ERC6L_MOUSE
ID ERC6L_MOUSE Reviewed; 1240 AA.
AC Q8BHK9; Q8BGN1; Q8BRC9; Q8CE49;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DNA excision repair protein ERCC-6-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q2NKX8};
DE AltName: Full=ATP-dependent helicase ERCC6-like;
GN Name=Ercc6l;
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=Heart;
RA Chen X.-G., Li Y., Zang M.-X., Pei X.-R., Xu Y.-J., Fang L.-F.;
RT "cDNA cloning and expression analysis of mouse gene encoding the protein
RT Ercc6l which is a novel member of SNF2 family.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 31:443-448(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Heart, and Skin;
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 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 [4]
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).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15917148; DOI=10.1016/j.toxlet.2005.02.013;
RA Xu Y.-J., Chen X.-G., Li Y.;
RT "Ercc6l, a gene of SNF2 family, may play a role in the teratogenic action
RT of alcohol.";
RL Toxicol. Lett. 157:233-239(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-998; SER-1001; SER-1021 AND
RP SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and 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: DNA helicase that acts as a tension sensor that associates
CC with catenated DNA which is stretched under tension until it is
CC resolved during anaphase. Functions as ATP-dependent DNA translocase.
CC Can promote Holliday junction branch migration (in vitro).
CC {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q2NKX8};
CC -!- SUBUNIT: Interacts with PLK1, which phosphorylates it. Both proteins
CC are mutually dependent on each other for correct subcellular
CC localization. Interacts (via N-terminal TPR repeat) with BEND3 (via BEN
CC domains 1 and 3); the interaction is direct.
CC {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome
CC {ECO:0000250|UniProtKB:Q2NKX8}. Note=Localizes to kinetochores, inner
CC centromeres and thin threads connecting separating chromosomes even
CC during anaphase. In prometaphase cells, it mostly concentrates in
CC between kinetochores. In metaphase, it localizes to numerous thin
CC threads that stretch between sister kinetochores of the aligned
CC chromosomes and are composed of catenated centromeric DNA. Evolution
CC from inner centromeres to thin threads takes place in response to
CC tension. Resolution of thin threads requires topoisomerase 2-alpha
CC (TOP2A) after anaphase onset. {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the neural tube and heart of
CC 10.5 dpc embryo. Significantly down-regulated after alcohol exposure in
CC embryonic brain and heart, but not in embryonic kidney, liver, or lung.
CC {ECO:0000269|PubMed:15917148}.
CC -!- PTM: Phosphorylation by PLK1 prevents the association with chromosome
CC arms and restricts its localization to the kinetochore-centromere
CC region. {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY172688; AAN87172.1; -; mRNA.
DR EMBL; AK029015; BAC26244.1; -; mRNA.
DR EMBL; AK045113; BAC32227.2; -; mRNA.
DR EMBL; AK084617; BAC39230.1; -; mRNA.
DR EMBL; AK084618; BAC39231.1; -; mRNA.
DR EMBL; AL807784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037660; AAH37660.1; -; mRNA.
DR CCDS; CCDS30321.1; -.
DR RefSeq; NP_666347.2; NM_146235.3.
DR AlphaFoldDB; Q8BHK9; -.
DR SMR; Q8BHK9; -.
DR BioGRID; 231820; 34.
DR IntAct; Q8BHK9; 33.
DR STRING; 10090.ENSMUSP00000050592; -.
DR iPTMnet; Q8BHK9; -.
DR PhosphoSitePlus; Q8BHK9; -.
DR EPD; Q8BHK9; -.
DR jPOST; Q8BHK9; -.
DR MaxQB; Q8BHK9; -.
DR PaxDb; Q8BHK9; -.
DR PeptideAtlas; Q8BHK9; -.
DR PRIDE; Q8BHK9; -.
DR ProteomicsDB; 275768; -.
DR Antibodypedia; 27876; 214 antibodies from 28 providers.
DR DNASU; 236930; -.
DR Ensembl; ENSMUST00000056904; ENSMUSP00000050592; ENSMUSG00000051220.
DR GeneID; 236930; -.
DR KEGG; mmu:236930; -.
DR UCSC; uc009tyk.2; mouse.
DR CTD; 54821; -.
DR MGI; MGI:2654144; Ercc6l.
DR VEuPathDB; HostDB:ENSMUSG00000051220; -.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000156837; -.
DR HOGENOM; CLU_004666_0_0_1; -.
DR InParanoid; Q8BHK9; -.
DR OMA; FTIEDFQ; -.
DR OrthoDB; 372069at2759; -.
DR PhylomeDB; Q8BHK9; -.
DR TreeFam; TF332843; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 236930; 22 hits in 112 CRISPR screens.
DR ChiTaRS; Ercc6l; mouse.
DR PRO; PR:Q8BHK9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BHK9; protein.
DR Bgee; ENSMUSG00000051220; Expressed in primary oocyte and 137 other tissues.
DR Genevisible; Q8BHK9; MM.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Helicase; Hydrolase; Kinetochore; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1240
FT /note="DNA excision repair protein ERCC-6-like"
FT /id="PRO_0000328832"
FT REPEAT 21..54
FT /note="TPR 1"
FT DOMAIN 110..278
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 467..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1191..1224
FT /note="TPR 2"
FT REGION 736..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 229..232
FT /note="DEAH box"
FT COMPBIAS 796..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1057
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT CONFLICT 1210
FT /note="A -> S (in Ref. 2; BAC26244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1240 AA; 138854 MW; 0B996A4286F51C27 CRC64;
MEASQGLAEV ETLSPQLAES YLRYVQEAKE AAKNGDLEES LKLFNLAKDI FPTKKVMSRI
QKLQEALEQL AEEEDDDEFI DVCSSGLLLY RELYEKLFEH QKEGIAFLYS LYKDGRKGGI
LADDMGLGKT VQIIAFLSGM FDASLVNHVL LIMPTNLINT WVNEFAKWTP GMRVKTFHGS
SKSERTRSLT RIQQRNGVVI TTYQMLLNNW QQLASFNGQA FVWDYVILDE AHKIKSASTK
SAVCARAIPA SNRLLLTGTP VQNNLQELWS LFDFACQGSL LGTLKTFKME YEHPIIRARE
KDATPGEKAL GLKISENLME IIKPYFLRRT KEEVQTKKAD NPEARLGEKN PAGEAICDMF
SLARKNDLIV WIRLLPLQEE IYRKFVSLDH IKELLMETRS PLAELGVLKK LCDHPRLLSA
RACRLLNLGT ATFSAQDENE QEDVSNMNSI DHLPDKTLIQ ESGKMIFLMS LLERLQDEGH
QTLVFSQSIK ILNIIERLLK NKHFKTLRID GTVTHLWERE KRIQLFQQNK EYSVFLLTTQ
VGGVGLTLTA ATRVVIFDPS WNPATDAQAV DRVYRIGQKE NVVVYRLITC GTVEEKIYRR
QVFKDSLIRQ TTGEKKNPFR YFTKQELKEL FTVGDLQKSA TQMQLQCLHA AQRRSDEKLD
EHIAYLHLLG IAGISDHDLM FTRDLSVKEE LDMLEDSQYI HQRVQKAQFL VESESQNTVQ
RQTTGIEETW LKAQEFPSQQ KKKGTEFNKP QPQPSRLLTK PTQVEAISSQ MASITICDQS
AESEPQEHSE VHDVTSLQGS HHFNSTSDAG TIASLPQGAE SIGEVSTDSL LSPAKGFAAE
NDAMQKKGLQ ASPGQEAPSE NLGSFHYLPR ESSKASLGPN LDLQDSVVLY HRSPTANENQ
NLESDVPMIE ISDDLSEPPS ALQGAQAIEA QLELKEDDPL KSPPQYACDF NLFLEDSADT
RQNLSSKFLE HVEKEKSLQS PAANSRAKSA LTLSLDSSPK SDEESEVISV KTKSKTRRIL
SDDEDEDEED AFKGSHTNSI NISPFPFSSV KQFDASTPQS GSNPSRRFFS PKTPGEVNTS
LHSRRSLASR RSLINVVLDD VEDMEERLDN SSEEESEPGL SEENNEEEAL ACTEEQPSGA
TLASGNKSSN LTMSEPTSPA PQSSPCAPEP SSSDPMPDPP QDLAVEAGND YESLVARGKE
LKECGKIQEA LNCLVKALDI KSADPEVMLM TLSLYKQLNI
