CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007779
UniProt Accession
Genbank Protein ID
 U72937; U72938; U72935; U72904; U72905; U72907; U72908; U72909; U72910; U72911; U72912; U72913; U72914; U72915; U72916; U72917; U72918; U72919; U72920; U72921; U72922; U72923; U72924; U72925; U72926; U72927; U72928; U72929; U72930; U72931; U72932; U72933; U72934; U72935; U72904; U72907; U72908; U72909; U72910; U72911; U72912; U72913; U72914; U72915; U72916; U72918; U72919; U72920; U72921; U72922; U72923; U72924; U72925; U72926; U72927; U72928; U72929; U72930; U72931; U72932; U72933; U72934; U72936; U72935; U72908; U72909; U72910; U72911; U72912; U72913; U72914; U72915; U72916; U72917; U72918; U72920; U72921; U72922; U72923; U72924; U72925; U72926; U72927; U72928; U72929; U72930; U72931; U72932; U72933; U72934; U75653; U97103; AF000157; AF000158; AF000159; AF000160; U97080; U97081; U97082; U97083; U97084; U97085; U97086; U97087; U97088; U97089; U97090; U97091; U97092; U97093; U97094; U97095; U97096; U97097; U97098; U97099; U97100; U97101; U97102; AB102641; AB101681; AB101682; AB101683; AB101685; AB101687; AB101689; AB101691; AB101693; AB101695; AB101700; AB101699; AB101698; AB101697; AB101696; AB101694; AB101692; AB101690; AB101688; AB101686; AB101684; AB208928; AB209545; AL121874; AL121874; AL109753; Z84487; Z84487; AL109753; AL121874; Z84487; AL109753; AL121874; AL109753; AL121874; Z84487; AL109753; AL121874; Z84487; CH471104; CH471104; U09820; L34363; X83753 
Genbank Nucleotide ID
 AAB49970.2; AAB49971.2; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40698.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB40699.1; AAB49969.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAB40700.1; AAC51655.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; AAC51657.1; BAC81110.1; BAC80270.1; BAC80271.1; BAC80272.1; BAC80274.1; BAC80276.1; BAC80278.1; BAC80280.1; BAC80282.1; BAC80284.1; BAC80289.1; BAC80288.1; BAC80287.1; BAC80286.1; BAC80285.1; BAC80283.1; BAC80281.1; BAC80279.1; BAC80277.1; BAC80275.1; BAC80273.1; BAD92165.1; BAD92782.1; CAB90351.2; CAI40710.1; CAI40710.1; CAI40710.1; CAI42674.1; CAI42674.1; CAI42674.1; CAI42675.1; CAI42675.1; CAI42675.1; CAI43115.1; CAI43115.1; CAI43115.1; CAI43116.1; CAI43116.1; CAI43116.1; EAW98611.1; EAW98615.1; AAC50069.1; AAA20872.1; CAA58711.1 
Protein Name
 Transcriptional regulator ATRX 
Protein Synonyms/Alias
 ATP-dependent helicase ATRX; X-linked helicase II; X-linked nuclear protein; XNP; Znf-HX 
Gene Name
 ATRX 
Gene Synonyms/Alias
 RAD54L; XH2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
202LICKNCFKYYMSDDIubiquitination[1, 2]
623KSCGLNPKLEKCGLGacetylation[3]
805AKSSIISKKKRQTQSacetylation[4]
806KSSIISKKKRQTQSEacetylation[4]
967GLSDIAEKFLKKDQSacetylation[3, 4, 5]
967GLSDIAEKFLKKDQSubiquitination[1, 2]
1530IEDASPTKCPITTKLubiquitination[6]
1699GRNVKSRKLKEIFNKubiquitination[6]
1701NVKSRKLKEIFNKALubiquitination[6]
1706KLKEIFNKALVDPGPubiquitination[6]
1725CDEGHILKNEASAVSubiquitination[6]
1733NEASAVSKAMNSIRSubiquitination[6]
1774ENLLGSIKEFRNRFIubiquitination[1, 2, 6, 7]
1818LAGCVQRKDYTALTKubiquitination[6]
1871GRGKAGAKLFQDFQMubiquitination[6]
1899DYISKENKGYFDEDSubiquitination[6]
1982NNPSVSLKLEESKATubiquitination[6, 7]
1987SLKLEESKATSSSNPubiquitination[7]
2076LIYKGEGKWLRNIDYubiquitination[6]
2096STTAQSRKKWAEEFNubiquitination[6]
2097TTAQSRKKWAEEFNDubiquitination[6]
2158VYRFGQTKPVYVYRFubiquitination[6]
2174AQGTMEDKIYDRQVTubiquitination[6]
2182IYDRQVTKQSLSFRVubiquitination[6]
2224DPNSEKKKKRDTPMLubiquitination[6]
2233RDTPMLPKDTILAELubiquitination[6]
2272ELTEEERKAAWAEYEubiquitination[6]
2282WAEYEAEKKGLTMRFubiquitination[7]
2283AEYEAEKKGLTMRFNubiquitination[6]
2334LINQGREKVVEATNSubiquitination[6]
2385ASQELDVKRREAIYNubiquitination[6]
2397IYNDVLTKQQMLISCubiquitination[6]
2490NPGPSQGKSM*****acetylation[3]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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]
 [7] 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
Functional Description
 Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis. 
Sequence Annotation
 DOMAIN 159 296 ADD.
 DOMAIN 1581 1768 Helicase ATP-binding.
 DOMAIN 2025 2205 Helicase C-terminal.
 ZN_FING 170 206 GATA-type; atypical.
 ZN_FING 217 272 PHD-type; atypical.
 NP_BIND 1594 1601 ATP (Potential).
 MOTIF 581 594 PxVxL motif.
 MOTIF 1719 1722 DEGH box.
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 89 89 Phosphotyrosine.
 MOD_RES 92 92 Phosphoserine.
 MOD_RES 112 112 Phosphoserine.
 MOD_RES 591 591 Phosphothreonine.
 MOD_RES 594 594 Phosphoserine.
 MOD_RES 596 596 Phosphoserine (By similarity).
 MOD_RES 598 598 Phosphoserine.
 MOD_RES 634 634 Phosphoserine.
 MOD_RES 674 674 Phosphothreonine.
 MOD_RES 675 675 Phosphoserine.
 MOD_RES 677 677 Phosphoserine.
 MOD_RES 729 729 Phosphoserine.
 MOD_RES 731 731 Phosphoserine.
 MOD_RES 875 875 Phosphoserine.
 MOD_RES 876 876 Phosphoserine.
 MOD_RES 889 889 Phosphoserine.
 MOD_RES 967 967 N6-acetyllysine.
 MOD_RES 1061 1061 Phosphoserine.
 MOD_RES 1063 1063 Phosphotyrosine.
 MOD_RES 1322 1322 Phosphoserine.
 MOD_RES 1324 1324 Phosphoserine.
 MOD_RES 1326 1326 Phosphoserine.
 MOD_RES 1348 1348 Phosphoserine.
 MOD_RES 1352 1352 Phosphoserine.
 MOD_RES 1527 1527 Phosphoserine.
 MOD_RES 1992 1992 Phosphoserine.
 MOD_RES 1996 1996 Phosphoserine.
 MOD_RES 2220 2220 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Disease mutation; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase; Mental retardation; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2492 AA 
Protein Sequence
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS 60
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS 120
LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH 180
FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC 240
KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV 300
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI 360
ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM 420
DAVNKEKNTK EHKVIDAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMHQNVPT 480
EEQRTNKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS 540
SVDHQGDGSS GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI 600
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK 660
TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK 720
QSETVDQNSD SDEMLAILKE VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK 780
RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR 840
IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT 900
IMELRDRLPK KQQASASTDG VDKLSGKEQS FTSLEVRKVA ETKEKSKHLK TKTCKKVQDG 960
LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK KVIKMEQQYE SSSDGTEKLP 1020
EREEICHFPK GIKQIKNGTT DGEKKSKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK 1080
KSKNGAYGRE KKRCKLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL 1140
SSKRNTKEIQ SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI 1200
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD 1260
DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV 1320
NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE 1380
DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS 1440
NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE 1500
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL 1560
KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS 1620
TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI 1680
IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS 1740
RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM 1800
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN 1860
SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM 1920
SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS 1980
LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF 2040
SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE 2100
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV 2160
YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS 2220
EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA 2280
EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN 2340
SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM 2400
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY 2460
QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM 2492 
Gene Ontology
 GO:0005720; C:nuclear heterochromatin; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003678; F:DNA helicase activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006306; P:DNA methylation; TAS:ProtInc.
 GO:0006310; P:DNA recombination; TAS:ProtInc.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; TAS:ProtInc. 
Interpro
 IPR025766; ADD.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR011011; Znf_FYVE_PHD.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00271; Helicase_C
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00490; HELICc
 SM00184; RING 
PROSITE
 PS51533; ADD
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS