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DNA excision repair protein ERCC-6-like (EC 3.6.4.12) (ATP-dependent helicase ERCC6-like) (PLK1-interacting checkpoint helicase) (Tumor antigen BJ-HCC-15)

 ERC6L_HUMAN             Reviewed;        1250 AA.
Q2NKX8; Q8NCI1; Q96H93; Q9NXQ8;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 1.
05-DEC-2018, entry version 131.
RecName: Full=DNA excision repair protein ERCC-6-like;
EC=3.6.4.12 {ECO:0000269|PubMed:23973328, ECO:0000269|PubMed:28977671};
AltName: Full=ATP-dependent helicase ERCC6-like;
AltName: Full=PLK1-interacting checkpoint helicase;
AltName: Full=Tumor antigen BJ-HCC-15;
Name=ERCC6L;
Synonyms=PICH {ECO:0000303|PubMed:17218258,
ECO:0000303|PubMed:28977671};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT THR-1063, INTERACTION WITH PLK1, AND MUTAGENESIS OF
127-GLY--THR-129 AND THR-1063.
PubMed=17218258; DOI=10.1016/j.cell.2006.11.041;
Baumann C., Koerner R., Hofmann K., Nigg E.A.;
"PICH, a centromere-associated SNF2 family ATPase, is regulated by
Plk1 and required for the spindle checkpoint.";
Cell 128:101-114(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1250.
TISSUE=Colon, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 603-1250.
Xueyuan D., Weifeng C.;
"Cloning and identification of genes which are differentially
expressed in carcinoma.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[5]
SUBCELLULAR LOCATION.
PubMed=17989990; DOI=10.1007/s00412-007-0131-7;
Wang L.-H., Schwarzbraun T., Speicher M.R., Nigg E.A.;
"Persistence of DNA threads in human anaphase cells suggests late
completion of sister chromatid decatenation.";
Chromosoma 117:123-135(2008).
[6]
SUBCELLULAR LOCATION.
PubMed=17599064; DOI=10.1038/sj.emboj.7601777;
Chan K.-L., North P.S., Hickson I.D.;
"BLM is required for faithful chromosome segregation and its
localization defines a class of ultrafine anaphase bridges.";
EMBO J. 26:3397-3409(2007).
[7]
SUBCELLULAR LOCATION.
PubMed=17956945; DOI=10.1242/jcs.013730;
Spence J.M., Phua H.-H., Mills W., Carpenter A.J., Porter A.C.G.,
Farr C.J.;
"Depletion of topoisomerase IIalpha leads to shortening of the
metaphase interkinetochore distance and abnormal persistence of PICH-
coated anaphase threads.";
J. Cell Sci. 120:3952-3964(2007).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH PLK1.
PubMed=17671160; DOI=10.1091/mbc.E07-05-0517;
Santamaria A., Neef R., Eberspaecher U., Eis K., Husemann M.,
Mumberg D., Prechtl S., Schulze V., Siemeister G., Wortmann L.,
Barr F.A., Nigg E.A.;
"Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate
functions of Plk1 in early and late stages of mitosis.";
Mol. Biol. Cell 18:4024-4036(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-755; SER-774;
SER-1181 AND SER-1188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-810; THR-813;
SER-820 AND SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028 AND SER-1098, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-807; SER-810;
SER-995 AND SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-1028 AND
SER-1069, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-774; SER-807;
SER-820; SER-969; SER-971; SER-1028 AND SER-1069, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-128.
PubMed=23973328; DOI=10.1016/j.molcel.2013.07.016;
Biebricher A., Hirano S., Enzlin J.H., Wiechens N., Streicher W.W.,
Huttner D., Wang L.H., Nigg E.A., Owen-Hughes T., Liu Y., Peterman E.,
Wuite G.J.L., Hickson I.D.;
"PICH: a DNA translocase specially adapted for processing anaphase
bridge DNA.";
Mol. Cell 51:691-701(2013).
[18]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 10-66 IN COMPLEX WITH BEND3,
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BEND3 AND PLK1, AND
MUTAGENESIS OF GLU-11; LEU-13 AND TYR-21.
PubMed=28977671; DOI=10.1093/nar/gkx792;
Pitchai G.P., Kaulich M., Bizard A.H., Mesa P., Yao Q., Sarlos K.,
Streicher W.W., Nigg E.A., Montoya G., Hickson I.D.;
"A novel TPR-BEN domain interaction mediates PICH-BEND3 association.";
Nucleic Acids Res. 45:11413-11424(2017).
-!- FUNCTION: DNA helicase that acts as an essential component of the
spindle assembly checkpoint. Contributes to the mitotic checkpoint
by recruiting MAD2 to kinetochores and monitoring tension on
centromeric chromatin (PubMed:17218258). Acts as a tension sensor
that associates with catenated DNA which is stretched under
tension until it is resolved during anaphase (PubMed:17218258,
PubMed:23973328). Functions as ATP-dependent DNA translocase
(PubMed:23973328, PubMed:28977671). Can promote Holliday junction
branch migration (in vitro) (PubMed:23973328).
{ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:23973328,
ECO:0000269|PubMed:28977671}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
Evidence={ECO:0000269|PubMed:23973328,
ECO:0000269|PubMed:28977671};
-!- SUBUNIT: Interacts with PLK1, which phosphorylates it
(PubMed:17218258, PubMed:17671160, PubMed:28977671). Both proteins
are mutually dependent on each other for correct subcellular
localization (PubMed:17218258, PubMed:17671160). Interacts (via N-
terminal TPR repeat) with BEND3 (via BEN domains 1 and 3); the
interaction is direct (PubMed:28977671).
{ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17671160,
ECO:0000269|PubMed:28977671}.
-!- INTERACTION:
P42858:HTT; NbExp=2; IntAct=EBI-1042535, EBI-466029;
P61968:LMO4; NbExp=3; IntAct=EBI-1042535, EBI-2798728;
P53350:PLK1; NbExp=3; IntAct=EBI-1042535, EBI-476768;
-!- SUBCELLULAR LOCATION: Chromosome, centromere
{ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17989990}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17218258}.
Chromosome {ECO:0000269|PubMed:17218258,
ECO:0000269|PubMed:17671160, ECO:0000269|PubMed:17989990}.
Note=Localizes to kinetochores, inner centromeres and thin threads
connecting separating chromosomes even during anaphase. In
prometaphase cells, it mostly concentrates in between
kinetochores. In metaphase, it localizes to numerous thin threads
that stretch between sister kinetochores of the aligned
chromosomes and are composed of catenated centromeric DNA.
Evolution from inner centromeres to thin threads takes place in
response to tension. Resolution of thin threads requires
topoisomerase 2-alpha (TOP2A) after anaphase onset.
{ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17671160,
ECO:0000269|PubMed:17956945, ECO:0000269|PubMed:17989990}.
-!- PTM: Phosphorylation by PLK1 prevents the association with
chromosome arms and restricts its localization to the kinetochore-
centromere region. {ECO:0000269|PubMed:17218258}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM82750.1; Type=Erroneous termination; Positions=803; Note=Translated as Lys.; Evidence={ECO:0000305};
Sequence=BAA90952.1; Type=Erroneous termination; Positions=803; Note=Translated as Lys.; Evidence={ECO:0000305};
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EMBL; EU069463; ABU25227.1; -; mRNA.
EMBL; BC008808; AAH08808.2; -; mRNA.
EMBL; BC111486; AAI11487.1; -; mRNA.
EMBL; AK000112; BAA90952.1; ALT_SEQ; mRNA.
EMBL; AK074719; BAC11160.1; -; mRNA.
EMBL; AY121802; AAM82750.1; ALT_SEQ; mRNA.
CCDS; CCDS35329.1; -.
RefSeq; NP_060139.2; NM_017669.2.
UniGene; Hs.47558; -.
PDB; 5JNO; X-ray; 2.20 A; B=10-66.
PDBsum; 5JNO; -.
ProteinModelPortal; Q2NKX8; -.
SMR; Q2NKX8; -.
BioGrid; 120176; 31.
ELM; Q2NKX8; -.
IntAct; Q2NKX8; 15.
MINT; Q2NKX8; -.
STRING; 9606.ENSP00000334675; -.
iPTMnet; Q2NKX8; -.
PhosphoSitePlus; Q2NKX8; -.
BioMuta; ERCC6L; -.
DMDM; 121948339; -.
EPD; Q2NKX8; -.
MaxQB; Q2NKX8; -.
PaxDb; Q2NKX8; -.
PeptideAtlas; Q2NKX8; -.
PRIDE; Q2NKX8; -.
