O00102 (UBC7_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2-18 kDa
EC=6.3.2.19

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

Gene names

Name:	ubc7
Synonyms:	ubcp3
ORF Names:	SPBP16F5.04

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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, 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) By similarity. Together with hrd1, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1. Has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors. Ref.3 Ref.4
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Post-translational modification	Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Thioester bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.4. Source: PomBase chromatin silencing at silent mating-type cassette Inferred from mutant phenotype Ref.3. Source: PomBase negative regulation of transcription by transcription factor catabolism Inferred from mutant phenotype Ref.4. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase ubiquitin ligase complex Inferred from sequence orthology. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Traceable author statement Ref.4. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 166	166	Ubiquitin-conjugating enzyme E2-18 kDa		PRO_0000082553
Sites
	Active site	90	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Cross-link	90		Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	6	1	A → P in BAA20373. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O00102 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: C376ACE52EF444EE	FASTA	166	18,720
	10 20 30 40 50 60 MSKAMALRRL MKEYKELTEN GPDGITAGPS NEDDFFTWDC LIQGPDGTPF EGGLYPATLK 70 80 90 100 110 120 FPSDYPLGPP TLKFECEFFH PNVYKDGTVC ISILHAPGDD PNMYESSSER WSPVQSVEKI 130 140 150 160 LLSVMSMLAE PNDESGANID ACKMWREDRE EYCRVVRRLA RKTLGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A ubiquitin-conjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis." Osaka F., Seino H., Seno T., Yamao F. Mol. Cell. Biol. 17:3388-3397(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 972 / ATCC 24843.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6 affect transcriptional silencing of the mating-type region." Nielsen I.S., Nielsen O., Murray J.M., Thon G. Eukaryot. Cell 1:613-625(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Degradation of sterol regulatory element-binding protein precursor requires the endoplasmic reticulum-associated degradation components Ubc7 and Hrd1 in fission yeast." Hughes B.T., Nwosu C.C., Espenshade P.J. J. Biol. Chem. 284:20512-20521(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85544 mRNA. Translation: BAA20373.1. CU329671 Genomic DNA. Translation: CAC08543.1.
PIR	T43235.
RefSeq	NP_595778.1. NM_001021678.2.
3D structure databases
ProteinModelPortal	O00102.
SMR	O00102. Positions 6-166.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBP16F5.04-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBP16F5.04.1; SPBP16F5.04.1:pep; SPBP16F5.04.
GeneID	2541252.
KEGG	spo:SPBP16F5.04.
Organism-specific databases
PomBase	SPBP16F5.04.
Phylogenomic databases
eggNOG	COG5078.
HOGENOM	HOG000233454.
KO	K04555.
OMA	RRLMAEY.
OrthoDB	EOG4X6GJN.
Enzyme and pathway databases
UniPathway	UPA00143.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. 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. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802364.

Entry information

Entry name

UBC7_SCHPO

Accession

Primary (citable) accession number: O00102
Secondary accession number(s): Q9HDP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program