Q6FR76 (UBC2_CANGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 2
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein UBC2
Ubiquitin-protein ligase UBC2

Gene names

Name:	UBC2
Ordered Locus Names:	CAGL0I00352g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › Candida glabrata

Protein attributes

Sequence length	167 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation By similarity.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Sporulation Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW protein autoubiquitination Inferred from sequence orthology PubMed 16978390. Source: CGD protein import into peroxisome matrix, receptor recycling Inferred from sequence orthology PubMed 16978390. Source: CGD protein monoubiquitination Inferred from sequence orthology PubMed 16978390. Source: CGD regulation of transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from sequence orthology PubMed 16978390. Source: CGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from sequence orthology PubMed 16978390. Source: CGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 167	167	Ubiquitin-conjugating enzyme E2 2		PRO_0000082529
Sites
	Active site	88	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FR76 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A9EF7E08327079AE	FASTA	167	19,189
	10 20 30 40 50 60 MSTPARRRLM RDFKRMKEDS PPGVSASPLP DNVMVWNAMI IGPADTPYED GTFRLLLEFD 70 80 90 100 110 120 EDYPNKPPHV KFLSEMFHPN VYANGEICLD ILQNRWTPTY DVASILTSIQ SLFNDPNPAS 130 140 150 160 PANVEAATLF KDHKSQYIKR VKETVEKSWE DNMDDMDDSD EDDEDDE

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380955 Genomic DNA. Translation: CAG60205.1.
RefSeq	XP_447268.1. XM_447268.1.
3D structure databases
ProteinModelPortal	Q6FR76.
SMR	Q6FR76. Positions 2-154.
ModBase	Search...
MobiDB	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2889314.
KEGG	cgr:CAGL0I00352g.
Phylogenomic databases
KO	K10573.
OMA	ETVENSW.
OrthoDB	EOG7SBP18.
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. SSF54495. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBC2_CANGA

Accession

Primary (citable) accession number: Q6FR76

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 19, 2004
Last modified:	February 19, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program