(data stored in ACNUC18484 zone)

HOGENOM: MOUSE7_PE2117

ID   MOUSE7_PE2117                        STANDARD;      PRT;   1416 AA.
AC   MOUSE7_PE2117; O88700; O88198;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Bloom syndrome protein homolog; Short=mBLM; EC=3.6.4
DE   12;AltName: Full=RecQ helicase homolog; (MOUSE7.PE2117).
GN   Name=Blm;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE7.PE2117.
CC       Mus musculus chromosome 7 NCBIM37  sequence 1..152524553 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:BLM_MOUSE
CC   -!- FUNCTION: Participates in DNA replication and repair. Exhibits a
CC       magnesium-dependent ATP-dependent DNA-helicase activity that
CC       unwinds single- and double-stranded DNA in a 3'-5' direction.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Part of the BRCA1-associated genome surveillance complex
CC       (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and
CC       the RAD50-MRE11-NBS1 protein complex. This association could be a
CC       dynamic process changing throughout the cell cycle and within
CC       subnuclear domains. Interacts with ubiquitinated FANCD2. Interacts
CC       with RMI complex. Interacts directly with RMI1 component of RMI
CC       complex. Interacts with SUPV3L1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis 12-14 days after
CC       birth (corresponding to the pachytene phase) and at much lower
CC       levels in brain, heart, liver, lung, thymus, kidney and spleen.
CC   -!- PTM: Phosphorylated in response to DNA damage. Phosphorylation
CC       requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as
CC       well as the presence of RMI1 (By similarity).
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 HRDC domain.
CC   -!- GENE_FAMILY: HOG000095239 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000030528;ENSMUST00000081314;ENSMUSP00000080062.
DR   EMBL; AB008674; - ;
DR   EMBL; Z98263; - ;
DR   UniProtKB/Swiss-Prot; O88700; O88198; -.
DR   EMBL; Z98263; CAB10933.1; -; mRNA.
DR   EMBL; AB008674; BAA32001.1; -; mRNA.
DR   IPI; IPI00329943; -.
DR   RefSeq; NP_001035992.1; NM_001042527.2.
DR   RefSeq; NP_031576.4; NM_007550.4.
DR   UniGene; Mm.12932; -.
DR   ProteinModelPortal; O88700; -.
DR   SMR; O88700; 651-1198, 1205-1299.
DR   DIP; DIP-27643N; -.
DR   STRING; O88700; -.
DR   PhosphoSite; O88700; -.
DR   PRIDE; O88700; -.
DR   Ensembl; ENSMUST00000081314; ENSMUSP00000080062; ENSMUSG00000030528.
DR   GeneID; 12144; -.
DR   KEGG; mmu:12144; -.
DR   UCSC; uc009iaw.2; mouse.
DR   CTD; 641; -.
DR   MGI; MGI:1328362; Blm.
DR   eggNOG; roNOG06057; -.
DR   GeneTree; ENSGT00550000074520; -.
DR   InParanoid; O88700; -.
DR   OMA; NANDQAI; -.
DR   OrthoDB; EOG4640B3; -.
DR   PhylomeDB; O88700; -.
DR   Reactome; REACT_27235; Meiotic Recombination (mouse).
DR   NextBio; 280473; -.
DR   ArrayExpress; O88700; -.
DR   Bgee; O88700; -.
DR   CleanEx; MM_BLM; -.
DR   Genevestigator; O88700; -.
