Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Bloom syndrome protein (EC 3.6.4.12) (DNA helicase, RecQ-like type 2) (RecQ2) (RecQ protein-like 3)

 BLM_HUMAN               Reviewed;        1417 AA.
P54132; Q52M96;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=Bloom syndrome protein;
EC=3.6.4.12 {ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030};
AltName: Full=DNA helicase, RecQ-like type 2;
Short=RecQ2;
AltName: Full=RecQ protein-like 3;
Name=BLM; Synonyms=RECQ2, RECQL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS BLM ARG-672; ILE-843 AND
SER-1055.
PubMed=7585968; DOI=10.1016/0092-8674(95)90105-1;
Ellis N.A., Groden J., Ye T.-Z., Straughen J., Lennon D.J., Ciocci S.,
Proytcheva M., German J.;
"The Bloom's syndrome gene product is homologous to RecQ helicases.";
Cell 83:655-666(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=B-cell;
PubMed=9388193; DOI=10.1074/jbc.272.49.30611;
Karow J.K., Chakraverty R.K., Hickson I.D.;
"The Bloom's syndrome gene product is a 3'-5' DNA helicase.";
J. Biol. Chem. 272:30611-30614(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-137; MET-298;
GLN-591; LEU-868; ILE-1205 LYS-1213 AND ILE-1321.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEAR LOCALIZATION SIGNAL.
PubMed=9388480; DOI=10.1006/bbrc.1997.7648;
Kaneko H., Orii K.O., Matsui E., Shimozawa N., Fukao T., Matsumoto T.,
Shimamoto A., Furuichi Y., Hayakawa S., Kasahara K., Kondo N.;
"BLM (the causative gene of Bloom syndrome) protein translocation into
the nucleus by a nuclear localization signal.";
Biochem. Biophys. Res. Commun. 240:348-353(1997).
[6]
IDENTIFICATION OF BLM AS MEMBER OF BASC.
PubMed=10783165;
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
"BASC, a super complex of BRCA1-associated proteins involved in the
recognition and repair of aberrant DNA structures.";
Genes Dev. 14:927-939(2000).
[7]
INTERACTION WITH FANCD2, AND PHOSPHORYLATION.
PubMed=15257300; DOI=10.1038/sj.emboj.7600277;
Pichierri P., Franchitto A., Rosselli F.;
"BLM and the FANC proteins collaborate in a common pathway in response
to stalled replication forks.";
EMBO J. 23:3154-3163(2004).
[8]
FUNCTION IN DNA REPAIR.
PubMed=12019152;
Langland G., Elliott J., Li Y., Creaney J., Dixon K., Groden J.;
"The BLM helicase is necessary for normal DNA double-strand break
repair.";
Cancer Res. 62:2766-2770(2002).
[9]
IDENTIFICATION IN A COMPLEX WITH RMI1, AND PHOSPHORYLATION.
PubMed=15775963; DOI=10.1038/sj.emboj.7600622;
Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W.;
"BLAP75, an essential component of Bloom's syndrome protein complexes
that maintain genome integrity.";
EMBO J. 24:1465-1476(2005).
[10]
INTERACTION WITH RMI1.
PubMed=16595695; DOI=10.1074/jbc.C600051200;
Raynard S., Bussen W., Sung P.;
"A double Holliday junction dissolvasome comprising BLM, topoisomerase
III alpha, and BLAP75.";
J. Biol. Chem. 281:13861-13864(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND THR-508, 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).
[12]
INTERACTION WITH SUPV3L1.
PubMed=17961633; DOI=10.1016/j.mad.2007.09.001;
Pereira M., Mason P., Szczesny R.J., Maddukuri L., Dziwura S.,
Jedrzejczak R., Paul E., Wojcik A., Dybczynska L., Tudek B.,
Bartnik E., Klysik J., Bohr V.A., Stepien P.P.;
"Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of
the SUV3 gene results in mouse embryonic lethality.";
Mech. Ageing Dev. 128:609-617(2007).
[13]
INTERACTION WITH RMI1.
PubMed=18923082; DOI=10.1101/gad.1708608;
Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T.,
Brown G.W., Hoatlin M.E., Hickson I.D., Wang W.;
"RMI, a new OB-fold complex essential for Bloom syndrome protein to
maintain genome stability.";
Genes Dev. 22:2843-2855(2008).
[14]
INTERACTION WITH RMI1.
PubMed=18923083; DOI=10.1101/gad.1725108;
Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H.,
Andreassen P.R., Sung P., Meetei A.R.;
"BLAP18/RMI2, a novel OB-fold-containing protein, is an essential
component of the Bloom helicase-double Holliday junction
dissolvasome.";
Genes Dev. 22:2856-2868(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-57; THR-114;
SER-358; SER-419; SER-422; SER-1295; SER-1296 AND SER-1310, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-863, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-168; THR-171;
SER-419; SER-422 AND SER-426, 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).
[19]
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).
[20]
FUNCTION, AND INTERACTION WITH DNA2.
