CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008836
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bloom syndrome protein 
Protein Synonyms/Alias
 DNA helicase, RecQ-like type 2; RecQ2; RecQ protein-like 3 
Gene Name
 BLM 
Gene Synonyms/Alias
 RECQ2; RECQL3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
105ETQRGGSKSLLPDFLubiquitination[1]
129TQNTPTVKKSRDTALubiquitination[1]
317SASSSSSKCLSTLKDsumoylation[2, 3, 4]
331DLDTSDRKEDVLSTSsumoylation[2, 3, 4]
344TSKDLLSKPEKMSMQsumoylation[2]
347DLLSKPEKMSMQELNsumoylation[2]
390IDTIPDDKLKLLDCGubiquitination[1]
392TIPDDKLKLLDCGNEubiquitination[1]
409QQRNIRRKLLTEVDFubiquitination[1]
662MMKIFHKKFGLHNFRubiquitination[1]
755NIYLQLSKKDPIIKLacetylation[5]
769LLYVTPEKICASNRLubiquitination[1]
820RMNMLRQKFPSVPVMubiquitination[1]
863SFNRHNLKYYVLPKKacetylation[5]
1133IQSGIFGKGSAYSRHubiquitination[1]
1200ENSSSVKKQKALVAKubiquitination[1]
1207KQKALVAKVSQREEMubiquitination[1]
1411PINRPFLKPSYAFS*acetylation[5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Intra-nuclear trafficking of the BLM helicase to DNA damage-induced foci is regulated by SUMO modification.
 Eladad S, Ye TZ, Hu P, Leversha M, Beresten S, Matunis MJ, Ellis NA.
 Hum Mol Genet. 2005 May 15;14(10):1351-65. [PMID: 15829507]
 [3] Ubc9- and mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks.
 Branzei D, Sollier J, Liberi G, Zhao X, Maeda D, Seki M, Enomoto T, Ohta K, Foiani M.
 Cell. 2006 Nov 3;127(3):509-22. [PMID: 17081974]
 [4] SUMO modification regulates BLM and RAD51 interaction at damaged replication forks.
 Ouyang KJ, Woo LL, Zhu J, Huo D, Matunis MJ, Ellis NA.
 PLoS Biol. 2009 Dec;7(12):e1000252. [PMID: 19956565]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 676 851 Helicase ATP-binding.
 DOMAIN 877 1024 Helicase C-terminal.
 DOMAIN 1212 1292 HRDC.
 NP_BIND 689 696 ATP (By similarity).
 MOTIF 795 798 DEAH box.
 MOTIF 1334 1349 Nuclear localization signal (Potential).
 MOD_RES 28 28 Phosphoserine.
 MOD_RES 48 48 Phosphoserine.
 MOD_RES 57 57 Phosphothreonine.
 MOD_RES 114 114 Phosphothreonine.
 MOD_RES 168 168 Phosphoserine.
 MOD_RES 171 171 Phosphothreonine.
 MOD_RES 358 358 Phosphoserine.
 MOD_RES 419 419 Phosphoserine.
 MOD_RES 422 422 Phosphoserine.
 MOD_RES 426 426 Phosphoserine.
 MOD_RES 499 499 Phosphoserine.
 MOD_RES 508 508 Phosphothreonine.
 MOD_RES 863 863 N6-acetyllysine.
 MOD_RES 1295 1295 Phosphoserine.
 MOD_RES 1296 1296 Phosphoserine.
 MOD_RES 1310 1310 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Disease mutation; DNA replication; DNA-binding; Dwarfism; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1417 AA 
Protein Sequence
MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT NVSVAKTPVL 60
RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ RGGSKSLLPD FLQTPKEVVC 120
TTQNTPTVKK SRDTALKKLE FSSSPDSLST INDWDDMDDF DTSETSKSFV TPPQSHFVRV 180
STAQKSKKGK RNFFKAQLYT TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD 240
GPIAEVHINE DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF 300
VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM QELNPETSTD 360
CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL LQQRNIRRKL LTEVDFNKSD 420
ASLLGSLWRY RPDSLDGPME GDSCPTGNSM KELNFSHLPS NSVSPGDCLL TTTLGKTGFS 480
ATRKNLFERP LFNTHLQKSF VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI 540
NDLERETQPS YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL 600
SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP HTKEMMKIFH 660
KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ LPACVSPGVT VVISPLRSLI 720
VDQVQKLTSL DIPATYLTGD KTDSEATNIY LQLSKKDPII KLLYVTPEKI CASNRLISTL 780
ENLYERKLLA RFVIDEAHCV SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD 840
ILTQLKILRP QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE 900
CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG MGIDKPDVRF 960
VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR LKRLIMMEKD GNHHTRETHF 1020
NNLYSMVHYC ENITECRRIQ LLAYFGENGF NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD 1080
VKSIVRFVQE HSSSQGMRNI KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH 1140
NAERLFKKLI LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK 1200
QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA ESLSSDPEVL 1260
LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS LSSSRGPGRS AAEELDEEIP 1320
VSSHYFASKT RNERKRKKMP ASQRSKRRKT ASSGSKAKGG SATCRKISSK TKSSSIIGSS 1380
SASHTSQATS GANSKLGIMA PPKPINRPFL KPSYAFS 1417 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0000800; C:lateral element; IDA:UniProtKB.
 GO:0001673; C:male germ cell nucleus; IEA:Compara.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0045120; C:pronucleus; IEA:Compara.
 GO:0005657; C:replication fork; IEA:Compara.
 GO:0036310; F:annealing helicase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:Compara.
 GO:0004003; F:ATP-dependent DNA helicase activity; IDA:UniProtKB.
 GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
 GO:0009378; F:four-way junction helicase activity; IDA:UniProtKB.
 GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
 GO:0046632; P:alpha-beta T cell differentiation; IEA:Compara.
 GO:0000729; P:DNA double-strand break processing; IDA:UniProtKB.
 GO:0000724; P:double-strand break repair via homologous recombination; NAS:UniProtKB.
 GO:0031572; P:G2 DNA damage checkpoint; NAS:UniProtKB.
 GO:0000085; P:G2 phase of mitotic cell cycle; NAS:UniProtKB.
 GO:0051782; P:negative regulation of cell division; IMP:UniProtKB.
 GO:0045910; P:negative regulation of DNA recombination; IMP:UniProtKB.
 GO:0045950; P:negative regulation of mitotic recombination; IEA:Compara.
 GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0051259; P:protein oligomerization; IDA:UniProtKB.
 GO:0051098; P:regulation of binding; IEA:Compara.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
 GO:0031297; P:replication fork processing; IDA:UniProtKB.
 GO:0048478; P:replication fork protection; NAS:UniProtKB.
 GO:0010165; P:response to X-ray; IDA:UniProtKB.
 GO:0000723; P:telomere maintenance; IEA:Compara. 
Interpro
 IPR012532; 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. 
Pfam
 PF08072; BDHCT
 PF00270; DEAD
 PF00271; Helicase_C
 PF00570; HRDC
 PF09382; RQC 
SMART
 SM00487; DEXDc
 SM00490; HELICc
 SM00341; HRDC
 SM00956; RQC 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS50967; HRDC 
PRINTS