CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020301
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fanconi anemia group J protein 
Protein Synonyms/Alias
 Protein FACJ; ATP-dependent RNA helicase BRIP1; BRCA1-associated C-terminal helicase 1; BRCA1-interacting protein C-terminal helicase 1; BRCA1-interacting protein 1 
Gene Name
 BRIP1 
Gene Synonyms/Alias
 BACH1; FANCJ 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39ILRGLNSKQHCLLESubiquitination[1]
141LAAKLSAKKQASIYRacetylation[2]
142AAKLSAKKQASIYRDubiquitination[1]
194VDSGKTVKLNSPLEKacetylation[2]
222SRCCCSTKQGNSQESubiquitination[1]
234QESSNTIKKDHTGKSubiquitination[3]
235ESSNTIKKDHTGKSKubiquitination[3]
297GNFNRNEKCMELLDGubiquitination[1]
345EELVSLGKKLKACPYubiquitination[1, 3]
346ELVSLGKKLKACPYYubiquitination[1]
348VSLGKKLKACPYYTAubiquitination[1]
510KISPIYGKEEAREVPubiquitination[1]
656GTIGSGPKGRNLCATubiquitination[1]
732VEPQGGEKTNFDELLubiquitination[3]
764LVAVCRGKVSEGLDFubiquitination[1, 3]
797KDLQVELKRQYNDHHubiquitination[1, 3]
862RYISGLSKWVRQQIQubiquitination[1, 4, 5]
897KVLNVSIKDRTNIQDacetylation[2]
897KVLNVSIKDRTNIQDubiquitination[1, 3]
954QCPKIITKNSPLPSSacetylation[2]
954QCPKIITKNSPLPSSubiquitination[1]
966PSSIISRKEKNDPVFacetylation[2]
1015LGQYFTGKIPKATPEacetylation[2]
1240NFKPSPSKNKGMFPGacetylation[2]
1242KPSPSKNKGMFPGFKacetylation[2]
1249KGMFPGFK*******acetylation[2]
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] FANCJ/BACH1 acetylation at lysine 1249 regulates the DNA damage response.
 Xie J, Peng M, Guillemette S, Quan S, Maniatis S, Wu Y, Venkatesh A, Shaffer SA, Brosh RM Jr, Cantor SB.
 PLoS Genet. 2012 Jul;8(7):e1002786. [PMID: 22792074]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1. 
Sequence Annotation
 DOMAIN 11 442 Helicase ATP-binding.
 NP_BIND 185 192 ATP (By similarity).
 REGION 888 1063 Interaction with BRCA1.
 MOTIF 158 175 Nuclear localization signal (Potential).
 MOTIF 393 396 DEAH box.
 METAL 283 283 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 298 298 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 310 310 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 350 350 Iron-sulfur (4Fe-4S) (By similarity).
 MOD_RES 927 927 Phosphoserine.
 MOD_RES 930 930 Phosphoserine.
 MOD_RES 990 990 Phosphoserine.
 MOD_RES 1032 1032 Phosphoserine.
 MOD_RES 1237 1237 Phosphoserine.  
Keyword
 3D-structure; 4Fe-4S; Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; Fanconi anemia; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1249 AA 
Protein Sequence
MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS GKSLALLCSA 60
LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM NQGTSRHFNY PSTPPSERNG 120
TSSTCQDSPE KTTLAAKLSA KKQASIYRDE NDDFQVEKKR IRPLETTQQI RKRHCFGTEV 180
HNLDAKVDSG KTVKLNSPLE KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK 240
SKIPKIYFGT RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 300
LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC PYYTARELIQ 360
DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED CARESASYSV TEVQLRFARD 420
ELDSMVNNNI RKKDHEPLRA VCCSLINWLE ANAEYLVERD YESACKIWSG NEMLLTLHKM 480
GITTATFPIL QGHFSAVLQK EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ 540
NSRFADDYKI AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 600
SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT IGSGPKGRNL 660
CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL LEKLKERWLS TGLWHNLELV 720
KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG EKDGALLVAV CRGKVSEGLD FSDDNARAVI 780
TIGIPFPNVK DLQVELKRQY NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG 840
ALILVDDRFR NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 900
NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK IITKNSPLPS 960
SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV SWSSFNSLGQ YFTGKIPKAT 1020
PELGSSENSA SSPPRFKTEK MESKTVLPFT DKCESSNLTV NTSFGSCPQS ETIISSLKID 1080
ATLTRKNHSE HPLCSEEALD PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE 1140
DTDEEKNDLA ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH 1200
IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK 1249 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004003; F:ATP-dependent DNA helicase activity; NAS:UniProtKB.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000077; P:DNA damage checkpoint; NAS:UniProtKB.
 GO:0006302; P:double-strand break repair; NAS:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI. 
Interpro
 IPR006555; ATP-dep_Helicase_C.
 IPR010614; DEAD_2.
 IPR013020; DNA_helicase_DNA-repair_Rad3.
 IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
 IPR014001; Helicase_ATP-bd.
 IPR027417; P-loop_NTPase. 
Pfam
 PF06733; DEAD_2
 PF13307; Helicase_C_2 
SMART
 SM00487; DEXDc
 SM00491; HELICc2 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51193; HELICASE_ATP_BIND_2 
PRINTS