CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001714
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dystrophin 
Protein Synonyms/Alias
  
Gene Name
 DMD 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Canis familiaris (Dog) (Canis lupus familiaris) 
NCBI Taxa ID
 9615 
Lysine Modification
Position
Peptide
Type
References
3303VAAAETAKHQAKCNIubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
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 (By similarity). 
Sequence Annotation
 DOMAIN 1 237 Actin-binding.
 DOMAIN 15 119 CH 1.
 DOMAIN 134 237 CH 2.
 REPEAT 340 448 Spectrin 1.
 REPEAT 449 557 Spectrin 2.
 REPEAT 560 668 Spectrin 3.
 REPEAT 720 829 Spectrin 4.
 REPEAT 831 935 Spectrin 5.
 REPEAT 944 1047 Spectrin 6.
 REPEAT 1050 1156 Spectrin 7.
 REPEAT 1159 1265 Spectrin 8.
 REPEAT 1268 1369 Spectrin 9.
 REPEAT 1370 1465 Spectrin 10.
 REPEAT 1470 1570 Spectrin 11.
 REPEAT 1573 1678 Spectrin 12.
 REPEAT 1681 1780 Spectrin 13.
 REPEAT 1781 1876 Spectrin 14.
 REPEAT 1879 1981 Spectrin 15.
 REPEAT 1994 2103 Spectrin 16.
 REPEAT 2106 2210 Spectrin 17.
 REPEAT 2213 2320 Spectrin 18.
 REPEAT 2321 2418 Spectrin 19.
 REPEAT 2470 2572 Spectrin 20.
 REPEAT 2575 2681 Spectrin 21.
 REPEAT 2684 2797 Spectrin 22.
 REPEAT 2803 2925 Spectrin 23.
 REPEAT 2930 3035 Spectrin 24.
 DOMAIN 3050 3083 WW.
 ZN_FING 3302 3349 ZZ-type.
 REGION 63 72 ANK2- and ANK-3 binding (By similarity).
 REGION 1418 1915 Interaction with SYNM (By similarity).
 REGION 3053 3403 Interaction with SYNM (By similarity).
 REGION 3461 3513 Binds to SNTB1 (By similarity).
 MOD_RES 3478 3478 Phosphoserine (By similarity).
 MOD_RES 3607 3607 Phosphoserine (By similarity).
 MOD_RES 3608 3608 Phosphoserine (By similarity).
 MOD_RES 3612 3612 Phosphoserine (By similarity).
 MOD_RES 3618 3618 Phosphoserine (By similarity).
 MOD_RES 3619 3619 Phosphoserine (By similarity).
 MOD_RES 3661 3661 Phosphoserine (By similarity).  
Keyword
 Actin-binding; Calcium; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3680 AA 
Protein Sequence
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ 60
KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV 120
KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL 180
FDWNSVVCQQ SATQRLEHAF NIAKYQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP 240
QQVSIEAIQE VEMLPRPSQV TREEHFQIHH QMHYSQQITV SLAQGYERAP SFPKPRFKSY 300
AYTQAAYVTT SDPTRSPLPS QHLETPEDKS FGRSLTETEA NLDSYQTALE EVLSWLLSAE 360
DALQAQGEIS NDVEEVKEQF HTHEGYMMDL TSHQGRVGNV LQLGSQLIGT GKLSEDEETE 420
VQEQMNLLNS RWECLRVASM EKQSNLHKVL MDLQNQQLKE LNDWLTKTEE RTRKMEKEPL 480
GPDIEDLKRQ VQQHKVLQED LEQEQVRVNS LTHMVVVVDE SSGDHATAAL EEQLKVLGDR 540
WANICRWTED RWVLLQDILL KWQRFTEEQC LFSAWLSEKE DAVNKIHTTG FKDQSEVLSN 600
LQKLAVLKTD LEKKKQTMDK LCSLNQDLLS ALKNTVVAHK MEAWLDNFAQ RWDNLVQKLE 660
KSSAQISQAV TTTQPSLTQT TVMETVTMVT TREHILVKHA QEELPPPPPQ KKRQIIVDSE 720
IRKRLDVDIT ELHSWITRSE AVLQSPEFAI YRKEGNFSDL KEKVNAIERE KAEKFRKLQD 780
ASRSAQALVE QMVNEGVNAD SIKQASEQLN SRWIEFCQLL SERLNWLEYQ NNIITFYNQL 840
QQLEQMTTTA ENWLKTQPTT TSEPTAIKSQ LKICKDEINR LSALQPQIER LKIQSIALKE 900
KGQGPMFLDA DFVAFTNHFN QVFADVQARE KELQTIFDSL PPMRYQETMS TILTWIQQSE 960
TKLSIPQVTV TEYDIMEQRL GELQALQSSL QEQQNGLNYL STTVKEMSKK APLSDISRKY 1020
QSEFEEIEGR WKKLSSQLVE HCQKLEEQMA KLRKIQNHIK TLKKWITEVD VFLKEEWPAL 1080
GDSEILKRQL KQCRLLVNDI QTIQPSLNSV NEGAQKMKNE AEPEFAGRLE TELRELNTQW 1140
DYMCRQVYAR KEALKGGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE 1200
EMKRAKEEAQ QKEAKVKLLT ESVNSVIAQA PPAAQEALKK ELDTLTTNYQ WLCTRLNGKC 1260
KTLEEVWACW HELLSYLEKA NKWLSEVEVK LKTTENISGG AEEIAEVLDS LENLMQHSED 1320
NPNQIRILAQ TLTDGGVMDE LINEELETFN SRWRELHEEA VRRQKLLEQS IQSAQEIEKS 1380
LHLIQESLSS IDKQLAAYIA DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKETAQ 1440
RVLSQIDVAQ KKLQDVSMKF RLFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV 1500
QSQLNHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK 1560
VTERKQQLEK CLKLSRKMRK EMNALTEWLA ATDMELTKRS AVEGMPSNLD SEVAWGKATQ 1620
KEIEKQKVHL KSVTEVGEAL KTVLGKKEML VEDKLSLLNS NWIAVTSRAE EWLNLLLEYQ 1680
KHMETFDQNV DYITNWIIQA DALLDESEKK KPQQKEDILK RLKAEMNDIR PKVDSTRDQA 1740
ANLMANRGDH CRKVVEPKIS ELNHRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE 1800
AEIQQGVNLK EEDFNKDMSE DNEGTVKELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH 1860
NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDDIEK KLASLPEPRD ERKIKEIDRE 1920
LQKKKEELNA VRRQAEGLSE DGAAMAVEPT QIQLSKRWRE IESKFAQFRR LNFAQIHTVH 1980
EESVVAMTED MPLEISYVPS TYLTEITHVS QALSEVEELL NAPDLCAQDF EDLFKQEESL 2040
KNIKDSLQQI SGRIDIIHNK KTAALHSATP AERAKLQEAL SRLDFQWERV NNMYKDRQGR 2100
FDRSVEKWRR FHYDMKILNQ WLTEAEQFLK KTQIPENWEH AKYKWYLKEL QDGIGQRQSV 2160
VRVLNATGEE IIQQSSKTDA SILQEKLGSL NLRWQEVCKQ LAERKKRLEE QKNILSEFQR 2220
DVNEFVLWLE EADNVANIPL EPGNEQQLKE KLEQVKLLAE ELPLRQGILK QLNETGGTVL 2280
VSAPLSPEEQ DKLENKLKQT NLQWIKVSRN LPEKQEEIEA HVKDLGQLEE QLNHLLLWLS 2340
PIRNQLEIYN QPNQTGPFDI KEIEVAVQAK QPDVEGILSK GQHLYKEKPA TQPAKRKLED 2400
LSSDWKVVTQ LLQELRAKQP GPAPGLTTVR APPSQTVTLV TQPAVTKETA ISKLEMPSSL 2460
LLEVPALADF NRAWTELTDW LSLLDRVIKS QRVMVGDLED INEMIIKQKA TLQDLEQRRP 2520
QLEELITAAQ NLKNKTSNQE ARTIITDRIE RIQSQWDEVQ EHLQNRRLQL TEMLKDSTQW 2580
LEAKEEAEQV LGQARAKLES WKEAPYTVDA IQKKITETKQ LAKDLRQWQI NVDVANDLAL 2640
KLLRDYSADD TRKVHMITEN INASWASIHK RLSEREAALE ETHRLLQQFP LDLEKFLAWL 2700
TEAETTANVL QDATHKERLL EDSKGVRELM KQWQDLQGEI EAHTDIYHNL DENGQKVLRS 2760
LEGSDDAALL QRRLDNMNFK WSELRKKSLN IRSHLEASSD QWKRLHLSLQ ELLVWLQLKD 2820
DELSRQAPIG GDFPAVQKQN DVHRAFKREL KTKEPVIMST LETVRIFLTE QPLEGLEKLY 2880
QEPRELPPEE RAQNVTRLLR KQAEEVNTQW EKLNVHSADW QRKIDEALER LQELQEATDE 2940
LDLKLRQAEV IKGSWQPVGD LLIDSLQDHL EKVKALRGEI TPLKENVSYV NDLARQLTTL 3000
GIQLSPYNLN TLEDLNTRWK LLQVAIEDRI RQLHEAHRDF GPASQHFLST SVQGPWERAI 3060
SPNKVPYYIN HETQTTCWDH PKMTELYQSL ADLNNVRFSA YRTAMKLRRL QKALCLDLLS 3120
LSAACDALDQ HNLKQNDQPM DILQVINCLT TIYDRLEQEH NNLVNVPLCV DMCLNWLLNV 3180
YDTGRTGRIR VLSFKTGIIS LCKAHLEDKY RYLFKQVASS TGFCDQRRLG LLLHDSIQIP 3240
RQLGEVASFG GSNIEPSVRS CFQFANNKPE IEAALFLDWM RLEPQSMVWL PVLHRVAAAE 3300
TAKHQAKCNI CKECPIIGFR YRSLKHFNYD ICQSCFFSGR VAKGHKMHYP MVEYCTPTTS 3360
GEDVRDFAKV LKNKFRTKRY FAKHPRMGYL PVQTVLEGDN METPVTLINF WPVDSAPASS 3420
PQLSHDDTHS RIEHYASRLK KMENSNGSYL NDSISPNESI DDEHLLIQHY WRSLNQESPL 3480
SQPRSPAQIL ISLESEERGE LERILADLEG RNRNLQAEYD RLKQQHEHKG LSPLPSPPEM 3540
MPTSPQSPRD AELIAEAKLL RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ LLEQPQAEAK 3600
VNGTTVSSPS TSLQRSDSSQ PMLLRVVGSQ TSESMGEEDL LSPPQDTSTG LEEVMEQLNH 3660
SFPSSRGRNT PGKPMREDTM 3680 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
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