Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bloom syndrome protein

Gene

BLM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Negatively regulates sister chromatid exchange (SCE).4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi689 – 696ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • annealing helicase activity Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • ATP-dependent 3'-5' DNA helicase activity Source: GO_Central
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • ATP-dependent helicase activity Source: UniProtKB
  • bubble DNA binding Source: UniProtKB
  • four-way junction helicase activity Source: UniProtKB
  • G-quadruplex DNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB
  • p53 binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to camptothecin Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydroxyurea Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • DNA double-strand break processing Source: UniProtKB
  • DNA recombination Source: UniProtKB
  • DNA repair Source: UniProtKB
  • DNA replication Source: Reactome
  • DNA synthesis involved in DNA repair Source: Reactome
  • double-strand break repair via homologous recombination Source: UniProtKB
  • mitotic G2 DNA damage checkpoint Source: UniProtKB
  • negative regulation of cell division Source: UniProtKB
  • negative regulation of DNA recombination Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein oligomerization Source: UniProtKB
  • protein sumoylation Source: Reactome
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • replication fork processing Source: UniProtKB
  • replication fork protection Source: UniProtKB
  • response to X-ray Source: UniProtKB
  • strand displacement Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiP54132.

Names & Taxonomyi

Protein namesi
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 namesi
Name:BLM
Synonyms:RECQ2, RECQL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:1058. BLM.

Subcellular locationi

  • Nucleus 1 Publication

  • 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.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • lateral element Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Bloom syndrome (BLM)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:210900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006901672Q → R in BLM. 1 PublicationCorresponds to variant rs747281324dbSNPEnsembl.1
Natural variantiVAR_016032841I → T in BLM. Corresponds to variant rs767086502dbSNPEnsembl.1
Natural variantiVAR_006902843T → I in BLM. 1 PublicationCorresponds to variant rs137853152dbSNPEnsembl.1
Natural variantiVAR_016033878C → R in BLM. 1 Publication1
Natural variantiVAR_009138891G → E in BLM. 1
Natural variantiVAR_009139901C → Y in BLM. Corresponds to variant rs758311406dbSNPEnsembl.1
Natural variantiVAR_0091401036C → F in BLM. 1 PublicationCorresponds to variant rs137853153dbSNPEnsembl.1
Natural variantiVAR_0069031055C → S in BLM. 1 PublicationCorresponds to variant rs367543029dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi641.
MalaCardsiBLM.
MIMi210900. phenotype.
OpenTargetsiENSG00000197299.
Orphaneti125. Bloom syndrome.
PharmGKBiPA25369.

Chemistry databases

ChEMBLiCHEMBL1293237.

Polymorphism and mutation databases

BioMutaiBLM.
DMDMi1705486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050391 – 1417Bloom syndrome proteinAdd BLAST1417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineCombined sources1
Modified residuei48PhosphoserineCombined sources1
Modified residuei57PhosphothreonineCombined sources1
Modified residuei114PhosphothreonineCombined sources1
Modified residuei168PhosphoserineCombined sources1
Modified residuei171PhosphothreonineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Cross-linki331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei338PhosphoserineCombined sources1
Modified residuei358PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei464PhosphoserineCombined sources1
Cross-linki484Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei499PhosphoserineCombined sources1
Modified residuei508PhosphothreonineCombined sources1
Cross-linki594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei863N6-acetyllysineCombined sources1
Modified residuei1197PhosphoserineCombined sources1
Modified residuei1295PhosphoserineCombined sources1
Modified residuei1296PhosphoserineCombined sources1
Modified residuei1310PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP54132.
MaxQBiP54132.
PaxDbiP54132.
PeptideAtlasiP54132.
PRIDEiP54132.

PTM databases

iPTMnetiP54132.
PhosphoSitePlusiP54132.

Miscellaneous databases

PMAP-CutDBP54132.

Expressioni

Gene expression databases

BgeeiENSG00000197299.
CleanExiHS_BLM.
ExpressionAtlasiP54132. baseline and differential.
GenevisibleiP54132. HS.

