ERC6L_HUMAN
ID ERC6L_HUMAN Reviewed; 1250 AA.
AC Q2NKX8; Q8NCI1; Q96H93; Q9NXQ8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DNA excision repair protein ERCC-6-like;
DE EC=3.6.4.12 {ECO:0000269|PubMed:23973328, ECO:0000269|PubMed:28977671};
DE AltName: Full=ATP-dependent helicase ERCC6-like;
DE AltName: Full=PLK1-interacting checkpoint helicase;
DE AltName: Full=Tumor antigen BJ-HCC-15;
GN Name=ERCC6L;
GN Synonyms=PICH {ECO:0000303|PubMed:17218258, ECO:0000303|PubMed:28977671};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-1063, INTERACTION WITH PLK1, AND MUTAGENESIS OF 127-GLY--THR-129 AND
RP THR-1063.
RX PubMed=17218258; DOI=10.1016/j.cell.2006.11.041;
RA Baumann C., Koerner R., Hofmann K., Nigg E.A.;
RT "PICH, a centromere-associated SNF2 family ATPase, is regulated by Plk1 and
RT required for the spindle checkpoint.";
RL Cell 128:101-114(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1250.
RC TISSUE=Colon, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 603-1250.
RA Xueyuan D., Weifeng C.;
RT "Cloning and identification of genes which are differentially expressed in
RT carcinoma.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=17989990; DOI=10.1007/s00412-007-0131-7;
RA Wang L.-H., Schwarzbraun T., Speicher M.R., Nigg E.A.;
RT "Persistence of DNA threads in human anaphase cells suggests late
RT completion of sister chromatid decatenation.";
RL Chromosoma 117:123-135(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17599064; DOI=10.1038/sj.emboj.7601777;
RA Chan K.-L., North P.S., Hickson I.D.;
RT "BLM is required for faithful chromosome segregation and its localization
RT defines a class of ultrafine anaphase bridges.";
RL EMBO J. 26:3397-3409(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17956945; DOI=10.1242/jcs.013730;
RA Spence J.M., Phua H.-H., Mills W., Carpenter A.J., Porter A.C.G.,
RA Farr C.J.;
RT "Depletion of topoisomerase IIalpha leads to shortening of the metaphase
RT interkinetochore distance and abnormal persistence of PICH-coated anaphase
RT threads.";
RL J. Cell Sci. 120:3952-3964(2007).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PLK1.
RX PubMed=17671160; DOI=10.1091/mbc.e07-05-0517;
RA Santamaria A., Neef R., Eberspaecher U., Eis K., Husemann M., Mumberg D.,
RA Prechtl S., Schulze V., Siemeister G., Wortmann L., Barr F.A., Nigg E.A.;
RT "Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate functions
RT of Plk1 in early and late stages of mitosis.";
RL Mol. Biol. Cell 18:4024-4036(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-755; SER-774;
RP SER-1181 AND SER-1188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-810; THR-813; SER-820
RP AND SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028 AND SER-1098, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP LACK OF ROLE IN SPINDLE CHECKPOINT.
RX PubMed=19904549; DOI=10.1007/s00412-009-0244-2;
RA Hubner N.C., Wang L.H., Kaulich M., Descombes P., Poser I., Nigg E.A.;
RT "Re-examination of siRNA specificity questions role of PICH and Tao1 in the
RT spindle checkpoint and identifies Mad2 as a sensitive target for small
RT RNAs.";
RL Chromosoma 119:149-165(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-807; SER-810; SER-995
RP AND SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-1028 AND SER-1069,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-774; SER-807;
RP SER-820; SER-969; SER-971; SER-1028 AND SER-1069, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-128.
RX PubMed=23973328; DOI=10.1016/j.molcel.2013.07.016;
RA Biebricher A., Hirano S., Enzlin J.H., Wiechens N., Streicher W.W.,
RA Huttner D., Wang L.H., Nigg E.A., Owen-Hughes T., Liu Y., Peterman E.,
RA Wuite G.J.L., Hickson I.D.;
RT "PICH: a DNA translocase specially adapted for processing anaphase bridge
RT DNA.";
RL Mol. Cell 51:691-701(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 10-66 IN COMPLEX WITH BEND3,
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BEND3 AND PLK1, AND
RP MUTAGENESIS OF GLU-11; LEU-13 AND TYR-21.
RX PubMed=28977671; DOI=10.1093/nar/gkx792;
RA Pitchai G.P., Kaulich M., Bizard A.H., Mesa P., Yao Q., Sarlos K.,
RA Streicher W.W., Nigg E.A., Montoya G., Hickson I.D.;
RT "A novel TPR-BEN domain interaction mediates PICH-BEND3 association.";
RL Nucleic Acids Res. 45:11413-11424(2017).
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 (PubMed:17218258, PubMed:23973328). Functions
CC as ATP-dependent DNA translocase (PubMed:23973328, PubMed:28977671).
CC Can promote Holliday junction branch migration (in vitro)
CC (PubMed:23973328). {ECO:0000269|PubMed:17218258,
CC ECO:0000269|PubMed:23973328, ECO:0000269|PubMed:28977671}.
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:0000269|PubMed:23973328, ECO:0000269|PubMed:28977671};
CC -!- SUBUNIT: Interacts with PLK1, which phosphorylates it (PubMed:17218258,
CC PubMed:17671160, PubMed:28977671). Both proteins are mutually dependent
CC on each other for correct subcellular localization (PubMed:17218258,
CC PubMed:17671160). Interacts (via N-terminal TPR repeat) with BEND3 (via
CC BEN domains 1 and 3); the interaction is direct (PubMed:28977671).
CC {ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17671160,
CC ECO:0000269|PubMed:28977671}.
CC -!- INTERACTION:
CC Q2NKX8; P42858: HTT; NbExp=20; IntAct=EBI-1042535, EBI-466029;
CC Q2NKX8; P61968: LMO4; NbExp=3; IntAct=EBI-1042535, EBI-2798728;
CC Q2NKX8; P53350: PLK1; NbExp=4; IntAct=EBI-1042535, EBI-476768;
CC Q2NKX8; O76024: WFS1; NbExp=3; IntAct=EBI-1042535, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17989990}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:17218258}. Chromosome
CC {ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17671160,
CC ECO:0000269|PubMed:17989990}. 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:0000269|PubMed:17218258,
CC ECO:0000269|PubMed:17671160, ECO:0000269|PubMed:17956945,
CC ECO:0000269|PubMed:17989990}.
CC -!- PTM: Phosphorylation by PLK1 prevents the association with chromosome
CC arms and restricts its localization to the kinetochore-centromere
CC region. {ECO:0000269|PubMed:17218258}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to play a role in the spindle
CC checkpoint. However, it was later shown that phenotypes initially
CC observed are due to off-target effects of the siRNA used which results
CC in MAD2L1 down-regulation and mis-localization.
CC {ECO:0000305|PubMed:17218258, ECO:0000305|PubMed:19904549}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM82750.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90952.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU069463; ABU25227.1; -; mRNA.
DR EMBL; BC008808; AAH08808.2; -; mRNA.
DR EMBL; BC111486; AAI11487.1; -; mRNA.
DR EMBL; AK000112; BAA90952.1; ALT_SEQ; mRNA.
DR EMBL; AK074719; BAC11160.1; -; mRNA.
DR EMBL; AY121802; AAM82750.1; ALT_SEQ; mRNA.
DR CCDS; CCDS35329.1; -.
DR RefSeq; NP_060139.2; NM_017669.2.
DR PDB; 5JNO; X-ray; 2.20 A; B=10-66.
DR PDBsum; 5JNO; -.
DR AlphaFoldDB; Q2NKX8; -.
DR SMR; Q2NKX8; -.
DR BioGRID; 120176; 61.
DR ELM; Q2NKX8; -.
DR IntAct; Q2NKX8; 34.
DR MINT; Q2NKX8; -.
DR STRING; 9606.ENSP00000334675; -.
DR GlyGen; Q2NKX8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2NKX8; -.
DR PhosphoSitePlus; Q2NKX8; -.
DR BioMuta; ERCC6L; -.
DR DMDM; 121948339; -.
DR EPD; Q2NKX8; -.
DR jPOST; Q2NKX8; -.
DR MassIVE; Q2NKX8; -.
DR MaxQB; Q2NKX8; -.
DR PaxDb; Q2NKX8; -.
DR PeptideAtlas; Q2NKX8; -.
DR PRIDE; Q2NKX8; -.
DR ProteomicsDB; 61414; -.
DR Antibodypedia; 27876; 214 antibodies from 28 providers.
DR DNASU; 54821; -.
DR Ensembl; ENST00000334463.4; ENSP00000334675.3; ENSG00000186871.7.
DR GeneID; 54821; -.
DR KEGG; hsa:54821; -.
DR MANE-Select; ENST00000334463.4; ENSP00000334675.3; NM_017669.4; NP_060139.2.
DR UCSC; uc004eaq.2; human.
DR CTD; 54821; -.
DR DisGeNET; 54821; -.
DR GeneCards; ERCC6L; -.
DR HGNC; HGNC:20794; ERCC6L.
DR HPA; ENSG00000186871; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 300687; gene.
DR neXtProt; NX_Q2NKX8; -.
DR OpenTargets; ENSG00000186871; -.
DR PharmGKB; PA162385290; -.
DR VEuPathDB; HostDB:ENSG00000186871; -.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000156837; -.
DR HOGENOM; CLU_004666_0_0_1; -.
DR InParanoid; Q2NKX8; -.
DR OMA; FTIEDFQ; -.
DR OrthoDB; 372069at2759; -.
DR PhylomeDB; Q2NKX8; -.
DR TreeFam; TF332843; -.
DR PathwayCommons; Q2NKX8; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q2NKX8; -.
DR SIGNOR; Q2NKX8; -.
DR BioGRID-ORCS; 54821; 94 hits in 710 CRISPR screens.
DR GenomeRNAi; 54821; -.
DR Pharos; Q2NKX8; Tbio.
DR PRO; PR:Q2NKX8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q2NKX8; protein.
DR Bgee; ENSG00000186871; Expressed in secondary oocyte and 79 other tissues.
DR ExpressionAtlas; Q2NKX8; baseline and differential.
DR Genevisible; Q2NKX8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IDA: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.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; DNA-binding; Helicase; Hydrolase; Kinetochore; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1250
FT /note="DNA excision repair protein ERCC-6-like"
FT /id="PRO_0000328831"
FT REPEAT 21..54
FT /note="TPR 1"
FT DOMAIN 109..277
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 464..620
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1200..1233
FT /note="TPR 2"
FT REGION 735..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 228..231
FT /note="DEAH box"
FT COMPBIAS 1110..1150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 813
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHK9"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1063
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000269|PubMed:17218258"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHK9"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MUTAGEN 11
FT /note="E->A: Decreased affinity for BEND3, and abolishes
FT BEND3-mediated stimulation of ATPase activity; when
FT associated with A-13 and A-21."
FT /evidence="ECO:0000269|PubMed:28977671"
FT MUTAGEN 13
FT /note="L->A: Decreased affinity for BEND3, and abolishes
FT BEND3-mediated stimulation of ATPase activity; when
FT associated with A-11 and A-21."
FT /evidence="ECO:0000269|PubMed:28977671"
FT MUTAGEN 21
FT /note="Y->A: Decreased affinity for BEND3, and abolishes
FT BEND3-mediated stimulation of ATPase activity; when
FT associated with A-11 and A-13."
FT /evidence="ECO:0000269|PubMed:28977671"
FT MUTAGEN 127..129
FT /note="GKT->AAA: Abolishes chromatin association."
FT /evidence="ECO:0000269|PubMed:17218258"
FT MUTAGEN 128
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:23973328"
FT MUTAGEN 1063
FT /note="T->A: Induces a decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:17218258"
FT CONFLICT 145
FT /note="V -> M (in Ref. 3; BAC11160)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="R -> G (in Ref. 3; BAC11160)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="A -> T (in Ref. 3; BAA90952 and 4; AAM82750)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="I -> V (in Ref. 3; BAC11160)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="R -> K (in Ref. 3; BAA90952 and 4; AAM82750)"
FT /evidence="ECO:0000305"
FT HELIX 15..34
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5JNO"
SQ SEQUENCE 1250 AA; 141103 MW; C27DB2846F07C45D CRC64;
MEASRRFPEA EALSPEQAAH YLRYVKEAKE ATKNGDLEEA FKLFNLAKDI FPNEKVLSRI
QKIQEALEEL AEQGDDEFTD VCNSGLLLYR ELHNQLFEHQ KEGIAFLYSL YRDGRKGGIL
ADDMGLGKTV QIIAFLSGMF DASLVNHVLL IMPTNLINTW VKEFIKWTPG MRVKTFHGPS
KDERTRNLNR IQQRNGVIIT TYQMLINNWQ QLSSFRGQEF VWDYVILDEA HKIKTSSTKS
AICARAIPAS NRLLLTGTPI QNNLQELWSL FDFACQGSLL GTLKTFKMEY ENPITRAREK
DATPGEKALG FKISENLMAI IKPYFLRRTK EDVQKKKSSN PEARLNEKNP DVDAICEMPS
LSRKNDLIIW IRLVPLQEEI YRKFVSLDHI KELLMETRSP LAELGVLKKL CDHPRLLSAR
ACCLLNLGTF SAQDGNEGED SPDVDHIDQV TDDTLMEESG KMIFLMDLLK RLRDEGHQTL
VFSQSRQILN IIERLLKNRH FKTLRIDGTV THLLEREKRI NLFQQNKDYS VFLLTTQVGG
VGLTLTAATR VVIFDPSWNP ATDAQAVDRV YRIGQKENVV VYRLITCGTV EEKIYRRQVF
KDSLIRQTTG EKKNPFRYFS KQELRELFTI EDLQNSVTQL QLQSLHAAQR KSDIKLDEHI
AYLQSLGIAG ISDHDLMYTC DLSVKEELDV VEESHYIQQR VQKAQFLVEF ESQNKEFLME
QQRTRNEGAW LREPVFPSST KKKCPKLNKP QPQPSPLLST HHTQEEDISS KMASVVIDDL
PKEGEKQDLS SIKVNVTTLQ DGKGTGSADS IATLPKGFGS VEELCTNSSL GMEKSFATKN
EAVQKETLQE GPKQEALQED PLESFNYVLS KSTKADIGPN LDQLKDDEIL RHCNPWPIIS
ITNESQNAES NVSIIEIADD LSASHSALQD AQASEAKLEE EPSASSPQYA CDFNLFLEDS
ADNRQNFSSQ SLEHVEKENS LCGSAPNSRA GFVHSKTCLS WEFSEKDDEP EEVVVKAKIR
SKARRIVSDG EDEDDSFKDT SSINPFNTSL FQFSSVKQFD ASTPKNDISP PGRFFSSQIP
SSVNKSMNSR RSLASRRSLI NMVLDHVEDM EERLDDSSEA KGPEDYPEEG VEESSGEASK
YTEEDPSGET LSSENKSSWL MTSKPSALAQ ETSLGAPEPL SGEQLVGSPQ DKAAEATNDY
ETLVKRGKEL KECGKIQEAL NCLVKALDIK SADPEVMLLT LSLYKQLNNN