DR   GermOnline; ENSMUSG00000030528; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0045120; C:pronucleus; IDA:MGI.
DR   GO; GO:0005657; C:replication fork; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
DR   GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045950; P:negative regulation of mitotic recombination; IMP:MGI.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:MGI.
DR   GO; GO:0051098; P:regulation of binding; IDA:MGI.
DR   InterPro; IPR012532; BDHCT.
DR   InterPro; IPR014001; DEAD-like_helicase.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR002121; Helicase/RNaseD_C.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like.
DR   InterPro; IPR018982; RQC_domain.
DR   PANTHER; PTHR13710; RecQ; 1.
DR   Pfam; PF08072; BDHCT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF47819; HRDC_like; 1.
DR   TIGRFAMs; TIGR00614; RecQ_fam; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
DR   HOGENOMDNA; MOUSE7.PE2117; -.
KW   ENSMUSG000000305285old_1320000031; ENSMUSP000000800621old_1320000031;
KW   AB008674; Z98263;
KW   Acetylation; ATP-binding; Complete proteome; DNA replication;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
SQ   SEQUENCE   1416 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAAVPLNNLQ EQLQRHSARK LNNQPSLSKP KSLGFTFKKK TSEGDVSVTS VSVVKTPALS
     DKDVNVSEAF SFTESPLHKP KQQAKIEGFF KHFPGRQQSK GTCSEPSLPA TVQTAQDTLC
     TTPKTPTAKK LPVAVFKKLE FSSSADSLSD WADMDDFDMS ASDAFASLAK NPATRVSTAQ
     KMKKTKRNFF KPPPRKANAV KTDLTPPSPE CLQVDLTKES EEEEEEEEEA EGADCLSRDV
     ICIDNDSASE ELTEKDTQES QSLKAHLGAE RGDSEKKSHE DEAVFHSVQN TEYFEHNDND
     YDIDFVPPSP EEIISTASSS LKCSSMLKDL DDSDKEKGIL STSEELLSKP EEMTTHKSDA
     GTSKDCDAQQ IRIQQQLIHV MEHICKLVDT VPTDELEALN CGTELLQQRN IRRKLLAEAG
     FNGNDVRLLG SLWRHRPDSL DNTVQGDSCP VGHPNKELNS PYLLSHSPST EECLPTTTPG
     KTGFSATPKN LFERPLLNSH LQKSFVSSNW AETPRMENRN ESTDFPGSVL TSTTVKAQSK
     QAASGWNVER HGQASYDIDN FNIDDFDDDD DDDDWENIMH NFPASKSSTA TYPPIKEGGP
     VKSLSERISS AKAKFLPVVS TAQNTNLSES IQNCSDKLAQ NLSSKNPKHE HFQSLNFPHT
     KEMMKIFHKK FGLHNFRTNQ LEAINAALLG EDCFILMPTG GGKSLCYQLP ACVSPGVTIV
     ISPLRSLIVD QVQKLTSFDI PATYLTGDKT DSEAANIYLQ LSKKDPIIKL LYVTPEKVCA
     SNRLISTLEN LYERKLLARF VIDEAHCVSQ WGHDFRQDYK RMNMLRQKFP SVPVMALTAT
     ANPRVQKDIL TQLKILRPQV FSMSFNRHNL KYYVLPKKPK KVAFDCLEWI RKHHPYDSGI
     IYCLSRRECD TMADTLQREG LAALAYHAGL SDSARDEVQH KWINQDNCQV ICATIAFGMG
     IDKPDVRFVI HASLPKSMEG YYQESGRAGR DGEISHCVLF YTYHDVTRLK RLIMMEKDGN
     YHTKETHVNN LYSMVHYCEN ITECRRIQLL AYFGEKGFNP DFCKKYPDVS CDNCCKTKDY
     KTKDVTDDVK NIIRFVQEHS SSPGTRNIGP AGRFTLNMLV DIFLGSKSAK VKSGIFGKGT
     TYSRHNAERL FKKLILDKIL DEDLYINAND QPIAYVMLGT KAHSVLSGHL KVDFMETENS
     SSIKKQKALV AKVSQREEVV KKCLGELTEV CKLLGKVFGV HYFNIFNTAT LKKLAESLSS
     DPEVLLQIDG VTEDKLEKYG AEVIPVLQKY SEWTVPAEDG SPGARGAPED TEEEEEEAPV
     SSHYFANQTR NERKRKKMSA THKPKRRRTS YGGFRAKGGS TTCRKTTSKS KFYGVTGSRS
     ASCASQATSS ASRKLGIMAP PKPVNRTFLR PSYAFS
//

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