CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003945
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
1644ALKTVLGKKETLVEDubiquitination[1, 2]
1645LKTVLGKKETLVEDKubiquitination[2]
3308VAAAETAKHQAKCNIubiquitination[3, 4]
3563AELIAEAKLLRQHKGubiquitination[3]
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] 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]
 [4] 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
 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
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ 60
KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV 120
KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL 180
FDWNSVVCQQ SATQRLEHAF NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP 240
QQVSIEAIQE VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA 300
YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE VLSWLLSAED 360
TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL QLGSKLIGTG KLSEDEETEV 420
QEQMNLLNSR WECLRVASME KQSNLHRVLM DLQNQKLKEL NDWLTKTEER TRKMEEEPLG 480
PDLEDLKRQV QQHKVLQEDL EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW 540
ANICRWTEDR WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL 600
QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC WDNLVQKLEK 660
STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ EELPPPPPQK KRQITVDSEI 720
RKRLDVDITE LHSWITRSEA VLQSPEFAIF RKEGNFSDLK EKVNAIEREK AEKFRKLQDA 780
SRSAQALVEQ MVNEGVNADS IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ 840
QLEQMTTTAE NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK 900
GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA IRTWVQQSET 960
KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS TTVKEMSKKA PSEISRKYQS 1020
EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL RKIQNHIQTL KKWMAEVDVF LKEEWPALGD 1080
SEILKKQLKQ CRLLVSDIQT IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH 1140
MCQQVYARKE ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM 1200
KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL CTRLNGKCKT 1260
LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE EISEVLDSLE NLMRHSEDNP 1320
NQIRILAQTL TDGGVMDELI NEELETFNSR WRELHEEAVR RQKLLEQSIQ SAQETEKSLH 1380
LIQESLTFID KQLAAYIADK VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV 1440
LSQIDVAQKK LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS 1500
QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL HYNELGAKVT 1560
ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV EGMPSNLDSE VAWGKATQKE 1620
IEKQKVHLKS ITEVGEALKT VLGKKETLVE DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH 1680
METFDQNVDH ITKWIIQADT LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN 1740
LMANRGDHCR KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE 1800
IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK QQLLQTKHNA 1860
LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL ASLPEPRDER KIKEIDRELQ 1920
KKKEELNAVR RQAEGLSEDG AAMAVEPTQI QLSKRWREIE SKFAQFRRLN FAQIHTVREE 1980
TMMVMTEDMP LEISYVPSTY LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN 2040
IKDSLQQSSG RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD 2100
RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD GIGQRQTVVR 2160
TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS DRKKRLEEQK NILSEFQRDL 2220
NEFVLWLEEA DNIASIPLEP GKEQQLKEKL EQVKLLVEEL PLRQGILKQL NETGGPVLVS 2280
APISPEEQDK LENKLKQTNL QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL 2340
LLWLSPIRNQ LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK 2400
RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV TKETAISKLE 2460
MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL 2520
EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK 2580
DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA 2640
NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK 2700
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ 2760
KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW 2820
LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG 2880
LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ 2940
EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR 3000
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP 3060
WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC 3120
LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN 3180
WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD 3240
SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR 3300
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC 3360
TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS 3420
APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN 3480
QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP 3540
SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP 3600
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM 3660
EQLNNSFPSS RGRNTPGKPM REDTM 3685 
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