RAD18_SCHPO
ID RAD18_SCHPO Reviewed; 387 AA.
AC O74747;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Postreplication repair E3 ubiquitin-protein ligase rad18;
DE EC=2.3.2.27;
DE AltName: Full=RAD18 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase rad18 {ECO:0000305};
GN Name=rhp18; ORFNames=SPBC1734.06;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=11702950; DOI=10.1016/s1534-5807(01)00037-5;
RA Kitamura K., Katayama S., Dhut S., Sato M., Watanabe Y., Yamamoto M.,
RA Toda T.;
RT "Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual
RT differentiation via ubiquitin proteolysis and 14-3-3 protein in fission
RT yeast.";
RL Dev. Cell 1:389-399(2001).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11523791; DOI=10.1007/s004380100494;
RA Verkade H.M., Teli T., Laursen L.V., Murray J.M., O'Connell M.J.;
RT "A homologue of the Rad18 postreplication repair gene is required for DNA
RT damage responses throughout the fission yeast cell cycle.";
RL Mol. Genet. Genomics 265:993-1003(2001).
CC -!- FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis
CC group. Associates to the E2 ubiquitin conjugating enzyme ubc2/rad6 to
CC form the ubc2-rad18 ubiquitin ligase complex involved in
CC postreplicative repair (PRR) of damaged DNA (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11523791,
CC ECO:0000269|PubMed:11702950}.
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: Interacts with E2 ubc2, forming a complex with ubiquitin
CC ligase activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD18 family. {ECO:0000305}.
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DR EMBL; AB079544; BAB84669.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21300.1; -; Genomic_DNA.
DR PIR; T39653; T39653.
DR RefSeq; NP_595423.1; NM_001021331.2.
DR AlphaFoldDB; O74747; -.
DR SMR; O74747; -.
DR BioGRID; 276241; 57.
DR IntAct; O74747; 2.
DR MINT; O74747; -.
DR STRING; 4896.SPBC1734.06.1; -.
DR iPTMnet; O74747; -.
DR SwissPalm; O74747; -.
DR MaxQB; O74747; -.
DR PaxDb; O74747; -.
DR PRIDE; O74747; -.
DR EnsemblFungi; SPBC1734.06.1; SPBC1734.06.1:pep; SPBC1734.06.
DR GeneID; 2539686; -.
DR KEGG; spo:SPBC1734.06; -.
DR PomBase; SPBC1734.06; rhp18.
DR VEuPathDB; FungiDB:SPBC1734.06; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_2_0_1; -.
DR InParanoid; O74747; -.
DR OMA; ERTQGGH; -.
DR PhylomeDB; O74747; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR PRO; PR:O74747; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097505; C:Rad6-Rad18 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:PomBase.
DR GO; GO:0006301; P:postreplication repair; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR004580; Rad18_fungi.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14134; PTHR14134; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR TIGRFAMs; TIGR00599; rad18; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..387
FT /note="Postreplication repair E3 ubiquitin-protein ligase
FT rad18"
FT /id="PRO_0000056159"
FT DOMAIN 240..274
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT ZN_FING 29..67
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 156..183
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 119..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 387 AA; 43438 MW; 1E8140F8B645299B CRC64;
MNELDATDPS DWNQTKIPSL KGLDSSLRCL ICHEYFRAPL ITSCSHTFCS FCIRDYLREH
PMCPACRAPE QESRLRKNTI LEEILESFKV IRPTLFEFLK VENVPKPVLQ APETVIAQDS
ASGDEEWEDD LASNSSPASI AKKTSRDSKK RKREDLVHCP ACSNLVPHNQ INQHLDSCLN
SPSSPSSSSS PYKNKDNSKS NSLLSFKTDD DSITKRRLRS FNSADELPLK DRVRLPKLTY
ALLSESKIRS KLSEMGLPTD GHKQLLQRRH AKWVTLYNSN LDQKQPVSKR NLIRQLIDWE
RVQSKSIGVE KEKLGGGDWE KAYAEDFADL INRAKQSTTN KNDSLRNTAV ESSTEPSTSN
GFPATSVSPP LTIDLTNSQT GSDGPQS
