P23566 (UBC2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
RAD6 homolog
Ubiquitin carrier protein 2
Ubiquitin-protein ligase 2

Gene names

Name:	rhp6
Synonyms:	ubc2
ORF Names:	SPAC18B11.07c

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	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Component of the histone H2B ubiquitin ligase complex (HULC) which 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. Required for obr1 ubiquitination, which regulates mating-type silencing. With cut8, regulates the nuclear accumulation of the proteasome. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the histone H2B ubiquitin ligase complex (HULC) composed of at least brl1, brl2, rhp6 and shf1. Ref.9
Subcellular location	Cytoplasm. Nucleus Ref.8.
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 Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication-independent nucleosome assembly Traceable author statement PubMed 17374714. Source: PomBase chromatin remodeling Inferred from mutant phenotype Ref.3. Source: PomBase chromatin silencing at silent mating-type cassette Inferred from genetic interaction Ref.4. Source: PomBase histone H2B conserved C-terminal lysine ubiquitination Inferred from direct assay PubMed 17374714. Source: PomBase postreplication repair Inferred from genetic interaction Ref.1. Source: PomBase proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype PubMed 11702950. Source: PomBase proteasome localization Inferred from mutant phenotype Ref.7. Source: PomBase regulation of histone H3-K4 methylation Inferred from mutant phenotype PubMed 17374714. Source: PomBase sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	HULC complex Inferred from direct assay Ref.9PubMed 17374714. Source: PomBase cytosol Inferred from direct assay Ref.8. Source: PomBase nuclear chromatin Non-traceable author statement. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay PubMed 11702950Ref.6Ref.7. Source: PomBase
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_0000082536
Sites
	Active site	88	1	Glycyl thioester intermediate
Experimental info
	Mutagenesis	88	1	C → A: No derepression of transcription. Ref.4
	Mutagenesis	88	1	C → S: No derepression of transcription. Ref.4
	Sequence conflict	111	1	S → R in CAA37340. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23566 [UniParc]. Last modified November 1, 1995. Version 3. Checksum: E4A88A40ECF35709	FASTA	151	17,097
	10 20 30 40 50 60 MSTTARRRLM RDFKRMQQDP PAGVSASPVS DNVMLWNAVI IGPADTPFED GTFKLVLSFD 70 80 90 100 110 120 EQYPNKPPLV KFVSTMFHPN VYANGELCLD ILQNRWSPTY DVAAILTSIQ SLLNDPNNAS 130 140 150 PANAEAAQLH RENKKEYVRR VRKTVEDSWE S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The rhp6+ gene of Schizosaccharomyces pombe: a structural and functional homolog of the RAD6 gene from the distantly related yeast Saccharomyces cerevisiae." Reynolds P., Koken M.H.M., Hoeijmakers J.H.J., Prakash S., Prakash L. EMBO J. 9:1423-1430(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]	"A novel function of the DNA repair gene rhp6 in mating-type silencing by chromatin remodeling in fission yeast." Singh J., Goel V., Klar A.J.S. Mol. Cell. Biol. 18:5511-5522(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"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, MUTAGENESIS OF CYS-88.
[5]	"Two ubiquitin-conjugating enzymes, Rhp6 and UbcX, regulate heterochromatin silencing in Schizosaccharomyces pombe." Choi E.S., Kim H.S., Jang Y.K., Hong S.H., Park S.D. Mol. Cell. Biol. 22:8366-8374(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Identification of Uhp1, a ubiquitinated histone-like protein, as a target/mediator of Rhp6 in mating-type silencing in fission yeast." Naresh A., Saini S., Singh J. J. Biol. Chem. 278:9185-9194(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8." Takeda K., Yanagida M. Cell 122:393-405(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"HULC, a histone H2B ubiquitinating complex, modulates heterochromatin independent of histone methylation in fission yeast." Zofall M., Grewal S.I.S. J. Biol. Chem. 282:14065-14072(2007) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE HULC COMPLEX, FUNCTION OF THE HULC COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53252 Genomic DNA. Translation: CAA37340.1. CU329670 Genomic DNA. Translation: CAA90592.1.
PIR	S12529. T45220.
RefSeq	NP_592876.1. NM_001018276.2.
3D structure databases
ProteinModelPortal	P23566.
SMR	P23566. Positions 2-150.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23566. 4 interactions.
MINT	MINT-4687768.
STRING	4896.SPAC18B11.07c-1.
Proteomic databases
PaxDb	P23566.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC18B11.07c.1; SPAC18B11.07c.1:pep; SPAC18B11.07c.
GeneID	2542622.
KEGG	spo:SPAC18B11.07c.
Organism-specific databases
PomBase	SPAC18B11.07c.
Phylogenomic databases
eggNOG	COG5078.
HOGENOM	HOG000233454.
KO	K10573.
OMA	YANGELC.
OrthoDB	EOG4B01ZN.
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	20803671.

Entry information

Entry name

UBC2_SCHPO

Accession

Primary (citable) accession number: P23566

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program