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P23566

- UBC2_SCHPO

UniProt

P23566 - UBC2_SCHPO

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Protein

Ubiquitin-conjugating enzyme E2 2

Gene

rhp6

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 PublicationsPROSITE-ProRule annotation

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediate

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin protein ligase activity Source: PomBase

GO - Biological processi

  1. cellular response to hyperoxia Source: PomBase
  2. chromatin assembly Source: PomBase
  3. chromatin remodeling Source: PomBase
  4. chromatin silencing Source: PomBase
  5. chromatin silencing at silent mating-type cassette Source: PomBase
  6. DNA repair Source: UniProtKB-KW
  7. DNA replication-independent nucleosome assembly Source: PomBase
  8. histone H2B conserved C-terminal lysine ubiquitination Source: PomBase
  9. negative regulation of SREBP signaling pathway by positive regulation of transcription factor catabolic process in response to increased oxygen levels Source: PomBase
  10. negative regulation of transcription by transcription factor catabolism Source: PomBase
  11. proteasome localization Source: PomBase
  12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: PomBase
  13. regulation of histone H3-K4 methylation Source: PomBase
  14. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
  15. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

DNA damage, DNA repair, Sporulation, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:rhp6
Synonyms:ubc2
ORF Names:SPAC18B11.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC18B11.07c.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. HULC complex Source: PomBase
  3. nuclear chromatin Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 881C → A: No derepression of transcription. 1 Publication
Mutagenesisi88 – 881C → S: No derepression of transcription. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Ubiquitin-conjugating enzyme E2 2PRO_0000082536Add
BLAST

Proteomic databases

MaxQBiP23566.
PaxDbiP23566.

Interactioni

Subunit structurei

Component of the histone H2B ubiquitin ligase complex (HULC) composed of at least brl1, brl2, rhp6 and shf1.1 Publication

Protein-protein interaction databases

BioGridi279076. 10 interactions.
IntActiP23566. 4 interactions.
MINTiMINT-4687768.
STRINGi4896.SPAC18B11.07c-1.

Structurei

3D structure databases

ProteinModelPortaliP23566.
SMRiP23566. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiP23566.
KOiK10573.
OMAiPVPDNVM.
OrthoDBiEOG7SBP18.
PhylomeDBiP23566.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23566-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTTARRRLM RDFKRMQQDP PAGVSASPVS DNVMLWNAVI IGPADTPFED
60 70 80 90 100
GTFKLVLSFD EQYPNKPPLV KFVSTMFHPN VYANGELCLD ILQNRWSPTY
110 120 130 140 150
DVAAILTSIQ SLLNDPNNAS PANAEAAQLH RENKKEYVRR VRKTVEDSWE

S
Length:151
Mass (Da):17,097
Last modified:November 1, 1995 - v3
Checksum:iE4A88A40ECF35709
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111S → R in CAA37340. (PubMed:2184030)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53252 Genomic DNA. Translation: CAA37340.1.
CU329670 Genomic DNA. Translation: CAA90592.1.
PIRiS12529.
T45220.
RefSeqiNP_592876.1. NM_001018276.2.

Genome annotation databases

EnsemblFungiiSPAC18B11.07c.1; SPAC18B11.07c.1:pep; SPAC18B11.07c.
GeneIDi2542622.
KEGGispo:SPAC18B11.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53252 Genomic DNA. Translation: CAA37340.1 .
CU329670 Genomic DNA. Translation: CAA90592.1 .
PIRi S12529.
T45220.
RefSeqi NP_592876.1. NM_001018276.2.

3D structure databases

ProteinModelPortali P23566.
SMRi P23566. Positions 2-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 279076. 10 interactions.
IntActi P23566. 4 interactions.
MINTi MINT-4687768.
STRINGi 4896.SPAC18B11.07c-1.

Proteomic databases

MaxQBi P23566.
PaxDbi P23566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC18B11.07c.1 ; SPAC18B11.07c.1:pep ; SPAC18B11.07c .
GeneIDi 2542622.
KEGGi spo:SPAC18B11.07c.

Organism-specific databases

PomBasei SPAC18B11.07c.

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233454.
InParanoidi P23566.
KOi K10573.
OMAi PVPDNVM.
OrthoDBi EOG7SBP18.
PhylomeDBi P23566.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi 20803671.
PROi P23566.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: IDENTIFICATION IN THE HULC COMPLEX, FUNCTION OF THE HULC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiUBC2_SCHPO
AccessioniPrimary (citable) accession number: P23566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3