CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011017
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
1421NNTLRCLKLELERKDubiquitination[1, 2]
1554AEKENNDKIQRLNEEmethylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
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 RLEEEEIKRC KETSEHGAYS DLLQRQKATV LENSKLTGKI 1140
SELERMVAEL KKQKSRVEEE LPKVREAAEN ELRKQQRNVE DISLQKIRAE SEAKQYRREL 1200
ETIVREKEAA ERELERVRQL TIEAEAKRAA VEENLLNFRN QLEENTFTRR TLEDHLKRKD 1260
LSLNDLEQQK NKLMEELRRK RDNEEELLKL IKQMEKDLAF QKQVAEKQLK EKQKIELEAR 1320
RKITEIQYTC RENALPVCPI TQATSCRAVT GLQQEHDKQK AEELKQQVDE LTAANRKAEQ 1380
DMRELTYELN ALQLEKTSSE EKARLLKDKL DETNNTLRCL KLELERKDQA EKGYSQQLRE 1440
LGRQLNQTTG KAEEAMQEAS DLKKIKRNYQ LELESLNHEK GKLQREVDRI TRAHAVAEKN 1500
IQHLNSQIHS FRDEKELERL QICQRKSDHL KEQFEKSHEQ LLQNIKAEKE NNDKIQRLNE 1560
ELEKSNECAE MLKQKVEELT RQNNETKLMM QRIQAESENI VLEKQTIQQR CEALKIQADG 1620
FKDQLRSTNE HLHKQTKTEQ DFQRKIKCLE EDLAKSQNLV SEFKQKCDQQ NIIIQNTKKE 1680
VRNLNAELNA SKEEKRRGEQ KVQLQQAQVQ ELNNRLKKVQ DELHLKTIEE QMTHRKMVLF 1740
QEESGKFKQS AEEFRKKMEK LMESKVITEN DISGIRLDFV SLQQENSRAQ ENAKLCETNI 1800
KELERQLQQY REQMQQGQHM EANHYQKCQK LEDELIAQKR EVENLKQKMD QQIKEHEHQL 1860
VLLQCEIQKK STAKDCTFKP DFEMTVKECQ HSGELSSRNT GHLHPTPRSP LLRWTQEPQP 1920
LEEKWQHRVV EQIPKEVQFQ PPGAPLEKEK SQQCYSEYFS QTSTELQITF DETNPITRLS 1980
EIEKIRDQAL NNSRPPVRYQ DNACEMELVK VLTPLEIAKN KQYDMHTEVT TLKQEKNPVP 2040
SAEEWMLEGC RASGGLKKGD FLKKGLEPET FQNFDGDHAC SVRDDEFKFQ GLRHTVTARQ 2100
LVEAKLLDMR TIEQLRLGLK TVEEVQKTLN KFLTKATSIA GLYLESTKEK ISFASAAERI 2160
IIDKMVALAF LEAQAATGFI IDPISGQTYS VEDAVLKGVV DPEFRIRLLE AEKAAVGYSY 2220
SSKTLSVFQA MENRMLDRQK GKHILEAQIA SGGVIDPVRG IRVPPEIALQ QGLLNNAILQ 2280
FLHEPSSNTR VFPNPNNKQA LYYSELLRMC VFDVESQCFL FPFGERNISN LNVKKTHRIS 2340
VVDTKTGSEL TVYEAFQRNL IEKSIYLELS GQQYQWKEAM FFESYGHSSH MLTDTKTGLH 2400
FNINEAIEQG TIDKALVKKY QEGLITLTEL ADSLLSRLVP KKDLHSPVAG YWLTASGERI 2460
SVLKASRRNL VDRITALRCL EAQVSTGGII DPLTGKKYRV AEALHRGLVD EGFAQQLRQC 2520
ELVITGIGHP ITNKMMSVVE AVNANIINKE MGIRCLEFQY LTGGLIEPQV HSRLSIEEAL 2580
QVGIIDVLIA TKLKDQKSYV RNIICPQTKR KLTYKEALEK ADFDFHTGLK LLEVSEPLMT 2640
GISSLYYSS 2649 
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