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P23566 (UBC2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDNA damage
DNA repair
Sporulation
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication-independent nucleosome assembly

Traceable author statement PubMed 17374714. Source: PomBase

cellular response to hyperoxia

Inferred from mutant phenotype PubMed 22017871. Source: PomBase

chromatin assembly

Inferred from mutant phenotype PubMed 17374714. Source: PomBase

chromatin remodeling

Inferred from mutant phenotype Ref.3. Source: PomBase

chromatin silencing

Inferred from mutant phenotype Ref.5. 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

negative regulation of SREBP signaling pathway by positive regulation of transcription factor catabolic process in response to increased oxygen levels

Inferred from direct assay PubMed 22017871. Source: PomBase

negative regulation of transcription by transcription factor catabolism

Inferred from mutant phenotype PubMed 22017871. Source: PomBase

proteasome localization

Inferred from mutant phenotype Ref.7. Source: PomBase

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 11702950. 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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentHULC 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

nucleus

Inferred from direct assay Ref.8. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23416107. Source: PomBase

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 11702950Ref.6Ref.7Ref.9. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Ubiquitin-conjugating enzyme E2 2
PRO_0000082536

Sites

Active site881Glycyl thioester intermediate

Experimental info

Mutagenesis881C → A: No derepression of transcription. Ref.4
Mutagenesis881C → S: No derepression of transcription. Ref.4
Sequence conflict1111S → R in CAA37340. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23566 [UniParc].

Last modified November 1, 1995. Version 3.
Checksum: E4A88A40ECF35709

FASTA15117,097
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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: IDENTIFICATION IN THE HULC COMPLEX, FUNCTION OF THE HULC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53252 Genomic DNA. Translation: CAA37340.1.
CU329670 Genomic DNA. Translation: CAA90592.1.
PIRS12529.
T45220.
RefSeqNP_592876.1. NM_001018276.2.

3D structure databases

ProteinModelPortalP23566.
SMRP23566. Positions 2-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279076. 10 interactions.
IntActP23566. 4 interactions.
MINTMINT-4687768.
STRING4896.SPAC18B11.07c-1.

Proteomic databases

MaxQBP23566.
PaxDbP23566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC18B11.07c.1; SPAC18B11.07c.1:pep; SPAC18B11.07c.
GeneID2542622.
KEGGspo:SPAC18B11.07c.

Organism-specific databases

PomBaseSPAC18B11.07c.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
KOK10573.
OMAPVPDNVM.
OrthoDBEOG7SBP18.
PhylomeDBP23566.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803671.
PROP23566.

Entry information

Entry nameUBC2_SCHPO
AccessionPrimary (citable) accession number: P23566
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways