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E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (Postreplication repair protein RAD18) (mRAD18Sc) (RING-type E3 ubiquitin transferase RAD18)

 RAD18_MOUSE             Reviewed;         509 AA.
Q9QXK2; Q9CZB8;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
28-FEB-2018, entry version 134.
RecName: Full=E3 ubiquitin-protein ligase RAD18;
EC=2.3.2.27;
AltName: Full=Postreplication repair protein RAD18;
Short=mRAD18Sc;
AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000305};
Name=Rad18; Synonyms=Rad18sc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
PubMed=11013078; DOI=10.1006/geno.2000.6220;
van der Laan R., Roest H.P., Hoogerbrugge J.W., Smit E.M.E.,
Slater R., Baarends W.M., Hoeijmakers J.H.J., Grootegoed J.A.;
"Characterization of mRAD18Sc, a mouse homolog of the yeast
postreplication repair gene RAD18.";
Genomics 69:86-94(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: E3 ubiquitin-protein ligase involved in postreplication
repair of UV-damaged DNA. Postreplication repair functions in gap-
filling of a daughter strand on replication of damaged DNA.
Associates to the E2 ubiquitin conjugating enzyme UBE2B to form
the UBE2B-RAD18 ubiquitin ligase complex involved in mono-
ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA
binding activity.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. Interacts with UBE2A and UBE2B, one homodimer
binding one molecule of UBE2B. Interacts with HLTF. Interacts with
SHPRH. Interacts with SPRTN; leading to enhance chromatin
association of RAD18 and RAD18-mediated PCNA ubiquitination and
translesion DNA synthesis. Interacts (via C-terminus and
phosphorylated form) with SLF1 (via BRCT domains); this
interaction is required for efficient repair of UV-induced DNA
damage. Interacts with SLF2. Interacts with SMC5; this interaction
is increased in a SLF1 or SLF2-dependent manner.
{ECO:0000250|UniProtKB:Q9NS91}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NS91}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q9NS91}. Note=Associates with chromatin.
Colocalizes with SLF1 in the nucleus and to centrosomes.
Relocalizes with SLF1 to nuclear foci in response to DNA damage.
Accumulates with the SLF1-SLF2 and SMC5-SMC6 complexes at
replication-coupled DNA interstrand repair and DNA double-strand
breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner.
{ECO:0000250|UniProtKB:Q9NS91}.
-!- TISSUE SPECIFICITY: Expressed in thymus, spleen, brain, and ovary.
-!- SIMILARITY: Belongs to the RAD18 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF205278; AAF19193.1; -; mRNA.
EMBL; AK012795; BAB28475.1; -; mRNA.
CCDS; CCDS39589.1; -.
RefSeq; NP_067360.2; NM_021385.2.
UniGene; Mm.103812; -.
ProteinModelPortal; Q9QXK2; -.
SMR; Q9QXK2; -.
BioGrid; 208379; 3.
IntAct; Q9QXK2; 2.
iPTMnet; Q9QXK2; -.
PhosphoSitePlus; Q9QXK2; -.
EPD; Q9QXK2; -.
MaxQB; Q9QXK2; -.
PRIDE; Q9QXK2; -.
Ensembl; ENSMUST00000077088; ENSMUSP00000076341; ENSMUSG00000030254.
GeneID; 58186; -.
KEGG; mmu:58186; -.
UCSC; uc009dec.2; mouse.
CTD; 56852; -.
MGI; MGI:1890476; Rad18.
GeneTree; ENSGT00390000011230; -.
HOGENOM; HOG000234845; -.
HOVERGEN; HBG054721; -.
InParanoid; Q9QXK2; -.
KO; K10627; -.
PhylomeDB; Q9QXK2; -.
Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
UniPathway; UPA00143; -.
ChiTaRS; Rad18; mouse.
PRO; PR:Q9QXK2; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030254; -.
CleanEx; MM_RAD18; -.
ExpressionAtlas; Q9QXK2; baseline and differential.
Genevisible; Q9QXK2; MM.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0097505; C:Rad6-Rad18 complex; IBA:GO_Central.
GO; GO:0005657; C:replication fork; ISO:MGI.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0001741; C:XY body; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISO:MGI.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0000403; F:Y-form DNA binding; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
GO; GO:0045910; P:negative regulation of DNA recombination; IMP:MGI.
GO; GO:0051984; P:positive regulation of chromosome segregation; ISS:UniProtKB.
GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
GO; GO:0009411; P:response to UV; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
Gene3D; 1.10.720.30; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
InterPro; IPR006642; Znf_Rad18_put.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF02037; SAP; 1.
SMART; SM00184; RING; 1.
SMART; SM00513; SAP; 1.
SMART; SM00734; ZnF_Rad18; 1.
PROSITE; PS50800; SAP; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage;
DNA repair; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 509 E3 ubiquitin-protein ligase RAD18.
/FTId=PRO_0000056150.
DOMAIN 248 282 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186}.
ZN_FING 25 64 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 201 224 UBZ-type.
MOTIF 232 240 LR motif.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9NS91}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS91}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS91}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS91}.
CONFLICT 9 9 W -> C (in Ref. 1; AAF19193).
{ECO:0000305}.
CONFLICT 268 268 Q -> P (in Ref. 1; AAF19193).
{ECO:0000305}.
SEQUENCE 509 AA; 57412 MW; BF7717D1A69738F9 CRC64;
MEVLAEPRWP PGLAVMKTID DLLRCGICFE YFNIAVIIPQ CSHNYCSLCI RKFLSYKTQC
PTCCVAVTEP DLRNNRLLDE LVKSMNFART HLLQFALESP PISPVSSTSK KVVVKVHNAD
AAQHPVKQAN RLMDKFLIRE TGDCVFELLG KENERKFSPQ KELSTSAEIK ETSLLGKPVL
GLSDANGPVT PSTSTMKLDT KVSCPVCGVS IPENHINKHL DSCLSREEKK ESLRSSAHKR
KPLPKTVYNL LSDRDLKKKL KQYGLSVQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI
VQEIESMEKT RMRLEASKLN ENVMVFTKNQ TEKEIEEVHS EYRKKHQNAF QLLVDQAKKG
YKKTGRVSQA AAMRTDEPAE TLPSMRTDEP AETLPSMRTD EPAETLPLMR ADEPAETLPS
ECIAQEDNVS FSDTVSVTNH FPQPQLDSPG PSEPERPDDS SSCTDILFSS DSDSCNRNDQ
NREVSPQQTR RTRASECVEI EPRNKRNKN


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