Organism-specific databases

HPAiHPA005689.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRIP1Q9BX6316EBI-621372,EBI-3509650
FEN1P397484EBI-621372,EBI-707816
RAD51DO757714EBI-621372,EBI-1055693
RMI1Q9H9A711EBI-621372,EBI-621339
RPA1P276944EBI-621372,EBI-621389
TERF1P542743EBI-621372,EBI-710997
TERF2Q155548EBI-621372,EBI-706637
UIMC1Q96RL12EBI-621372,EBI-725300
WRNQ141919EBI-621372,EBI-368417

GO - Molecular functioni

  • p53 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107110. 123 interactors.
DIPiDIP-33322N.
IntActiP54132. 37 interactors.
MINTiMINT-131918.
STRINGi9606.ENSP00000347232.

Chemistry databases

BindingDBiP54132.

Structurei

Secondary structure

11417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi643 – 645Combined sources3
Helixi652 – 661Combined sources10
Helixi672 – 680Combined sources9
Beta strandi685 – 688Combined sources4
Helixi697 – 705Combined sources9
Beta strandi706 – 713Combined sources8
Helixi717 – 729Combined sources13
Beta strandi734 – 741Combined sources8
Helixi743 – 753Combined sources11
Beta strandi755 – 757Combined sources3
Beta strandi762 – 765Combined sources4
Helixi769 – 772Combined sources4
Helixi774 – 785Combined sources12
Beta strandi789 – 795Combined sources7
Helixi797 – 800Combined sources4
Helixi811 – 820Combined sources10
Beta strandi826 – 830Combined sources5
Helixi835 – 845Combined sources11
Beta strandi851 – 853Combined sources3
Beta strandi862 – 868Combined sources7
Helixi871 – 873Combined sources3
Helixi874 – 885Combined sources12
Beta strandi891 – 894Combined sources4
Helixi898 – 910Combined sources13
Beta strandi915 – 919Combined sources5
Helixi924 – 935Combined sources12
Beta strandi941 – 945Combined sources5
Helixi947 – 950Combined sources4
Beta strandi960 – 965Combined sources6
Helixi970 – 977Combined sources8
Turni979 – 983Combined sources5
Beta strandi987 – 993Combined sources7
Helixi995 – 1005Combined sources11
Helixi1015 – 1031Combined sources17
Helixi1037 – 1044Combined sources8
Helixi1054 – 1057Combined sources4
Helixi1059 – 1061Combined sources3
Helixi1064 – 1067Combined sources4
Turni1069 – 1071Combined sources3
Beta strandi1074 – 1076Combined sources3
Helixi1078 – 1090Combined sources13
Beta strandi1096 – 1099Combined sources4
Helixi1111 – 1119Combined sources9
Turni1129 – 1136Combined sources8
Helixi1139 – 1151Combined sources13
Beta strandi1154 – 1161Combined sources8
Beta strandi1163 – 1166Combined sources4
Beta strandi1167 – 1173Combined sources7
Helixi1177 – 1181Combined sources5
Beta strandi1188 – 1190Combined sources3
Helixi1195 – 1197Combined sources3
Beta strandi1207 – 1209Combined sources3
Helixi1210 – 1233Combined sources24
Helixi1237 – 1239Combined sources3
Helixi1243 – 1252Combined sources10
Helixi1257 – 1260Combined sources4
Beta strandi1263 – 1265Combined sources3
Helixi1268 – 1283Combined sources16
Turni1284 – 1288Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KV2NMR-A1210-1294[»]
2MH9NMR-A1067-1210[»]
2RRDNMR-A1200-1295[»]
3WE2X-ray2.70A/B1068-1209[»]
3WE3X-ray2.90A/B1068-1209[»]
4CDGX-ray2.79A/B636-1298[»]
4CGZX-ray3.20A636-1298[»]
4O3MX-ray2.30A640-1298[»]
ProteinModelPortaliP54132.
SMRiP54132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini676 – 851Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST176
Domaini877 – 1024Helicase C-terminalPROSITE-ProRule annotationAdd BLAST148
Domaini1212 – 1292HRDCPROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni301 – 600Necessary for interaction with SPIDR1 PublicationAdd BLAST300

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi795 – 798DEAH box4
Motifi1334 – 1349Nuclear localization signalSequence analysisAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi292 – 299Poly-Asp8
Compositional biasi310 – 316Poly-Ser7
Compositional biasi557 – 566Poly-Asp10

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HRDC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000095239.
HOVERGENiHBG004850.
InParanoidiP54132.
KOiK10901.
OMAiCENITEC.
OrthoDBiEOG091G021X.
PhylomeDBiP54132.
TreeFamiTF317801.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.80. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR012532. BDHCT.
IPR032439. BDHCT_assoc.
IPR032437. BLM_N.
IPR011545. DEAD/DEAH_box_helicase_dom.
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.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08072. BDHCT. 1 hit.
PF16204. BDHCT_assoc. 1 hit.
PF16202. BLM_N. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT
60 70 80 90 100
NVSVAKTPVL RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ
110 120 130 140 150
RGGSKSLLPD FLQTPKEVVC TTQNTPTVKK SRDTALKKLE FSSSPDSLST
160 170 180 190 200
INDWDDMDDF DTSETSKSFV TPPQSHFVRV STAQKSKKGK RNFFKAQLYT
210 220 230 240 250
TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD GPIAEVHINE
260 270 280 290 300
DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF
310 320 330 340 350
VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM
360 370 380 390 400
QELNPETSTD CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL
410 420 430 440 450
LQQRNIRRKL LTEVDFNKSD ASLLGSLWRY RPDSLDGPME GDSCPTGNSM
460 470 480 490 500
KELNFSHLPS NSVSPGDCLL TTTLGKTGFS ATRKNLFERP LFNTHLQKSF
510 520 530 540 550
VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI NDLERETQPS
560 570 580 590 600
YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL
610 620 630 640 650
SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP
660 670 680 690 700
HTKEMMKIFH KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ
710 720 730 740 750
LPACVSPGVT VVISPLRSLI VDQVQKLTSL DIPATYLTGD KTDSEATNIY
760 770 780 790 800
LQLSKKDPII KLLYVTPEKI CASNRLISTL ENLYERKLLA RFVIDEAHCV
810 820 830 840 850
SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD ILTQLKILRP
860 870 880 890 900
QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE
910 920 930 940 950
CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG
960 970 980 990 1000
MGIDKPDVRF VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR
1010 1020 1030 1040 1050
LKRLIMMEKD GNHHTRETHF NNLYSMVHYC ENITECRRIQ LLAYFGENGF
1060 1070 1080 1090 1100
NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD VKSIVRFVQE HSSSQGMRNI
1110 1120 1130 1140 1150
KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH NAERLFKKLI
1160 1170 1180 1190 1200
LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK
1210 1220 1230 1240 1250
QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA
1260 1270 1280 1290 1300
ESLSSDPEVL LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS
1310 1320 1330 1340 1350
LSSSRGPGRS AAEELDEEIP VSSHYFASKT RNERKRKKMP ASQRSKRRKT
1360 1370 1380 1390 1400
ASSGSKAKGG SATCRKISSK TKSSSIIGSS SASHTSQATS GANSKLGIMA
1410
PPKPINRPFL KPSYAFS
Length:1,417
Mass (Da):159,000
Last modified:October 1, 1996 - v1
Checksum:i423DF5F381194E11
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022295137K → R.1 PublicationCorresponds to variant rs28384988dbSNPEnsembl.1
Natural variantiVAR_022296298T → M.1 PublicationCorresponds to variant rs28384991dbSNPEnsembl.1
Natural variantiVAR_022297591R → Q.1 PublicationCorresponds to variant rs28385012dbSNPEnsembl.1
Natural variantiVAR_006901672Q → R in BLM. 1 PublicationCorresponds to variant rs747281324dbSNPEnsembl.1
Natural variantiVAR_016032841I → T in BLM. Corresponds to variant rs767086502dbSNPEnsembl.1
Natural variantiVAR_006902843T → I in BLM. 1 PublicationCorresponds to variant rs137853152dbSNPEnsembl.1
Natural variantiVAR_022298868P → L.1 PublicationCorresponds to variant rs2227935dbSNPEnsembl.1
Natural variantiVAR_016033878C → R in BLM. 1 Publication1
Natural variantiVAR_009138891G → E in BLM. 1
Natural variantiVAR_009139901C → Y in BLM. Corresponds to variant rs758311406dbSNPEnsembl.1
Natural variantiVAR_0091401036C → F in BLM. 1 PublicationCorresponds to variant rs137853153dbSNPEnsembl.1
Natural variantiVAR_0517311043A → D.Corresponds to variant rs2229035dbSNPEnsembl.1
Natural variantiVAR_0069031055C → S in BLM. 1 PublicationCorresponds to variant rs367543029dbSNPEnsembl.1
Natural variantiVAR_0222991205V → I.Corresponds to variant rs28385141dbSNPEnsembl.1
Natural variantiVAR_0149121209S → T.Corresponds to variant rs1801256dbSNPEnsembl.1
Natural variantiVAR_0223001213E → K.1 PublicationCorresponds to variant rs28385142dbSNPEnsembl.1
Natural variantiVAR_0223011321V → I.1 PublicationCorresponds to variant rs7167216dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10363.1.
PIRiA57570.
RefSeqiNP_000048.1. NM_000057.3.
NP_001274175.1. NM_001287246.1.
NP_001274176.1. NM_001287247.1.
NP_001274177.1. NM_001287248.1.
UniGeneiHs.725208.

Genome annotation databases

EnsembliENST00000355112; ENSP00000347232; ENSG00000197299.
GeneIDi641.
KEGGihsa:641.
UCSCiuc002bpr.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

BLMbase

BLM mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10363.1.
PIRiA57570.
RefSeqiNP_000048.1. NM_000057.3.
NP_001274175.1. NM_001287246.1.
NP_001274176.1. NM_001287247.1.
NP_001274177.1. NM_001287248.1.
UniGeneiHs.725208.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KV2NMR-A1210-1294[»]
2MH9NMR-A1067-1210[»]
2RRDNMR-A1200-1295[»]
3WE2X-ray2.70A/B1068-1209[»]
3WE3X-ray2.90A/B1068-1209[»]
4CDGX-ray2.79A/B636-1298[»]
4CGZX-ray3.20A636-1298[»]
4O3MX-ray2.30A640-1298[»]
ProteinModelPortaliP54132.
SMRiP54132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107110. 123 interactors.
DIPiDIP-33322N.
IntActiP54132. 37 interactors.
MINTiMINT-131918.
STRINGi9606.ENSP00000347232.

Chemistry databases

BindingDBiP54132.
ChEMBLiCHEMBL1293237.

PTM databases

iPTMnetiP54132.
PhosphoSitePlusiP54132.

Polymorphism and mutation databases

BioMutaiBLM.
DMDMi1705486.

Proteomic databases

EPDiP54132.
MaxQBiP54132.
PaxDbiP54132.
PeptideAtlasiP54132.
PRIDEiP54132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355112; ENSP00000347232; ENSG00000197299.
GeneIDi641.
KEGGihsa:641.
UCSCiuc002bpr.5. human.

Organism-specific databases

CTDi641.
DisGeNETi641.
GeneCardsiBLM.
GeneReviewsiBLM.
HGNCiHGNC:1058. BLM.
HPAiHPA005689.
MalaCardsiBLM.
MIMi210900. phenotype.
604610. gene.
neXtProtiNX_P54132.
OpenTargetsiENSG00000197299.
Orphaneti125. Bloom syndrome.
PharmGKBiPA25369.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000095239.
HOVERGENiHBG004850.
InParanoidiP54132.
KOiK10901.
OMAiCENITEC.
OrthoDBiEOG091G021X.
PhylomeDBiP54132.
TreeFamiTF317801.

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiP54132.

Miscellaneous databases

EvolutionaryTraceiP54132.
GeneWikiiBloom_syndrome_protein.
GenomeRNAii641.
PMAP-CutDBP54132.
PROiP54132.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197299.
CleanExiHS_BLM.
ExpressionAtlasiP54132. baseline and differential.
GenevisibleiP54132. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.80. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR012532. BDHCT.
IPR032439. BDHCT_assoc.
IPR032437. BLM_N.
IPR011545. DEAD/DEAH_box_helicase_dom.
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.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08072. BDHCT. 1 hit.
PF16204. BDHCT_assoc. 1 hit.
PF16202. BLM_N. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBLM_HUMAN
AccessioniPrimary (citable) accession number: P54132
Secondary accession number(s): Q52M96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.