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Protein

Bloom syndrome protein homolog

Gene

Blm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:9840919). Participates in DNA replication and repair (By similarity). 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:9840919). Negatively regulates sister chromatid exchange (SCE) (PubMed:9840919, PubMed:27010503). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity).By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei7253' overhang DNA-bindingBy similarity1
Sitei8163' overhang DNA-bindingBy similarity1
Sitei9283' overhang DNA-binding; via amide nitrogenBy similarity1
Sitei9543' overhang DNA-bindingBy similarity1
Sitei9763' overhang DNA-bindingBy similarity1
Binding sitei990ATPBy similarity1
Metal bindingi1044ZincBy similarity1
Metal bindingi1063ZincBy similarity1
Metal bindingi1071ZincBy similarity1
Metal bindingi1074ZincBy similarity1
Sitei11153' overhang DNA-bindingBy similarity1
Binding sitei1247ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi676 – 680ATPBy similarity5
Nucleotide bindingi700 – 704ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

  • alpha-beta T cell differentiation Source: MGI
  • cellular response to camptothecin Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to drug Source: MGI
  • cellular response to hydroxyurea Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • chromosome organization Source: MGI
  • DNA double-strand break processing Source: UniProtKB
  • DNA duplex unwinding Source: MGI
  • DNA repair Source: MGI
  • DNA replication Source: BHF-UCL
  • G-quadruplex DNA unwinding Source: BHF-UCL
  • mitotic G2 DNA damage checkpoint Source: MGI
  • negative regulation of cell division Source: MGI
  • negative regulation of DNA recombination Source: MGI
  • negative regulation of mitotic recombination Source: UniProtKB
  • negative regulation of thymocyte apoptotic process Source: MGI
  • positive regulation of alpha-beta T cell proliferation Source: MGI
  • positive regulation of double-strand break repair via homologous recombination Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • protein complex oligomerization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein oligomerization Source: MGI
  • regulation of binding Source: MGI
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: MGI
  • regulation of DNA-dependent DNA replication Source: UniProtKB
  • replication-born double-strand break repair via sister chromatid exchange Source: MGI
  • replication fork processing Source: MGI
  • response to X-ray Source: MGI
  • telomere maintenance Source: MGI
  • telomeric D-loop disassembly Source: MGI

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, DNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Bloom syndrome protein homolog (EC:3.6.4.12By similarity)
Short name:
mBLM
Alternative name(s):
RecQ helicase homolog
Gene namesi
Name:Blm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1328362. Blm.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi680Q → P: Reduced ATPase and helicase activities. 1 Publication1
Mutagenesisi703K → A: Reduced ATPase and helicase activities. 1 Publication1
Mutagenesisi849I → T: Reduced ATPase and helicase activities. 1 Publication1
Mutagenesisi1063C → S: Reduced ATPase and helicase activities. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050401 – 1416Bloom syndrome protein homologAdd BLAST1416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineBy similarity1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei47PhosphoserineBy similarity1
Cross-linki55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei56PhosphothreonineBy similarity1
Cross-linki62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei114PhosphothreonineBy similarity1
Cross-linki129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei247PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1
Modified residuei333PhosphoserineBy similarity1
Modified residuei343PhosphoserineBy similarity1
Cross-linki349Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei363PhosphoserineBy similarity1
Modified residuei431PhosphoserineBy similarity1
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei469PhosphoserineBy similarity1
Cross-linki481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki489Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei504PhosphoserineBy similarity1
Modified residuei513PhosphothreonineBy similarity1
Cross-linki536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki596Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki602Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei871N6-acetyllysineBy similarity1
Cross-linki1130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1202PhosphoserineBy similarity1
Cross-linki1204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1301PhosphoserineBy similarity1
Modified residuei1311PhosphothreonineCombined sources1
Cross-linki1371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1394Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO88700.
MaxQBiO88700.
PaxDbiO88700.
PeptideAtlasiO88700.
PRIDEiO88700.

PTM databases

iPTMnetiO88700.
PhosphoSitePlusiO88700.

Expressioni

Tissue specificityi

Highly expressed in testis 12-14 days after birth (corresponding to the pachytene phase) and at much lower levels in brain, heart, liver, lung, thymus, kidney and spleen (PubMed:9840919, PubMed:27010503). Expressed in bone marrow (PubMed:27010503).2 Publications

Gene expression databases

BgeeiENSMUSG00000030528.
CleanExiMM_BLM.
ExpressionAtlasiO88700. baseline and differential.
GenevisibleiO88700. MM.

Interactioni

Subunit structurei

Monomer. Homodimer (via N-terminus). Homotetramer (via N-terminus); dimer of dimers. Homohexamer (via N-terminus). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomer complexes dissociate into monomer in presence of ATP. 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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

CORUMiO88700.
DIPiDIP-27643N.
STRINGi10090.ENSMUSP00000127995.

Structurei

3D structure databases

ProteinModelPortaliO88700.
SMRiO88700.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini684 – 859Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST176
Domaini885 – 1032Helicase C-terminalPROSITE-ProRule annotationBy similarityAdd BLAST148
Domaini1217 – 1297HRDCPROSITE-ProRule annotationBy similarityAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 419Necessary for dimerization and homooligomerizationBy similarityAdd BLAST53
Regioni878 – 8813' overhang DNA-bindingBy similarity4
Regioni905 – 9073' overhang DNA-bindingBy similarity3
Regioni1008 – 10113' overhang DNA-bindingBy similarity4
Regioni1102 – 1144DNA Holliday junction bindingBy similarityAdd BLAST43
Regioni1115 – 11173' overhang DNA-bindingBy similarity3
Regioni1126 – 11303' overhang DNA-bindingBy similarity5
Regioni1165 – 11713' overhang DNA-bindingBy similarity7
Regioni1232 – 1249Necessary for ssDNA and DNA Holliday junction bindingBy similarityAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi803 – 806DEAH box4
Motifi1333 – 1348Nuclear localization signalSequence analysisAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi219 – 231Poly-GluAdd BLAST13
Compositional biasi564 – 574Poly-AspAdd BLAST11
Compositional biasi1312 – 1317Poly-Glu6

Domaini

The N-terminal region mediates dimerization and homooligomerization. Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner. The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding.By similarity

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000095239.
HOVERGENiHBG004850.
InParanoidiO88700.
KOiK10901.
PhylomeDBiO88700.

Family and domain databases

CDDicd00079. HELICc. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR012532. 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_sf.
IPR002121. HRDC_dom.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR036388. WH-like_DNA-bd_sf.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF08072. 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.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiView protein in PROSITE
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.

Sequencei

Sequence statusi: Complete.

