NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
DOI=10.1126/science.1095781; PubMed=15001715 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.;
"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome.";
Science 304:304-307(2004).

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).
SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE016814; AAS50523.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_982699.1; -.

3D structure databases

HSSP

P06104; 1AYZ. [HSSP ENTRY / PDB]

SMR

Q75EB8; 2-153.

ModBase

Q75EB8.

Organism-specific databases

AGD

AAR156C; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0004842;	Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from UniProtKB-KW).
GO:0043687;	Biological process: post-translational protein modification (inferred from electronic annotation from InterPro).
GO:0051246;	Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0030435;	Biological process: sporulation resulting in formation of a cellular spore (inferred from electronic annotation from UniProtKB-KW).
GO:0006511;	Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.

PANTHER

PTHR11621; UBQ-conjugat_E2; 1.

Pfam

PF00179; UQ_con; 1.
Pfam graphical view of domain structure.

ProDom

PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00212; UBCc; 1.
SMART graphical view of domain structure.

PROSITE

PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q75EB8.

Genome annotation databases

4618613; -.

fig|33169.1.peg.344; -.

Phylogenomic databases

HOGENOM

Q75EB8; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chromatin regulator; Complete proteome; Cytoplasm; DNA damage; DNA repair; Ligase; Nucleus; Sporulation; Transcription; Transcription regulation; Ubl conjugation pathway.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 170`	`170`	`Ubiquitin-conjugating enzyme E2 2.`	`PRO_0000082526`
`ACT_SITE`	`88 88`		`Glycyl thioester intermediate (By similarity).`

Sequence information

Length: 170 AA [This is the length of the unprocessed precursor]

Molecular weight: 19443 Da [This is the MW of the unprocessed precursor]

CRC64: E7A881C8190F22F3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTPARRRLM RDFKRMKEDA PPGVSASPLP DNVMVWNAMI IGPADTPYED GTFRLLLEFD 

        70         80         90        100        110        120 
EEYPNKPPHV KFLSEMFHPN VYANGEICLD ILQNRWTPTY DVASILTSIQ SLFNDPNPAS 

       130        140        150        160        170 
PANVEAATLF KDHKSQYVKR VKETVEKSWE DDLKDMDDGD DDDDDDDDDD

Q75EB8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools