P54132 (BLM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bloom syndrome protein
EC=3.6.4.12

Alternative name(s):
DNA helicase, RecQ-like type 2
Short name=RecQ2
RecQ protein-like 3

Gene names

Name:	BLM
Synonyms:	RECQ2, RECQL3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1417 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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. Ref.2 Ref.8 Ref.20
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	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. Interacts with SUPV3L1. Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.20
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1. Ref.7 Ref.9
Involvement in disease	Bloom syndrome (BLM) [MIM:210900]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.21 Ref.22
Sequence similarities	Belongs to the helicase family. RecQ subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HRDC domain.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA double-strand break processing Inferred from direct assay Ref.20. Source: UniProtKB G2 DNA damage checkpoint Non-traceable author statement PubMed 11309417. Source: UniProtKB G2 phase of mitotic cell cycle Non-traceable author statement PubMed 11309417. Source: UniProtKB alpha-beta T cell differentiation Inferred from electronic annotation. Source: Compara double-strand break repair via homologous recombination Non-traceable author statement PubMed 11309417. Source: UniProtKB negative regulation of DNA recombination Inferred from mutant phenotype PubMed 9671747. Source: UniProtKB negative regulation of cell division Inferred from mutant phenotype PubMed 11781842. Source: UniProtKB negative regulation of mitotic recombination Inferred from electronic annotation. Source: Compara positive regulation of alpha-beta T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 11781842. Source: UniProtKB protein oligomerization Inferred from direct assay PubMed 10359700. Source: UniProtKB regulation of binding Inferred from electronic annotation. Source: Compara regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from mutant phenotype PubMed 15604258. Source: UniProtKB replication fork processing Inferred from direct assay PubMed 17115688. Source: UniProtKB replication fork protection Non-traceable author statement PubMed 10779560. Source: UniProtKB response to X-ray Inferred from direct assay PubMed 11309417. Source: UniProtKB telomere maintenance Inferred from electronic annotation. Source: Compara
Cellular_component	PML body Inferred from direct assay PubMed 10728666. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA lateral element Inferred from direct assay PubMed 10728666. Source: UniProtKB male germ cell nucleus Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from direct assay PubMed 11309417. Source: UniProtKB nucleolus Inferred from direct assay PubMed 10779560. Source: UniProtKB pronucleus Inferred from electronic annotation. Source: Compara replication fork Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from direct assay PubMed 17878217. Source: UniProtKB ATP-dependent 3'-5' DNA helicase activity Inferred from electronic annotation. Source: Compara ATP-dependent DNA helicase activity Inferred from direct assay Ref.2. Source: UniProtKB G-quadruplex DNA binding Inferred from direct assay PubMed 11433031. Source: UniProtKB annealing helicase activity Inferred from direct assay PubMed 17878217. Source: UniProtKB bubble DNA binding Inferred from direct assay PubMed 11433031. Source: UniProtKB four-way junction helicase activity Inferred from direct assay PubMed 11433031PubMed 12818200. Source: UniProtKB single-stranded DNA binding Inferred from direct assay PubMed 12818200. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FEN1	P39748	4	EBI-621372,EBI-707816
RMI1	Q9H9A7	7	EBI-621372,EBI-621339
RPA1	P27694	3	EBI-621372,EBI-621389
TERF1	P54274	3	EBI-621372,EBI-710997
TERF2	Q15554	8	EBI-621372,EBI-706637
WRN	Q14191	9	EBI-621372,EBI-368417

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1417

1417

Bloom syndrome protein

PRO_0000205039

Regions

Domain

676 – 851

176

Helicase ATP-binding

Domain

877 – 1024

148

Helicase C-terminal

Domain

1212 – 1292

81

HRDC

Nucleotide binding

689 – 696

8

ATP By similarity

Motif

795 – 798

4

DEAH box

Motif

1334 – 1349

16

Nuclear localization signal Potential

Compositional bias

292 – 299

8

Poly-Asp

Compositional bias

310 – 316

7

Poly-Ser

Compositional bias

557 – 566

10

Poly-Asp

Amino acid modifications

Modified residue

28

1

Phosphoserine Ref.18

Modified residue

48

1

Phosphoserine Ref.15

Modified residue

57

1

Phosphothreonine Ref.15

Modified residue

114

1

Phosphothreonine Ref.15

Modified residue

168

1

Phosphoserine Ref.18

Modified residue

171

1

Phosphothreonine Ref.18

Modified residue

358

1

Phosphoserine Ref.15

Modified residue

419

1

Phosphoserine Ref.15 Ref.18

Modified residue

422

1

Phosphoserine Ref.15 Ref.18

Modified residue

426

1

Phosphoserine Ref.18

Modified residue

499

1

Phosphoserine Ref.11 Ref.16

Modified residue

508

1

Phosphothreonine Ref.11

Modified residue

863

1

N6-acetyllysine Ref.17

Modified residue

1295

1

Phosphoserine Ref.15

Modified residue

1296

1

Phosphoserine Ref.15

Modified residue

1310

1

Phosphoserine Ref.15

Natural variations

Natural variant

137

1

K → R. Ref.3
Corresponds to variant rs28384988 [ dbSNP | Ensembl ].

VAR_022295

Natural variant

298

1

T → M. Ref.3
Corresponds to variant rs28384991 [ dbSNP | Ensembl ].

VAR_022296

Natural variant

591

1

R → Q. Ref.3
Corresponds to variant rs28385012 [ dbSNP | Ensembl ].

VAR_022297

Natural variant

672

1

Q → R in BLM. Ref.1

VAR_006901

Natural variant

841

1

I → T in BLM.

VAR_016032

Natural variant

843

1

T → I in BLM. Ref.1

VAR_006902

Natural variant

868

1

P → L. Ref.3
Corresponds to variant rs11852361 [ dbSNP | Ensembl ].

VAR_022298

Natural variant

878

1

C → R in BLM. Ref.22

VAR_016033

Natural variant

891

1

G → E in BLM.

VAR_009138

Natural variant

901

1

C → Y in BLM.

VAR_009139

Natural variant

1036

1

C → F in BLM. Ref.21

VAR_009140

Natural variant

1043

1

A → D.
Corresponds to variant rs2229035 [ dbSNP | Ensembl ].

VAR_051731

Natural variant

1055

1

C → S in BLM. Ref.1

VAR_006903

Natural variant

1205

1

V → I. Ref.3
Corresponds to variant rs28385141 [ dbSNP | Ensembl ].

VAR_022299

Natural variant

1209

1

S → T.
Corresponds to variant rs1801256 [ dbSNP | Ensembl ].

VAR_014912

Natural variant

1213

1

E → K. Ref.3
Corresponds to variant rs28385142 [ dbSNP | Ensembl ].

VAR_022300

Natural variant

1321

1

V → I. Ref.3
Corresponds to variant rs7167216 [ dbSNP | Ensembl ].

VAR_022301

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1417

Helix Strand Turn

Details...

Beta strand

1207 – 1209

3

Helix

1211 – 1233

23

Helix

1237 – 1240

4

Helix

1243 – 1252

10

Helix

1257 – 1261

5

Beta strand

1263 – 1265

3

Helix

1268 – 1273

6

Helix

1275 – 1288

14

Sequences

	Sequence		Length	Mass (Da)
	P54132 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 423DF5F381194E11	FASTA	1,417	159,000
	10 20 30 40 50 60 MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT NVSVAKTPVL 70 80 90 100 110 120 RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ RGGSKSLLPD FLQTPKEVVC 130 140 150 160 170 180 TTQNTPTVKK SRDTALKKLE FSSSPDSLST INDWDDMDDF DTSETSKSFV TPPQSHFVRV 190 200 210 220 230 240 STAQKSKKGK RNFFKAQLYT TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD 250 260 270 280 290 300 GPIAEVHINE DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF 310 320 330 340 350 360 VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM QELNPETSTD 370 380 390 400 410 420 CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL LQQRNIRRKL LTEVDFNKSD 430 440 450 460 470 480 ASLLGSLWRY RPDSLDGPME GDSCPTGNSM KELNFSHLPS NSVSPGDCLL TTTLGKTGFS 490 500 510 520 530 540 ATRKNLFERP LFNTHLQKSF VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI 550 560 570 580 590 600 NDLERETQPS YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL 610 620 630 640 650 660 SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP HTKEMMKIFH 670 680 690 700 710 720 KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ LPACVSPGVT VVISPLRSLI 730 740 750 760 770 780 VDQVQKLTSL DIPATYLTGD KTDSEATNIY LQLSKKDPII KLLYVTPEKI CASNRLISTL 790 800 810 820 830 840 ENLYERKLLA RFVIDEAHCV SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD 850 860 870 880 890 900 ILTQLKILRP QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE 910 920 930 940 950 960 CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG MGIDKPDVRF 970 980 990 1000 1010 1020 VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR LKRLIMMEKD GNHHTRETHF 1030 1040 1050 1060 1070 1080 NNLYSMVHYC ENITECRRIQ LLAYFGENGF NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD 1090 1100 1110 1120 1130 1140 VKSIVRFVQE HSSSQGMRNI KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH 1150 1160 1170 1180 1190 1200 NAERLFKKLI LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK 1210 1220 1230 1240 1250 1260 QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA ESLSSDPEVL 1270 1280 1290 1300 1310 1320 LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS LSSSRGPGRS AAEELDEEIP 1330 1340 1350 1360 1370 1380 VSSHYFASKT RNERKRKKMP ASQRSKRRKT ASSGSKAKGG SATCRKISSK TKSSSIIGSS 1390 1400 1410 SASHTSQATS GANSKLGIMA PPKPINRPFL KPSYAFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bloom's syndrome gene product is homologous to RecQ helicases." Ellis N.A., Groden J., Ye T.-Z., Straughen J., Lennon D.J., Ciocci S., Proytcheva M., German J. Cell 83:655-666(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS BLM ARG-672; ILE-843 AND SER-1055.
[2]	"The Bloom's syndrome gene product is a 3'-5' DNA helicase." Karow J.K., Chakraverty R.K., Hickson I.D. J. Biol. Chem. 272:30611-30614(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: B-cell.
[3]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-137; MET-298; GLN-591; LEU-868; ILE-1205 LYS-1213 AND ILE-1321.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"BLM (the causative gene of Bloom syndrome) protein translocation into the nucleus by a nuclear localization signal." Kaneko H., Orii K.O., Matsui E., Shimozawa N., Fukao T., Matsumoto T., Shimamoto A., Furuichi Y., Hayakawa S., Kasahara K., Kondo N. Biochem. Biophys. Res. Commun. 240:348-353(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEAR LOCALIZATION SIGNAL.
[6]	"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 S.J., Qin J. Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF BLM AS MEMBER OF BASC.
[7]	"BLM and the FANC proteins collaborate in a common pathway in response to stalled replication forks." Pichierri P., Franchitto A., Rosselli F. EMBO J. 23:3154-3163(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FANCD2, PHOSPHORYLATION.
[8]	"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. 62:2766-2770(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA REPAIR.
[9]	"BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity." Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W. EMBO J. 24:1465-1476(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RMI1, PHOSPHORYLATION.
[10]	"A double Holliday junction dissolvasome comprising BLM, topoisomerase III alpha, and BLAP75." Raynard S., Bussen W., Sung P. J. Biol. Chem. 281:13861-13864(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RMI1.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND THR-508, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of the SUV3 gene results in mouse embryonic lethality." 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. Mech. Ageing Dev. 128:609-617(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUPV3L1.
[13]	"RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability." Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W., Hoatlin M.E., Hickson I.D., Wang W. Genes Dev. 22:2843-2855(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RMI1.
[14]	"BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome." Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H., Andreassen P.R., Sung P., Meetei A.R. Genes Dev. 22:2856-2868(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RMI1.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-57; THR-114; SER-358; SER-419; SER-422; SER-1295; SER-1296 AND SER-1310, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-863, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-168; THR-171; SER-419; SER-422 AND SER-426, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair." Nimonkar A.V., Genschel J., Kinoshita E., Polaczek P., Campbell J.L., Wyman C., Modrich P., Kowalczykowski S.C. Genes Dev. 25:350-362(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DNA2.
[21]	"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. 6:1427-1434(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BLM PHE-1036.
[22]	"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. 15:584-585(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BLM ARG-878.
+	Additional computationally mapped references.

Web resources

BLMbase

BLM mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U39817 mRNA. Translation: AAA87850.1.
AY886902 Genomic DNA. Translation: AAW62255.1.
BC093622 mRNA. Translation: AAH93622.1.
BC101567 mRNA. Translation: AAI01568.1.
BC115030 mRNA. Translation: AAI15031.1.
BC115032 mRNA. Translation: AAI15033.1.

IPI

IPI00004859.

PIR

A57570.

RefSeq

NP_000048.1. NM_000057.2.

UniGene

Hs.725208.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KV2	NMR	-	A	1210-1294	[»]
2RRD	NMR	-	A	1200-1295	[»]

ProteinModelPortal

P54132.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33322N.

IntAct

P54132. 13 interactions.

MINT

MINT-131918.

STRING

9606.ENSP00000347232.

PTM databases

PhosphoSite

P54132.

Polymorphism databases

DMDM

1705486.

Proteomic databases

PaxDb

P54132.

PRIDE

P54132.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355112; ENSP00000347232; ENSG00000197299.

GeneID

641.

KEGG

hsa:641.

UCSC

uc002bpr.3. human.

Organism-specific databases

CTD

641.

GeneCards

GC15P091260.

HGNC

HGNC:1058. BLM.

HPA

HPA005689.

MIM

210900. phenotype.
604610. gene.

neXtProt

NX_P54132.

Orphanet

125. Bloom syndrome.

PharmGKB

PA25369.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0514.

HOGENOM

HOG000095239.

HOVERGEN

HBG004850.

InParanoid

P54132.

KO

K10901.

OMA

NANDQAI.

OrthoDB

EOG4640B3.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_111183. Meiosis.

Gene expression databases

ArrayExpress

P54132.

Bgee

P54132.

CleanEx

HS_BLM.

Genevestigator

P54132.

GermOnline

ENSG00000197299. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
1.10.150.80. 1 hit.

InterPro

IPR012532. BDHCT.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF08072. BDHCT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view]

SUPFAM

SSF47819. HRDC_like. 1 hit.

TIGRFAMs

TIGR00614. recQ_fam. 1 hit.

PROSITE

PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1293237.

EvolutionaryTrace

P54132.

GenomeRNAi

641.

NextBio

2600.

PMAP-CutDB

P54132.

SOURCE

Search...

Entry information

Entry name

BLM_HUMAN

Accession

Primary (citable) accession number: P54132
Secondary accession number(s): Q52M96

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.