CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004392
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Desmoplakin 
Protein Synonyms/Alias
 DP; 250/210 kDa paraneoplastic pemphigus antigen 
Gene Name
 DSP 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
94LIVQPELKYGDGIQLubiquitination[1, 2, 3, 4]
140QPCDAYQKRLLQLQEubiquitination[5]
154EQMRALYKAISVPRVubiquitination[1, 4]
245IKADLREKSAIYQLEubiquitination[2, 3]
931MRFLNEQKNLHSEISubiquitination[1, 4]
949DKSEEVQKIAELCANubiquitination[1, 4]
1033DLKLKNTKIEVLEEEubiquitination[2]
1167SEKAIKEKEYEIERLacetylation[6]
1250SRENRDLKDEIVRLNubiquitination[2]
2393LPVDIAYKRGYFNEEubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] 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
 Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin- plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes. 
Sequence Annotation
 REPEAT 178 271 Spectrin 1.
 REPEAT 272 375 Spectrin 2.
 REPEAT 376 446 Spectrin 3a.
 DOMAIN 447 515 SH3.
 REPEAT 516 545 Spectrin 3b.
 REPEAT 546 627 Spectrin 4.
 REPEAT 654 769 Spectrin 5.
 REPEAT 770 883 Spectrin 6.
 REPEAT 2009 2045 Plectin 1.
 REPEAT 2046 2083 Plectin 2.
 REPEAT 2084 2121 Plectin 3.
 REPEAT 2122 2159 Plectin 4.
 REPEAT 2163 2197 Plectin 5.
 REPEAT 2198 2233 Plectin 6.
 REPEAT 2251 2288 Plectin 7.
 REPEAT 2289 2326 Plectin 8.
 REPEAT 2327 2364 Plectin 9.
 REPEAT 2365 2402 Plectin 10.
 REPEAT 2406 2440 Plectin 11.
 REPEAT 2456 2493 Plectin 12.
 REPEAT 2507 2544 Plectin 13.
 REPEAT 2610 2647 Plectin 14.
 REPEAT 2648 2685 Plectin 15.
 REPEAT 2724 2761 Plectin 16.
 REPEAT 2762 2799 Plectin 17.
 REGION 1 1056 Globular 1.
 REGION 1 584 Interacts with plakophilin 1 and junction
 REGION 1057 1945 Central fibrous rod domain.
 REGION 1946 2871 Globular 2.
 REGION 1960 2208 4.5 X 38 AA tandem repeats (Domain A).
 REGION 2244 2446 4.5 X 38 AA tandem repeats (Domain B).
 REGION 2609 2822 4.5 X 38 AA tandem repeats (Domain C).
 REGION 2824 2847 6 X 4 AA tandem repeats of G-S-R-[SR].
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 176 176 Phosphoserine.
 MOD_RES 2024 2024 Phosphoserine.
 MOD_RES 2207 2207 Phosphoserine.
 MOD_RES 2209 2209 Phosphoserine.
 MOD_RES 2815 2815 Phosphoserine.
 MOD_RES 2820 2820 Phosphoserine.
 MOD_RES 2821 2821 Phosphoserine.
 MOD_RES 2825 2825 Phosphoserine.
 MOD_RES 2849 2849 Phosphoserine.
 MOD_RES 2853 2853 Phosphothreonine.
 MOD_RES 2868 2868 Phosphoserine.