PubMed=21325134; DOI=10.1101/gad.2003811;
Nimonkar A.V., Genschel J., Kinoshita E., Polaczek P., Campbell J.L.,
Wyman C., Modrich P., Kowalczykowski S.C.;
"BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end
resection machineries for human DNA break repair.";
Genes Dev. 25:350-362(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; THR-171; SER-328;
SER-338; SER-358; SER-422; SER-464; SER-499; SER-1197 AND SER-1310,
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).
[22]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH SPIDR AND RAD51,
INTERACTION WITH RMI1; SPIDR AND TOP3A, AND SUBCELLULAR LOCATION.
PubMed=23509288; DOI=10.1073/pnas.1220921110;
Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.;
"Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
helicase with homologous recombination repair.";
Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-484, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-331 AND LYS-594, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-31; LYS-38; LYS-56;
LYS-63; LYS-87; LYS-91; LYS-105; LYS-116; LYS-129; LYS-195; LYS-205;
LYS-331; LYS-344; LYS-347; LYS-451; LYS-476; LYS-484; LYS-498;
LYS-513; LYS-514; LYS-531; LYS-535; LYS-588; LYS-594; LYS-604;
LYS-1125; LYS-1199; LYS-1207; LYS-1329; LYS-1372 AND LYS-1395, 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).
[26]
STRUCTURE BY NMR OF 1200-1295.
PubMed=20739603; DOI=10.1093/jb/mvq097;
Sato A., Mishima M., Nagai A., Kim S.Y., Ito Y., Hakoshima T.,
Jee J.G., Kitano K.;
"Solution structure of the HRDC domain of human Bloom syndrome protein
BLM.";
J. Biochem. 148:517-525(2010).
[27]
STRUCTURE BY NMR OF 1210-1294, MUTAGENESIS OF LYS-1227; TYR-1237;
ASN-1239; THR-1243 AND VAL-1244, DNA-BINDING, DOMAIN, AND REGION.
PubMed=20639533; DOI=10.1093/nar/gkq586;
Kim Y.M., Choi B.S.;
"Structure and function of the regulatory HRDC domain from human Bloom
syndrome protein.";
Nucleic Acids Res. 38:7764-7777(2010).
[28]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1068-1209, MUTAGENESIS OF
1094-SER--VAL-1103; SER-1121; LYS-1125 AND ARG-1139, DNA-BINDING, AND
REGION.
PubMed=24257077; DOI=10.1038/srep03294;
Kim S.Y., Hakoshima T., Kitano K.;
"Structure of the RecQ C-terminal domain of human Bloom syndrome
protein.";
Sci. Rep. 3:3294-3294(2013).
[29]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 640-1298 IN COMPLEX WITH
DNA; ADP AND ZINC IONS, FUNCTION, DNA-BINDING, CATALYTIC ACTIVITY,
COFACTOR, ZINC-BINDING MOTIF, DNA-BINDING DOMAIN, AND MUTAGENESIS OF
ASN-1164.
PubMed=24816114; DOI=10.1107/S139900471400501X;
Swan M.K., Legris V., Tanner A., Reaper P.M., Vial S., Bordas R.,
Pollard J.R., Charlton P.A., Golec J.M., Bertrand J.A.;
"Structure of human Bloom's syndrome helicase in complex with ADP and
duplex DNA.";
Acta Crystallogr. D 70:1465-1475(2014).
[30]
STRUCTURE BY NMR OF 1067-1210.
PubMed=24435566; DOI=10.1007/s10858-014-9812-8;
Park C.J., Ko J., Ryu K.S., Choi B.S.;
"Solution structure of the RecQ C-terminal domain of human Bloom
syndrome protein.";
J. Biomol. NMR 58:141-147(2014).
[31]
X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 636-1298 IN COMPLEX WITH
DNA; ADP AND ZINC IONS, FUNCTION, DNA-BINDING, CATALYTIC ACTIVITY,
COFACTOR, AND MUTAGENESIS OF HIS-666; SER-729 AND LYS-1270.
PubMed=25901030; DOI=10.1093/NAR/GKV373;
Newman J.A., Savitsky P., Allerston C.K., Bizard A.H., Ozer O.,
Sarlos K., Liu Y., Pardon E., Steyaert J., Hickson I.D., Gileadi O.;
"Crystal structure of the Bloom's syndrome heli case indicates a role
for the HRDC domain in conformational changes.";
Nucleic Acids Res. 43:5221-5235(2015).
[32]
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 362-414 OF HOMODIMER,
SUBUNIT, HOMOOLIGOMERIZATION, AND REGION.
PubMed=28228481; DOI=10.1074/jbc.M116.761510;
Shi J., Chen W.F., Zhang B., Fan S.H., Ai X., Liu N.N., Rety S.,
Xi X.G.;
"A helical bundle in the N-terminal domain of the BLM helicase
mediates dimer and potentially hexamer formation.";
J. Biol. Chem. 292:5909-5920(2017).
[33]
VARIANT BLM PHE-1036.
PubMed=9285778; DOI=10.1093/hmg/6.9.1427;
Foucault F., Vaury C., Barakat A., Thibout D., Planchon P., Jaulin C.,
Praz F., Amor-Gueret M.;
"Characterization of a new BLM mutation associated with a
topoisomerase II alpha defect in a patient with Bloom's syndrome.";
Hum. Mol. Genet. 6:1427-1434(1997).
[34]
VARIANT BLM ARG-878.
PubMed=10862105;
DOI=10.1002/1098-1004(200006)15:6<584::AID-HUMU28>3.0.CO;2-I;
Barakat A., Ababou M., Onclercq R., Dutertre S., Chadli E., Hda N.,
Benslimane A., Amor-Gueret M.;
"Identification of a novel BLM missense mutation (2706T>C) in a
Moroccan patient with Bloom's syndrome.";
Hum. Mutat. 15:584-585(2000).
-!- FUNCTION: ATP-dependent DNA helicase that unwinds single- and
double-stranded DNA in a 3'-5' direction (PubMed:9388193,
PubMed:24816114, PubMed:25901030). Participates in DNA replication
and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288).
Involved in 5'-end resection of DNA during double-strand break
(DSB) repair: unwinds DNA and recruits DNA2 which mediates the
cleavage of 5'-ssDNA (PubMed:21325134). Negatively regulates
sister chromatid exchange (SCE) (PubMed:25901030). Stimulates DNA
4-way junction branch migration and DNA Holliday junction
dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA),
forked duplex DNA and DNA Holliday junction (PubMed:20639533,
PubMed:24257077, PubMed:25901030). {ECO:0000269|PubMed:12019152,
ECO:0000269|PubMed:20639533, ECO:0000269|PubMed:21325134,
ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:24257077,
ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030,
ECO:0000269|PubMed:9388193}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030};
-!- SUBUNIT: Monomer (PubMed:28228481). Homodimer (via N-terminus)
(PubMed:28228481). Homotetramer (via N-terminus); dimer of dimers
(PubMed:28228481). Homohexamer (via N-terminus) (PubMed:28228481).
Self-association negatively regulates DNA unwinding amplitude and
rate. Oligomeric complexes dissociate into monomer in presence of
ATP (PubMed:28228481). 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 (via N-terminal region) component of RMI
complex. Interacts with SUPV3L1. Found in a complex, at least
composed of BLM, RAD51 and SPIDR; the complex formation is
mediated by SPIDR. Interacts with TOP3A (via N-terminal region).
Interacts with SPIDR (via C-terminal region); the interaction is
direct and required to target BLM to sites of DNA damage.
{ECO:0000269|PubMed:15257300, ECO:0000269|PubMed:15775963,
ECO:0000269|PubMed:16595695, ECO:0000269|PubMed:17961633,
ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083,
ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:23509288,
ECO:0000269|PubMed:28228481}.
-!- INTERACTION:
Q9BX63:BRIP1; NbExp=16; IntAct=EBI-621372, EBI-3509650;
P39748:FEN1; NbExp=4; IntAct=EBI-621372, EBI-707816;
P53350:PLK1; NbExp=4; IntAct=EBI-621372, EBI-476768;
O75771:RAD51D; NbExp=4; IntAct=EBI-621372, EBI-1055693;
Q9H9A7:RMI1; NbExp=12; IntAct=EBI-621372, EBI-621339;
P27694:RPA1; NbExp=4; IntAct=EBI-621372, EBI-621389;
P42677:RPS27; NbExp=4; IntAct=EBI-621372, EBI-356336;
P54274:TERF1; NbExp=3; IntAct=EBI-621372, EBI-710997;
Q15554:TERF2; NbExp=8; IntAct=EBI-621372, EBI-706637;
Q96RL1:UIMC1; NbExp=2; IntAct=EBI-621372, EBI-725300;
Q14191:WRN; NbExp=9; IntAct=EBI-621372, EBI-368417;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23509288}.
Note=Together with SPIDR, is redistributed in discrete nuclear DNA
damage-induced foci following hydroxyurea (HU) or camptothecin
(CPT) treatment. Accumulated at sites of DNA damage in a RMI
complex- and SPIDR-dependent manner.
-!- DOMAIN: The N-terminal region mediates dimerization and
homooligomerization (PubMed:28228481). Both the helicase ATP-
binding domain and the helicase C-terminal domain form
intramolecular interactions with the HRDC domain in a ATP-
dependent manner (PubMed:25901030). The HRDC domain is required
for single-stranded DNA (ssDNA) and DNA Holliday junction binding
(PubMed:20639533). {ECO:0000269|PubMed:20639533,
ECO:0000269|PubMed:25901030, ECO:0000269|PubMed:28228481}.
-!- PTM: Phosphorylated in response to DNA damage. Phosphorylation
requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as
well as the presence of RMI1. {ECO:0000269|PubMed:15257300,
ECO:0000269|PubMed:15775963}.
-!- DISEASE: Bloom syndrome (BLM) [MIM:210900]: An autosomal recessive
disorder. It is characterized by proportionate pre- and postnatal
growth deficiency, sun-sensitive telangiectatic hypo- and
hyperpigmented skin, predisposition to malignancy, and chromosomal
instability. {ECO:0000269|PubMed:10862105,
ECO:0000269|PubMed:7585968, ECO:0000269|PubMed:9285778}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=BLMbase; Note=BLM mutation db;
URL="http://structure.bmc.lu.se/idbase/BLMbase/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BLMID109.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/blm/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U39817; AAA87850.1; -; mRNA.
EMBL; AY886902; AAW62255.1; -; Genomic_DNA.
EMBL; BC093622; AAH93622.1; -; mRNA.
EMBL; BC101567; AAI01568.1; -; mRNA.
EMBL; BC115030; AAI15031.1; -; mRNA.
EMBL; BC115032; AAI15033.1; -; mRNA.
CCDS; CCDS10363.1; -.
PIR; A57570; A57570.
RefSeq; NP_000048.1; NM_000057.3.
RefSeq; NP_001274175.1; NM_001287246.1.
RefSeq; NP_001274176.1; NM_001287247.1.
RefSeq; NP_001274177.1; NM_001287248.1.
UniGene; Hs.725208; -.
PDB; 2KV2; NMR; -; A=1210-1294.
PDB; 2MH9; NMR; -; A=1067-1210.
PDB; 2RRD; NMR; -; A=1200-1295.
PDB; 3WE2; X-ray; 2.70 A; A/B=1068-1209.
PDB; 3WE3; X-ray; 2.90 A; A/B=1068-1209.
PDB; 4CDG; X-ray; 2.79 A; A/B=636-1298.
PDB; 4CGZ; X-ray; 3.20 A; A=636-1298.
PDB; 4O3M; X-ray; 2.30 A; A=640-1298.
PDB; 5LUP; X-ray; 2.03 A; A/B/C/D/E/F/G/I/J/K/L=362-414, H=367-414.
PDB; 5MK5; X-ray; 2.16 A; A/B/C/D=362-414.
PDBsum; 2KV2; -.
PDBsum; 2MH9; -.
PDBsum; 2RRD; -.
PDBsum; 3WE2; -.
PDBsum; 3WE3; -.
PDBsum; 4CDG; -.
PDBsum; 4CGZ; -.
PDBsum; 4O3M; -.
PDBsum; 5LUP; -.
PDBsum; 5MK5; -.
ProteinModelPortal; P54132; -.
SMR; P54132; -.
BioGrid; 107110; 135.
CORUM; P54132; -.
DIP; DIP-33322N; -.
ELM; P54132; -.
IntAct; P54132; 43.
MINT; MINT-131918; -.
STRING; 9606.ENSP00000347232; -.
BindingDB; P54132; -.
ChEMBL; CHEMBL1293237; -.
iPTMnet; P54132; -.
PhosphoSitePlus; P54132; -.
BioMuta; BLM; -.
DMDM; 1705486; -.
EPD; P54132; -.
MaxQB; P54132; -.
PaxDb; P54132; -.
PeptideAtlas; P54132; -.
PRIDE; P54132; -.
Ensembl; ENST00000355112; ENSP00000347232; ENSG00000197299.
GeneID; 641; -.
KEGG; hsa:641; -.
UCSC; uc002bpr.5; human.
CTD; 641; -.
DisGeNET; 641; -.
EuPathDB; HostDB:ENSG00000197299.10; -.
GeneCards; BLM; -.
GeneReviews; BLM; -.
HGNC; HGNC:1058; BLM.
HPA; HPA005689; -.
MalaCards; BLM; -.
MIM; 210900; phenotype.
MIM; 604610; gene.
neXtProt; NX_P54132; -.
OpenTargets; ENSG00000197299; -.
Orphanet; 125; Bloom syndrome.
PharmGKB; PA25369; -.
eggNOG; KOG0351; Eukaryota.
eggNOG; COG0514; LUCA.
GeneTree; ENSGT00550000074520; -.
HOGENOM; HOG000095239; -.
HOVERGEN; HBG004850; -.
InParanoid; P54132; -.
KO; K10901; -.
OMA; CENITEC; -.
OrthoDB; EOG091G021X; -.
PhylomeDB; P54132; -.
TreeFam; TF317801; -.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-912446; Meiotic recombination.
SIGNOR; P54132; -.
EvolutionaryTrace; P54132; -.
GeneWiki; Bloom_syndrome_protein; -.
GenomeRNAi; 641; -.
PMAP-CutDB; P54132; -.
PRO; PR:P54132; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000197299; -.
CleanEx; HS_BLM; -.
ExpressionAtlas; P54132; baseline and differential.
Genevisible; P54132; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000800; C:lateral element; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; ISS:BHF-UCL.
GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; IDA:BHF-UCL.
GO; GO:0036310; F:annealing helicase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IBA:GO_Central.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:UniProtKB.
