CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015892
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable helicase senataxin 
Protein Synonyms/Alias
 Amyotrophic lateral sclerosis 4 protein; SEN1 homolog 
Gene Name
 SETX 
Gene Synonyms/Alias
 ALS4; KIAA0625; SCAR1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19ASTIDFLKRYASNTPubiquitination[1, 2, 3]
49ECVAEYHKARDELPFubiquitination[2, 4]
75RLINHFEKSMKAEIGubiquitination[2, 5]
119VPLLEILKYPYLLLHubiquitination[5, 6]
180LTARNLGKVDRDDYYubiquitination[6]
218YTSSVLEKGKLILLPubiquitination[5, 7]
220SSVLEKGKLILLPSHubiquitination[2]
339RNSSVRTKLEPESYLubiquitination[2, 4, 6]
544QLIRSLLKEGYQLGQubiquitination[4]
556LGQQSLCKRFWDKLNubiquitination[2]
561LCKRFWDKLNLFLRGubiquitination[2]
598IIRNIKFKAPPCNTFubiquitination[2, 4]
621ISPASYNKEESEQMGubiquitination[2, 5, 6]
629EESEQMGKTSRKDMHubiquitination[2, 5, 6]
651TFSKEPMKVQDSVLIubiquitination[5]
659VQDSVLIKADNTIEGubiquitination[2, 5]
675NNEQNYIKDVKLEDHubiquitination[2, 4, 5, 7]
690LLAGSCLKQSSKNIFubiquitination[2, 3]
694SCLKQSSKNIFTERAubiquitination[2]
706ERAEDQIKISTRKQKubiquitination[2, 5]
716TRKQKSVKEISSYTPubiquitination[2]
724EISSYTPKDCTSRNGubiquitination[2]
757SSTDALEKVSTSNEDubiquitination[2, 5]
768SNEDFSLKDDALAKTubiquitination[2, 3, 5, 6, 7]
774LKDDALAKTSKRKTKubiquitination[2, 5]
827IESFYSRKDTGVQKGubiquitination[5]
833RKDTGVQKGDGFIHNubiquitination[5]
852PSGVLDDKNGEQKSQubiquitination[5]
857DDKNGEQKSQNNVLPubiquitination[5]
894QEFHVDGKELIPFTEubiquitination[5]
908EMTNASEKKSSPFKDubiquitination[2, 5]
914EKKSSPFKDLMTVPEubiquitination[5]
949QAPDISPKSDTLTDSubiquitination[4, 5]
1032ERILSLEKLTKQDKIubiquitination[5]
1035LSLEKLTKQDKICLEubiquitination[5]
1038EKLTKQDKICLEREHubiquitination[2]
1056HVSTVNSKEEKNPVKubiquitination[5]
1109SVQDGEKKCLAPIANubiquitination[2]
1132DYVSEVVKKGAEGIEubiquitination[5]
1133YVSEVVKKGAEGIEEubiquitination[6]
1167PKRKRSEKPMAEDPVubiquitination[2, 5]
1190EGQSDTNKRDLVGNDubiquitination[5]
1315AQLRDHGKTVGVVDTubiquitination[2, 5]
1552SGTKCKYKDCLETTKubiquitination[2]
1572CPKHSEVKAADEDVFubiquitination[5]
1602TTKIFSSKSTSRIAGubiquitination[2]
1612SRIAGLSKSLETSSAubiquitination[2, 5]
1625SALSPSLKNKSKGIQubiquitination[5]
1627LSPSLKNKSKGIQSIubiquitination[2]
1636KGIQSILKVPQPVPLubiquitination[2]
1647PVPLIAQKPVGEMKNacetylation[8, 9, 10]
1647PVPLIAQKPVGEMKNubiquitination[2, 5, 7]
1680KVPFGESKYFPSSSPubiquitination[4, 5]
1806LAKQLYPKENDLVFLubiquitination[2, 5]
1917NPMDFCTKDLLTTTSubiquitination[2, 3, 4, 6]
1950ETAYAMVKHSPSVAKubiquitination[2]
1969HGPPGTGKSKTIVGLubiquitination[2]
1971PPGTGKSKTIVGLLYubiquitination[2]
2019AVDELMKKIILEFKEubiquitination[2]
2025KKIILEFKEKCKDKKubiquitination[2]
2027IILEFKEKCKDKKNPmethylation[11]
2050LVRLGPEKSINSEVLubiquitination[2, 5]
2058SINSEVLKFSLDSQVubiquitination[2]
2084VQAMHKRKEFLDYQLubiquitination[2]
2118ELDENISKVSKERQEubiquitination[5]
2201PLIHRCNKLILVGDPubiquitination[2]
2349IGIITHYKAQKTMIQubiquitination[3]
2352ITHYKAQKTMIQKDLubiquitination[2]
2366LDKEFDRKGPAEVDTubiquitination[2, 3, 5]
2443QLIQDAQKRGAIIKTubiquitination[2]
2464HDAVKILKLKPVLQRubiquitination[2]
2466AVKILKLKPVLQRSLubiquitination[2]
2494QGGLPSSKLDSGFAKubiquitination[5]
2501KLDSGFAKTSVAASLubiquitination[2, 5]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] 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]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [11] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510
Functional Description
 Probable helicase, which may be involved in RNA maturation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress. 
Sequence Annotation
 NP_BIND 1963 1970 ATP (Potential).
 REGION 2661 2677 Necessary for nuclear localization.
 MOTIF 2070 2087 Bipartite nuclear localization signal
 MOD_RES 615 615 Phosphoserine.
 MOD_RES 1017 1017 Phosphoserine.
 MOD_RES 1019 1019 Phosphoserine.
 MOD_RES 1621 1621 Phosphoserine.  
Keyword
 Alternative splicing; Amyotrophic lateral sclerosis; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Disease mutation; DNA damage; DNA repair; Helicase; Hydrolase; Neurodegeneration; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2677 AA 
Protein Sequence
MSTCCWCTPG GASTIDFLKR YASNTPSGEF QTADEDLCYC LECVAEYHKA RDELPFLHEV 60
LWELETLRLI NHFEKSMKAE IGDDDELYIV DNNGEMPLFD ITGQDFENKL RVPLLEILKY 120
PYLLLHERVN ELCVEALCRM EQANCSFQVF DKHPGIYLFL VHPNEMVRRW AILTARNLGK 180
VDRDDYYDLQ EVLLCLFKVI ELGLLESPDI YTSSVLEKGK LILLPSHMYD TTNYKSYWLG 240
ICMLLTILEE QAMDSLLLGS DKQNDFMQSI LHTMEREADD DSVDPFWPAL HCFMVILDRL 300
GSKVWGQLMD PIVAFQTIIN NASYNREIRH IRNSSVRTKL EPESYLDDMV TCSQIVYNYN 360
PEKTKKDSGW RTAICPDYCP NMYEEMETLA SVLQSDIGQD MRVHNSTFLW FIPFVQSLMD 420
LKDLGVAYIA QVVNHLYSEV KEVLNQTDAV CDKVTEFFLL ILVSVIELHR NKKCLHLLWV 480
SSQQWVEAVV KCAKLPTTAF TRSSEKSSGN CSKGTAMISS LSLHSMPSNS VQLAYVQLIR 540
SLLKEGYQLG QQSLCKRFWD KLNLFLRGNL SLGWQLTSQE THELQSCLKQ IIRNIKFKAP 600
PCNTFVDLTS ACKISPASYN KEESEQMGKT SRKDMHCLEA SSPTFSKEPM KVQDSVLIKA 660
DNTIEGDNNE QNYIKDVKLE DHLLAGSCLK QSSKNIFTER AEDQIKISTR KQKSVKEISS 720
YTPKDCTSRN GPERGCDRGI IVSTRLLTDS STDALEKVST SNEDFSLKDD ALAKTSKRKT 780
KVQKDEICAK LSHVIKKQHR KSTLVDNTIN LDENLTVSNI ESFYSRKDTG VQKGDGFIHN 840
LSLDPSGVLD DKNGEQKSQN NVLPKEKQLK NEELVIFSFH ENNCKIQEFH VDGKELIPFT 900
EMTNASEKKS SPFKDLMTVP ESRDEEMSNS TSVIYSNLTR EQAPDISPKS DTLTDSQIDR 960
DLHKLSLLAQ ASVITFPSDS PQNSSQLQRK VKEDKRCFTA NQNNVGDTSR GQVIIISDSD 1020
DDDDERILSL EKLTKQDKIC LEREHPEQHV STVNSKEEKN PVKEEKTETL FQFEESDSQC 1080
FEFESSSEVF SVWQDHPDDN NSVQDGEKKC LAPIANTTNG QGCTDYVSEV VKKGAEGIEE 1140
HTRPRSISVE EFCEIEVKKP KRKRSEKPMA EDPVRPSSSV RNEGQSDTNK RDLVGNDFKS 1200
IDRRTSTPNS RIQRATTVSQ KKSSKLCTCT EPIRKVPVSK TPKKTHSDAK KGQNRSSNYL 1260
SCRTTPAIVP PKKFRQCPEP TSTAEKLGLK KGPRKAYELS QRSLDYVAQL RDHGKTVGVV 1320
DTRKKTKLIS PQNLSVRNNK KLLTSQELQM QRQIRPKSQK NRRRLSDCES TDVKRAGSHT 1380
AQNSDIFVPE SDRSDYNCTG GTEVLANSNR KQLIKCMPSE PETIKAKHGS PATDDACPLN 1440
QCDSVVLNGT VPTNEVIVST SEDPLGGGDP TARHIEMAAL KEGEPDSSSD AEEDNLFLTQ 1500
NDPEDMDLCS QMENDNYKLI ELIHGKDTVE VEEDSVSRPQ LESLSGTKCK YKDCLETTKN 1560
QGEYCPKHSE VKAADEDVFR KPGLPPPASK PLRPTTKIFS SKSTSRIAGL SKSLETSSAL 1620
SPSLKNKSKG IQSILKVPQP VPLIAQKPVG EMKNSCNVLH PQSPNNSNRQ GCKVPFGESK 1680
YFPSSSPVNI LLSSQSVSDT FVKEVLKWKY EMFLNFGQCG PPASLCQSIS RPVPVRFHNY 1740
GDYFNVFFPL MVLNTFETVA QEWLNSPNRE NFYQLQVRKF PADYIKYWEF AVYLEECELA 1800
KQLYPKENDL VFLAPERINE EKKDTERNDI QDLHEYHSGY VHKFRRTSVM RNGKTECYLS 1860
IQTQENFPAN LNELVNCIVI SSLVTTQRKL KAMSLLGSRN QLARAVLNPN PMDFCTKDLL 1920
TTTSERIIAY LRDFNEDQKK AIETAYAMVK HSPSVAKICL IHGPPGTGKS KTIVGLLYRL 1980
LTENQRKGHS DENSNAKIKQ NRVLVCAPSN AAVDELMKKI ILEFKEKCKD KKNPLGNCGD 2040
INLVRLGPEK SINSEVLKFS LDSQVNHRMK KELPSHVQAM HKRKEFLDYQ LDELSRQRAL 2100
CRGGREIQRQ ELDENISKVS KERQELASKI KEVQGRPQKT QSIIILESHI ICCTLSTSGG 2160
LLLESAFRGQ GGVPFSCVIV DEAGQSCEIE TLTPLIHRCN KLILVGDPKQ LPPTVISMKA 2220
QEYGYDQSMM ARFCRLLEEN VEHNMISRLP ILQLTVQYRM HPDICLFPSN YVYNRNLKTN 2280
RQTEAIRCSS DWPFQPYLVF DVGDGSERRD NDSYINVQEI KLVMEIIKLI KDKRKDVSFR 2340
NIGIITHYKA QKTMIQKDLD KEFDRKGPAE VDTVDAFQGR QKDCVIVTCV RANSIQGSIG 2400
FLASLQRLNV TITRAKYSLF ILGHLRTLME NQHWNQLIQD AQKRGAIIKT CDKNYRHDAV 2460
KILKLKPVLQ RSLTHPPTIA PEGSRPQGGL PSSKLDSGFA KTSVAASLYH TPSDSKEITL 2520
TVTSKDPERP PVHDQLQDPR LLKRMGIEVK GGIFLWDPQP SSPQHPGATP PTGEPGFPVV 2580
HQDLSHIQQP AAVVAALSSH KPPVRGEPPA ASPEASTCQS KCDDPEEELC HRREARAFSE 2640
GEQEKCGSET HHTRRNSRWD KRTLEQEDSS SKKRKLL 2677 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IC:UniProtKB.
 GO:0003678; F:DNA helicase activity; TAS:UniProtKB.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0007623; P:circadian rhythm; IEA:Compara.
 GO:0006302; P:double-strand break repair; IDA:UniProtKB.
 GO:0006396; P:RNA processing; TAS:UniProtKB.
 GO:0006369; P:termination of RNA polymerase II transcription; IEA:Compara. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR026121; Senataxin. 
Pfam
  
SMART
  
PROSITE
  
PRINTS