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CSB

Protein FULL name:

DNA excision repair protein ERCC-6, ATP-dependent helicase ERCC6, Cockayne syndrome protein CSB.,


Protein SHORT name:

CSB, CS-B, ERCC6, ERCC-6


CSB (Homo sapiens) is product of expression of ERCC6 gene.

Human diseases related to this protein:

CSB is involved in:

NER in Homo sapiens

Keywords:



FUNCTION: Is involved in the preferential repair of active genes. Presumed DNA or RNA unwinding function. Corrects the UV survival and RNA synthesis after UV exposure of Cockayne syndrome complementation group B.

SUBUNIT: Interacts with the CSA protein and 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.

INTERACTION: Q13216-1:ERCC8; NbExp=1; IntAct=EBI-295284, EBI-596556;

SUBCELLULAR LOCATION: Nucleus (Probable).

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

DISEASE: Defects in ERCC6 are the cause of Cockayne syndrome type B (CSB) [MIM:133540]. Cockayne syndrome is 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.

DISEASE: Defects in ERCC6 are the cause of cerebro-oculo-facio- skeletal syndrome type 1 (COFS1) [MIM:214150]; also known as COFS syndrome or Pena-Shokeir syndrome type 2. COFS is a degenerative autosomal recessive disorder of prenatal onset affecting the brain, eye and spinal cord. After birth, it leads to brain atrophy, hypoplasia of the corpus callosum, hypotonia, cataracts, microcornea, optic atrophy, progressive joint contractures and growth failure. Facial dysmorphism is a constant feature. Abnormalities of the skull, eyes, limbs, heart and kidney also occur.

DISEASE: Defects in ERCC6 are a cause of De Sanctis-Cacchione syndrome (DSC) [MIM:278800]; also known as xerodermic idiocy. DSC is an autosomal recessive syndrome consisting of xeroderma pigmentosum associated with mental retardation, retarded growth, gonadal hypoplasia and sometimes neurologic complications.

DISEASE: Genetic variation in ERCC6 is associated with susceptibility to age-related macular degeneration type 5 (ARMD5) [MIM:609413]. ARMD is 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 (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.

DISEASE: Defects in ERCC6 are a cause of UV-sensitive syndrome (UVS) [MIM:600630]. UVS is a rare autosomal recessive disorder characterized by photosensitivity and mild freckling but without neurological abnormalities or skin tumors.

SIMILARITY: Belongs to the SNF2/RAD54 helicase family.

SIMILARITY: Contains 1 helicase ATP-binding domain.

SIMILARITY: Contains 1 helicase C-terminal domain.

WEB RESOURCE: Name=Allelic variations of the XP genes; [LINK]

WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; [LINK]

WEB RESOURCE: Name=GeneReviews; [LINK]

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 416959
4557565
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q03468 Q03468
PFAM: PF00271
PF00176
PF00271
PF00176
InterPro: IPR014001
IPR001650
IPR014021
IPR000330
IPR014001
IPR001650
IPR014021
IPR000330
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MPNEGIPHSSQTQEQDCLQSQPVSNNEEMAIKQESGGDGEVEEYLSFRSV
GDGLSTSAVGCASAAPRRGPALLHIDRHQIQAVEPSAQALELQGLGVDVY
DQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQI
NKIIEQLSPQAATSRDINRKLDSVKRQKYNKEQQLKKITAKQKHLQAILG
GAEVKIELDHASLEEDAEPGPSSLGSMLMPVQETAWEELIRTGQMTPFGT
QIPQKQEKKPRKIMLNEASGFEKYLADQAKLSFERKKQGCNKRAARKAPA
PVTPPAPVQNKNKPNKKARVLSKKEERLKKHIKKLQKRALQFQGKVGLPK
ARRPWESDMRPEAEGDSEGEESEYFPTEEEEEEEDDEVEGAEADLSGDGT
DYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVG
RYRDDGDEDYYKQRLRRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVP
GFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLS
YSKIRTRGSNYRFEGLGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHET
GSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHK
IRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTL
PVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRMKSDV
KMSLSLPDKNEQVLFCRLTDEQHKVYQNFVDSKEVYRILNGEMQIFSGLI
ALRKICNHPDLFSGGPKNLKGLPDDELEEDQFGYWKRSGKMIVVESLLKI
WHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITR
YNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQARERAWR
IGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVLKDPKQRRFFKSND
LYELFTLTSPDASQSTETSAIFAGTGSDVQTPKCHLKRRIQPAFGADHDV
PKRKKFPASNISVNDATSSEEKSEAKGAEVNAVTSNRSDPLKDDPHMSSN
VTSNDRLGEETNAVSGPEELSVISGNGECSNSSGTGKTSMPSGDESIDEK
LGLSYKRERPSQAQTEAFWENKQMENNFYKHKSKTKHHSVAEEETLEKHL
RPKQKPKNSKHCRDAKFEGTRIPHLVKKRRYQKQDSENKSEAKEQSNDDY
VLEKLFKKSVGVHSVMKHDAIMDGASPDYVLVEAEANRVAQDALKALRLS
RQRCLGAVSGVPTWTGHRGISGAPAGKKSRFGKKRNSNFSVQHPSSTSPT
EKCQDGIMKKEGKDNVPEHFSGRAEDADSSSGPLASSSLLAKMRARNHLI
LPERLESESGHLQEASALLPTTEHDDLLVEMRNFIAFQAHTDGQASTREI
LQEFESKLSASQSCVFRELLRNLCTFHRTSGGEGIWKLKPEYC

CSB (Homo sapiens) is able to recognize following damages:
CSB (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Troelstra C, van Gool A, de Wit J, Vermeulen W, Bootsma D, Hoeijmakers JH Cell Dec. 11, 1992
Structure and expression of the excision repair gene ERCC6, involved in the human disorder Cockayne's syndrome group B. Troelstra C, Hesen W, Bootsma D, Hoeijmakers JH Nucleic Acids Res Jan. 11, 1993
Molecular analysis of mutations in the CSB (ERCC6) gene in patients with Cockayne syndrome. Mallery DL, Tanganelli B, Colella S, Steingrimsdottir H, van Gool AJ, Troelstra C, Stefanini M, Lehmann AR Am J Hum Genet Feb. 1, 1998
A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. Cleaver JE, Thompson LH, Richardson AS, States JC Hum Mutat Jan. 1, 1999
Manitoba aboriginal kindred with original cerebro-oculo- facio-skeletal syndrome has a mutation in the Cockayne syndrome group B (CSB) gene. Meira LB, Graham JM Jr, Greenberg CR, Busch DB, Doughty AT, Ziffer DW, Coleman DM, Savre-Train I, Friedberg EC Am J Hum Genet April 1, 2000
Identical mutations in the CSB gene associated with either Cockayne syndrome or the DeSanctis-cacchione variant of xeroderma pigmentosum. Colella S, Nardo T, Botta E, Lehmann AR, Stefanini M Hum Mol Genet May 1, 2000
The DNA sequence and comparative analysis of human chromosome 10. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, 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 AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J Nature May 27, 2004
Complete absence of Cockayne syndrome group B gene product gives rise to UV-sensitive syndrome but not Cockayne syndrome. Horibata K, Iwamoto Y, Kuraoka I, Jaspers NG, Kurimasa A, Oshimura M, Ichihashi M, Tanaka K Proc Natl Acad Sci U S A Oct. 26, 2004
The CSB protein actively wraps DNA. Beerens N, Hoeijmakers JH, Kanaar R, Vermeulen W, Wyman C J Biol Chem Jan. 11, 2005
The Cockayne syndrome group B protein is a functional dimer. Christiansen M, Thorslund T, Jochimsen B, Bohr VA, Stevnsner T FEBS J Sept. 1, 2005
Phosphoproteome analysis of the human mitotic spindle. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R Proc Natl Acad Sci U S A April 4, 2006
CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. Groisman R, Kuraoka I, Chevallier O, Gaye N, Magnaldo T, Tanaka K, Kisselev AF, Harel-Bellan A, Nakatani Y Genes Dev June 1, 2006
Synergic effect of polymorphisms in ERCC6 5' flanking region and complement factor H on age-related macular degeneration predisposition. Tuo J, Ning B, Bojanowski CM, Lin ZN, Ross RJ, Reed GF, Shen D, Jiao X, Zhou M, Chew EY, Kadlubar FF, Chan CC Proc Natl Acad Sci U S A June 13, 2006
The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription. Cavellan E, Asp P, Percipalle P, Farrants AK J Biol Chem June 16, 2006
Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo. Fousteri M, Vermeulen W, van Zeeland AA, Mullenders LH Mol Cell Aug. 1, 2006
A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP Nat Biotechnol Oct. 1, 2006
The consensus coding sequences of human breast and colorectal cancers. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE Science Oct. 13, 2006
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD J Proteome Res Nov. 1, 2007
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell Aug. 8, 2008
DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK Nature Nov. 6, 2008
Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Wang B, Malik R, Nigg EA, Korner R Anal Chem Dec. 15, 2008
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009
Mutation update for the CSB/ERCC6 and CSA/ERCC8 genes involved in Cockayne syndrome. Laugel V, Dalloz C, Durand M, Sauvanaud F, Kristensen U, Vincent MC, Pasquier L, Odent S, Cormier-Daire V, Gener B, Tobias ES, Tolmie JL, 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 AR, 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 JM, Lehmann AR, Sarasin A, Dollfus H Hum Mutat Jan. 1, 2010
A ubiquitin-binding domain in Cockayne syndrome B required for transcription-coupled nucleotide excision repair. Anindya R, Mari PO, Kristensen U, Kool H, Giglia-Mari G, Mullenders LH, Fousteri M, Vermeulen W, Egly JM, Svejstrup JQ Mol Cell June 11, 2010


Last modification of this entry: Oct. 19, 2010.

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