GenomeNet

Database: UniProt
Entry: Q9JIM3
LinkDB: Q9JIM3
Original site: Q9JIM3 
ID   ER6L2_MOUSE             Reviewed;        1537 AA.
AC   Q9JIM3; E9Q4J6; Q6DI94; Q8BIV4; Q8BM40; Q8K267; Q8R2Z6; Q9DA70;
AC   Q9DD01;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 3.
DT   16-OCT-2019, entry version 130.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   repair 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
RT   project: 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in early DNA damage response.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NEK6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Colocalizes with
CC       NEK6 in the centrosome. In response to DNA damage, translocates
CC       from the cytosol to mitochondria and nucleus in a reactive oxygen
CC       species (ROS)-dependent manner. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9JIM3-1; Sequence=Displayed;
CC         Note=Gene prediction based on partial EST data.;
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.
CC       {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};
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; 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   STRING; 10090.ENSMUSP00000093392; -.
DR   iPTMnet; Q9JIM3; -.
DR   PhosphoSitePlus; Q9JIM3; -.
DR   EPD; Q9JIM3; -.
DR   PaxDb; Q9JIM3; -.
DR   PRIDE; Q9JIM3; -.
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   eggNOG; KOG0387; Eukaryota.
DR   eggNOG; ENOG410XP4Z; LUCA.
DR   GeneTree; ENSGT00940000161328; -.
DR   HOGENOM; HOG000074171; -.
DR   InParanoid; Q9JIM3; -.
DR   KO; K20098; -.
DR   OMA; QTRYFEG; -.
DR   OrthoDB; 372069at2759; -.
DR   ChiTaRS; Ercc6l2; mouse.
DR   PRO; PR:Q9JIM3; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000021470; Expressed in 261 organ(s), highest expression level in metanephric cortical collecting duct.
DR   ExpressionAtlas; Q9JIM3; baseline and differential.
DR   Genevisible; Q9JIM3; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase 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   Gene3D; 3.40.50.10810; -; 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   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 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; Complete proteome; Cytoplasm;
KW   Cytoskeleton; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1   1537       DNA excision repair protein ERCC-6-like
FT                                2.
FT                                /FTId=PRO_0000326087.
FT   DOMAIN      134    319       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      510    660       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     147    154       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       270    273       DEAH box.
FT   MOD_RES     968    968       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     971    971       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ       1    116       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_054670.
FT   VAR_SEQ     117    156       TINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQ
FT                                -> MPGSRPTCRALLAAESGGAAGCLPLARWTSPPRSPAQT
FT                                PAK (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_054671.
FT   VAR_SEQ     261    273       SLEWSAIIVDEAH -> RQTFCSSHHEHAS (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_054672.
FT   VAR_SEQ     274   1537       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_054673.
FT   VAR_SEQ     583   1537       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_054674.
FT   VAR_SEQ     699    699       R -> V (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_054675.
FT   VAR_SEQ     700   1537       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_054676.
FT   CONFLICT     18     18       C -> M (in Ref. 1; BAC38652).
FT                                {ECO:0000305}.
FT   CONFLICT     26     26       P -> Q (in Ref. 1; BAC28927).
FT                                {ECO:0000305}.
FT   CONFLICT     86     86       K -> E (in Ref. 3; AAF73858).
FT                                {ECO:0000305}.
FT   CONFLICT    301    301       V -> I (in Ref. 3; AAF73858).
FT                                {ECO:0000305}.
FT   CONFLICT    453    453       V -> I (in Ref. 3; AAF73858 and 4;
FT                                AAH32964). {ECO:0000305}.
FT   CONFLICT    581    581       T -> P (in Ref. 1; BAC28927).
FT                                {ECO:0000305}.
FT   CONFLICT   1294   1294       E -> R (in Ref. 1; BAB24414).
FT                                {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
//
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