ProteomicsDB; 61414; -.
DNASU; 54821; -.
Ensembl; ENST00000334463; ENSP00000334675; ENSG00000186871.
GeneID; 54821; -.
KEGG; hsa:54821; -.
UCSC; uc004eaq.2; human.
CTD; 54821; -.
DisGeNET; 54821; -.
EuPathDB; HostDB:ENSG00000186871.6; -.
GeneCards; ERCC6L; -.
H-InvDB; HIX0016867; -.
HGNC; HGNC:20794; ERCC6L.
HPA; HPA050492; -.
MIM; 300687; gene.
neXtProt; NX_Q2NKX8; -.
OpenTargets; ENSG00000186871; -.
PharmGKB; PA162385290; -.
eggNOG; KOG0387; Eukaryota.
eggNOG; ENOG410XP4Z; LUCA.
GeneTree; ENSGT00940000156837; -.
HOGENOM; HOG000074172; -.
HOVERGEN; HBG107854; -.
InParanoid; Q2NKX8; -.
KO; K20093; -.
OMA; ICEMPSL; -.
OrthoDB; EOG091G058Q; -.
PhylomeDB; Q2NKX8; -.
TreeFam; TF332843; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SIGNOR; Q2NKX8; -.
GenomeRNAi; 54821; -.
PRO; PR:Q2NKX8; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000186871; Expressed in 80 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_ERCC6L; -.
ExpressionAtlas; Q2NKX8; baseline and differential.
Genevisible; Q2NKX8; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0015616; F:DNA translocase activity; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
InterPro; IPR013026; TPR-contain_dom.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cell division; Centromere;
Chromosome; Complete proteome; DNA-binding; Helicase; Hydrolase;
Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; TPR repeat.
CHAIN 1 1250 DNA excision repair protein ERCC-6-like.
/FTId=PRO_0000328831.
REPEAT 21 54 TPR 1.
DOMAIN 109 277 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 464 620 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
REPEAT 1200 1233 TPR 2.
NP_BIND 122 129 ATP. {ECO:0000305}.
MOTIF 228 231 DEAH box.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 807 807 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 810 810 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 813 813 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 820 820 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 969 969 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1004 1004 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BHK9}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1063 1063 Phosphothreonine; by PLK1.
{ECO:0000269|PubMed:17218258}.
MOD_RES 1069 1069 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1118 1118 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BHK9}.
MOD_RES 1181 1181 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 1188 1188 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MUTAGEN 11 11 E->A: Decreased affinity for BEND3, and
abolishes BEND3-mediated stimulation of
ATPase activity; when associated with A-
13 and A-21.
{ECO:0000269|PubMed:28977671}.
MUTAGEN 13 13 L->A: Decreased affinity for BEND3, and
abolishes BEND3-mediated stimulation of
ATPase activity; when associated with A-
11 and A-21.
{ECO:0000269|PubMed:28977671}.
MUTAGEN 21 21 Y->A: Decreased affinity for BEND3, and
abolishes BEND3-mediated stimulation of
ATPase activity; when associated with A-
11 and A-13.
{ECO:0000269|PubMed:28977671}.
MUTAGEN 127 129 GKT->AAA: Abolishes chromatin
association.
{ECO:0000269|PubMed:17218258}.
MUTAGEN 128 128 K->A: Abolishes ATPase activity.
{ECO:0000269|PubMed:23973328}.
MUTAGEN 1063 1063 T->A: Induces a decrease in
phosphorylation.
{ECO:0000269|PubMed:17218258}.
CONFLICT 145 145 V -> M (in Ref. 3; BAC11160).
{ECO:0000305}.
CONFLICT 172 172 R -> G (in Ref. 3; BAC11160).
{ECO:0000305}.
CONFLICT 812 812 A -> T (in Ref. 3; BAA90952 and 4;
AAM82750). {ECO:0000305}.
CONFLICT 889 889 I -> V (in Ref. 3; BAC11160).
{ECO:0000305}.
CONFLICT 989 989 R -> K (in Ref. 3; BAA90952 and 4;
AAM82750). {ECO:0000305}.
HELIX 15 34 {ECO:0000244|PDB:5JNO}.
HELIX 37 50 {ECO:0000244|PDB:5JNO}.
HELIX 54 57 {ECO:0000244|PDB:5JNO}.
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


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