CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003947
UniProt Accession
Genbank Protein ID
 M18533; X14298; M92650; AL031542; AC004468; AC006061; AC078958; AC079143; AC079175; AC079177; AC079864; AC090632; AC093167; AC093193; AC096506; AL031643; AL096699; AL109609; AL139278; AL451144; AL031643; AC004468; AC006061; AC078958; AC079143; AC079175; AC079177; AC079864; AC090632; AC093167; AC093193; AC096506; AL031542; AL096699; AL109609; AL139278; AL451144; AL049643; AL050305; AL096699; AC004468; AC006061; AC078958; AC079143; AC079175; AC079177; AC079864; AC090632; AC093167; AC093193; AC096506; AL031542; AL031643; AL109609; AL139278; AL451144; AL109609; AC004468; AC006061; AC078958; AC079143; AC079175; AC079177; AC079864; AC090632; AC093167; AC093193; AC096506; AL031542; AL031643; AL096699; AL139278; AL451144; AL121880; AL139278; AC004468; AC006061; AC078958; AC079143; AC079175; AC079177; AC079864; AC090632; AC093167; AC093193; AC096506; AL031542; AL031643; AL096699; AL109609; AL451144; AL139401; AL451144; AC004468; AC006061; AC078958; AC079143; AC079175; AC079177; AC079864; AC090632; AC093167; AC093193; AC096506; AL031542; AL031643; AL096699; AL109609; AL139278; AL596023; CH471074; BC028720; BC070078; BC094758; U27203; U27203; X15148; X06178; X06179; X13045; X13046; X13047; X13048; X15495; X54820 
Genbank Nucleotide ID
 AAA53189.1; CAA32479.1; AAA52316.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI42229.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI43058.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42225.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42950.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI42991.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; CAI39566.1; EAW99065.1; AAH28720.1; AAH70078.1; AAH94758.1; AAA86115.1; AAA86116.1; CAA33245.1; CAA29544.1; CAA29545.1; CAA31451.1; CAA31452.1; CAA31453.1; CAA31454.1; CAA33518.1; CAA38589.1 
Protein Name
 Dystrophin 
Protein Synonyms/Alias
  
Gene Name
 DMD 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
255ATDMELTKRSAVEGMubiquitination[1]
274DSEVAWGKATQKEIEubiquitination[1]
1967VAAAETAKHQAKCNIubiquitination[1]
2222AELIAEAKLLRQHKGubiquitination[2]
Reference
 [1] 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]
 [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] 
Functional Description
 Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin- associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. 
Sequence Annotation
 DOMAIN 1 240 Actin-binding.
 DOMAIN 15 119 CH 1.
 DOMAIN 134 237 CH 2.
 REPEAT 339 447 Spectrin 1.
 REPEAT 448 556 Spectrin 2.
 REPEAT 559 667 Spectrin 3.
 REPEAT 719 828 Spectrin 4.
 REPEAT 830 934 Spectrin 5.
 REPEAT 943 1045 Spectrin 6.
 REPEAT 1048 1154 Spectrin 7.
 REPEAT 1157 1263 Spectrin 8.
 REPEAT 1266 1367 Spectrin 9.
 REPEAT 1368 1463 Spectrin 10.
 REPEAT 1468 1568 Spectrin 11.
 REPEAT 1571 1676 Spectrin 12.
 REPEAT 1679 1778 Spectrin 13.
 REPEAT 1779 1874 Spectrin 14.
 REPEAT 1877 1979 Spectrin 15.
 REPEAT 1992 2101 Spectrin 16.
 REPEAT 2104 2208 Spectrin 17.
 REPEAT 2211 2318 Spectrin 18.
 REPEAT 2319 2423 Spectrin 19.
 REPEAT 2475 2577 Spectrin 20.
 REPEAT 2580 2686 Spectrin 21.
 REPEAT 2689 2802 Spectrin 22.
 REPEAT 2808 2930 Spectrin 23.
 REPEAT 2935 3040 Spectrin 24.
 DOMAIN 3055 3088 WW.
 ZN_FING 3307 3354 ZZ-type.
 REGION 63 72 ANK2- and ANK-3 binding (By similarity).
 REGION 1415 1913 Interaction with SYNM (By similarity).
 REGION 3058 3408 Interaction with SYNM (By similarity).
 REGION 3466 3518 Binds to SNTB1.
 MOD_RES 3483 3483 Phosphoserine.
 MOD_RES 3612 3612 Phosphoserine.
 MOD_RES 3613 3613 Phosphoserine.
 MOD_RES 3617 3617 Phosphoserine.
 MOD_RES 3623 3623 Phosphoserine.
 MOD_RES 3624 3624 Phosphoserine (By similarity).
 MOD_RES 3666 3666 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Calcium; Cardiomyopathy; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3685 AA 
Protein Sequence
MTEIILLIFF PAYFLNAVRR QKLLEQSIQS AQETEKSLHL IQESLTFIDK QLAAYIADKV 60
DAAQMPQEAQ KIQSDLTSHE ISLEEMKKHN QGKEAAQRVL SQIDVAQKKL QDVSMKFRLF 120
QKPANFEQRL QESKMILDEV KMHLPALETK SVEQEVVQSQ LNHCVNLYKS LSEVKSEVEM 180
VIKTGRQIVQ KKQTENPKEL DERVTALKLH YNELGAKVTE RKQQLEKCLK LSRKMRKEMN 240
VLTEWLAATD MELTKRSAVE GMPSNLDSEV AWGKATQKEI EKQKVHLKSI TEVGEALKTV 300
LGKKETLVED KLSLLNSNWI AVTSRAEEWL NLLLEYQKHM ETFDQNVDHI TKWIIQADTL 360
LDESEKKKPQ QKEDVLKRLK AELNDIRPKV DSTRDQAANL MANRGDHCRK LVEPQISELN 420
HRFAAISHRI KTGKASIPLK ELEQFNSDIQ KLLEPLEAEI QQGVNLKEED FNKDMNEDNE 480
GTVKELLQRG DNLQQRITDE RKREEIKIKQ QLLQTKHNAL KDLRSQRRKK ALEISHQWYQ 540
YKRQADDLLK CLDDIEKKLA SLPEPRDERK IKEIDRELQK KKEELNAVRR QAEGLSEDGA 600
AMAVEPTQIQ LSKRWREIES KFAQFRRLNF AQIHTVREET MMVMTEDMPL EISYVPSTYL 660
TEITHVSQAL LEVEQLLNAP DLCAKDFEDL FKQEESLKNI KDSLQQSSGR IDIIHSKKTA 720
ALQSATPVER VKLQEALSQL DFQWEKVNKM YKDRQGRFDR SVEKWRRFHY DIKIFNQWLT 780
EAEQFLRKTQ IPENWEHAKY KWYLKELQDG IGQRQTVVRT LNATGEEIIQ QSSKTDASIL 840
QEKLGSLNLR WQEVCKQLSD RKKRLEEQKN ILSEFQRDLN EFVLWLEEAD NIASIPLEPG 900
KEQQLKEKLE QVKLLVEELP LRQGILKQLN ETGGPVLVSA PISPEEQDKL ENKLKQTNLQ 960
WIKVSRALPE KQGEIEAQIK DLGQLEKKLE DLEEQLNHLL LWLSPIRNQL EIYNQPNQEG 1020
PFDVKETEIA VQAKQPDVEE ILSKGQHLYK EKPATQPVKR KLEDLSSEWK AVNRLLQELR 1080
AKQPDLAPGL TTIGASPTQT VTLVTQPVVT KETAISKLEM PSSLMLEVPA LADFNRAWTE 1140
LTDWLSLLDQ VIKSQRVMVG DLEDINEMII KQKATMQDLE QRRPQLEELI TAAQNLKNKT 1200
SNQEARTIIT DRIERIQNQW DEVQEHLQNR RQQLNEMLKD STQWLEAKEE AEQVLGQARA 1260
KLESWKEGPY TVDAIQKKIT ETKQLAKDLR QWQTNVDVAN DLALKLLRDY SADDTRKVHM 1320
ITENINASWR SIHKRVSERE AALEETHRLL QQFPLDLEKF LAWLTEAETT ANVLQDATRK 1380
ERLLEDSKGV KELMKQWQDL QGEIEAHTDV YHNLDENSQK ILRSLEGSDD AVLLQRRLDN 1440
MNFKWSELRK KSLNIRSHLE ASSDQWKRLH LSLQELLVWL QLKDDELSRQ APIGGDFPAV 1500
QKQNDVHRAF KRELKTKEPV IMSTLETVRI FLTEQPLEGL EKLYQEPREL PPEERAQNVT 1560
RLLRKQAEEV NTEWEKLNLH SADWQRKIDE TLERLQELQE ATDELDLKLR QAEVIKGSWQ 1620
PVGDLLIDSL QDHLEKVKAL RGEIAPLKEN VSHVNDLARQ LTTLGIQLSP YNLSTLEDLN 1680
TRWKLLQVAV EDRVRQLHEA HRDFGPASQH FLSTSVQGPW ERAISPNKVP YYINHETQTT 1740
CWDHPKMTEL YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSLSAACD ALDQHNLKQN 1800
DQPMDILQII NCLTTIYDRL EQEHNNLVNV PLCVDMCLNW LLNVYDTGRT GRIRVLSFKT 1860
GIISLCKAHL EDKYRYLFKQ VASSTGFCDQ RRLGLLLHDS IQIPRQLGEV ASFGGSNIEP 1920
SVRSCFQFAN NKPEIEAALF LDWMRLEPQS MVWLPVLHRV AAAETAKHQA KCNICKECPI 1980
IGFRYRSLKH FNYDICQSCF FSGRVAKGHK MHYPMVEYCT PTTSGEDVRD FAKVLKNKFR 2040
TKRYFAKHPR MGYLPVQTVL EGDNMETPVT LINFWPVDSA PASSPQLSHD DTHSRIEHYA 2100
SRLAEMENSN GSYLNDSISP NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP AQILISLESE 2160
ERGELERILA DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ SPRDAELIAE 2220
AKLLRQHKGR LEARMQILED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV SSPSTSLQRS 2280
DSSQPMLLRV VGSQTSDSMG EEDLLSPPQD TSTGLEEVME QLNNSFPSSR GRNTPGKPMR 2340
EDTM 2344 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0030055; C:cell-substrate junction; IEA:Compara.
 GO:0043034; C:costamere; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; TAS:ProtInc.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
 GO:0030175; C:filopodium; IDA:BHF-UCL.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0044306; C:neuron projection terminus; IEA:Compara.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0042383; C:sarcolemma; IDA:BHF-UCL.
 GO:0030018; C:Z disc; IEA:Compara.
 GO:0003779; F:actin binding; TAS:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0017022; F:myosin binding; IDA:BHF-UCL.
 GO:0050998; F:nitric-oxide synthase binding; ISS:BHF-UCL.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
 GO:0043623; P:cellular protein complex assembly; ISS:BHF-UCL.
 GO:0034613; P:cellular protein localization; IMP:BHF-UCL.
 GO:0008065; P:establishment of blood-nerve barrier; IEA:Compara.
 GO:0060857; P:establishment of glial blood-brain barrier; IEA:Compara.
 GO:0009296; P:flagellum assembly; TAS:BHF-UCL.
 GO:0046716; P:muscle cell homeostasis; IEA:Compara.
 GO:0048747; P:muscle fiber development; IEA:Compara.
 GO:0030049; P:muscle filament sliding; TAS:Reactome.
 GO:0007517; P:muscle organ development; NAS:ProtInc.
 GO:0014904; P:myotube cell development; IEA:Compara.
 GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:BHF-UCL.
 GO:0045213; P:neurotransmitter receptor metabolic process; IEA:Compara.
 GO:0051647; P:nucleus localization; IEA:Compara.
 GO:0021629; P:olfactory nerve structural organization; IEA:Compara.
 GO:0043043; P:peptide biosynthetic process; IDA:UniProtKB.
 GO:0045666; P:positive regulation of neuron differentiation; IMP:BHF-UCL.
 GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
 GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
 GO:0086001; P:regulation of cardiac muscle cell action potential; ISS:BHF-UCL.
 GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
 GO:0090287; P:regulation of cellular response to growth factor stimulus; IMP:BHF-UCL.
 GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
 GO:2000169; P:regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
 GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
 GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; ISS:BHF-UCL.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:Compara.
 GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:BHF-UCL. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR016344; Dystrophin/utrophin.
 IPR011992; EF-hand-like_dom.
 IPR015153; EF-hand_dom_typ1.
 IPR015154; EF-hand_dom_typ2.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat.
 IPR001202; WW_dom.
 IPR000433; Znf_ZZ. 
Pfam
 PF00307; CH
 PF09068; efhand_1
 PF09069; efhand_2
 PF00435; Spectrin
 PF00397; WW
 PF00569; ZZ 
SMART
 SM00033; CH
 SM00150; SPEC
 SM00456; WW
 SM00291; ZnF_ZZ 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2
 PS01357; ZF_ZZ_1
 PS50135; ZF_ZZ_2 
PRINTS