ERCC8_MOUSE
ID ERCC8_MOUSE Reviewed; 397 AA.
AC Q8CFD5; Q3U066; Q8VDC4; Q9CWK7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA excision repair protein ERCC-8;
DE AltName: Full=Cockayne syndrome WD repeat protein CSA homolog;
GN Name=Ercc8; Synonyms=Ckn1, Csa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=12509261; DOI=10.1016/s1568-7864(01)00010-6;
RA van der Horst G.T.J., Meira L., Gorgels T.G.M.F., de Wit J.,
RA Velasco-Miguel S., Richardson J.A., Kamp Y., Vreeswijk M.P.G., Smit B.,
RA Bootsma D., Hoeijmakers J.H.J., Friedberg E.C.;
RT "UVB irradiation-induced cancer predisposition in Cockayne syndrome group A
RT (Csa) mutant mice.";
RL DNA Repair 1:143-157(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Substrate-recognition component of the CSA complex, a DCX
CC (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in
CC transcription-coupled nucleotide excision repair (By similarity). The
CC CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and
CC subsequent proteasomal degradation of ERCC6 in a UV-dependent manner;
CC ERCC6 degradation is essential for the recovery of RNA synthesis after
CC transcription-coupled repair (By similarity). It is required for the
CC recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled
CC repair complex which removes RNA polymerase II-blocking lesions from
CC the transcribed strand of active genes (By similarity). Plays a role in
CC DNA single-strand and double-strand breaks (DSSBs) repair; involved in
CC repair of DSSBs by non-homologous end joining (NHEJ) (By similarity).
CC {ECO:0000250|UniProtKB:Q13216}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the CSA complex (DCX(ERCC8) complex), a DCX E3
CC ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and
CC CUL4A; the CSA complex interacts with RNA polymerase II; upon UV
CC irradiation it interacts with the COP9 signalosome and preferentially
CC with the hyperphosphorylated form of RNA polymerase II. Interacts with
CC ERCC6 and KIAA1530/UVSSA. Interacts with a subunit of RNA polymerase II
CC TFIIH. Interacts with DDB1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CFD5; Q3U4B1: Ssbp4; NbExp=2; IntAct=EBI-26682118, EBI-26666280;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13216}. Nucleus
CC matrix {ECO:0000250|UniProtKB:Q13216}. Note=UV-induced translocation to
CC the nuclear matrix is dependent on ERCC6.
CC {ECO:0000250|UniProtKB:Q13216}.
CC -!- MISCELLANEOUS: Ercc8 deficient mice develop normally, but show a loss
CC of retinal photoreceptors after 4 months of age, and enhanced UV-
CC sensitivity.
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DR EMBL; AJ427222; CAD20255.1; -; mRNA.
DR EMBL; AK010576; BAB27039.1; -; mRNA.
DR EMBL; AK157175; BAE33989.1; -; mRNA.
DR EMBL; BC037200; AAH37200.1; -; mRNA.
DR CCDS; CCDS26761.1; -.
DR RefSeq; NP_082318.2; NM_028042.3.
DR AlphaFoldDB; Q8CFD5; -.
DR SMR; Q8CFD5; -.
DR BioGRID; 215079; 10.
DR IntAct; Q8CFD5; 12.
DR STRING; 10090.ENSMUSP00000059211; -.
DR PhosphoSitePlus; Q8CFD5; -.
DR MaxQB; Q8CFD5; -.
DR PaxDb; Q8CFD5; -.
DR PRIDE; Q8CFD5; -.
DR ProteomicsDB; 275939; -.
DR Antibodypedia; 11400; 348 antibodies from 26 providers.
DR Ensembl; ENSMUST00000054835; ENSMUSP00000059211; ENSMUSG00000021694.
DR GeneID; 71991; -.
DR KEGG; mmu:71991; -.
DR UCSC; uc007rux.1; mouse.
DR CTD; 1161; -.
DR MGI; MGI:1919241; Ercc8.
DR VEuPathDB; HostDB:ENSMUSG00000021694; -.
DR eggNOG; KOG4283; Eukaryota.
DR GeneTree; ENSGT00390000009065; -.
DR HOGENOM; CLU_032951_2_2_1; -.
DR InParanoid; Q8CFD5; -.
DR OMA; MTAVKAF; -.
DR OrthoDB; 800636at2759; -.
DR PhylomeDB; Q8CFD5; -.
DR TreeFam; TF101237; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71991; 1 hit in 107 CRISPR screens.
DR PRO; PR:Q8CFD5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CFD5; protein.
DR Bgee; ENSMUSG00000021694; Expressed in spermatocyte and 196 other tissues.
DR ExpressionAtlas; Q8CFD5; baseline and differential.
DR Genevisible; Q8CFD5; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0009411; P:response to UV; IMP:MGI.
DR GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR042238; Rad28/ERCC8/Ckn1/ATCSA-1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR46202; PTHR46202; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..397
FT /note="DNA excision repair protein ERCC-8"
FT /id="PRO_0000050971"
FT REPEAT 41..81
FT /note="WD 1"
FT REPEAT 97..137
FT /note="WD 2"
FT REPEAT 184..224
FT /note="WD 3"
FT REPEAT 243..282
FT /note="WD 4"
FT REPEAT 332..371
FT /note="WD 5"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13216"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13216"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13216"
FT CONFLICT 90
FT /note="V -> I (in Ref. 3; AAH37200)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="R -> M (in Ref. 2; BAB27039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 43689 MW; 1B35EA61A00A611B CRC64;
MLSFLSARQS GLEDPLRLRR AQSTRRVLGL ELNKDRDVER IHGSGVNTLD IEPVEGRYML
SGGSDGVVVL YDLENASRQP HYTCKAVCSV GRSHPDVHKY SVETVQWYPH DTGMFTSSSF
DKTLKVWDTN TLQAADVFNF EETVYSHHMS PAATKHCLVA VGTRGPKVQL CDLKSGSCSH
ILQGHRQEIL AVSWSPRHDY ILATASADSR VKLWDVRRAS GCLLTLDQHN GKKSQAAESA
NTAHNGKVNG LCFTSDGLHL LTIGTDNRMR LWNSSSGDNT LVNYGKVCND SRKGLQFAVS
CGCSSEFVFV PHGSTIAVYA VHSGERLAML KGHYKSVDCC VFQPNFQELY SGSRDCNILA
WVPPSYEPVP DDDDEAPAKS QLNPAFADAW SSSDEDG
