NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS.
DOI=10.1038/sj.onc.1202389; PubMed=9840919 [NCBI, ExPASy, EBI, Israel, Japan]
Bahr A., de Graeve F., Kedinger C., Chatton B.;
"Point mutations causing Bloom's syndrome abolish ATPase and DNA helicase activities of the BLM protein.";
Oncogene 17:2565-2571(1998).

[2]

NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=BALB/c;
TISSUE=Brain, Spermatocyte, and Testis;
DOI=10.1016/S0167-4781(98)00066-9; PubMed=9655940 [NCBI, ExPASy, EBI, Israel, Japan]
Seki T., Wang W.-S., Okumura N., Seki M., Katada T., Enomoto T.;
"cDNA cloning of mouse BLM gene, the homologue to human Bloom's syndrome gene, which is highly expressed in the testis at the mRNA level.";
Biochim. Biophys. Acta 1398:377-381(1998).

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.
SUBUNIT: 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 (By similarity).
SUBCELLULAR LOCATION: Nucleus (By similarity).
TISSUE SPECIFICITY: 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.
PTM: 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).
SIMILARITY: Belongs to the helicase family. RecQ subfamily.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
SIMILARITY: Contains 1 HRDC domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z98263; CAB10933.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB008674; BAA32001.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00329943; -.

NP_001035992.1; -.

3D structure databases

ModBase

O88700.

Protein-protein interaction databases

DIP

DIP:27643N; -.

PTM databases

PhosphoSite

O88700; -.

Organism-specific databases

MGI

MGI:1328362; Blm.

Gene expression databases

O88700; -.

O88700; -.

MM_BLM; -.

ENSMUSG00000030528; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0001673;	Cellular component: male germ cell nucleus (inferred from direct assay from MGI).
GO:0045120;	Cellular component: pronucleus (inferred from direct assay from MGI).
GO:0005657;	Cellular component: replication fork (inferred from direct assay from MGI).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0043140;	Molecular function: ATP-dependent 3'-5' DNA helicase activity (inferred from direct assay from MGI).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0046632;	Biological process: alpha-beta T cell differentiation (inferred from mutant phenotype from MGI).
GO:0006310;	Biological process: DNA recombination (inferred from electronic annotation from InterPro).
GO:0006281;	Biological process: DNA repair (inferred from direct assay from MGI).
GO:0006260;	Biological process: DNA replication (inferred from electronic annotation from UniProtKB-KW).
GO:0045950;	Biological process: negative regulation of mitotic recombination (inferred from mutant phenotype from MGI).
GO:0046641;	Biological process: positive regulation of alpha-beta T cell proliferation (inferred from mutant phenotype from MGI).
GO:0051098;	Biological process: regulation of binding (inferred from direct assay from MGI).
GO:0000723;	Biological process: telomere maintenance (inferred from genetic interaction from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR012532; BDHCT.
IPR014001; DEAD-like_N.
IPR001650; DNA/RNA_helicase_C.
IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464; DNA/RNA_helicase_DEAH_CS.
IPR004589; DNA_helicase_ATP-dep_RecQ.
IPR018329; DNA_helicase_ATP-dep_RecQ_N.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR002121; HRDC.
IPR018982; RQC_domain.
Graphical view of domain structure.

PANTHER

PTHR13710; RecQ; 1.

Pfam

PF08072; BDHCT; 1.
PF00270; DEAD; 1.
PF00271; Helicase_C; 1.
PF00570; HRDC; 1.
PF09382; RQC; 1.
Pfam graphical view of domain structure.

SMART

SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SM00341; HRDC; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00614; recQ_fam; 1.

PROSITE

PS00690; DEAH_ATP_HELICASE; 1.
PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PS50967; HRDC; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000030528; Mus musculus. [Contig view]

GeneID

12144; -.

KEGG

mmu:12144; -.

Phylogenomic databases

HOGENOM

O88700; -.

HOVERGEN

O88700; -.

OMA

O88700; PHTKEMM.

Other

280473; -.

Blm; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1416`	`1416`	`Bloom syndrome protein homolog.`	`PRO_0000205040`
`DOMAIN`	`684 859`	`176`	`Helicase ATP-binding.`
`DOMAIN`	`885 1032`	`148`	`Helicase C-terminal.`
`DOMAIN`	`1217 1297`	`81`	`HRDC.`
`NP_BIND`	`697 704`	`8`	`ATP (By similarity).`
`MOTIF`	`803 806`	`4`	`DEAH box.`
`MOTIF`	`1333 1348`	`16`	`Nuclear localization signal (Potential).`
`COMPBIAS`	`219 231`	`13`	`Poly-Glu.`
`COMPBIAS`	`564 574`	`11`	`Poly-Asp.`
`COMPBIAS`	`1312 1317`	`6`	`Poly-Glu.`
`MOD_RES`	`47 47`		`Phosphoserine (By similarity).`
`MOD_RES`	`52 52`		`Phosphoserine (By similarity).`
`MOD_RES`	`56 56`		`Phosphothreonine (By similarity).`
`MOD_RES`	`114 114`		`Phosphothreonine (By similarity).`
`MOD_RES`	`363 363`		`Phosphoserine (By similarity).`
`MOD_RES`	`485 485`		`Phosphoserine (By similarity).`
`MOD_RES`	`504 504`		`Phosphoserine (By similarity).`
`MOD_RES`	`513 513`		`Phosphothreonine (By similarity).`
`MOD_RES`	`1301 1301`		`Phosphoserine (By similarity).`
`MUTAGEN`	`680 680`		`Q->P: Reduced ATPase and helicase activities.`
`MUTAGEN`	`703 703`		`K->A: Reduced ATPase and helicase activities.`
`MUTAGEN`	`849 849`		`I->T: Reduced ATPase and helicase activities.`
`MUTAGEN`	`1063 1063`		`C->S: Reduced ATPase and helicase activities.`
`CONFLICT`	`131 131`		`L -> P (in Ref. 2; BAA32001).`
`CONFLICT`	`229 229`		`E -> EE (in Ref. 2; BAA32001).`
`CONFLICT`	`535 535`		`V -> M (in Ref. 2; BAA32001).`
`CONFLICT`	`546 547`		`WN -> RT (in Ref. 2; BAA32001).`
`CONFLICT`	`574 574`		`Missing (in Ref. 2; BAA32001).`
`CONFLICT`	`591 591`		`T -> A (in Ref. 2; BAA32001).`
`CONFLICT`	`621 621`		`T -> N (in Ref. 2; BAA32001).`
`CONFLICT`	`1295 1295`		`V -> L (in Ref. 2; BAA32001).`

