O00103 (UBC11_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2-20 kDa
EC=6.3.2.19

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

Gene names

Name:	ubc11
Synonyms:	ubcp4
ORF Names:	SPCC1259.15c

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	176 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW cyclin catabolic process Inferred from genetic interaction Ref.1. Source: PomBase mitotic sister chromatid segregation Inferred from mutant phenotype Ref.1. Source: PomBase regulation of mitotic metaphase/anaphase transition Inferred from mutant phenotype Ref.1. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Traceable author statement Ref.1. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 176	176	Ubiquitin-conjugating enzyme E2-20 kDa		PRO_0000082566
Sites
	Active site	113	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O00103 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 6C80769C37AD4950	FASTA	176	19,664
	10 20 30 40 50 60 MDSDMQNQNP HTNSKNSSSA GMAVDGHSVT KRLRSELMSL MMSNTPGISA FPDSDSNLLH 70 80 90 100 110 120 WAGTITGPSD TYYEGLKFKI SMSFPANYPY SPPTIIFTSP MWHPNVDMSG NICLDILKDK 130 140 150 160 170 WSAVYNVQTI LLSLQSLLGE PNNASPLNAQ AAELWSKDPI EYKRLLMQRY KEIDEI

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 [GENOMIC DNA]. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85545 Genomic DNA. Translation: BAA20375.1. CU329672 Genomic DNA. Translation: CAB38416.1.
PIR	T40902.
RefSeq	NP_588069.1. NM_001023061.2.
3D structure databases
ProteinModelPortal	O00103.
SMR	O00103. Positions 27-171.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC1259.15c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1259.15c.1; SPCC1259.15c.1:pep; SPCC1259.15c.
GeneID	2539190.
KEGG	spo:SPCC1259.15c.
Organism-specific databases
PomBase	SPCC1259.15c.
Phylogenomic databases
eggNOG	COG5078.
HOGENOM	HOG000233454.
KO	K06688.
OMA	NICMDIL.
OrthoDB	EOG43JGF2.
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	20800361.

Entry information

Entry name

UBC11_SCHPO

Accession

Primary (citable) accession number: O00103

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program