Reviewed, UniProtKB/Swiss-Prot Q4WLA7 (UBC2_ASPFU)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 2
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase ubc2
    Ubiquitin carrier protein ubc2

Gene names

Name:	ubc2
ORF Names:	AFUA_6G14210

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 151	151	Ubiquitin-conjugating enzyme E2 2		PRO_0000082527
Sites
	Active site	88	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WLA7-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 89345B6BA251A556	FASTA	151	17,169
	10 20 30 40 50 60 MSTSARRRLM RDFKRMQTDP PAGVSASPVA DNVMTWNAVI IGPADTPFED GTFRLVMHFE 70 80 90 100 110 120 EQYPNKPPGV KFISQMFHPN VYGTGELCLD ILQNRWSPTY DVAAILTSIQ SLLNDPNTSS 130 140 150 PANVEASNLY KDNRKEYIKR VRETVEKSWE D

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000006 Genomic DNA. Translation: EAL89257.1.
RefSeq	XP_751295.1.
3D structure databases
SMR	Q4WLA7. Positions 2-151.
ModBase	Search...
Genome annotation databases
GeneID	3508612.
KEGG	afm:AFUA_6G14210.
Phylogenomic databases
HOGENOM	Q4WLA7.
OMA	Q4WLA7. ANGELCL.
Enzyme and pathway databases
BRENDA	6.3.2.19. 18841.
Family and domain databases
InterPro	IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
ProDom	PD000461. UBQ_conjugat. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00212. UBCc. 1 hit. [Graphical view]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBC2_ASPFU

Accession

Primary (citable) accession number: Q4WLA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)