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Protein

E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1

Gene

rfp1

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

Functioni

Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Involved in maintaining genome stability where it acts in the cellular response to DNA damage. Has a role in meiosis.4 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri189 – 23850RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA repair Source: PomBase
  • meiotic cell cycle Source: UniProtKB-KW
  • negative regulation of protein sumoylation Source: PomBase
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of ubiquitin-protein transferase activity Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Meiosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1 (EC:6.3.2.-)
Alternative name(s):
Meiotically up-regulated gene 140 protein
RING finger protein 1
Gene namesi
Name:rfp1
Synonyms:mug140
ORF Names:SPAC19A8.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC19A8.10.
PomBaseiSPAC19A8.10. rfp1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
  • site of double-strand break Source: PomBase
  • SUMO-targeted ubiquitin ligase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1PRO_0000056333Add
BLAST

Interactioni

Subunit structurei

Part of an E3 ubiquitin complex including rfp1, rfp2 and slx8. Interacts with slx8, chk1, nse5, pmt3 and rad60.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
chk1P342083EBI-3647269,EBI-768535
pmt3O133515EBI-3647269,EBI-966336
slx8P871764EBI-3647269,EBI-7588105

Protein-protein interaction databases

BioGridi278999. 16 interactions.
IntActiO13826. 10 interactions.
MINTiMINT-4668274.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 574Poly-Arg

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri189 – 23850RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiO13826.
OrthoDBiEOG7DVDN1.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF14634. zf-RING_5. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFNGSNGID ESSVIDLTRS PSPPVETSIS STNIIDLDAI PDDSFPSSPV
60 70 80 90 100
LSPRRRRMNR RRNERSRNFP SNHLSYLEDM IYLGPQVSTR RSSSRRDLMG
110 120 130 140 150
MIARTFPEFS SVNSLSPSLF QLIVNRMRFD AIHPEWTNGS DDEYFSNHFE
160 170 180 190 200
ESYDDFTSSL ENIKQSYKPP GPPKSGFTRS FNNDTLMVCP RCQEPLGTSK
210 220 230 240 250
SKEKSALWAT KCGHVYCGSC AKVLKTSKRS QSKCLVNDCG RYLNTKNAMW

ELFY
Length:254
Mass (Da):28,903
Last modified:January 1, 1998 - v1
Checksum:iE47B9E2B35E573DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11646.1.
PIRiT37951.
RefSeqiNP_593782.1. NM_001019211.2.

Genome annotation databases

EnsemblFungiiSPAC19A8.10.1; SPAC19A8.10.1:pep; SPAC19A8.10.
GeneIDi2542542.
KEGGispo:SPAC19A8.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11646.1.
PIRiT37951.
RefSeqiNP_593782.1. NM_001019211.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278999. 16 interactions.
IntActiO13826. 10 interactions.
MINTiMINT-4668274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC19A8.10.1; SPAC19A8.10.1:pep; SPAC19A8.10.
GeneIDi2542542.
KEGGispo:SPAC19A8.10.

Organism-specific databases

EuPathDBiFungiDB:SPAC19A8.10.
PomBaseiSPAC19A8.10. rfp1.

Phylogenomic databases

InParanoidiO13826.
OrthoDBiEOG7DVDN1.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiO13826.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF14634. zf-RING_5. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events."
    Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L., Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P., Smith G.R., Moreno S.
    Curr. Biol. 15:2056-2062(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEIOSIS.
  3. "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].
  4. Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, IDENTIFICATION IN A E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH RFP2 AND SLX8, INTERACTION WITH SLX8; NSE5 AND RAD60, SUBCELLULAR LOCATION.
  5. "Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins."
    Sun H., Leverson J.D., Hunter T.
    EMBO J. 26:4102-4112(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH PMT3, SUBCELLULAR LOCATION.
  6. "Fission yeast Rnf4 homologs are required for DNA repair."
    Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.
    J. Biol. Chem. 282:20388-20394(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH CHK1.

Entry informationi

Entry nameiRFP1_SCHPO
AccessioniPrimary (citable) accession number: O13826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 105 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.