GO; GO:0008026; F:ATP-dependent helicase activity; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003678; F:DNA helicase activity; IDA:BHF-UCL.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0061749; F:forked DNA-dependent helicase activity; IDA:UniProtKB.
GO; GO:0000400; F:four-way junction DNA binding; IDA:UniProtKB.
GO; GO:0009378; F:four-way junction helicase activity; IDA:UniProtKB.
GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0061821; F:telomeric D-loop binding; IDA:BHF-UCL.
GO; GO:0061849; F:telomeric G-quadruplex DNA binding; IC:BHF-UCL.
GO; GO:0000403; F:Y-form DNA binding; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0072757; P:cellular response to camptothecin; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; IDA:UniProtKB.
GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; IDA:UniProtKB.
GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
GO; GO:0006310; P:DNA recombination; NAS:UniProtKB.
GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
GO; GO:0006260; P:DNA replication; ISS:BHF-UCL.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:BHF-UCL.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0051782; P:negative regulation of cell division; IMP:UniProtKB.
GO; GO:0045910; P:negative regulation of DNA recombination; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0035786; P:protein complex oligomerization; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0090329; P:regulation of DNA-dependent DNA replication; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
GO; GO:0048478; P:replication fork protection; NAS:UniProtKB.
GO; GO:0010165; P:response to X-ray; IDA:UniProtKB.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0090656; P:t-circle formation; TAS:BHF-UCL.
GO; GO:0061820; P:telomeric D-loop disassembly; IDA:BHF-UCL.
CDD; cd00079; HELICc; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR012532; BDHCT.
InterPro; IPR032439; BDHCT_assoc.
InterPro; IPR032437; BLM_N.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR010997; HRDC-like.
InterPro; IPR002121; HRDC_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032284; RecQ_Zn-bd.
InterPro; IPR018982; RQC_domain.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF08072; BDHCT; 1.
Pfam; PF16204; BDHCT_assoc; 1.
Pfam; PF16202; BLM_N; 1.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00570; HRDC; 1.
Pfam; PF16124; RecQ_Zn_bind; 1.
Pfam; PF09382; RQC; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00341; HRDC; 1.
SMART; SM00956; RQC; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF47819; SSF47819; 1.
SUPFAM; SSF52540; SSF52540; 3.
TIGRFAMs; TIGR00614; recQ_fam; 1.
PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50967; HRDC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome;
Disease mutation; DNA damage; DNA repair; DNA replication;
DNA-binding; Dwarfism; Helicase; Hydrolase; Isopeptide bond;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation; Zinc.
CHAIN 1 1417 Bloom syndrome protein.
/FTId=PRO_0000205039.
DOMAIN 676 851 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541,
ECO:0000305|PubMed:24816114}.
DOMAIN 877 1024 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542,
ECO:0000305|PubMed:24816114}.
DOMAIN 1212 1292 HRDC. {ECO:0000255|PROSITE-
ProRule:PRU00328,
ECO:0000269|PubMed:20639533,
ECO:0000305|PubMed:20639533}.
NP_BIND 668 672 ATP. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
NP_BIND 692 696 ATP. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
REGION 301 600 Necessary for interaction with SPIDR.
{ECO:0000269|PubMed:23509288}.
REGION 362 414 Necessary for dimerization and
homooligomerization.
{ECO:0000269|PubMed:28228481}.
REGION 870 873 3' overhang DNA-binding.
{ECO:0000269|PubMed:25901030}.
REGION 897 899 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
REGION 1000 1003 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
REGION 1094 1139 DNA Holliday junction binding.
{ECO:0000269|PubMed:24257077}.
REGION 1110 1112 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
REGION 1121 1125 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
REGION 1160 1166 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
REGION 1227 1244 Necessary for ssDNA and DNA Holliday
junction binding.
{ECO:0000269|PubMed:20639533}.
MOTIF 795 798 DEAH box.
MOTIF 1334 1349 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 292 299 Poly-Asp.
COMPBIAS 310 316 Poly-Ser.
COMPBIAS 557 566 Poly-Asp.
METAL 1036 1036 Zinc. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
METAL 1055 1055 Zinc. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
METAL 1063 1063 Zinc. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
METAL 1066 1066 Zinc. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
BINDING 982 982 ATP. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000269|PubMed:25901030}.
BINDING 1242 1242 ATP. {ECO:0000244|PDB:4CDG,
ECO:0000244|PDB:4CGZ,
ECO:0000269|PubMed:25901030}.
SITE 717 717 3' overhang DNA-binding.
{ECO:0000269|PubMed:25901030}.
SITE 808 808 3' overhang DNA-binding.
{ECO:0000269|PubMed:25901030}.
SITE 920 920 3' overhang DNA-binding; via amide
nitrogen. {ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
SITE 946 946 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
SITE 968 968 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
SITE 1110 1110 3' overhang DNA-binding.
