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P54132

- BLM_HUMAN

UniProt

P54132 - BLM_HUMAN

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Protein

Bloom syndrome protein

Gene
BLM, RECQ2, RECQL3
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi689 – 6968ATP By similarity

GO - Molecular functioni

  1. annealing helicase activity Source: UniProtKB
  2. ATPase activity Source: UniProtKB
  3. ATP binding Source: UniProtKB
  4. ATP-dependent 3'-5' DNA helicase activity Source: Ensembl
  5. ATP-dependent DNA helicase activity Source: UniProtKB
  6. ATP-dependent helicase activity Source: UniProtKB
  7. bubble DNA binding Source: UniProtKB
  8. four-way junction helicase activity Source: UniProtKB
  9. G-quadruplex DNA binding Source: UniProtKB
  10. helicase activity Source: UniProtKB
  11. p53 binding Source: UniProtKB
  12. protein binding Source: UniProtKB
  13. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. alpha-beta T cell differentiation Source: Ensembl
  2. ATP catabolic process Source: GOC
  3. cellular response to camptothecin Source: UniProtKB
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. cellular response to hydroxyurea Source: UniProtKB
  6. cellular response to ionizing radiation Source: UniProtKB
  7. DNA double-strand break processing Source: UniProtKB
  8. DNA duplex unwinding Source: GOC
  9. DNA recombination Source: UniProtKB
  10. DNA repair Source: UniProtKB
  11. DNA strand renaturation Source: GOC
  12. double-strand break repair via homologous recombination Source: UniProtKB
  13. G2 DNA damage checkpoint Source: UniProtKB
  14. mitotic G2 phase Source: UniProtKB
  15. negative regulation of cell division Source: UniProtKB
  16. negative regulation of DNA recombination Source: UniProtKB
  17. negative regulation of mitotic recombination Source: Ensembl
  18. negative regulation of thymocyte apoptotic process Source: Ensembl
  19. positive regulation of alpha-beta T cell proliferation Source: Ensembl
  20. positive regulation of transcription, DNA-templated Source: UniProtKB
  21. protein oligomerization Source: UniProtKB
  22. regulation of binding Source: Ensembl
  23. regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  24. replication fork processing Source: UniProtKB
  25. replication fork protection Source: UniProtKB
  26. response to X-ray Source: UniProtKB
  27. telomere maintenance Source: Ensembl
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

ReactomeiREACT_27271. Meiotic recombination.

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
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:1058. BLM.

Subcellular locationi

Nucleus
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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. lateral element Source: UniProtKB
  3. male germ cell nucleus Source: Ensembl
  4. nuclear chromosome Source: UniProtKB
  5. nuclear matrix Source: UniProtKB
  6. nucleolus Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. PML body Source: UniProtKB
  9. pronucleus Source: Ensembl
  10. replication fork Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti672 – 6721Q → R in BLM. 1 Publication
VAR_006901
Natural varianti841 – 8411I → T in BLM.
VAR_016032
Natural varianti843 – 8431T → I in BLM. 1 Publication
VAR_006902
Natural varianti878 – 8781C → R in BLM. 1 Publication
VAR_016033
Natural varianti891 – 8911G → E in BLM.
VAR_009138
Natural varianti901 – 9011C → Y in BLM.
VAR_009139
Natural varianti1036 – 10361C → F in BLM. 1 Publication
VAR_009140
Natural varianti1055 – 10551C → S in BLM. 1 Publication
VAR_006903

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi210900. phenotype.
Orphaneti125. Bloom syndrome.
PharmGKBiPA25369.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14171417Bloom syndrome proteinPRO_0000205039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei57 – 571Phosphothreonine1 Publication
Modified residuei114 – 1141Phosphothreonine1 Publication
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei171 – 1711Phosphothreonine1 Publication
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei419 – 4191Phosphoserine2 Publications
Modified residuei422 – 4221Phosphoserine2 Publications
Modified residuei426 – 4261Phosphoserine1 Publication
Modified residuei499 – 4991Phosphoserine2 Publications
Modified residuei508 – 5081Phosphothreonine1 Publication
Modified residuei863 – 8631N6-acetyllysine1 Publication
Modified residuei1295 – 12951Phosphoserine1 Publication
Modified residuei1296 – 12961Phosphoserine1 Publication
Modified residuei1310 – 13101Phosphoserine1 Publication

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, Phosphoprotein

Proteomic databases

MaxQBiP54132.
PaxDbiP54132.
PRIDEiP54132.

PTM databases

PhosphoSiteiP54132.

Miscellaneous databases

PMAP-CutDBP54132.

Expressioni

Gene expression databases

ArrayExpressiP54132.
BgeeiP54132.
CleanExiHS_BLM.
GenevestigatoriP54132.

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
RMI1Q9H9A710EBI-621372,EBI-621339
RPA1P276943EBI-621372,EBI-621389
TERF1P542743EBI-621372,EBI-710997
TERF2Q155548EBI-621372,EBI-706637
UIMC1Q96RL12EBI-621372,EBI-725300
WRNQ141919EBI-621372,EBI-368417

Protein-protein interaction databases

BioGridi107110. 72 interactions.
DIPiDIP-33322N.
IntActiP54132. 22 interactions.
MINTiMINT-131918.
STRINGi9606.ENSP00000347232.

Structurei

Secondary structure

1
1417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi643 – 6453
Helixi652 – 66110
Helixi672 – 6809
Beta strandi685 – 6884
Helixi697 – 7059
Beta strandi706 – 7138
Helixi717 – 72913
Beta strandi734 – 7418
Helixi743 – 75311
Beta strandi755 – 7573
Beta strandi762 – 7654
Helixi769 – 7724
Helixi774 – 78512
Beta strandi789 – 7957
Helixi797 – 8004
Helixi811 – 82010
Beta strandi826 – 8305
Helixi835 – 84511
Beta strandi851 – 8533
Beta strandi862 – 8687
Helixi871 – 8733
Helixi874 – 88512
Beta strandi891 – 8944
Helixi898 – 91013
Beta strandi915 – 9195
Helixi924 – 93512
Beta strandi941 – 9455
Helixi947 – 9504
Beta strandi960 – 9656
Helixi970 – 9778
Turni979 – 9835
Beta strandi987 – 9937
Helixi995 – 100511
Helixi1015 – 103117
Helixi1037 – 10448
Helixi1054 – 10574
Helixi1059 – 10613
Helixi1064 – 10674
Turni1069 – 10713
Beta strandi1074 – 10763
Helixi1078 – 109013
Beta strandi1096 – 10994
Helixi1111 – 11199
Turni1129 – 11368
Helixi1139 – 115113
Beta strandi1154 – 11618
Beta strandi1163 – 11664
Beta strandi1167 – 11737
Helixi1177 – 11815
Beta strandi1188 – 11903
Helixi1195 – 11973
Beta strandi1207 – 12093
Helixi1210 – 123324
Helixi1237 – 12393
Helixi1243 – 125210
Helixi1257 – 12604
Beta strandi1263 – 12653
Helixi1268 – 128316
Turni1284 – 12885

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KV2NMR-A1210-1294[»]
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. Positions 639-1295.

Miscellaneous databases

EvolutionaryTraceiP54132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini676 – 851176Helicase ATP-bindingAdd
BLAST
Domaini877 – 1024148Helicase C-terminalAdd
BLAST
Domaini1212 – 129281HRDCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni301 – 600300Necessary for interaction with SPIDRAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi795 – 7984DEAH box
Motifi1334 – 134916Nuclear localization signal Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi292 – 2998Poly-Asp
Compositional biasi310 – 3167Poly-Ser
Compositional biasi557 – 56610Poly-Asp

Sequence similaritiesi

Contains 1 HRDC domain.

Phylogenomic databases

eggNOGiCOG0514.
HOGENOMiHOG000095239.
HOVERGENiHBG004850.
InParanoidiP54132.
KOiK10901.
OMAiCLEWIRK.
OrthoDBiEOG72NRPB.
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.
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.
IPR027417. P-loop_NTPase.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08072. BDHCT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 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]
SUPFAMiSSF47819. 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

MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT     50
NVSVAKTPVL RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ 100
RGGSKSLLPD FLQTPKEVVC TTQNTPTVKK SRDTALKKLE FSSSPDSLST 150
INDWDDMDDF DTSETSKSFV TPPQSHFVRV STAQKSKKGK RNFFKAQLYT 200
TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD GPIAEVHINE 250
DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF 300
VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM 350
QELNPETSTD CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL 400
LQQRNIRRKL LTEVDFNKSD ASLLGSLWRY RPDSLDGPME GDSCPTGNSM 450
KELNFSHLPS NSVSPGDCLL TTTLGKTGFS ATRKNLFERP LFNTHLQKSF 500
VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI NDLERETQPS 550
YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL 600
SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP 650
HTKEMMKIFH KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ 700
LPACVSPGVT VVISPLRSLI VDQVQKLTSL DIPATYLTGD KTDSEATNIY 750
LQLSKKDPII KLLYVTPEKI CASNRLISTL ENLYERKLLA RFVIDEAHCV 800
SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD ILTQLKILRP 850
QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE 900
CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG 950
MGIDKPDVRF VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR 1000
LKRLIMMEKD GNHHTRETHF NNLYSMVHYC ENITECRRIQ LLAYFGENGF 1050
NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD VKSIVRFVQE HSSSQGMRNI 1100
KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH NAERLFKKLI 1150
LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK 1200
QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA 1250
ESLSSDPEVL LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS 1300
LSSSRGPGRS AAEELDEEIP VSSHYFASKT RNERKRKKMP ASQRSKRRKT 1350
ASSGSKAKGG SATCRKISSK TKSSSIIGSS SASHTSQATS GANSKLGIMA 1400
PPKPINRPFL KPSYAFS 1417
Length:1,417
Mass (Da):159,000
Last modified:October 1, 1996 - v1
Checksum:i423DF5F381194E11
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371K → R.1 Publication
Corresponds to variant rs28384988 [ dbSNP | Ensembl ].
VAR_022295
Natural varianti298 – 2981T → M.1 Publication
Corresponds to variant rs28384991 [ dbSNP | Ensembl ].
VAR_022296
Natural varianti591 – 5911R → Q.1 Publication
Corresponds to variant rs28385012 [ dbSNP | Ensembl ].
VAR_022297
Natural varianti672 – 6721Q → R in BLM. 1 Publication
VAR_006901
Natural varianti841 – 8411I → T in BLM.
VAR_016032
Natural varianti843 – 8431T → I in BLM. 1 Publication
VAR_006902
Natural varianti868 – 8681P → L.1 Publication
Corresponds to variant rs11852361 [ dbSNP | Ensembl ].
VAR_022298
Natural varianti878 – 8781C → R in BLM. 1 Publication
VAR_016033
Natural varianti891 – 8911G → E in BLM.
VAR_009138
Natural varianti901 – 9011C → Y in BLM.
VAR_009139
Natural varianti1036 – 10361C → F in BLM. 1 Publication
VAR_009140
Natural varianti1043 – 10431A → D.
Corresponds to variant rs2229035 [ dbSNP | Ensembl ].
VAR_051731
Natural varianti1055 – 10551C → S in BLM. 1 Publication
VAR_006903
Natural varianti1205 – 12051V → I.1 Publication
Corresponds to variant rs28385141 [ dbSNP | Ensembl ].
VAR_022299
Natural varianti1209 – 12091S → T.
Corresponds to variant rs1801256 [ dbSNP | Ensembl ].
VAR_014912
Natural varianti1213 – 12131E → K.1 Publication
Corresponds to variant rs28385142 [ dbSNP | Ensembl ].
VAR_022300
Natural varianti1321 – 13211V → I.1 Publication
Corresponds to variant rs7167216 [ dbSNP | Ensembl ].
VAR_022301

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi1705486.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10363.1.
PIRi A57570.
RefSeqi NP_000048.1. NM_000057.3.
NP_001274175.1. NM_001287246.1.
NP_001274176.1. NM_001287247.1.
NP_001274177.1. NM_001287248.1.
UniGenei Hs.725208.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KV2 NMR - A 1210-1294 [» ]
2RRD NMR - A 1200-1295 [» ]
3WE2 X-ray 2.70 A/B 1068-1209 [» ]
3WE3 X-ray 2.90 A/B 1068-1209 [» ]
4CDG X-ray 2.79 A/B 636-1298 [» ]
4CGZ X-ray 3.20 A 636-1298 [» ]
4O3M X-ray 2.30 A 640-1298 [» ]
ProteinModelPortali P54132.
SMRi P54132. Positions 639-1295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107110. 72 interactions.
DIPi DIP-33322N.
IntActi P54132. 22 interactions.
MINTi MINT-131918.
STRINGi 9606.ENSP00000347232.

Chemistry

ChEMBLi CHEMBL1293237.

PTM databases

PhosphoSitei P54132.

Polymorphism databases

DMDMi 1705486.

Proteomic databases

MaxQBi P54132.
PaxDbi P54132.
PRIDEi P54132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355112 ; ENSP00000347232 ; ENSG00000197299 .
GeneIDi 641.
KEGGi hsa:641.
UCSCi uc002bpr.3. human.

Organism-specific databases

CTDi 641.
GeneCardsi GC15P091260.
GeneReviewsi BLM.
HGNCi HGNC:1058. BLM.
HPAi HPA005689.
MIMi 210900. phenotype.
604610. gene.
neXtProti NX_P54132.
Orphaneti 125. Bloom syndrome.
PharmGKBi PA25369.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0514.
HOGENOMi HOG000095239.
HOVERGENi HBG004850.
InParanoidi P54132.
KOi K10901.
OMAi CLEWIRK.
OrthoDBi EOG72NRPB.
PhylomeDBi P54132.
TreeFami TF317801.

Enzyme and pathway databases

Reactomei REACT_27271. Meiotic recombination.

Miscellaneous databases

EvolutionaryTracei P54132.
GeneWikii Bloom_syndrome_protein.
GenomeRNAii 641.
NextBioi 2600.
PMAP-CutDB P54132.
PROi P54132.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54132.
Bgeei P54132.
CleanExi HS_BLM.
Genevestigatori P54132.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.10.150.80. 1 hit.
3.40.50.300. 2 hits.
InterProi 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.
IPR027417. P-loop_NTPase.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF08072. BDHCT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view ]
SUPFAMi SSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsi TIGR00614. recQ_fam. 1 hit.
PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view ]
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Publicationsi

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  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. 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. "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
    Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
    Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SPIDR AND RAD51, INTERACTION WITH RMI1; SPIDR AND TOP3A, SUBCELLULAR LOCATION.
  22. "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.
  23. "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.

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: September 3, 2014
This is version 152 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

External Data

Dasty 3

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