 LIPID 2480 2480 Omega-hydroxyceramide glutamate ester  
Keyword
 3D-structure; Alternative splicing; Cardiomyopathy; Cell junction; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Epidermolysis bullosa; Lipoprotein; Palmoplantar keratoderma; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2871 AA 
Protein Sequence
MSCNGGSHPR INTLGRMIRA ESGPDLRYEV TSGGGGTSRM YYSRRGVITD QNSDGYCQTG 60
TMSRHQNQNT IQELLQNCSD CLMRAELIVQ PELKYGDGIQ LTRSRELDEC FAQANDQMEI 120
LDSLIREMRQ MGQPCDAYQK RLLQLQEQMR ALYKAISVPR VRRASSKGGG GYTCQSGSGW 180
DEFTKHVTSE CLGWMRQQRA EMDMVAWGVD LASVEQHINS HRGIHNSIGD YRWQLDKIKA 240
DLREKSAIYQ LEEEYENLLK ASFERMDHLR QLQNIIQATS REIMWINDCE EEELLYDWSD 300
KNTNIAQKQE AFSIRMSQLE VKEKELNKLK QESDQLVLNQ HPASDKIEAY MDTLQTQWSW 360
ILQITKCIDV HLKENAAYFQ FFEEAQSTEA YLKGLQDSIR KKYPCDKNMP LQHLLEQIKE 420
LEKEREKILE YKRQVQNLVN KSKKIVQLKP RNPDYRSNKP IILRALCDYK QDQKIVHKGD 480
ECILKDNNER SKWYVTGPGG VDMLVPSVGL IIPPPNPLAV DLSCKIEQYY EAILALWNQL 540
YINMKSLVSW HYCMIDIEKI RAMTIAKLKT MRQEDYMKTI ADLELHYQEF IRNSQGSEMF 600
GDDDKRKIQS QFTDAQKHYQ TLVIQLPGYP QHQTVTTTEI THHGTCQDVN HNKVIETNRE 660
NDKQETWMLM ELQKIRRQIE HCEGRMTLKN LPLADQGSSH HITVKINELK SVQNDSQAIA 720
EVLNQLKDML ANFRGSEKYC YLQNEVFGLF QKLENINGVT DGYLNSLCTV RALLQAILQT 780
EDMLKVYEAR LTEEETVCLD LDKVEAYRCG LKKIKNDLNL KKSLLATMKT ELQKAQQIHS 840
QTSQQYPLYD LDLGKFGEKV TQLTDRWQRI DKQIDFRLWD LEKQIKQLRN YRDNYQAFCK 900
WLYDAKRRQD SLESMKFGDS NTVMRFLNEQ KNLHSEISGK RDKSEEVQKI AELCANSIKD 960
YELQLASYTS GLETLLNIPI KRTMIQSPSG VILQEAADVH ARYIELLTRS GDYYRFLSEM 1020
LKSLEDLKLK NTKIEVLEEE LRLARDANSE NCNKNKFLDQ NLQKYQAECS QFKAKLASLE 1080
ELKRQAELDG KSAKQNLDKC YGQIKELNEK ITRLTYEIED EKRRRKSVED RFDQQKNDYD 1140
QLQKARQCEK ENLGWQKLES EKAIKEKEYE IERLRVLLQE EGTRKREYEN ELAKVRNHYN 1200
EEMSNLRNKY ETEINITKTT IKEISMQKED DSKNLRNQLD RLSRENRDLK DEIVRLNDSI 1260
LQATEQRRRA EENALQQKAC GSEIMQKKQH LEIELKQVMQ QRSEDNARHK QSLEEAAKTI 1320
QDKNKEIERL KAEFQEEAKR RWEYENELSK VRNNYDEEII SLKNQFETEI NITKTTIHQL 1380
TMQKEEDTSG YRAQIDNLTR ENRSLSEEIK RLKNTLTQTT ENLRRVEEDI QQQKATGSEV 1440
SQRKQQLEVE LRQVTQMRTE ESVRYKQSLD DAAKTIQDKN KEIERLKQLI DKETNDRKCL 1500
EDENARLQRV QYDLQKANSS ATETINKLKV QEQELTRLRI DYERVSQERT VKDQDITRFQ 1560
NSLKELQLQK QKVEEELNRL KRTASEDSCK RKKLEEELEG MRRSLKEQAI KITNLTQQLE 1620
QASIVKKRSE DDLRQQRDVL DGHLREKQRT QEELRRLSSE VEALRRQLLQ EQESVKQAHL 1680
RNEHFQKAIE DKSRSLNESK IEIERLQSLT ENLTKEHLML EEELRNLRLE YDDLRRGRSE 1740
ADSDKNATIL ELRSQLQISN NRTLELQGLI NDLQRERENL RQEIEKFQKQ ALEASNRIQE 1800
SKNQCTQVVQ ERESLLVKIK VLEQDKARLQ RLEDELNRAK STLEAETRVK QRLECEKQQI 1860
QNDLNQWKTQ YSRKEEAIRK IESEREKSER EKNSLRSEIE RLQAEIKRIE ERCRRKLEDS 1920
TRETQSQLET ERSRYQREID KLRQRPYGSH RETQTECEWT VDTSKLVFDG LRKKVTAMQL 1980
YECQLIDKTT LDKLLKGKKS VEEVASEIQP FLRGAGSIAG ASASPKEKYS LVEAKRKKLI 2040
SPESTVMLLE AQAATGGIID PHRNEKLTVD SAIARDLIDF DDRQQIYAAE KAITGFDDPF 2100
SGKTVSVSEA IKKNLIDRET GMRLLEAQIA SGGVVDPVNS VFLPKDVALA RGLIDRDLYR 2160
SLNDPRDSQK NFVDPVTKKK VSYVQLKERC RIEPHTGLLL LSVQKRSMSF QGIRQPVTVT 2220
ELVDSGILRP STVNELESGQ ISYDEVGERI KDFLQGSSCI AGIYNETTKQ KLGIYEAMKI 2280
GLVRPGTALE LLEAQAATGF IVDPVSNLRL PVEEAYKRGL VGIEFKEKLL SAERAVTGYN 2340
DPETGNIISL FQAMNKELIE KGHGIRLLEA QIATGGIIDP KESHRLPVDI AYKRGYFNEE 2400
LSEILSDPSD DTKGFFDPNT EENLTYLQLK ERCIKDEETG LCLLPLKEKK KQVQTSQKNT 2460
LRKRRVVIVD PETNKEMSVQ EAYKKGLIDY ETFKELCEQE CEWEEITITG SDGSTRVVLV 2520
DRKTGSQYDI QDAIDKGLVD RKFFDQYRSG SLSLTQFADM ISLKNGVGTS SSMGSGVSDD 2580
VFSSSRHESV SKISTISSVR NLTIRSSSFS DTLEESSPIA AIFDTENLEK ISITEGIERG 2640
IVDSITGQRL LEAQACTGGI IHPTTGQKLS LQDAVSQGVI DQDMATRLKP AQKAFIGFEG 2700
VKGKKKMSAA EAVKEKWLPY EAGQRFLEFQ YLTGGLVDPE VHGRISTEEA IRKGFIDGRA 2760
AQRLQDTSSY AKILTCPKTK LKISYKDAIN RSMVEDITGL RLLEAASVSS KGLPSPYNMS 2820
SAPGSRSGSR SGSRSGSRSG SRSGSRRGSF DATGNSSYSY SYSFSSSSIG H 2871 
Gene Ontology
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0001533; C:cornified envelope; IDA:UniProtKB.
 GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
 GO:0014704; C:intercalated disc; IDA:BHF-UCL.
 GO:0005882; C:intermediate filament; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0034332; P:adherens junction organization; IEA:Compara.
 GO:0086069; P:bundle of His cell to Purkinje myocyte communication; IMP:BHF-UCL.
 GO:0016337; P:cell-cell adhesion; IEA:Compara.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0002934; P:desmosome organization; ISS:BHF-UCL.
 GO:0045109; P:intermediate filament organization; ISS:BHF-UCL.
 GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
 GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
 GO:0071896; P:protein localization to adherens junction; ISS:BHF-UCL.
 GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
 GO:0086005; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
 GO:0043588; P:skin development; IEA:Compara.
 GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:BHF-UCL. 
Interpro
 IPR001101; Plectin_repeat.
 IPR018159; Spectrin/alpha-actinin. 
Pfam
 PF00681; Plectin 
SMART
 SM00250; PLEC
 SM00150; SPEC 
PROSITE
 PS50002; SH3 
PRINTS