Sequence information

Length: 1416 AA [This is the length of the unprocessed precursor]

Molecular weight: 158366 Da [This is the MW of the unprocessed precursor]

CRC64: 447C8110A775DD42 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVPLNNLQ EQLQRHSARK LNNQPSLSKP KSLGFTFKKK TSEGDVSVTS VSVVKTPALS 

        70         80         90        100        110        120 
DKDVNVSEAF SFTESPLHKP KQQAKIEGFF KHFPGRQQSK GTCSEPSLPA TVQTAQDTLC 

       130        140        150        160        170        180 
TTPKTPTAKK LPVAVFKKLE FSSSADSLSD WADMDDFDMS ASDAFASLAK NPATRVSTAQ 

       190        200        210        220        230        240 
KMKKTKRNFF KPPPRKANAV KTDLTPPSPE CLQVDLTKES EEEEEEEEEA EGADCLSRDV 

       250        260        270        280        290        300 
ICIDNDSASE ELTEKDTQES QSLKAHLGAE RGDSEKKSHE DEAVFHSVQN TEYFEHNDND 

       310        320        330        340        350        360 
YDIDFVPPSP EEIISTASSS LKCSSMLKDL DDSDKEKGIL STSEELLSKP EEMTTHKSDA 

       370        380        390        400        410        420 
GTSKDCDAQQ IRIQQQLIHV MEHICKLVDT VPTDELEALN CGTELLQQRN IRRKLLAEAG 

       430        440        450        460        470        480 
FNGNDVRLLG SLWRHRPDSL DNTVQGDSCP VGHPNKELNS PYLLSHSPST EECLPTTTPG 

       490        500        510        520        530        540 
KTGFSATPKN LFERPLLNSH LQKSFVSSNW AETPRMENRN ESTDFPGSVL TSTTVKAQSK 

       550        560        570        580        590        600 
QAASGWNVER HGQASYDIDN FNIDDFDDDD DDDDWENIMH NFPASKSSTA TYPPIKEGGP 

       610        620        630        640        650        660 
VKSLSERISS AKAKFLPVVS TAQNTNLSES IQNCSDKLAQ NLSSKNPKHE HFQSLNFPHT 

       670        680        690        700        710        720 
KEMMKIFHKK FGLHNFRTNQ LEAINAALLG EDCFILMPTG GGKSLCYQLP ACVSPGVTIV 

       730        740        750        760        770        780 
ISPLRSLIVD QVQKLTSFDI PATYLTGDKT DSEAANIYLQ LSKKDPIIKL LYVTPEKVCA 

       790        800        810        820        830        840 
SNRLISTLEN LYERKLLARF VIDEAHCVSQ WGHDFRQDYK RMNMLRQKFP SVPVMALTAT 

       850        860        870        880        890        900 
ANPRVQKDIL TQLKILRPQV FSMSFNRHNL KYYVLPKKPK KVAFDCLEWI RKHHPYDSGI 

       910        920        930        940        950        960 
IYCLSRRECD TMADTLQREG LAALAYHAGL SDSARDEVQH KWINQDNCQV ICATIAFGMG 

       970        980        990       1000       1010       1020 
IDKPDVRFVI HASLPKSMEG YYQESGRAGR DGEISHCVLF YTYHDVTRLK RLIMMEKDGN 

      1030       1040       1050       1060       1070       1080 
YHTKETHVNN LYSMVHYCEN ITECRRIQLL AYFGEKGFNP DFCKKYPDVS CDNCCKTKDY 

      1090       1100       1110       1120       1130       1140 
KTKDVTDDVK NIIRFVQEHS SSPGTRNIGP AGRFTLNMLV DIFLGSKSAK VKSGIFGKGT 

      1150       1160       1170       1180       1190       1200 
TYSRHNAERL FKKLILDKIL DEDLYINAND QPIAYVMLGT KAHSVLSGHL KVDFMETENS 

      1210       1220       1230       1240       1250       1260 
SSIKKQKALV AKVSQREEVV KKCLGELTEV CKLLGKVFGV HYFNIFNTAT LKKLAESLSS 

      1270       1280       1290       1300       1310       1320 
DPEVLLQIDG VTEDKLEKYG AEVIPVLQKY SEWTVPAEDG SPGARGAPED TEEEEEEAPV 

      1330       1340       1350       1360       1370       1380 
SSHYFANQTR NERKRKKMSA THKPKRRRTS YGGFRAKGGS TTCRKTTSKS KFYGVTGSRS 

      1390       1400       1410 
ASCASQATSS ASRKLGIMAP PKPVNRTFLR PSYAFS

O88700 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools