P33296 (UBC6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 6
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein UBC6
Ubiquitin-protein ligase UBC6

Gene names

Name:	UBC6
Synonyms:	DOA2
Ordered Locus Names:	YER100W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Ref.6 Ref.7
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Endoplasmic reticulum membrane.
Miscellaneous	Present with 1900 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype PubMed 8641272PubMed 8781238. Source: SGD protein monoubiquitination Traceable author statement PubMed 8982460. Source: SGD protein polyubiquitination Traceable author statement PubMed 8982460. Source: SGD
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.1. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RSP5	P39940	2	EBI-19745,EBI-16219

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 250	250	Ubiquitin-conjugating enzyme E2 6		PRO_0000082552
Regions
	Topological domain	1 – 232	232	Cytoplasmic Potential
	Transmembrane	233 – 249	17	Helical; Potential
Sites
	Active site	87	1	Glycyl thioester intermediate
Amino acid modifications
	Modified residue	178	1	Phosphothreonine Ref.9 Ref.10 Ref.11
Experimental info
	Mutagenesis	87	1	C → S: Loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	P33296 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 6D80C35ECC9CF5AD	FASTA	250	28,383
	10 20 30 40 50 60 MATKQAHKRL TKEYKLMVEN PPPYILARPN EDNILEWHYI ITGPADTPYK GGQYHGTLTF 70 80 90 100 110 120 PSDYPYKPPA IRMITPNGRF KPNTRLCLSM SDYHPDTWNP GWSVSTILNG LLSFMTSDEA 130 140 150 160 170 180 TTGSITTSDH QKKTLARNSI SYNTFQNVRF KLIFPEVVQE NVETLEKRKL DEGDAANTGD 190 200 210 220 230 240 ETEDPFTKAA KEKVISLEEI LDPEDRIRAE QALRQSENNS KKDGKEPNDS SSMVYIGIAI 250 FLFLVGLFMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum." Sommer T., Jentsch S. Nature 365:176-179(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor." Chen P., Johnson P., Sommer T., Jentsch S., Hochstrasser M. Cell 74:357-369(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway." Johnson P.R., Swanson R., Rakhilina L., Hochstrasser M. Cell 94:217-227(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation." Swanson R., Locher M., Hochstrasser M. Genes Dev. 15:2660-2674(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Ubx2 links the Cdc48 complex to ER-associated protein degradation." Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T. Nat. Cell Biol. 7:993-998(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SSM4.
[9]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, MASS SPECTROMETRY. Strain: ADR376.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, MASS SPECTROMETRY.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73234 Genomic DNA. Translation: CAA51706.1. U18839 Genomic DNA. Translation: AAB64655.1. BK006939 Genomic DNA. Translation: DAA07761.1.
PIR	S36769.
RefSeq	NP_011026.3. NM_001178991.3.
3D structure databases
ProteinModelPortal	P33296.
SMR	P33296. Positions 6-160.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1713N.
IntAct	P33296. 16 interactions.
MINT	MINT-393639.
STRING	4932.YER100W.
Proteomic databases
PaxDb	P33296.
PeptideAtlas	P33296.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER100W; YER100W; YER100W.
GeneID	856837.
KEGG	sce:YER100W. sce:YER104W.
Organism-specific databases
CYGD	YER100w.
SGD	S000000902. UBC6.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00530000063379.
HOGENOM	HOG000170329.
KO	K04554.
OMA	SFMTGDE.
OrthoDB	EOG441TMP.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	P33296.
GermOnline	YER100W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	983144.

Entry information

Entry name

UBC6_YEAST

Accession

Primary (citable) accession number: P33296
Secondary accession number(s): D3DM07

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program