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DNA excision repair protein ERCC-6 (EC 3.6.4.-) (ATP-dependent helicase ERCC6) (Cockayne syndrome protein CSB)

 ERCC6_HUMAN             Reviewed;        1493 AA.
Q03468; D3DX94; E7EV46; Q5W0L9;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
30-AUG-2017, entry version 190.
RecName: Full=DNA excision repair protein ERCC-6;
EC=3.6.4.-;
AltName: Full=ATP-dependent helicase ERCC6;
AltName: Full=Cockayne syndrome protein CSB;
Name=ERCC6; Synonyms=CSB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1339317; DOI=10.1016/0092-8674(92)90390-X;
Troelstra C., van Gool A., de Wit J., Vermeulen W., Bootsma D.,
Hoeijmakers J.H.J.;
"ERCC6, a member of a subfamily of putative helicases, is involved in
Cockayne's syndrome and preferential repair of active genes.";
Cell 71:939-953(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8382798; DOI=10.1093/nar/21.3.419;
Troelstra C., Hesen V., Bootsma D., Hoeijmakers J.H.J.;
"Structure and expression of the excision repair gene ERCC6, involved
in the human disorder Cockayne's syndrome group B.";
Nucleic Acids Res. 21:419-426(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-399; ALA-425;
ASP-446; MET-942; CYS-1002; ARG-1095; VAL-1097; GLY-1213; PRO-1230;
LEU-1308; VAL-1322; ARG-1372; ARG-1382; ARG-1410; ARG-1413 AND
ILE-1441.
NIEHS SNPs program;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
REVIEW ON VARIANTS CSB.
PubMed=10447254;
DOI=10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6;
Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.;
"A summary of mutations in the UV-sensitive disorders: xeroderma
pigmentosum, Cockayne syndrome, and trichothiodystrophy.";
Hum. Mutat. 14:9-22(1999).
[7]
DISEASE.
PubMed=10739753; DOI=10.1086/302867;
Meira L.B., Graham J.M. Jr., Greenberg C.R., Busch D.B.,
Doughty A.T.B., Ziffer D.W., Coleman D.M., Savre-Train I.,
Friedberg E.C.;
"Manitoba aboriginal kindred with original cerebro-oculo-facio-
skeletal syndrome has a mutation in the Cockayne syndrome group B
(CSB) gene.";
Am. J. Hum. Genet. 66:1221-1228(2000).
[8]
DISEASE.
PubMed=10767341; DOI=10.1093/hmg/9.8.1171;
Colella S., Nardo T., Botta E., Lehmann A.R., Stefanini M.;
"Identical mutations in the CSB gene associated with either Cockayne
syndrome or the DeSanctis-Cacchione variant of xeroderma
pigmentosum.";
Hum. Mol. Genet. 9:1171-1175(2000).
[9]
INVOLVEMENT IN UVSS1.
PubMed=15486090; DOI=10.1073/pnas.0404587101;
Horibata K., Iwamoto Y., Kuraoka I., Jaspers N.G.J., Kurimasa A.,
Oshimura M., Ichihashi M., Tanaka K.;
"Complete absence of Cockayne syndrome group B gene product gives rise
to UV-sensitive syndrome but not Cockayne syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 101:15410-15415(2004).
[10]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16128801; DOI=10.1111/j.1742-4658.2005.04844.x;
Christiansen M., Thorslund T., Jochimsen B., Bohr V.A., Stevnsner T.;
"The Cockayne syndrome group B protein is a functional dimer.";
FEBS J. 272:4306-4314(2005).
[11]
FUNCTION, SUBUNIT, AND DNA-BINDING.
PubMed=15548521; DOI=10.1074/jbc.M409147200;
Beerens N., Hoeijmakers J.H., Kanaar R., Vermeulen W., Wyman C.;
"The CSB protein actively wraps DNA.";
J. Biol. Chem. 280:4722-4729(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
INTERACTION WITH ERCC8, UBIQUITINATION BY THE CSA COMPLEX, AND
PROTEASOMAL DEGRADATION.
PubMed=16751180; DOI=10.1101/gad.378206;
Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T.,
Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y.;
"CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway
establishes a link between complementation factors of the Cockayne
syndrome.";
Genes Dev. 20:1429-1434(2006).
[14]
IDENTIFICATION IN THE B-WICH COMPLEX.
PubMed=16603771; DOI=10.1074/jbc.M600233200;
Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
"The WSTF-SNF2h chromatin remodeling complex interacts with several
nuclear proteins in transcription.";
J. Biol. Chem. 281:16264-16271(2006).
[15]
FUNCTION.
PubMed=16916636; DOI=10.1016/j.molcel.2006.06.029;
Fousteri M., Vermeulen W., van Zeeland A.A., Mullenders L.H.;
"Cockayne syndrome A and B proteins differentially regulate
recruitment of chromatin remodeling and repair factors to stalled RNA
polymerase II in vivo.";
Mol. Cell 23:471-482(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
INVOLVEMENT IN ARMD5.
PubMed=16754848; DOI=10.1073/pnas.0603485103;
Tuo J., Ning B., Bojanowski C.M., Lin Z.-N., Ross R.J., Reed G.F.,
Shen D., Jiao X., Zhou M., Chew E.Y., Kadlubar F.F., Chan C.-C.;
"Synergic effect of polymorphisms in ERCC6 5' flanking region and
complement factor H on age-related macular degeneration
predisposition.";
Proc. Natl. Acad. Sci. U.S.A. 103:9256-9261(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, 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).
[19]
METHYLATION AT LYS-170; LYS-297; LYS-448 AND LYS-1054.
PubMed=18438403; DOI=10.1038/nchembio.88;
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Nat. Chem. Biol. 4:344-346(2008).
[20]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
PubMed=18369450; DOI=10.1371/journal.pgen.1000031;
Newman J.C., Bailey A.D., Fan H.Y., Pavelitz T., Weiner A.M.;
"An abundant evolutionarily conserved CSB-PiggyBac fusion protein
expressed in Cockayne syndrome.";
PLoS Genet. 4:E1000031-E1000031(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-429; SER-430;
SER-1142 AND SER-1348, 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).
[22]
FUNCTION, DOMAIN, UBIQUITIN-BINDING, UBIQUITINATION AT THE C-TERMINUS,
AND MUTAGENESIS OF 1427-LEU-LEU-1428.
PubMed=20541997; DOI=10.1016/j.molcel.2010.04.017;
Anindya R., Mari P.O., Kristensen U., Kool H., Giglia-Mari G.,
Mullenders L.H., Fousteri M., Vermeulen W., Egly J.M., Svejstrup J.Q.;
"A ubiquitin-binding domain in cockayne syndrome B required for
transcription-coupled nucleotide excision repair.";
Mol. Cell 38:637-648(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, 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).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-430; SER-486
AND SER-489, 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).
[26]
FUNCTION.
PubMed=22483866; DOI=10.1016/j.dnarep.2012.02.004;
Bailey A.D., Gray L.T., Pavelitz T., Newman J.C., Horibata K.,
Tanaka K., Weiner A.M.;
"The conserved Cockayne syndrome B-piggyBac fusion protein (CSB-PGBD3)
affects DNA repair and induces both interferon-like and innate
antiviral responses in CSB-null cells.";
DNA Repair 11:488-501(2012).
[27]
UBIQUITINATION.
PubMed=22466610; DOI=10.1038/ng.2229;
Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M.,
Nardo T., Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M.,
Kinoshita A., Ono S., Takenaka K., Masuyama R., Kudo T., Slor H.,
Utani A., Tateishi S., Yamashita S., Stefanini M., Lehmann A.R.,
Yoshiura K.I., Ogi T.;
"Mutations in UVSSA cause UV-sensitive syndrome and impair RNA
polymerase IIo processing in transcription-coupled nucleotide-excision
repair.";
Nat. Genet. 44:586-592(2012).
[28]
UBIQUITINATION.
PubMed=22466611; DOI=10.1038/ng.2230;
Schwertman P., Lagarou A., Dekkers D.H., Raams A., van der Hoek A.C.,
Laffeber C., Hoeijmakers J.H., Demmers J.A., Fousteri M.,
Vermeulen W., Marteijn J.A.;
"UV-sensitive syndrome protein UVSSA recruits USP7 to regulate
transcription-coupled repair.";
Nat. Genet. 44:598-602(2012).
[29]
UBIQUITINATION, AND INTERACTION WITH UVSSA.
PubMed=22466612; DOI=10.1038/ng.2228;
Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I.,
Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.;
"Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6
in transcription-coupled DNA repair.";
Nat. Genet. 44:593-597(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-1348, 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).
[31]
INVOLVEMENT IN POF11, VARIANTS POF11 ASP-746 AND ILE-1056 (ISOFORM 2),
CHARACTERIZATION OF VARIANTS POF11 ASP-746 AND ILE-1056 (ISOFORM 2),
AND TISSUE SPECIFICITY.
PubMed=26218421; DOI=10.1371/journal.pgen.1005419;
Qin Y., Guo T., Li G., Tang T.S., Zhao S., Jiao X., Gong J., Gao F.,
Guo C., Simpson J.L., Chen Z.J.;
"CSB-PGBD3 mutations cause premature ovarian failure.";
PLoS Genet. 11:E1005419-E1005419(2015).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-255, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[33]
VARIANTS CSB TRP-670; ARG-851; GLY-957 AND LEU-1042, AND VARIANTS
THR-255; ASP-399; ARG-1095; VAL-1097; GLY-1213 AND ARG-1413.
PubMed=9443879; DOI=10.1086/301686;
Mallery D.L., Tanganelli B., Colella S., Steingrimsdottir H.,
van Gool A.J., Troelstra C., Stefanini M., Lehmann A.R.;
"Molecular analysis of mutations in the CSB (ERCC6) gene in patients
with Cockayne syndrome.";
Am. J. Hum. Genet. 62:77-85(1998).
[34]
VARIANTS [LARGE SCALE ANALYSIS] ALA-591; LEU-652; THR-1038; GLN-1119
AND VAL-1119.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[35]
VARIANT [LARGE SCALE ANALYSIS] TRP-134.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[36]
VARIANTS CSB TRP-670; ASP-680; CYS-686; LEU-687; ARG-851; GLY-957 AND
LEU-1042, VARIANTS COFS1 PRO-871 AND PRO-987, AND VARIANTS ARG-1095
AND GLY-1213.
PubMed=19894250; DOI=10.1002/humu.21154;
Laugel V., Dalloz C., Durand M., Sauvanaud F., Kristensen U.,
Vincent M.C., Pasquier L., Odent S., Cormier-Daire V., Gener B.,
Tobias E.S., Tolmie J.L., Martin-Coignard D., Drouin-Garraud V.,
Heron D., Journel H., Raffo E., Vigneron J., Lyonnet S., Murday V.,
Gubser-Mercati D., Funalot B., Brueton L., Sanchez Del Pozo J.,
Munoz E., Gennery A.R., Salih M., Noruzinia M., Prescott K., Ramos L.,
Stark Z., Fieggen K., Chabrol B., Sarda P., Edery P., Bloch-Zupan A.,
Fawcett H., Pham D., Egly J.M., Lehmann A.R., Sarasin A., Dollfus H.;
"Mutation update for the CSB/ERCC6 and CSA/ERCC8 genes involved in
Cockayne syndrome.";
Hum. Mutat. 31:113-126(2010).
-!- FUNCTION: Essential factor involved in transcription-coupled
nucleotide excision repair which allows RNA polymerase II-blocking
lesions to be rapidly removed from the transcribed strand of
active genes. Upon DNA-binding, it locally modifies DNA
conformation by wrapping the DNA around itself, thereby modifying
the interface between stalled RNA polymerase II and DNA. It is
required for transcription-coupled repair complex formation. It
recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision
repair proteins and EP300 to the at sites of RNA polymerase II-
blocking lesions. {ECO:0000269|PubMed:15548521,
ECO:0000269|PubMed:16916636, ECO:0000269|PubMed:20541997}.
-!- FUNCTION: Isoform 2: Like isoform 1, it is involved in repair of
DNA damage, acting on its own or synergistically with isoform 1.
May bind to PiggyBac transposable elements known as MER85
scattered in the genome and may therefore regulate the expression
of nearby genes. Able to stimulate the antiviral response and
modulate the expression of genes involved in metabolism
regulation. {ECO:0000269|PubMed:22483866}.
-!- SUBUNIT: Homodimer. Binds DNA. Interacts with ERCC8. Interacts
with a subunit of RNA polymerase II TFIIH. Component of the B-WICH
complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1,
DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with
KIAA1530/UVSSA. {ECO:0000269|PubMed:15548521,
ECO:0000269|PubMed:16128801, ECO:0000269|PubMed:16603771,
ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:22466612}.
-!- INTERACTION:
Q13216-1:ERCC8; NbExp=2; IntAct=EBI-295284, EBI-596556;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16128801}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q03468-1; Sequence=Displayed;
Name=2; Synonyms=CSB-PGBD3 {ECO:0000303|PubMed:18369450};
IsoId=Q03468-2; Sequence=VSP_058677, VSP_058678;
Note=Major transcript, generated by alternative splicing of
ERCC6 exon 5 to a domesticated PiggyBac transposon, PGBD3,
located within ERCC6 intron 5. The fusion protein consists of
the N-terminal 465 residues of ERCC6 tethered to the entire
PGBD3 sequence. Variant in position: 746:G->D (in POF11, the
mutation results in weaker cellular response to DNA damage as
indicated by delayed recruitement of mutant protein to DNA
damaged sites, interaction with RNA polymerase II is not
affected either after UV or H(2)O(2) damage). Variant in
position: 1056:V->I (in POF11, the mutation results in weaker
cellular response to DNA damage as indicated by delayed
recruitement of mutant protein to DNA damaged sites, interaction
with RNA polymerase II is not affected either after UV or
H(2)O(2) damage). {ECO:0000269|PubMed:18369450,
ECO:0000269|PubMed:26218421};
-!- TISSUE SPECIFICITY: Expressed in heart, ovary, but not in
granulosa cells. {ECO:0000269|PubMed:26218421}.
-!- DOMAIN: A C-terminal ubiquitin-binding domain (UBD) is essential
for transcription-coupled nucleotide excision repair to proceed.
{ECO:0000269|PubMed:20541997}.
-!- PTM: Ubiquitinated at the C-terminus. Ubiquitination by the CSA
complex leads to ERCC6 proteasomal degradation in a UV-dependent
manner. Stabilized following interaction with KIAA1530/UVSSA,
which promotes recruitment of deubiquitinating enzyme USP7,
leading to deubiquitination of ERCC6 thereby preventing UV-induced
degradation of ERCC6 by the proteasome.
{ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:20541997,
ECO:0000269|PubMed:22466610, ECO:0000269|PubMed:22466611,
ECO:0000269|PubMed:22466612}.
-!- DISEASE: Cockayne syndrome B (CSB) [MIM:133540]: A rare disorder
characterized by cutaneous sensitivity to sunlight, abnormal and
slow growth, cachectic dwarfism, progeroid appearance, progressive
pigmentary retinopathy and sensorineural deafness. There is
delayed neural development and severe progressive neurologic
degeneration resulting in mental retardation. Two clinical forms
are recognized: in the classical form or Cockayne syndrome type 1,
the symptoms are progressive and typically become apparent within
the first few years or life; the less common Cockayne syndrome
type 2 is characterized by more severe symptoms that manifest
prenatally. Cockayne syndrome shows some overlap with certain
forms of xeroderma pigmentosum. Unlike xeroderma pigmentosum,
patients with Cockayne syndrome do not manifest increased
freckling and other pigmentation abnormalities in the skin and
have no significant increase in skin cancer.
{ECO:0000269|PubMed:10447254, ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cerebro-oculo-facio-skeletal syndrome 1 (COFS1)
[MIM:214150]: A disorder of prenatal onset characterized by
microcephaly, congenital cataracts, facial dysmorphism, neurogenic
arthrogryposis, growth failure and severe psychomotor retardation.
COFS is considered to be part of the nucleotide-excision repair
disorders spectrum that include also xeroderma pigmentosum,
trichothiodystrophy and Cockayne syndrome.
{ECO:0000269|PubMed:19894250}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: De Sanctis-Cacchione syndrome (DSC) [MIM:278800]: An
autosomal recessive syndrome consisting of xeroderma pigmentosum
associated with severe neurological and developmental involvement.
In addition to the clinical signs of xeroderma pigmentosum,
patients present with mental retardation, dwarfism, gonadal
hypoplasia, microcephaly and various neurologic complications of
early onset. Note=The disease is caused by mutations affecting the
gene represented in this entry.
-!- DISEASE: Macular degeneration, age-related, 5 (ARMD5)
[MIM:613761]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:16754848}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: UV-sensitive syndrome 1 (UVSS1) [MIM:600630]: An
autosomal recessive disorder characterized by cutaneous
photosensitivity and mild freckling in the absence of neurological
abnormalities or skin tumors. {ECO:0000269|PubMed:15486090}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Premature ovarian failure 11 (POF11) [MIM:616946]: An
ovarian disorder defined as the cessation of ovarian function
under the age of 40 years. It is characterized by oligomenorrhea
or amenorrhea, in the presence of elevated levels of serum
gonadotropins and low estradiol. {ECO:0000269|PubMed:26218421}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Allelic variations of the XP genes;
URL="http://www.xpmutations.org/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CSBID302.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ercc6/";
-----------------------------------------------------------------------
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EMBL; L04791; AAA52397.1; -; mRNA.
EMBL; AY204752; AAO13487.1; -; Genomic_DNA.
EMBL; AC073366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138760; CAH70291.1; -; Genomic_DNA.
EMBL; CH471187; EAW93094.1; -; Genomic_DNA.
EMBL; CH471187; EAW93097.1; -; Genomic_DNA.
CCDS; CCDS60529.1; -. [Q03468-2]
CCDS; CCDS7229.1; -. [Q03468-1]
PIR; A44224; A44224.
RefSeq; NP_000115.1; NM_000124.3. [Q03468-1]
RefSeq; NP_001333369.1; NM_001346440.1. [Q03468-1]
UniGene; Hs.49063; -.
PDB; 4CVO; X-ray; 1.85 A; A=84-160.
PDBsum; 4CVO; -.
ProteinModelPortal; Q03468; -.
SMR; Q03468; -.
BioGrid; 108386; 52.
DIP; DIP-193N; -.
IntAct; Q03468; 19.
MINT; MINT-1193928; -.
STRING; 9606.ENSP00000348089; -.
iPTMnet; Q03468; -.
PhosphoSitePlus; Q03468; -.
BioMuta; ERCC6; -.
DMDM; 416959; -.
EPD; Q03468; -.
MaxQB; Q03468; -.
PaxDb; Q03468; -.
PeptideAtlas; Q03468; -.
PRIDE; Q03468; -.
Ensembl; ENST00000355832; ENSP00000348089; ENSG00000225830. [Q03468-1]
Ensembl; ENST00000447839; ENSP00000387966; ENSG00000225830. [Q03468-2]
Ensembl; ENST00000515869; ENSP00000423550; ENSG00000225830. [Q03468-2]
GeneID; 2074; -.
KEGG; hsa:2074; -.
UCSC; uc001jhs.6; human. [Q03468-1]
UCSC; uc001jhu.4; human.
CTD; 2074; -.
DisGeNET; 2074; -.
DisGeNET; 267004; -.
GeneCards; ERCC6; -.
GeneReviews; ERCC6; -.
HGNC; HGNC:3438; ERCC6.
HPA; HPA025825; -.
HPA; HPA066830; -.
MalaCards; ERCC6; -.
MIM; 133540; phenotype.
MIM; 214150; phenotype.
MIM; 278800; phenotype.
MIM; 600630; phenotype.
MIM; 609413; gene.
MIM; 613761; phenotype.
MIM; 616946; phenotype.
neXtProt; NX_Q03468; -.
OpenTargets; ENSG00000225830; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 90321; Cockayne syndrome type 1.
Orphanet; 90322; Cockayne syndrome type 2.
Orphanet; 90324; Cockayne syndrome type 3.
Orphanet; 1466; COFS syndrome.
Orphanet; 178338; UV-sensitive syndrome.
PharmGKB; PA27852; -.
eggNOG; ENOG410IHMN; Eukaryota.
eggNOG; KOG0387; Eukaryota.
eggNOG; ENOG410XP4Z; LUCA.
eggNOG; ENOG410ZDPG; LUCA.
GeneTree; ENSGT00590000083118; -.
HOGENOM; HOG000170952; -.
HOVERGEN; HBG051502; -.
InParanoid; Q03468; -.
KO; K10841; -.
OMA; HETGSYT; -.
OrthoDB; EOG091G05IL; -.
PhylomeDB; Q03468; -.
TreeFam; TF101236; -.
TreeFam; TF328011; -.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
SIGNOR; Q03468; -.
ChiTaRS; ERCC6; human.
GeneWiki; ERCC6; -.
GenomeRNAi; 101243544; -.
GenomeRNAi; 2074; -.
PRO; PR:Q03468; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000225830; -.
CleanEx; HS_ERCC6; -.
ExpressionAtlas; Q03468; baseline and differential.
Genevisible; Q03468; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
GO; GO:0007256; P:activation of JNKK activity; IEA:Ensembl.
GO; GO:0007257; P:activation of JUN kinase activity; IEA:Ensembl.
GO; GO:0006284; P:base-excision repair; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
GO; GO:0000303; P:response to superoxide; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; NAS:UniProtKB.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:UniProtKB.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000330; SNF2_N.
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.
1: Evidence at protein level;
3D-structure; Age-related macular degeneration; Alternative splicing;
ATP-binding; Cataract; Cockayne syndrome; Complete proteome; Deafness;
Disease mutation; DNA damage; DNA repair; DNA-binding; Dwarfism;
Helicase; Hydrolase; Isopeptide bond; Mental retardation; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Premature ovarian failure; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Xeroderma pigmentosum.
CHAIN 1 1493 DNA excision repair protein ERCC-6.
/FTId=PRO_0000074314.
DOMAIN 519 695 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 843 1002 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 532 539 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1400 1428 Ubiquitin-binding domain (UBD).
MOTIF 466 481 Nuclear localization signal.
{ECO:0000255}.
MOTIF 646 649 DEGH box.
MOTIF 1038 1055 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 356 394 Asp/Glu-rich (acidic).
COMPBIAS 442 446 Gly-rich.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 170 170 N6-methylated lysine; by EHMT2.
{ECO:0000269|PubMed:18438403}.
MOD_RES 297 297 N6-methylated lysine; by EHMT2.
{ECO:0000269|PubMed:18438403}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 448 448 N6-methylated lysine; by EHMT2.
{ECO:0000269|PubMed:18438403}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1054 1054 N6-methylated lysine; by EHMT2.
{ECO:0000269|PubMed:18438403}.
MOD_RES 1142 1142 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1348 1348 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 466 1061 RRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKK
LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLA
GLSYSKIRTRGSNYRFEGLGPTVIVCPTTVMHQWVKEFHTW
WPPFRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIR
LMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHR
IILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPI
TMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRMKSDVKM
SLSLPDKNEQVLFCRLTDEQHKVYQNFVDSKEVYRILNGEM
QIFSGLIALRKICNHPDLFSGGPKNLKGLPDDELEEDQFGY
WKRSGKMIVVESLLKIWHKQGQRVLLFSQSRQMLDILEVFL
RAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRV
GGLGVNLTGANRVVIYDPDWNPSTDTQARERAWRIGQKKQV
TVYRLLTAGTIEEKIYHRQIFKQFLTNRVLKDPKQRRFFKS
NDLYELFTLTSPDASQSTETSAIFAGTGSDVQTPKCHLKRR
IQPAFGADHDVPKRKKFPASNI -> SPKMPRTLSLHEITD
LLETDDSIEASAIVIQPPENATAPVSDEESGDEEGGTINNL
PGSLLHTAAYLIQDGSDAESDSDDPSYAPKDDSPDEVPSTF
TVQQPPPSRRRKMTKILCKWKKADLTVQPVAGRVTAPPNDF
FTVMRTPTEILELFLDDEVIELIVKYSNLYACSKGVHLGLT
SSEFKCFLGIIFLSGYVSVPRRRMFWEQRTDVHNVLVSAAM
RRDRFETIFSNLHVADNANLDPVDKFSKLRPLISKLNERCM
KFVPNETYFSFDEFMVPYFGRHGCKQFIRGKPIRFGYKFWC
GATCLGYICWFQPYQGKNPNTKHEEYGVGASLVLQFSEALT
EAHPGQYHFVFNNFFTSIALLDKLSSMGHQATGTVRKDHID
RVPLESDVALKKKERGTFDYRIDGKGNIVCRWNDNSVVTVA
SSGAGIHPLCLVSRYSQKLKKKIQVQQPNMIKVYNQFMGGV
DRADENIDKYRASIRGKKWYSSPLLFCFELVLQNAWQLHKT
YDEKPVDFLEFRRRVVCHYLETHGHPPEPGQKGRPQKRNID
SRYDGINHVIVKQGKQTRCAECHKNTTFRCEKCDVALHVKC
SVEYHTE (in isoform 2).
{ECO:0000269|PubMed:18369450}.
/FTId=VSP_058677.
VAR_SEQ 1062 1493 Missing (in isoform 2).
{ECO:0000269|PubMed:18369450}.
/FTId=VSP_058678.
VARIANT 134 134 R -> W (in dbSNP:rs148095899).
{ECO:0000269|PubMed:18987736}.
/FTId=VAR_054153.
VARIANT 255 255 K -> T. {ECO:0000269|PubMed:9443879}.
/FTId=VAR_001216.
VARIANT 399 399 G -> D (in dbSNP:rs2228528).
{ECO:0000269|PubMed:9443879,
ECO:0000269|Ref.3}.
/FTId=VAR_001217.
VARIANT 425 425 D -> A (in dbSNP:rs4253046).
{ECO:0000269|Ref.3}.
/FTId=VAR_016301.
VARIANT 446 446 G -> D (in dbSNP:rs4253047).
{ECO:0000269|Ref.3}.
/FTId=VAR_016302.
VARIANT 591 591 P -> A (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036021.
VARIANT 652 652 R -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036022.
VARIANT 670 670 R -> W (in CSB; dbSNP:rs202080674).
{ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879}.
/FTId=VAR_001218.
VARIANT 680 680 N -> D (in CSB).
{ECO:0000269|PubMed:19894250}.
/FTId=VAR_063511.
VARIANT 686 686 W -> C (in CSB; dbSNP:rs751292948).
{ECO:0000269|PubMed:19894250}.
/FTId=VAR_063512.
VARIANT 687 687 S -> L (in CSB).
{ECO:0000269|PubMed:19894250}.
/FTId=VAR_063513.
VARIANT 851 851 W -> R (in CSB; dbSNP:rs368728467).
{ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879}.
/FTId=VAR_001219.
VARIANT 871 871 L -> P (in COFS1).
{ECO:0000269|PubMed:19894250}.
/FTId=VAR_063514.
VARIANT 942 942 T -> M (in dbSNP:rs2228525).
{ECO:0000269|Ref.3}.
/FTId=VAR_016303.
VARIANT 957 957 V -> G (in CSB).
{ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879}.
/FTId=VAR_001220.
VARIANT 987 987 L -> P (in COFS1; dbSNP:rs121917905).
{ECO:0000269|PubMed:19894250}.
/FTId=VAR_063515.
VARIANT 1002 1002 Y -> C (in dbSNP:rs4253206).
{ECO:0000269|Ref.3}.
/FTId=VAR_016304.
VARIANT 1038 1038 R -> T (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036023.
VARIANT 1042 1042 P -> L (in CSB).
{ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879}.
/FTId=VAR_001221.
VARIANT 1095 1095 P -> R (in dbSNP:rs4253208).
{ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879,
ECO:0000269|Ref.3}.
/FTId=VAR_001222.
VARIANT 1097 1097 M -> V (in dbSNP:rs2228526).
{ECO:0000269|PubMed:9443879,
ECO:0000269|Ref.3}.
/FTId=VAR_001223.
VARIANT 1119 1119 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036024.
VARIANT 1119 1119 E -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036025.
VARIANT 1213 1213 R -> G (in dbSNP:rs2228527).
{ECO:0000269|PubMed:19894250,
ECO:0000269|PubMed:9443879,
ECO:0000269|Ref.3}.
/FTId=VAR_001224.
VARIANT 1220 1220 T -> I (in dbSNP:rs34704611).
/FTId=VAR_037436.
VARIANT 1230 1230 R -> P (in dbSNP:rs4253211).
{ECO:0000269|Ref.3}.
/FTId=VAR_016305.
VARIANT 1308 1308 V -> L (in dbSNP:rs2229761).
{ECO:0000269|Ref.3}.
/FTId=VAR_016306.
VARIANT 1322 1322 G -> V (in dbSNP:rs4253219).
{ECO:0000269|Ref.3}.
/FTId=VAR_016307.
VARIANT 1355 1355 D -> E (in dbSNP:rs34917815).
/FTId=VAR_037437.
VARIANT 1372 1372 G -> R (in dbSNP:rs4253227).
{ECO:0000269|Ref.3}.
/FTId=VAR_016308.
VARIANT 1382 1382 G -> R (in dbSNP:rs4253228).
{ECO:0000269|Ref.3}.
/FTId=VAR_016309.
VARIANT 1410 1410 G -> R (in dbSNP:rs4253229).
{ECO:0000269|Ref.3}.
/FTId=VAR_016310.
VARIANT 1413 1413 Q -> R (in dbSNP:rs2228529).
{ECO:0000269|PubMed:9443879,
ECO:0000269|Ref.3}.
/FTId=VAR_001225.
VARIANT 1441 1441 T -> I (in dbSNP:rs4253230).
{ECO:0000269|Ref.3}.
/FTId=VAR_016311.
MUTAGEN 1427 1428 LL->GG: Fails to bind polyubiquitin
chains. {ECO:0000269|PubMed:20541997}.
HELIX 93 96 {ECO:0000244|PDB:4CVO}.
HELIX 102 104 {ECO:0000244|PDB:4CVO}.
HELIX 109 155 {ECO:0000244|PDB:4CVO}.
SEQUENCE 1493 AA; 168416 MW; 285257E2AEC071AC CRC64;
MPNEGIPHSS QTQEQDCLQS QPVSNNEEMA IKQESGGDGE VEEYLSFRSV GDGLSTSAVG
CASAAPRRGP ALLHIDRHQI QAVEPSAQAL ELQGLGVDVY DQDVLEQGVL QQVDNAIHEA
SRASQLVDVE KEYRSVLDDL TSCTTSLRQI NKIIEQLSPQ AATSRDINRK LDSVKRQKYN
KEQQLKKITA KQKHLQAILG GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI
RTGQMTPFGT QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQGC NKRAARKAPA
PVTPPAPVQN KNKPNKKARV LSKKEERLKK HIKKLQKRAL QFQGKVGLPK ARRPWESDMR
PEAEGDSEGE ESEYFPTEEE EEEEDDEVEG AEADLSGDGT DYELKPLPKG GKRQKKVPVQ
EIDDDFFPSS GEEAEAASVG EGGGGGRKVG RYRDDGDEDY YKQRLRRWNK LRLQDKEKRL
KLEDDSEESD AEFDEGFKVP GFLFKKLFKY QQTGVRWLWE LHCQQAGGIL GDEMGLGKTI
QIIAFLAGLS YSKIRTRGSN YRFEGLGPTV IVCPTTVMHQ WVKEFHTWWP PFRVAILHET
GSYTHKKEKL IRDVAHCHGI LITSYSYIRL MQDDISRYDW HYVILDEGHK IRNPNAAVTL
ACKQFRTPHR IILSGSPMQN NLRELWSLFD FIFPGKLGTL PVFMEQFSVP ITMGGYSNAS
PVQVKTAYKC ACVLRDTINP YLLRRMKSDV KMSLSLPDKN EQVLFCRLTD EQHKVYQNFV
DSKEVYRILN GEMQIFSGLI ALRKICNHPD LFSGGPKNLK GLPDDELEED QFGYWKRSGK
MIVVESLLKI WHKQGQRVLL FSQSRQMLDI LEVFLRAQKY TYLKMDGTTT IASRQPLITR
YNEDTSIFVF LLTTRVGGLG VNLTGANRVV IYDPDWNPST DTQARERAWR IGQKKQVTVY
RLLTAGTIEE KIYHRQIFKQ FLTNRVLKDP KQRRFFKSND LYELFTLTSP DASQSTETSA
IFAGTGSDVQ TPKCHLKRRI QPAFGADHDV PKRKKFPASN ISVNDATSSE EKSEAKGAEV
NAVTSNRSDP LKDDPHMSSN VTSNDRLGEE TNAVSGPEEL SVISGNGECS NSSGTGKTSM
PSGDESIDEK LGLSYKRERP SQAQTEAFWE NKQMENNFYK HKSKTKHHSV AEEETLEKHL
RPKQKPKNSK HCRDAKFEGT RIPHLVKKRR YQKQDSENKS EAKEQSNDDY VLEKLFKKSV
GVHSVMKHDA IMDGASPDYV LVEAEANRVA QDALKALRLS RQRCLGAVSG VPTWTGHRGI
SGAPAGKKSR FGKKRNSNFS VQHPSSTSPT EKCQDGIMKK EGKDNVPEHF SGRAEDADSS
SGPLASSSLL AKMRARNHLI LPERLESESG HLQEASALLP TTEHDDLLVE MRNFIAFQAH
TDGQASTREI LQEFESKLSA SQSCVFRELL RNLCTFHRTS GGEGIWKLKP EYC


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