CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011018
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dystonin 
Protein Synonyms/Alias
 230 kDa bullous pemphigoid antigen; 230/240 kDa bullous pemphigoid antigen; Bullous pemphigoid antigen 1; BPA; Bullous pemphigoid antigen; Dystonia musculorum protein; Hemidesmosomal plaque protein 
Gene Name
 DST 
Gene Synonyms/Alias
 BP230; BP240; BPAG1; DMH; DT; KIAA0728 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
350LKLTYAEKLHRLESQacetylation[1]
Reference
 [1] 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] 
Functional Description
 Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin- containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two- dimensional mesh. 
Sequence Annotation
 DOMAIN 35 252 Actin-binding.
 DOMAIN 35 138 CH 1.
 DOMAIN 151 252 CH 2.
 REPEAT 701 797 Spectrin 1.
 DOMAIN 890 942 SH3.
 REPEAT 1584 1626 Plectin 1.
 REPEAT 1660 1703 Plectin 2.
 REPEAT 1774 1817 Plectin 3.
 REPEAT 1818 1855 Plectin 4.
 REPEAT 1856 1891 Plectin 5.
 REPEAT 3924 4000 Spectrin 2.
 REPEAT 4069 4153 Spectrin 3.
 REPEAT 4514 4622 Spectrin 4.
 REPEAT 4626 4731 Spectrin 5.
 REPEAT 4849 4952 Spectrin 6.
 REPEAT 5281 5389 Spectrin 7.
 REPEAT 5396 5497 Spectrin 8.
 REPEAT 5504 5606 Spectrin 9.
 REPEAT 5829 5933 Spectrin 10.
 REPEAT 5940 6042 Spectrin 11.
 REPEAT 6048 6154 Spectrin 12.
 REPEAT 6184 6264 Spectrin 13.
 REPEAT 6270 6373 Spectrin 14.
 REPEAT 6379 6481 Spectrin 15.
 REPEAT 6490 6592 Spectrin 16.
 REPEAT 6597 6700 Spectrin 17.
 REPEAT 6705 6811 Spectrin 18.
 REPEAT 6818 6918 Spectrin 19.
 REPEAT 6923 7026 Spectrin 20.
 DOMAIN 7197 7232 EF-hand 1.
 DOMAIN 7233 7268 EF-hand 2.
 DOMAIN 7273 7351 GAR.
 MOTIF 1383 1389 Nuclear localization signal; in isoform 6
 MOTIF 7550 7553 Microtubule tip localization signal.
 MOD_RES 2919 2919 Phosphoserine.
 MOD_RES 7364 7364 Phosphoserine (By similarity).
 MOD_RES 7432 7432 Phosphoserine.
 CROSSLNK 5470 5470 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Actin-binding; Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Intermediate filament; Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Microtubule; Muscle protein; Neuropathy; Nucleus; Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain; Transmembrane; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 7570 AA 
Protein Sequence
MHSSSYSYRS SDSVFSNTTS TRTSLDSNEN LLLVHCGPTL INSCISFGSE SFDGHRLEML 60
QQIANRVQRD SVICEDKLIL AGNALQSDSK RLESGVQFQN EAEIAGYILE CENLLRQHVI 120
DVQILIDGKY YQADQLVQRV AKLRDEIMAL RNECSSVYSK GRILTTEQTK LMISGITQSL 180
NSGFAQTLHP SLTSGLTQSL TPSLTSSSMT SGLSSGMTSR LTPSVTPAYT PGFPSGLVPN 240
FSSGVEPNSL QTLKLMQIRK PLLKSSLLDQ NLTEEEINMK FVQDLLNWVD EMQVQLDRTE 300
WGSDLPSVES HLENHKNVHR AIEEFESSLK EAKISEIQMT APLKLTYAEK LHRLESQYAK 360
LLNTSRNQER HLDTLHNFVS RATNELIWLN EKEEEEVAYD WSERNTNIAR KKDYHAELMR 420
ELDQKEENIK SVQEIAEQLL LENHPARLTI EAYRAAMQTQ WSWILQLCQC VEQHIKENTA 480
YFEFFNDAKE ATDYLRNLKD AIQRKYSCDR SSSIHKLEDL VQESMEEKEE LLQYKSTIAN 540
LMGKAKTIIQ LKPRNSDCPL KTSIPIKAIC DYRQIEITIY KDDECVLANN SHRAKWKVIS 600
PTGNEAMVPS VCFTVPPPNK EAVDLANRIE QQYQNVLTLW HESHINMKSV VSWHYLINEI 660
DRIRASNVAS IKTMLPGEHQ QVLSNLQSRF EDFLEDSQES QVFSGSDITQ LEKEVNVCKQ 720
YYQELLKSAE REEQEESVYN LYISEVRNIR LRLENCEDRL IRQIRTPLER DDLHESVFRI 780
TEQEKLKKEL ERLKDDLGTI TNKCEEFFSQ AAASSSVPTL RSELNVVLQN MNQVYSMSST 840
YIDKLKTVNL VLKNTQAAEA LVKLYETKLC EEEAVIADKN NIENLISTLK QWRSEVDEKR 900
QVFHALEDEL QKAKAISDEM FKTYKERDLD FDWHKEKADQ LVERWQNVHV QIDNRLRDLE 960
GIGKSLKYYR DTYHPLDDWI QQVETTQRKI QENQPENSKT LATQLNQQKM LVSEIEMKQS 1020
KMDECQKYAE QYSATVKDYE LQTMTYRAMV DSQQKSPVKR RRMQSSADLI IQEFMDLRTR 1080
YTALVTLMTQ YIKFAGDSLK RLEEEEKSLE EEKKEHVEKA KELQKWVSNI SKTLKDAEKA 1140
GKPPFSKQKI SSEEISTKKE QLSEALQTIQ LFLAKHGDKM TDEERNELEK QVKTLQESYN 1200
LLFSESLKQL QESQTSGDVK VEEKIVAERQ QEYKEKLQGI CDLLTQTENR LIGHQEAFMI 1260
GDGTVELKKY QSKQEELQKD MQGSAQALAE VVKNTENFLK ENGEKLSQED KALIEQKLNE 1320
AKIKCEQLNL KAEQSKKELD KVVTTAIKEE TEKVAAVKQL EESKTKIENL LDWLSNVDKD 1380
SERAGTKHKQ VIEQNGTHFQ EGDGKSAIGE EDEVNGNLLE TDVDGQVGTT QENLNQQYQK 1440
VKAQHEKIIS QHQAVIIATQ SAQVLLEKQG QYLSPEEKEK LQKNMKELKV HYETALAESE 1500
KKMKLTHSLQ EELEKFDADY TEFEHWLQQS EQELENLEAG ADDINGLMTK LKRQKSFSED 1560
VISHKGDLRY ITISGNRVLE AAKSCSKRDG GKVDTSATHR EVQRKLDHAT DRFRSLYSKC 1620
NVLGNNLKDL VDKYQHYEDA SCGLLAGLQA CEATASKHLS EPIAVDPKNL QRQLEETKAL 1680
QGQISSQQVA VEKLKKTAEV LLDARGSLLP AKNDIQKTLD DIVGRYEDLS KSVNERNEKL 1740
QITLTRSLSV QDGLDEMLDW MGNVESSLKE QGQVPLNSTA LQDIISKNIM LEQDIAGRQS 1800
SINAMNEKVK KFMETTDPST ASSLQAKMKD LSARFSEASH KHKETLAKME ELKTKVELFE 1860
NLSEKLQTFL ETKTQALTEV DVPGKDVTEL SQYMQESTSE FLEHKKHLEV LHSLLKEISS 1920
HGLPSDKALV LEKTNNLSKK FKEMEDTIKE KKEAVTSCQE QLDAFQVLVK SLKSWIKETT 1980
KKVPIVQPSF GAEDLGKSLE DTKKLQEKWS LKTPEIQKVN NSGISLCNLI SAVTTPAKAI 2040
AAVKSGGAVL NGEGTATNTE EFWANKGLTS IKKDMTDISH GYEDLGLLLK DKIAELNTKL 2100
SKLQKAQEES SAMMQWLQKM NKTATKWQQT PAPTDTEAVK TQVEQNKSFE AELKQNVNKV 2160
QELKDKLTEL LEENPDTPEA PRWKQMLTEI DSKWQELNQL TIDRQQKLEE SSNNLTQFQT 2220
VEAQLKQWLV EKELMVSVLG PLSIDPNMLN TQRQQVQILL QEFATRKPQY EQLTAAGQGI 2280
LSRPGEDPSL RGIVKEQLAA VTQKWDSLTG QLSDRCDWID QAIVKSTQYQ SLLRSLSDKL 2340
SDLDNKLSSS LAVSTHPDAM NQQLETAQKM KQEIQQEKKQ IKVAQALCED LSALVKEEYL 2400
KAELSRQLEG ILKSFKDVEQ KAENHVQHLQ SACASSHQFQ QMSRDFQAWL DTKKEEQNKS 2460
HPISAKLDVL ESLIKDHKDF SKTLTAQSHM YEKTIAEGEN LLLKTQGSEK AALQLQLNTI 2520
KTNWDTFNKQ VKERENKLKE SLEKALKYKE QVETLWPWID KCQNNLEEIK FCLDPAEGEN 2580
SIAKLKSLQK EMDQHFGMVE LLNNTANSLL SVCEIDKEVV TDENKSLIQK VDMVTEQLHS 2640
KKFCLENMTQ KFKEFQEVSK ESKRQLQCAK EQLDIHDSLG SQAYSNKYLT MLQTQQKSLQ 2700
ALKHQVDLAK RLAQDLVVEA SDSKGTSDVL LQVETIAQEH STLSQQVDEK CSFLETKLQG 2760
IGHFQNTIRE MFSQFAEFDD ELDSMAPVGR DAETLQKQKE TIKAFLKKLE ALMASNDNAN 2820
KTCKMMLATE ETSPDLVGIK RDLEALSKQC NKLLDRAQAR EEQVEGTIKR LEEFYSKLKE 2880
FSILLQKAEE HEESQGPVGM ETETINQQLN MFKVFQKEEI EPLQGKQQDV NWLGQGLIQS 2940
AAKSTSTQGL EHDLDDVNAR WKTLNKKVAQ RAAQLQEALL HCGRFQDALE SLLSWMVDTE 3000
ELVANQKPPS AEFKVVKAQI QEQKLLQRLL DDRKSTVEVI KREGEKIATT AEPADKVKIL 3060
KQLSLLDSRW EALLNKAETR NRQLEGISVV AQQFHETLEP LNEWLTTIEK RLVNCEPIGT 3120
QASKLEEQIA QHKALEDDII NHNKHLHQAV SIGQSLKVLS SREDKDMVQS KLDFSQVWYI 3180
EIQEKSHSRS ELLQQALCNA KIFGEDEVEL MNWLNEVHDK LSKLSVQDYS TEGLWKQQSE 3240
LRVLQEDILL RKQNVDQALL NGLELLKQTT GDEVLIIQDK LEAIKARYKD ITKLSTDVAK 3300
TLEQALQLAR RLHSTHEELC TWLDKVEVEL LSYETQVLKG EEASQAQMRP KELKKEAKNN 3360
KALLDSLNEV SSALLELVPW RAREGLEKMV AEDNERYRLV SDTITQKVEE IDAAILRSQQ 3420
FDQAADAELS WITETEKKLM SLGDIRLEQD QTSAQLQVQK TFTMEILRHK DIIDDLVKSG 3480
HKIMTACSEE EKQSMKKKLD KVLKNYDTIC QINSERYLQL ERAQSLVNQF WETYEELWPW 3540
LTETQSIISQ LPAPALEYET LRQQQEEHRQ LRELIAEHKP HIDKMNKTGP QLLELSPGEG 3600
FSIQEKYVAA DTLYSQIKED VKKRAVALDE AISQSTQFHD KIDQILESLE RIVERLRQPP 3660
SISAEVEKIK EQISENKNVS VDMEKLQPLY ETLKQRGEEM IARSGGTDKD ISAKAVQDKL 3720
DQMVFIWENI HTLVEEREAK LLDVMELAEK FWCDHMSLIV TIKDTQDFIR DLEDPGIDPS 3780
VVKQQQEAAE TIREEIDGLQ EELDIVINLG SELIAACGEP DKPIVKKSID ELNSAWDSLN 3840
KAWKDRIDKL EEAMQAAVQY QDGLQAVFDW VDIAGGKLAS MSPIGTDLET VKQQIEELKQ 3900
FKSEAYQQQI EMERLNHQAE LLLKKVTEES DKHTVQDPLM ELKLIWDSLE ERIINRQHKL 3960
EGALLALGQF QHALDELLAW LTHTEGLLSE QKPVGGDPKA IEIELAKHHV LQNDVLAHQS 4020
TVEAVNKAGN DLIESSAGEE ASNLQNKLEV LNQRWQNVLE KTEQRKQQLD GALRQAKGFH 4080
GEIEDLQQWL TDTERHLLAS KPLGGLPETA KEQLNVHMEV CAAFEAKEET YKSLMQKGQQ 4140
MLARCPKSAE TNIDQDINNL KEKWESVETK LNERKTKLEE ALNLAMEFHN SLQDFINWLT 4200
QAEQTLNVAS RPSLILDTVL FQIDEHKVFA NEVNSHREQI IELDKTGTHL KYFSQKQDVV 4260
LIKNLLISVQ SRWEKVVQRL VERGRSLDDA RKRAKQFHEA WSKLMEWLEE SEKSLDSELE 4320
IANDPDKIKT QLAQHKEFQK SLGAKHSVYD TTNRTGRSLK EKTSLADDNL KLDDMLSELR 4380
DKWDTICGKS VERQNKLEEA LLFSGQFTDA LQALIDWLYR VEPQLAEDQP VHGDIDLVMN 4440
LIDNHKAFQK ELGKRTSSVQ ALKRSARELI EGSRDDSSWV KVQMQELSTR WETVCALSIS 4500
KQTRLEAALR QAEEFHSVVH ALLEWLAEAE QTLRFHGVLP DDEDALRTLI DQHKEFMKKL 4560
EEKRAELNKA TTMGDTVLAI CHPDSITTIK HWITIIRARF EEVLAWAKQH QQRLASALAG 4620
LIAKQELLEA LLAWLQWAET TLTDKDKEVI PQEIEEVKAL IAEHQTFMEE MTRKQPDVDK 4680
VTKTYKRRAA DPSSLQSHIP VLDKGRAGRK RFPASSLYPS GSQTQIETKN PRVNLLVSKW 4740
QQVWLLALER RRKLNDALDR LEELREFANF DFDIWRKKYM RWMNHKKSRV MDFFRRIDKD 4800
QDGKITRQEF IDGILSSKFP TSRLEMSAVA DIFDRDGDGY IDYYEFVAAL HPNKDAYKPI 4860
TDADKIEDEV TRQVAKCKCA KRFQVEQIGD NKYRFFLGNQ FGDSQQLRLV RILRSTVMVR 4920
VGGGWMALDE FLVKNDPCRA KGRTNMELRE KFILADGASQ GMAAFRPRGR RSRPSSRGAS 4980
PNRSTSVSSQ AAQAASPQVP ATTTPKILHP LTRNYGKPWL TNSKMSTPCK AAECSDFPVP 5040
SAEGTPIQGS KLRLPGYLSG KGFHSGEDSG LITTAAARVR TQFADSKKTP SRPGSRAGSK 5100
AGSRASSRRG SDASDFDISE IQSVCSDVET VPQTHRPTPR AGSRPSTAKP SKIPTPQRKS 5160
PASKLDKSSK R 5171 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
 GO:0030424; C:axon; IEA:UniProtKB-SubCell.
 GO:0033267; C:axon part; IDA:UniProtKB.
 GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
 GO:0005604; C:basement membrane; TAS:ProtInc.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0031252; C:cell leading edge; IDA:UniProtKB.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0031673; C:H zone; IEA:UniProtKB-SubCell.
 GO:0030056; C:hemidesmosome; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
 GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
 GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
 GO:0035371; C:microtubule plus end; IDA:UniProtKB.
 GO:0060053; C:neurofilament cytoskeleton; IEA:Compara.
 GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007050; P:cell cycle arrest; IEA:InterPro.
 GO:0048870; P:cell motility; IMP:UniProtKB.
 GO:0031122; P:cytoplasmic microtubule organization; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
 GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
 GO:0045104; P:intermediate filament cytoskeleton organization; IEP:UniProtKB.
 GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
 GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
 GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:Compara.
 GO:0009611; P:response to wounding; IDA:UniProtKB.
 GO:0008090; P:retrograde axon cargo transport; IEA:Compara. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR003108; GAS2_dom.
 IPR001101; Plectin_repeat.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF13499; EF_hand_5
 PF02187; GAS2
 PF00681; Plectin
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00054; EFh
 SM00243; GAS2
 SM00250; PLEC
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS51460; GAR
 PS50002; SH3 
PRINTS