O88700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVPLNNLQ EQLQRHSARK LNNQPSLSKP KSLGFTFKKK TSEGDVSVTS
60 70 80 90 100
VSVVKTPALS DKDVNVSEAF SFTESPLHKP KQQAKIEGFF KHFPGRQQSK
110 120 130 140 150
GTCSEPSLPA TVQTAQDTLC TTPKTPTAKK LPVAVFKKLE FSSSADSLSD
160 170 180 190 200
WADMDDFDMS ASDAFASLAK NPATRVSTAQ KMKKTKRNFF KPPPRKANAV
210 220 230 240 250
KTDLTPPSPE CLQVDLTKES EEEEEEEEEA EGADCLSRDV ICIDNDSASE
260 270 280 290 300
ELTEKDTQES QSLKAHLGAE RGDSEKKSHE DEAVFHSVQN TEYFEHNDND
310 320 330 340 350
YDIDFVPPSP EEIISTASSS LKCSSMLKDL DDSDKEKGIL STSEELLSKP
360 370 380 390 400
EEMTTHKSDA GTSKDCDAQQ IRIQQQLIHV MEHICKLVDT VPTDELEALN
410 420 430 440 450
CGTELLQQRN IRRKLLAEAG FNGNDVRLLG SLWRHRPDSL DNTVQGDSCP
460 470 480 490 500
VGHPNKELNS PYLLSHSPST EECLPTTTPG KTGFSATPKN LFERPLLNSH
510 520 530 540 550
LQKSFVSSNW AETPRMENRN ESTDFPGSVL TSTTVKAQSK QAASGWNVER
560 570 580 590 600
HGQASYDIDN FNIDDFDDDD DDDDWENIMH NFPASKSSTA TYPPIKEGGP
610 620 630 640 650
VKSLSERISS AKAKFLPVVS TAQNTNLSES IQNCSDKLAQ NLSSKNPKHE
660 670 680 690 700
HFQSLNFPHT KEMMKIFHKK FGLHNFRTNQ LEAINAALLG EDCFILMPTG
710 720 730 740 750
GGKSLCYQLP ACVSPGVTIV ISPLRSLIVD QVQKLTSFDI PATYLTGDKT
760 770 780 790 800
DSEAANIYLQ LSKKDPIIKL LYVTPEKVCA SNRLISTLEN LYERKLLARF
810 820 830 840 850
VIDEAHCVSQ WGHDFRQDYK RMNMLRQKFP SVPVMALTAT ANPRVQKDIL
860 870 880 890 900
TQLKILRPQV FSMSFNRHNL KYYVLPKKPK KVAFDCLEWI RKHHPYDSGI
910 920 930 940 950
IYCLSRRECD TMADTLQREG LAALAYHAGL SDSARDEVQH KWINQDNCQV
960 970 980 990 1000
ICATIAFGMG IDKPDVRFVI HASLPKSMEG YYQESGRAGR DGEISHCVLF
1010 1020 1030 1040 1050
YTYHDVTRLK RLIMMEKDGN YHTKETHVNN LYSMVHYCEN ITECRRIQLL
1060 1070 1080 1090 1100
AYFGEKGFNP DFCKKYPDVS CDNCCKTKDY KTKDVTDDVK NIIRFVQEHS
1110 1120 1130 1140 1150
SSPGTRNIGP AGRFTLNMLV DIFLGSKSAK VKSGIFGKGT TYSRHNAERL
1160 1170 1180 1190 1200
FKKLILDKIL DEDLYINAND QPIAYVMLGT KAHSVLSGHL KVDFMETENS
1210 1220 1230 1240 1250
SSIKKQKALV AKVSQREEVV KKCLGELTEV CKLLGKVFGV HYFNIFNTAT
1260 1270 1280 1290 1300
LKKLAESLSS DPEVLLQIDG VTEDKLEKYG AEVIPVLQKY SEWTVPAEDG
1310 1320 1330 1340 1350
SPGARGAPED TEEEEEEAPV SSHYFANQTR NERKRKKMSA THKPKRRRTS
1360 1370 1380 1390 1400
YGGFRAKGGS TTCRKTTSKS KFYGVTGSRS ASCASQATSS ASRKLGIMAP
1410
PKPVNRTFLR PSYAFS
Length:1,416
Mass (Da):158,366
Last modified:November 1, 1998 - v1
Checksum:i447C8110A775DD42
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131L → P in BAA32001 (PubMed:9655940).Curated1
Sequence conflicti229E → EE in BAA32001 (PubMed:9655940).Curated1
Sequence conflicti535V → M in BAA32001 (PubMed:9655940).Curated1
Sequence conflicti546 – 547WN → RT in BAA32001 (PubMed:9655940).Curated2
Sequence conflicti574Missing in BAA32001 (PubMed:9655940).Curated1
Sequence conflicti591T → A in BAA32001 (PubMed:9655940).Curated1
Sequence conflicti621T → N in BAA32001 (PubMed:9655940).Curated1
Sequence conflicti1295V → L in BAA32001 (PubMed:9655940).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98263 mRNA. Translation: CAB10933.1.
AB008674 mRNA. Translation: BAA32001.1.
CCDSiCCDS40000.1.
RefSeqiNP_001035992.1. NM_001042527.2.
NP_031576.4. NM_007550.4.
UniGeneiMm.12932.

Genome annotation databases

EnsembliENSMUST00000081314; ENSMUSP00000080062; ENSMUSG00000030528.
GeneIDi12144.
KEGGimmu:12144.
UCSCiuc009iax.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiBLM_MOUSE
AccessioniPrimary (citable) accession number: O88700
Secondary accession number(s): O88198
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: November 22, 2017
This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families