{ECO:0000244|PDB:4CGZ,
ECO:0000244|PDB:4O3M,
ECO:0000269|PubMed:24816114,
ECO:0000269|PubMed:25901030}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 114 114 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 171 171 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 426 426 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 508 508 Phosphothreonine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 863 863 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1197 1197 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1295 1295 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1310 1310 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 24 24 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 38 38 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 87 87 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 91 91 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 205 205 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 344 344 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 347 347 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 484 484 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 498 498 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 513 513 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 514 514 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 531 531 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 535 535 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 588 588 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 594 594 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 604 604 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1125 1125 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1199 1199 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1207 1207 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1329 1329 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1372 1372 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1395 1395 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 137 137 K -> R (in dbSNP:rs28384988).
{ECO:0000269|Ref.3}.
/FTId=VAR_022295.
VARIANT 298 298 T -> M (in dbSNP:rs28384991).
{ECO:0000269|Ref.3}.
/FTId=VAR_022296.
VARIANT 591 591 R -> Q (in dbSNP:rs28385012).
{ECO:0000269|Ref.3}.
/FTId=VAR_022297.
VARIANT 672 672 Q -> R (in BLM; dbSNP:rs747281324).
{ECO:0000269|PubMed:7585968}.
/FTId=VAR_006901.
VARIANT 841 841 I -> T (in BLM; dbSNP:rs767086502).
/FTId=VAR_016032.
VARIANT 843 843 T -> I (in BLM; dbSNP:rs137853152).
{ECO:0000269|PubMed:7585968}.
/FTId=VAR_006902.
VARIANT 868 868 P -> L (in dbSNP:rs2227935).
{ECO:0000269|Ref.3}.
/FTId=VAR_022298.
VARIANT 878 878 C -> R (in BLM).
{ECO:0000269|PubMed:10862105}.
/FTId=VAR_016033.
VARIANT 891 891 G -> E (in BLM).
/FTId=VAR_009138.
VARIANT 901 901 C -> Y (in BLM; dbSNP:rs758311406).
/FTId=VAR_009139.
VARIANT 1036 1036 C -> F (in BLM; dbSNP:rs137853153).
{ECO:0000269|PubMed:9285778}.
/FTId=VAR_009140.
VARIANT 1043 1043 A -> D (in dbSNP:rs2229035).
/FTId=VAR_051731.
VARIANT 1055 1055 C -> S (in BLM; dbSNP:rs367543029).
{ECO:0000269|PubMed:7585968}.
/FTId=VAR_006903.
VARIANT 1205 1205 V -> I (in dbSNP:rs28385141).
/FTId=VAR_022299.
VARIANT 1209 1209 S -> T (in dbSNP:rs1801256).
/FTId=VAR_014912.
VARIANT 1213 1213 E -> K (in dbSNP:rs28385142).
{ECO:0000269|Ref.3}.
/FTId=VAR_022300.
VARIANT 1321 1321 V -> I (in dbSNP:rs7167216).
{ECO:0000269|Ref.3}.
/FTId=VAR_022301.
MUTAGEN 666 666 H->A: Reduced intramolecular association
between both the helicase ATP-binding
domain and the helicase C-terminal domain
with the HRDC domain. No change in forked
duplex DNA helicase activity. No change
in DNA 4-way junction branch migration
and Holliday junction dissolution
activities. No change in suppression of
enhanced sister chromatide exchange
activity. {ECO:0000269|PubMed:25901030}.
MUTAGEN 729 729 S->A: Reduced intramolecular interaction
between both the helicase ATP-binding
domain and the helicase C-terminal domain
with the HRDC domain. No change in forked
duplex DNA helicase activity. No change
in DNA 4-way junction branch migration
and Holliday junction dissolution
activities. No change in suppression of
enhanced sister chromatide exchange
activity. {ECO:0000269|PubMed:25901030}.
MUTAGEN 1094 1103 Missing: Decreased DNA Holliday junction
binding. {ECO:0000269|PubMed:24257077}.
MUTAGEN 1121 1121 S->A: Decreased slightly DNA Holliday
junction binding.
{ECO:0000269|PubMed:24257077}.
MUTAGEN 1125 1125 K->A: Decreased DNA Holliday junction
binding. {ECO:0000269|PubMed:24257077}.
MUTAGEN 1139 1139 R->A: Decreased strongly DNA Holliday
junction binding.
{ECO:0000269|PubMed:24257077}.
MUTAGEN 1164 1164 N->A: Reduced strongly DNA helicase
activity. {ECO:0000269|PubMed:24816114}.
MUTAGEN 1227 1227 K->E: Reduced ssDNA binding. No change in
DNA Holliday junction binding.
{ECO:0000269|PubMed:20639533}.
MUTAGEN 1237 1237 Y->A: No change in ssDNA binding.
Increased DNA Holliday junction binding.
{ECO:0000269|PubMed:20639533}.
MUTAGEN 1239 1239 N->D: Reduced ssDNA binding. No change in
DNA Holliday junction binding.
{ECO:0000269|PubMed:20639533}.
MUTAGEN 1243 1243 T->A: No change in ssDNA binding.
