SLX8_SCHPO
ID SLX8_SCHPO Reviewed; 269 AA.
AC P87176; Q9US65;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein slx8;
DE AltName: Full=RING-dependent E3 ubiquitin-protein ligase slx8;
DE AltName: Full=RING-type E3 ubiquitin transferase slx8 {ECO:0000305};
DE AltName: Full=Synthetic lethal of unknown function protein 8;
GN Name=slx8; ORFNames=SPBC3D6.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-165, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, IDENTIFICATION IN A E3
RP UBIQUITIN-PROTEIN LIGASE COMPLEX WITH RFP1 AND RFP2, INTERACTION WITH RFP1
RP AND RFP2, AND SUBCELLULAR LOCATION.
RX PubMed=17762865; DOI=10.1038/sj.emboj.7601838;
RA Prudden J., Pebernard S., Raffa G., Slavin D.A., Perry J.J.P., Tainer J.A.,
RA McGowan C.H., Boddy M.N.;
RT "SUMO-targeted ubiquitin ligases in genome stability.";
RL EMBO J. 26:4089-4101(2007).
RN [4]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS.
RX PubMed=17762864; DOI=10.1038/sj.emboj.7601839;
RA Sun H., Leverson J.D., Hunter T.;
RT "Conserved function of RNF4 family proteins in eukaryotes: targeting a
RT ubiquitin ligase to SUMOylated proteins.";
RL EMBO J. 26:4102-4112(2007).
CC -!- FUNCTION: Mediates ubiquitination and subsequent
CC desumoylation/degradation of sumoylated proteins and proteins
CC containing SUMO-like domains. Acts as a critical suppressor of gross
CC chromosomal rearrangements (GCRs) during normal cell cycle progression.
CC Involved in stabilizing, restarting or resolving transiently stalled
CC replication forks. Prevents accumulation of DNA damage during cell
CC cycle progression (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:17762864, ECO:0000269|PubMed:17762865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of an E3 ubiquitin complex including rfp1, rfp2 and slx8.
CC Interacts with rfp1 and rfp2. {ECO:0000269|PubMed:17762865}.
CC -!- INTERACTION:
CC P87176; O13826: rfp1; NbExp=5; IntAct=EBI-7588105, EBI-3647269;
CC P87176; Q9UT72: rfp2; NbExp=3; IntAct=EBI-7588105, EBI-7587772;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:17762865}.
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DR EMBL; CU329671; CAB09120.1; -; Genomic_DNA.
DR EMBL; AB028016; BAA87320.1; -; Genomic_DNA.
DR PIR; T40371; T40371.
DR RefSeq; NP_595523.1; NM_001021432.2.
DR AlphaFoldDB; P87176; -.
DR SMR; P87176; -.
DR BioGRID; 277144; 37.
DR IntAct; P87176; 3.
DR MINT; P87176; -.
DR STRING; 4896.SPBC3D6.11c.1; -.
DR MaxQB; P87176; -.
DR PaxDb; P87176; -.
DR EnsemblFungi; SPBC3D6.11c.1; SPBC3D6.11c.1:pep; SPBC3D6.11c.
DR GeneID; 2540618; -.
DR KEGG; spo:SPBC3D6.11c; -.
DR PomBase; SPBC3D6.11c; slx8.
DR VEuPathDB; FungiDB:SPBC3D6.11c; -.
DR eggNOG; KOG0317; Eukaryota.
DR HOGENOM; CLU_1094820_0_0_1; -.
DR InParanoid; P87176; -.
DR OMA; INFQNDA; -.
DR PhylomeDB; P87176; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P87176; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0033768; C:SUMO-targeted ubiquitin ligase complex; IPI:PomBase.
DR GO; GO:0140082; F:SUMO-ubiquitin ligase activity; IDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006310; P:DNA recombination; IGI:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..269
FT /note="E3 ubiquitin-protein ligase complex slx8-rfp subunit
FT slx8"
FT /id="PRO_0000056331"
FT ZN_FING 206..247
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 29656 MW; 310A0F1DB88EEECB CRC64;
MPPAHKRDTN VRNLSAPYNI PSQSARVAAG NAAINRRRSS PVENSPGNGF PVSEDATDYP
SGTTSENESL PLNRAPRSLR EVASELAQEE TLPVETSDLN IDVESEVFDL EDINFQNDAD
DINQRFTYNN HPASVENSLT NVNSIHAQPT TISDMIDLTD ETSYDPRKQK FEQGKNPSTT
NAEIEKEEPS KKQVVPSSQR LADYKCVICL DSPENLSCTP CGHIFCNFCI LSALGTTAAT
QKCPVCRRKV HPNKVICLEM MLGSQKKKS
