(data stored in ACNUC18484 zone)

HOGENOM: HS15_PE1548

ID   HS15_PE1548                          STANDARD;      PRT;   1417 AA.
AC   HS15_PE1548; P54132; Q52M96;
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; EC=3.6.4 12;AltName: Full=DNA
DE   helicase, RecQ-like type 2; Short=RecQ2;AltName: Full=RecQ protein-like
DE   3; (HS15.PE1548).
GN   Name=BLM; Synonyms=RECQ2, RECQL3;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS15.PE1548.
CC       Homo sapiens chromosome 15 GRCh37  sequence 1..102521392 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:BLM_HUMAN
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.
CC   -!- INTERACTION:
CC       P39748:FEN1; NbExp=4; IntAct=EBI-621372, EBI-707816;
CC       Q9H9A7:RMI1; NbExp=7; IntAct=EBI-621372, EBI-621339;
CC       P27694:RPA1; NbExp=3; IntAct=EBI-621372, EBI-621389;
CC       P54274:TERF1; NbExp=3; IntAct=EBI-621372, EBI-710997;
CC       Q15554:TERF2; NbExp=8; IntAct=EBI-621372, EBI-706637;
CC       Q14191:WRN; NbExp=9; IntAct=EBI-621372, EBI-368417;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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.
CC   -!- DISEASE: Defects in BLM are the cause of Bloom syndrome (BLM)
CC       [MIM:210900]. BLM is an autosomal recessive disorder characterized
CC       by proportionate pre- and postnatal growth deficiency, sun-
CC       sensitive telangiectatic hypo- and hyperpigmented skin,
CC       predisposition to malignancy, and chromosomal instability.
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   -!- WEB RESOURCE: Name=BLMbase; Note=BLM mutation db;
CC       URL="http://bioinf.uta.fi/BLMbase/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/BLM109.html";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/BLM";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/blm/";
CC   -!- GENE_FAMILY: HOG000095239 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000197299;ENST00000355112;ENSP00000347232.
DR   EMBL; AK295194; - ;
DR   EMBL; AK303159; - ;
DR   EMBL; AK314262; - ;
DR   EMBL; AY886902; - ;
DR   EMBL; BC093622; - ;
DR   EMBL; BC101567; - ;
DR   EMBL; BC107423; - ;
DR   EMBL; BC115030; - ;
DR   EMBL; BC115032; - ;
DR   EMBL; BC143280; - ;
DR   EMBL; U39817; - ;
DR   UniProtKB/Swiss-Prot; P54132; Q52M96; -.
DR   EMBL; U39817; AAA87850.1; -; mRNA.
DR   EMBL; AY886902; AAW62255.1; -; Genomic_DNA.
DR   EMBL; BC093622; AAH93622.1; -; mRNA.
DR   EMBL; BC101567; AAI01568.1; -; mRNA.
DR   EMBL; BC115030; AAI15031.1; -; mRNA.
DR   EMBL; BC115032; AAI15033.1; -; mRNA.
DR   IPI; IPI00004859; -.
DR   PIR; A57570; A57570.
DR   RefSeq; NP_000048.1; NM_000057.2.
DR   UniGene; Hs.725208; -.
DR   PDB; 2KV2; NMR; -; A=1210-1294.
DR   PDB; 2RRD; NMR; -; A=1200-1295.
DR   PDBsum; 2KV2; -.
DR   PDBsum; 2RRD; -.
DR   ProteinModelPortal; P54132; -.
DR   SMR; P54132; 643-1193, 1200-1295.
DR   DIP; DIP-33322N; -.
DR   IntAct; P54132; 13.
DR   MINT; MINT-131918; -.
DR   STRING; P54132; -.
DR   PhosphoSite; P54132; -.
DR   PRIDE; P54132; -.
DR   Ensembl; ENST00000355112; ENSP00000347232; ENSG00000197299.
DR   GeneID; 641; -.
DR   KEGG; hsa:641; -.
DR   UCSC; uc002bpr.1; human.
DR   CTD; 641; -.
DR   GeneCards; GC15P067371; -.
DR   H-InvDB; HIX0038129; -.
DR   HGNC; HGNC:1058; BLM.
DR   HPA; HPA005689; -.
DR   MIM; 210900; phenotype.
DR   MIM; 604610; gene.
DR   neXtProt; NX_P54132; -.
DR   Orphanet; 125; Bloom syndrome.
DR   PharmGKB; PA25369; -.
DR   eggNOG; prNOG14706; -.
DR   InParanoid; P54132; -.
DR   OMA; NANDQAI; -.
DR   OrthoDB; EOG4640B3; -.
DR   PhylomeDB; P54132; -.
DR   Pathway_Interaction_DB; telomerasepathway; Regulation of Telomerase.
DR   Reactome; REACT_27271; Meiotic Recombination.
DR   NextBio; 2600; -.
DR   PMAP-CutDB; P54132; -.
DR   ArrayExpress; P54132; -.
DR   Bgee; P54132; -.
DR   CleanEx; HS_BLM; -.
DR   Genevestigator; P54132; -.
DR   GermOnline; ENSG00000197299; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0000800; C:lateral element; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
DR   GO; GO:0000739; F:DNA strand annealing activity; IDA:UniProtKB.
DR   GO; GO:0009378; F:four-way junction helicase activity; IDA:UniProtKB.
DR   GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; NAS:UniProtKB.
DR   GO; GO:0000085; P:G2 phase of mitotic cell cycle; NAS:UniProtKB.
DR   GO; GO:0031572; P:G2/M transition DNA damage checkpoint; NAS:UniProtKB.
DR   GO; GO:0051782; P:negative regulation of cell division; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR   GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein kinase activity; IMP:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR   GO; GO:0048478; P:replication fork protection; NAS:UniProtKB.
DR   GO; GO:0010165; P:response to X-ray; IDA:UniProtKB.
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; HS15.PE1548; -.
KW   ENSG000001972991755old_1320000031; ENSP000003472327901old_1320000031;
KW   B2RAN0_HUMAN; B7Z2X2_HUMAN; B7Z8C1_HUMAN; B7ZKN7_HUMAN; Q3B7X0_HUMAN;
KW   AK303159; AK314262; AY886902; BC093622; BC101567; BC107423; BC115030;
KW   BC143280; U39817;
KW   3D-structure; Acetylation; ATP-binding; Complete proteome;
KW   Disease mutation; DNA replication; DNA-binding; Dwarfism; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome.
SQ   SEQUENCE   1417 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT NVSVAKTPVL
     RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ RGGSKSLLPD FLQTPKEVVC
     TTQNTPTVKK SRDTALKKLE FSSSPDSLST INDWDDMDDF DTSETSKSFV TPPQSHFVRV
     STAQKSKKGK RNFFKAQLYT TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD
     GPIAEVHINE DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF
     VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM QELNPETSTD
     CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL LQQRNIRRKL LTEVDFNKSD
     ASLLGSLWRY RPDSLDGPME GDSCPTGNSM KELNFSHLPS NSVSPGDCLL TTTLGKTGFS
     ATRKNLFERP LFNTHLQKSF VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI
     NDLERETQPS YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL
     SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP HTKEMMKIFH
     KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ LPACVSPGVT VVISPLRSLI
     VDQVQKLTSL DIPATYLTGD KTDSEATNIY LQLSKKDPII KLLYVTPEKI CASNRLISTL
     ENLYERKLLA RFVIDEAHCV SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD
     ILTQLKILRP QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE
     CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG MGIDKPDVRF
     VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR LKRLIMMEKD GNHHTRETHF
     NNLYSMVHYC ENITECRRIQ LLAYFGENGF NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD
     VKSIVRFVQE HSSSQGMRNI KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH
     NAERLFKKLI LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK
     QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA ESLSSDPEVL
     LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS LSSSRGPGRS AAEELDEEIP
     VSSHYFASKT RNERKRKKMP ASQRSKRRKT ASSGSKAKGG SATCRKISSK TKSSSIIGSS
     SASHTSQATS GANSKLGIMA PPKPINRPFL KPSYAFS
//

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