Decreased DNA Holliday junction binding.
{ECO:0000269|PubMed:20639533}.
MUTAGEN 1244 1244 V->A: Reduced ssDNA binding. Increased
DNA Holliday junction binding.
{ECO:0000269|PubMed:20639533}.
MUTAGEN 1270 1270 K->V: Reduced intramolecular interaction
between both the helicase ATP-binding
domain and the helicase C-terminal domain
with the HRDC domain.
{ECO:0000269|PubMed:25901030}.
HELIX 365 384 {ECO:0000244|PDB:5MK5}.
HELIX 388 391 {ECO:0000244|PDB:5MK5}.
HELIX 397 411 {ECO:0000244|PDB:5MK5}.
HELIX 643 645 {ECO:0000244|PDB:4O3M}.
HELIX 652 661 {ECO:0000244|PDB:4O3M}.
HELIX 672 680 {ECO:0000244|PDB:4O3M}.
STRAND 685 688 {ECO:0000244|PDB:4O3M}.
HELIX 697 705 {ECO:0000244|PDB:4O3M}.
STRAND 706 713 {ECO:0000244|PDB:4O3M}.
HELIX 717 729 {ECO:0000244|PDB:4O3M}.
STRAND 734 741 {ECO:0000244|PDB:4O3M}.
HELIX 743 753 {ECO:0000244|PDB:4O3M}.
STRAND 755 757 {ECO:0000244|PDB:4O3M}.
STRAND 762 765 {ECO:0000244|PDB:4O3M}.
HELIX 769 772 {ECO:0000244|PDB:4O3M}.
HELIX 774 785 {ECO:0000244|PDB:4O3M}.
STRAND 789 795 {ECO:0000244|PDB:4O3M}.
HELIX 797 800 {ECO:0000244|PDB:4CDG}.
HELIX 811 820 {ECO:0000244|PDB:4O3M}.
STRAND 826 830 {ECO:0000244|PDB:4O3M}.
HELIX 835 845 {ECO:0000244|PDB:4O3M}.
STRAND 851 853 {ECO:0000244|PDB:4O3M}.
STRAND 862 868 {ECO:0000244|PDB:4O3M}.
HELIX 871 873 {ECO:0000244|PDB:4O3M}.
HELIX 874 885 {ECO:0000244|PDB:4O3M}.
STRAND 891 894 {ECO:0000244|PDB:4O3M}.
HELIX 898 910 {ECO:0000244|PDB:4O3M}.
STRAND 915 919 {ECO:0000244|PDB:4O3M}.
HELIX 924 935 {ECO:0000244|PDB:4O3M}.
STRAND 941 945 {ECO:0000244|PDB:4O3M}.
HELIX 947 950 {ECO:0000244|PDB:4CDG}.
STRAND 960 965 {ECO:0000244|PDB:4O3M}.
HELIX 970 977 {ECO:0000244|PDB:4O3M}.
TURN 979 983 {ECO:0000244|PDB:4CDG}.
STRAND 987 993 {ECO:0000244|PDB:4O3M}.
HELIX 995 1005 {ECO:0000244|PDB:4O3M}.
HELIX 1015 1031 {ECO:0000244|PDB:4O3M}.
HELIX 1037 1044 {ECO:0000244|PDB:4O3M}.
HELIX 1054 1057 {ECO:0000244|PDB:4O3M}.
HELIX 1059 1061 {ECO:0000244|PDB:4O3M}.
HELIX 1064 1067 {ECO:0000244|PDB:4O3M}.
TURN 1069 1071 {ECO:0000244|PDB:4CDG}.
STRAND 1074 1076 {ECO:0000244|PDB:4CDG}.
HELIX 1078 1090 {ECO:0000244|PDB:4O3M}.
STRAND 1096 1099 {ECO:0000244|PDB:3WE2}.
HELIX 1111 1119 {ECO:0000244|PDB:4O3M}.
TURN 1129 1136 {ECO:0000244|PDB:4O3M}.
HELIX 1139 1151 {ECO:0000244|PDB:4O3M}.
STRAND 1154 1161 {ECO:0000244|PDB:4O3M}.
STRAND 1163 1166 {ECO:0000244|PDB:4CGZ}.
STRAND 1167 1173 {ECO:0000244|PDB:4O3M}.
HELIX 1177 1181 {ECO:0000244|PDB:4O3M}.
STRAND 1188 1190 {ECO:0000244|PDB:4CDG}.
HELIX 1195 1197 {ECO:0000244|PDB:4CDG}.
STRAND 1207 1209 {ECO:0000244|PDB:2RRD}.
HELIX 1210 1233 {ECO:0000244|PDB:4O3M}.
HELIX 1237 1239 {ECO:0000244|PDB:4O3M}.
HELIX 1243 1252 {ECO:0000244|PDB:4O3M}.
HELIX 1257 1260 {ECO:0000244|PDB:4O3M}.
STRAND 1263 1265 {ECO:0000244|PDB:2KV2}.
HELIX 1268 1283 {ECO:0000244|PDB:4O3M}.
TURN 1284 1288 {ECO:0000244|PDB:4O3M}.
SEQUENCE 1417 AA; 159000 MW; 423DF5F381194E11 CRC64;
MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT NVSVAKTPVL
RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ RGGSKSLLPD FLQTPKEVVC
TTQNTPTVKK SRDTALKKLE FSSSPDSLST INDWDDMDDF DTSETSKSFV TPPQSHFVRV
STAQKSKKGK RNFFKAQLYT TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD
GPIAEVHINE DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF
VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM QELNPETSTD
CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL LQQRNIRRKL LTEVDFNKSD
ASLLGSLWRY RPDSLDGPME GDSCPTGNSM KELNFSHLPS NSVSPGDCLL TTTLGKTGFS
ATRKNLFERP LFNTHLQKSF VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI
NDLERETQPS YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL
SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP HTKEMMKIFH
KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ LPACVSPGVT VVISPLRSLI
VDQVQKLTSL DIPATYLTGD KTDSEATNIY LQLSKKDPII KLLYVTPEKI CASNRLISTL
ENLYERKLLA RFVIDEAHCV SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD
ILTQLKILRP QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE
CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG MGIDKPDVRF
VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR LKRLIMMEKD GNHHTRETHF
NNLYSMVHYC ENITECRRIQ LLAYFGENGF NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD
VKSIVRFVQE HSSSQGMRNI KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH
NAERLFKKLI LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK
QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA ESLSSDPEVL
LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS LSSSRGPGRS AAEELDEEIP
VSSHYFASKT RNERKRKKMP ASQRSKRRKT ASSGSKAKGG SATCRKISSK TKSSSIIGSS
SASHTSQATS GANSKLGIMA PPKPINRPFL KPSYAFS


Related products :

Catalog number Product name Quantity
EIAAB46449 DNA helicase, RecQ-like type 3,Exonuclease WRN,Homo sapiens,Human,RecQ protein-like 2,RecQ3,RECQ3,RECQL2,Werner syndrome ATP-dependent helicase,WRN
BLNK BLM Gene Bloom syndrome, RecQ helicase-like
18-272-197053 Blooms Syndrome Protein Blm - Rabbit polyclonal to Blooms Syndrome Protein Blm; EC 3.6.1.-; RecQ protein-like 3; DNA helicase. RecQ-like type 2 Polyclonal 0.05 mg
EIAAB34190 ATP-dependent DNA helicase Q4,DNA helicase, RecQ-like type 4,Homo sapiens,Human,RecQ protein-like 4,RecQ4,RECQ4,RECQL4,RTS
EIAAB34191 ATP-dependent DNA helicase Q5,DNA helicase, RecQ-like type 5,Homo sapiens,Human,RecQ protein-like 5,RecQ5,RECQ5,RECQL5
EIAAB34189 ATP-dependent DNA helicase Q4,DNA helicase, RecQ-like type 4,Mouse,Mus musculus,RecQ protein-like 4,RecQ4,Recq4,Recql4
CSB-EL002715CH Chicken Bloom syndrome, RecQ helicase-like (BLM) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL002715MO Mouse Bloom syndrome, RecQ helicase-like (BLM) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL002715HU Human Bloom syndrome, RecQ helicase-like (BLM) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB34186 ATP-dependent DNA helicase Q1,DNA helicase, RecQ-like type 1,DNA-dependent ATPase Q1,Homo sapiens,Human,RecQ protein-like 1,RecQ1,RECQ1,RECQL,RECQL1
WRN WRN Gene Werner syndrome, RecQ helicase-like
CSB-EL026149MO Mouse Werner syndrome, RecQ helicase-like (WRN) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL026149HU Human Werner syndrome, RecQ helicase-like (WRN) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL019537RA Rat RecQ protein-like (DNA helicase Q1-like) (RECQL) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL019537HU Human RecQ protein-like (DNA helicase Q1-like) (RECQL) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL019537MO Mouse RecQ protein-like (DNA helicase Q1-like) (RECQL) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB34187 ATP-dependent DNA helicase Q1,DNA-dependent ATPase Q1,Mouse,Mus musculus,RecQ protein-like 1,Recql,Recql1
EIAAB34188 ATP-dependent DNA helicase Q1,DNA-dependent ATPase Q1,Rat,Rattus norvegicus,RecQ protein-like 1,Recql,Recql1
RECQL RECQL Gene RecQ protein-like (DNA helicase Q1-like)
01-004 E.coli RecQ DNA helicase E.coli RecQ DNA helicase 100 ug
01-003 E.coli RecQ DNA helicase E.coli RecQ DNA helicase 20 ug
01-004 E.coli RecQ DNA helicase 100ug
01-003 E.coli RecQ DNA helicase 20ug
01-004 E.coli RecQ DNA helicase 100ug
01-003 E.coli RecQ DNA helicase 20ug


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur