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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. ATP binding Source: UniProtKB
  2. ATP-dependent 3'-5' DNA helicase activity Source: Ensembl
  3. ATP-dependent DNA helicase activity Source: UniProtKB
  4. ATP-dependent helicase activity Source: UniProtKB
  5. ATPase activity Source: UniProtKB
  6. G-quadruplex DNA binding Source: UniProtKB
  7. annealing helicase activity Source: UniProtKB
  8. bubble DNA binding Source: UniProtKB
  9. four-way junction helicase activity 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. ATP catabolic process Source: GOC
  2. DNA double-strand break processing Source: UniProtKB
  3. DNA duplex unwinding Source: GOC
  4. DNA recombination Source: UniProtKB
  5. DNA repair Source: UniProtKB
  6. DNA strand renaturation Source: GOC
  7. G2 DNA damage checkpoint Source: UniProtKB
  8. alpha-beta T cell differentiation Source: Ensembl
  9. cellular response to DNA damage stimulus Source: UniProtKB
  10. cellular response to camptothecin Source: UniProtKB
  11. cellular response to hydroxyurea Source: UniProtKB
  12. cellular response to ionizing radiation Source: UniProtKB
  13. double-strand break repair via homologous recombination Source: UniProtKB
  14. mitotic G2 phase Source: UniProtKB
  15. negative regulation of DNA recombination Source: UniProtKB
  16. negative regulation of cell division 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. PML body Source: UniProtKB
  2. cytoplasm Source: Ensembl
  3. lateral element Source: UniProtKB
  4. male germ cell nucleus Source: Ensembl
  5. nuclear chromosome Source: UniProtKB
  6. nuclear matrix Source: UniProtKB
  7. nucleolus Source: UniProtKB
  8. nucleus 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 protein
PRO_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

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-binding
Add
BLAST
Domaini877 – 1024148Helicase C-terminal
Add
BLAST
Domaini1212 – 129281HRDC
Add
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi795 – 7984DEAH box
Motifi1334 – 134916Nuclear localization signal Reviewed prediction
Add
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]
SUPFAMi