ER6L2_MOUSE
ID ER6L2_MOUSE Reviewed; 1537 AA.
AC Q9JIM3; E9Q4J6; Q6DI94; Q8BIV4; Q8BM40; Q8K267; Q8R2Z6; Q9DA70; Q9DD01;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DNA excision repair protein ERCC-6-like 2;
DE EC=3.6.4.-;
DE AltName: Full=DNA repair and recombination protein RAD26-like;
GN Name=Ercc6l2; Synonyms=Rad26l;
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 [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1155-1561 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-699 (ISOFORM 2).
RA Ramirez M.H., Shannon M.E., Thelen M.P.;
RT "Characterization of the mammalian Rad26L gene encoding a putative repair
RT and recombination helicase.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 280-699 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 946-1537 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, Mammary gland, and 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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968 AND SER-971, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in early DNA damage response. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NEK6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome. In
CC response to DNA damage, translocates from the cytosol to mitochondria
CC and nucleus in a reactive oxygen species (ROS)-dependent manner.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9JIM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIM3-2; Sequence=VSP_054675, VSP_054676;
CC Name=3;
CC IsoId=Q9JIM3-3; Sequence=VSP_054670, VSP_054671, VSP_054674;
CC Name=4;
CC IsoId=Q9JIM3-4; Sequence=VSP_054672, VSP_054673;
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26917.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH32964.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH75679.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24414.1; Type=Miscellaneous discrepancy; Note=The first 10 codons may be found on an alternative exon not observed on any other cDNA/EST.; Evidence={ECO:0000305};
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DR EMBL; AK002307; BAB22002.1; -; mRNA.
DR EMBL; AK006112; BAB24414.1; ALT_SEQ; mRNA.
DR EMBL; AK035054; BAC28927.1; -; mRNA.
DR EMBL; AK082850; BAC38652.1; -; mRNA.
DR EMBL; AC154248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF217319; AAF73858.1; -; mRNA.
DR EMBL; BC026917; AAH26917.1; ALT_INIT; mRNA.
DR EMBL; BC032964; AAH32964.1; ALT_FRAME; mRNA.
DR EMBL; BC075679; AAH75679.1; ALT_INIT; mRNA.
DR CCDS; CCDS26593.2; -. [Q9JIM3-1]
DR CCDS; CCDS36701.1; -. [Q9JIM3-2]
DR RefSeq; NP_001013626.2; NM_001013608.2. [Q9JIM3-1]
DR RefSeq; NP_075996.2; NM_023507.3. [Q9JIM3-2]
DR AlphaFoldDB; Q9JIM3; -.
DR SMR; Q9JIM3; -.
DR STRING; 10090.ENSMUSP00000093392; -.
DR iPTMnet; Q9JIM3; -.
DR PhosphoSitePlus; Q9JIM3; -.
DR EPD; Q9JIM3; -.
DR PaxDb; Q9JIM3; -.
DR PRIDE; Q9JIM3; -.
DR ProteomicsDB; 275640; -. [Q9JIM3-1]
DR ProteomicsDB; 275641; -. [Q9JIM3-2]
DR ProteomicsDB; 275642; -. [Q9JIM3-3]
DR DNASU; 76251; -.
DR Ensembl; ENSMUST00000067821; ENSMUSP00000069488; ENSMUSG00000021470. [Q9JIM3-2]
DR Ensembl; ENSMUST00000144763; ENSMUSP00000152142; ENSMUSG00000021470. [Q9JIM3-4]
DR Ensembl; ENSMUST00000238465; ENSMUSP00000158755; ENSMUSG00000021470. [Q9JIM3-1]
DR GeneID; 76251; -.
DR KEGG; mmu:76251; -.
DR UCSC; uc007qyb.2; mouse. [Q9JIM3-3]
DR UCSC; uc007qyc.2; mouse. [Q9JIM3-2]
DR UCSC; uc007qye.2; mouse. [Q9JIM3-1]
DR CTD; 375748; -.
DR MGI; MGI:1923501; Ercc6l2.
DR VEuPathDB; HostDB:ENSMUSG00000021470; -.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000161328; -.
DR HOGENOM; CLU_585201_0_0_1; -.
DR InParanoid; Q9JIM3; -.
DR OMA; VYTHRNE; -.
DR OrthoDB; 372069at2759; -.
DR BioGRID-ORCS; 76251; 8 hits in 104 CRISPR screens.
DR ChiTaRS; Ercc6l2; mouse.
DR PRO; PR:Q9JIM3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JIM3; protein.
DR Bgee; ENSMUSG00000021470; Expressed in metanephric cortical collecting duct and 243 other tissues.
DR ExpressionAtlas; Q9JIM3; baseline and differential.
DR Genevisible; Q9JIM3; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029256; Heliccase-ass-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF14773; VIGSSK; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1537
FT /note="DNA excision repair protein ERCC-6-like 2"
FT /id="PRO_0000326087"
FT DOMAIN 134..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 510..660
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 715..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 270..273
FT /note="DEAH box"
FT COMPBIAS 749..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_054670"
FT VAR_SEQ 117..156
FT /note="TINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQ -> MPGSRPTC
FT RALLAAESGGAAGCLPLARWTSPPRSPAQTPAK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_054671"
FT VAR_SEQ 261..273
FT /note="SLEWSAIIVDEAH -> RQTFCSSHHEHAS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_054672"
FT VAR_SEQ 274..1537
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_054673"
FT VAR_SEQ 583..1537
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_054674"
FT VAR_SEQ 699
FT /note="R -> V (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054675"
FT VAR_SEQ 700..1537
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054676"
FT CONFLICT 18
FT /note="C -> M (in Ref. 1; BAC38652)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="P -> Q (in Ref. 1; BAC28927)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="K -> E (in Ref. 3; AAF73858)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="V -> I (in Ref. 3; AAF73858)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="V -> I (in Ref. 3; AAF73858 and 4; AAH32964)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="T -> P (in Ref. 1; BAC28927)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294
FT /note="E -> R (in Ref. 1; BAB24414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1537 AA; 173873 MW; 6980D5307FB2FF22 CRC64;
MDISAPQSRA DSRKDRWCPG ERCLAPSLDN KKLCEASIKS ITVDGNGKPF AVVLYPDFQE
KTIPLQRLQE VKSTKDYSRS LIFDDKDLEK PYFPDRKIPS LASAFQLSED GDSIPYTINR
YLRDYQREGA QFLYRHYIEG RGCILGDDMG LGKTIQVISF LAAVLHKKGT REDIENNMPE
FLLKSMKKKP PSTAKKMFLI VAPLSVLYNW KDELDTWGYF RVTVLHGSKK DNELLRLKQR
KCEIALTTYE TLRLCLEELN SLEWSAIIVD EAHRIKNPKA RVTEVMKAVK CKVRIGLTGT
VLQNNMKELW CVMDWAVPGL LGSRIHFKKQ FSDPVEHGQR HTATKRELAT GRKAMHRLAK
KMSGWFLRRT KTLIKGQLPK KEDRMVYCSL TDFQKAVYQT VLETEDVALI LTSSQPCTCG
SGQKRRKCCY KTNSRGDTVR TLCLSYLTVL QKVANHVALL QAASTSKHQE TVIKRICDRV
FSRFPDFVQK SKDAAFETLS DPKYSGKMKV LQQLLNHFRK QRDKVLLFSF STKLLDVLQQ
YCMASGLDYR RLDGSTKSEE RLKIVKEFNS SQDVNICLVS TMAGGLGLNF VGANVVILFD
PTWNPANDLQ AVDRAYRIGQ CRDVKVLRLI SLGTVEEIMY LRQVYKQQLH CVVVGSENAK
RYFEAVQGSK EHRGELFGVH NLFKLRSQGS CLTRDILERE GQVEAGIMTA TTWLKGEPSA
QELETPRDPD CQEPTDVCEL YSDISDEESV GHSLGKTDKH KFSDTSRTPG FPAQLTLLQC
GFSKLFEAKY KSDQDGDGNP VPSDGSSDEQ PMCLSAEARQ AARQKTWDSV CTSEHQKSDN
IQTPDEKCVS DKSEKTLEQN VSSESDDETK DHRTAGHHCM GQGDTESEDS DVIFPTQYPT
QRIPKNHIRF KLLLGESEDS EAENPVKVNH GDDRQNSGRG NGPVPNLLCL ENMTSKSVRK
RKGTDDISDE SDDIDMFPKS RIRKQRATTS LKFKRKKENK RKLDNSPVTA KEANQVCAAD
GDRSSQVIED FSSSDDNLSL SHLSFTKLSH RAETVKDKIS LSPKLPGPDK KNNTFISRKP
PSFLNEGVIS QEQICNSMDK ILDGVQEVAY IHSNQNVIGS SRAENHMSRW ATRDVFELKQ
FSQLPANVAV CSSKTYKTQV KANIVSPTEK DQPPSDGGIS SPLYVSHPVV QKKKDVYRTN
HTTFIIGETP RGIRRKQFEE MASYYKLPVK EFAEQVTRAT SEERQKMLRD FYSLQHPEVK
EFFVNSASEL IKSVHKKEER VRNKSKEKES LLKENPSNDS TLSCYDSTNK MSQVYNRKIC
EGKSVRSQNH VFHREDTFSS DAEINKSPVS FTEELHSERK DHTPKDTTTV FCPNSNSEAL
EAELGNSPGR QWDLTGACGS RNRPLFKLRN KRVENPGSEN TPEDGLLGDT SILNDLFKSH
GEGPTQLPKN VLSGPVAKAK QKPKDFWDIL NEQNDDSLSK LTDLAVIETL CTKAPSTSAS
KRKDELEASL WKANEKFLWK TLSSDVDDES ISNTERE
