS-89, INTERACTION WITH UFD4, AND MUTAGENESIS OF
CYS-39; CYS-89 AND CYS-141.
PubMed=17310239; DOI=10.1038/ncb1558;
Ravid T., Hochstrasser M.;
"Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its
catalytic residue.";
Nat. Cell Biol. 9:422-427(2007).
[17]
X-RAY CRYSTALLOGRAPHY (2.93 ANGSTROMS).
PubMed=9048545; DOI=10.1021/bi962639e;
Cook W.J., Martin P.D., Edwards B.F.P., Yamazaki R.K., Chau V.;
"Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7)
from Saccharomyces cerevisiae at 2.9-A resolution.";
Biochemistry 36:1621-1627(1997).
-!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
proteins. Functions in degradation of misfolded or regulated
proteins localized in the endoplasmic reticulum (ER) lumen or
membrane via the ubiquitin-proteasome system. Cognate E2
conjugating enzyme for the DOA10 ubiquitin ligase complex, which
is part of the ERAD-C pathway responsible for the rapid
degradation of membrane proteins with misfolded cytoplasmic
domains, and of the HRD1 ubiquitin ligase complex, which is part
of the ERAD-L and ERAD-M pathways responsible for the rapid
degradation of soluble lumenal and membrane proteins with
misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
misfolded transmembrane domains (ERAD-M). Involved in resistance
to cadmium poisoning. {ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000269|PubMed:11146622, ECO:0000269|PubMed:11390656,
ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:16873066,
ECO:0000269|PubMed:8393731, ECO:0000269|PubMed:9388185,
ECO:0000269|PubMed:9695950}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:9172777}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Forms a heterodimer with CUE1. Interacts with SSM4/DOA10
and HDR1. Interacts with UFD4. {ECO:0000269|PubMed:11146622,
ECO:0000269|PubMed:16179953, ECO:0000269|PubMed:16873066,
ECO:0000269|PubMed:17310239, ECO:0000269|PubMed:9388185}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein; Cytoplasmic side. Note=Anchored via the membrane
protein CUE1 to the endoplasmic reticulum membrane.
-!- INDUCTION: By cadmium.
-!- PTM: Autoubiquitinated at Cys-89; undergoes 'Lys-48'-linked
polyubiquitination, which leads to proteasome-dependent protein
degradation. Degradation is autoregulated when its levels exceed
that of its binding partner CUE1. {ECO:0000269|PubMed:17310239}.
-!- MISCELLANEOUS: Present with 2100 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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EMBL; X66829; CAA47302.1; -; Genomic_DNA.
EMBL; X69100; CAA48846.1; -; Genomic_DNA.
EMBL; Z49211; CAA89125.1; -; Genomic_DNA.
EMBL; AY558116; AAS56442.1; -; Genomic_DNA.
EMBL; BK006946; DAA09920.1; -; Genomic_DNA.
PIR; S28951; S28951.
RefSeq; NP_013735.1; NM_001182518.1.
PDB; 2UCZ; X-ray; 2.93 A; A=1-165.
PDB; 4JQU; X-ray; 1.81 A; A=2-165.
PDBsum; 2UCZ; -.
PDBsum; 4JQU; -.
ProteinModelPortal; Q02159; -.
SMR; Q02159; -.
BioGrid; 35193; 249.
ComplexPortal; CPX-2948; CUE1-UBC7 ubiquitin-conjugating enzyme complex.
DIP; DIP-6583N; -.
IntAct; Q02159; 620.
STRING; 4932.YMR022W; -.
MaxQB; Q02159; -.
PaxDb; Q02159; -.
PRIDE; Q02159; -.
EnsemblFungi; YMR022W; YMR022W; YMR022W.
GeneID; 855036; -.
KEGG; sce:YMR022W; -.
EuPathDB; FungiDB:YMR022W; -.
SGD; S000004624; UBC7.
GeneTree; ENSGT00730000110436; -.
HOGENOM; HOG000233454; -.
InParanoid; Q02159; -.
KO; K04555; -.
OMA; PKMQFTC; -.
OrthoDB; EOG092C50OL; -.
BioCyc; YEAST:G3O-32727-MONOMER; -.
Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q02159; -.
PRO; PR:Q02159; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
GO; GO:0006333; P:chromatin assembly or disassembly; IMP:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:SGD.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cadmium; Cadmium resistance;
Complete proteome; Endoplasmic reticulum; Membrane;
Nucleotide-binding; Reference proteome; Thioester bond; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 165 Ubiquitin-conjugating enzyme E2 7.
/FTId=PRO_0000082554.
ACT_SITE 89 89 Glycyl thioester intermediate.
CROSSLNK 89 89 Glycyl cysteine thioester (Cys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17310239}.
MUTAGEN 39 39 C->S: No effect; when associated with S-
141. {ECO:0000269|PubMed:17310239}.
MUTAGEN 81 81 N->A: Impairs degradation of UBC7-
substrates, but does not prevent protein
degradation.
MUTAGEN 89 89 C->A,S: Prevents polyubiquitin chain
attachment and protein degradation.
{ECO:0000269|PubMed:17310239}.
MUTAGEN 141 141 C->S: No effect; when associated with S-
39. {ECO:0000269|PubMed:17310239}.
HELIX 2 19 {ECO:0000244|PDB:4JQU}.
STRAND 24 30 {ECO:0000244|PDB:4JQU}.
STRAND 33 42 {ECO:0000244|PDB:4JQU}.
TURN 48 51 {ECO:0000244|PDB:4JQU}.
STRAND 53 59 {ECO:0000244|PDB:4JQU}.
TURN 62 65 {ECO:0000244|PDB:4JQU}.
STRAND 70 75 {ECO:0000244|PDB:4JQU}.
STRAND 86 88 {ECO:0000244|PDB:4JQU}.
HELIX 91 93 {ECO:0000244|PDB:4JQU}.
STRAND 102 104 {ECO:0000244|PDB:2UCZ}.
TURN 105 108 {ECO:0000244|PDB:2UCZ}.
HELIX 116 128 {ECO:0000244|PDB:4JQU}.
HELIX 132 134 {ECO:0000244|PDB:4JQU}.
HELIX 138 146 {ECO:0000244|PDB:4JQU}.
HELIX 148 162 {ECO:0000244|PDB:4JQU}.
SEQUENCE 165 AA; 18520 MW; D3D297847DBB462D CRC64;
MSKTAQKRLL KELQQLIKDS PPGIVAGPKS ENNIFIWDCL IQGPPDTPYA DGVFNAKLEF
PKDYPLSPPK LTFTPSILHP NIYPNGEVCI SILHSPGDDP NMYELAEERW SPVQSVEKIL
LSVMSMLSEP NIESGANIDA CILWRDNRPE FERQVKLSIL KSLGF


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