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BLM

Protein FULL name:

Bloom syndrome protein, RECQ PROTEIN-LIKE 3; RECQL3; DNA HELICASE, RECQ-LIKE, TYPE 2; RECQ2; BLM GENE; BLM


Protein SHORT name:

RECQL3, RECQ2, BLM


BLM (Homo sapiens) is product of expression of BLM gene.

Human diseases related to this protein:

BLM is involved in:

DDS in Homo sapiens
     
HRR in Homo sapiens
     





FUNCTION: Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.

CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.

SUBUNIT: Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ubiquitinated FANCD2. Interacts with RMI complex. Interacts directly with RMI1 component of RMI complex.

INTERACTION: P39748:FEN1; NbExp=3; IntAct=EBI-621372, EBI-707816; P27694:RPA1; NbExp=1; IntAct=EBI-621372, EBI-621389; P54274:TERF1; NbExp=2; IntAct=EBI-621372, EBI-710997; Q15554:TERF2; NbExp=5; IntAct=EBI-621372, EBI-706637; Q14191:WRN; NbExp=4; IntAct=EBI-621372, EBI-368417;

SUBCELLULAR LOCATION: Nucleus.

PTM: Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1.

DISEASE: Defects in BLM are the cause of Bloom syndrome (BLM) [MIM:210900]. BLM is an autosomal recessive disorder characterized by proportionate pre- and postnatal growth deficiency, sun- sensitive telangiectatic hypo- and hyperpigmented skin, predisposition to malignancy, and chromosomal instability.

SIMILARITY: Belongs to the helicase family. RecQ subfamily.

SIMILARITY: Contains 1 helicase ATP-binding domain.

SIMILARITY: Contains 1 helicase C-terminal domain.

SIMILARITY: Contains 1 HRDC domain.

WEB RESOURCE: Name=BLMbase; Note=BLM mutation db; [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): 4557365
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P54132 P54132
PFAM: - P54132 (Link - using uniprot id)
InterPro: - P54132 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MAAVPQNNLQEQLERHSARTLNNKLSLSKPKFSGFTFKKKTSSDNNVSVT
NVSVAKTPVLRNKDVNVTEDFSFSEPLPNTTNQQRVKDFFKNAPAGQETQ
RGGSKSLLPDFLQTPKEVVCTTQNTPTVKKSRDTALKKLEFSSSPDSLST
INDWDDMDDFDTSETSKSFVTPPQSHFVRVSTAQKSKKGKRNFFKAQLYT
TNTVKTDLPPPSSESEQIDLTEEQKDDSEWLSSDVICIDDGPIAEVHINE
DAQESDSLKTHLEDERDNSEKKKNLEEAELHSTEKVPCIEFDDDDYDTDF
VPPSPEEIISASSSSSKCLSTLKDLDTSDRKEDVLSTSKDLLSKPEKMSM
QELNPETSTDCDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNEL
LQQRNIRRKLLTEVDFNKSDASLLGSLWRYRPDSLDGPMEGDSCPTGNSM
KELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSF
VSSNWAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPS
YDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAYQPIKEGRPIKSVSERL
SSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSLSFP
HTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQ
LPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDSEATNIY
LQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCV
SQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRP
QVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRE
CDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFG
MGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTR
LKRLIMMEKDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENGF
NPDFCKKHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNI
KHVGPSGRFTMNMLVDIFLGSKSAKIQSGIFGKGSAYSRHNAERLFKKLI
LDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLKVDFMETENSSSVKK
QKALVAKVSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLA
ESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPAEDSSPGIS
LSSSRGPGRSAAEELDEEIPVSSHYFASKTRNERKRKKMPASQRSKRRKT
ASSGSKAKGGSATCRKISSKTKSSSIIGSSSASHTSQATSGANSKLGIMA
PPKPINRPFLKPSYAFS

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

Title Authors Journal
The Bloom's syndrome gene product is homologous to RecQ helicases. Ellis NA, Groden J, Ye TZ, Straughen J, Lennon DJ, Ciocci S, Proytcheva M, German J Cell Nov. 17, 1995
Characterization of a new BLM mutation associated with a topoisomerase II alpha defect in a patient with Bloom's syndrome. Foucault F, Vaury C, Barakat A, Thibout D, Planchon P, Jaulin C, Praz F, Amor-Gueret M Hum Mol Genet Sept. 1, 1997
BLM (the causative gene of Bloom syndrome) protein translocation into the nucleus by a nuclear localization signal. Kaneko H, Orii KO, Matsui E, Shimozawa N, Fukao T, Matsumoto T, Shimamoto A, Furuichi Y, Hayakawa S, Kasahara K, Kondo N Biochem Biophys Res Commun Nov. 17, 1997
The Bloom's syndrome gene product is a 3'-5' DNA helicase. Karow JK, Chakraverty RK, Hickson ID J Biol Chem Dec. 5, 1997
BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Wang Y, Cortez D, Yazdi P, Neff N, Elledge SJ, Qin J Genes Dev April 15, 2000
Identification of a novel BLM missense mutation (2706T>C) in a Moroccan patient with Bloom's syndrome. Barakat A, Ababou M, Onclercq R, Dutertre S, Chadli E, Hda N, Benslimane A, Amor-Gueret M Hum Mutat June 1, 2000
The BLM helicase is necessary for normal DNA double-strand break repair. Langland G, Elliott J, Li Y, Creaney J, Dixon K, Groden J Cancer Res May 15, 2002
BLM and the FANC proteins collaborate in a common pathway in response to stalled replication forks. Pichierri P, Franchitto A, Rosselli F EMBO J Aug. 4, 2004
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A Aug. 17, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity. Yin J, Sobeck A, Xu C, Meetei AR, Hoatlin M, Li L, Wang W EMBO J April 6, 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
A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIalpha, and BLAP75. Raynard S, Bussen W, Sung P J Biol Chem May 19, 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
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
RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability. Xu D, Guo R, Sobeck A, Bachrati CZ, Yang J, Enomoto T, Brown GW, Hoatlin ME, Hickson ID, Wang W Genes Dev Oct. 15, 2008
BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome. Singh TR, Ali AM, Busygina V, Raynard S, Fan Q, Du CH, Andreassen PR, Sung P, Meetei AR Genes Dev Oct. 15, 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
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
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
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science Aug. 14, 2009


Last modification of this entry: Oct. 11, 2010.

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