CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012508
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Plectin 
Protein Synonyms/Alias
 PCN; PLTN; Hemidesmosomal protein 1; HD1; Plectin-1 
Gene Name
 PLEC 
Gene Synonyms/Alias
 PLEC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50VQKKTFTKWVNKHLIubiquitination[1]
99KGRMRFHKLQNVQIAubiquitination[1]
163EDMTAKEKLLLWSQRubiquitination[1]
201NAIIHRHKPLLIDMNubiquitination[1]
430VRLLAAGKVPQRAGEubiquitination[1]
460FNDVQTLKDGRHPQGubiquitination[1]
603RLDLQYAKLLNSSKAubiquitination[1]
1028QRIAEQQKAQAEVEGubiquitination[1]
1038AEVEGLGKGVARLSAubiquitination[1]
1073ELELTLGKLEQVRSLubiquitination[1]
1087LSAIYLEKLKTISLVubiquitination[1]
1273EECQRFAKQYINAIKubiquitination[1]
1588KRASFAEKTAQLERSubiquitination[1]
2310QQRALAEKMLKEKMQubiquitination[1]
2467EKLQQEAKLLQLKSEubiquitination[1]
2624ASQVAATKTLPNGRDubiquitination[1]
3094VGPEFHEKLLSAEKAubiquitination[1]
3247EVPVGGFKGRTVTVWubiquitination[1]
3283TGKVTVEKVIKILITubiquitination[1]
3339KDGKTTVKDLSELGSubiquitination[1]
3453SLFQAMQKGLVLRQHubiquitination[1]
3890LTFRGLRKQITMEELubiquitination[1]
3923TSIEEVTKNLQKFLEubiquitination[1]
4003VGPEFKDKLLSAERAubiquitination[1]
4015ERAVTGYKDPYSGKLubiquitination[1]
4150IVDPETGKEMSVYEAubiquitination[1]
4211DIDDAIAKNLIDRSAubiquitination[1]
4343VNKGLVDKIMVDRINubiquitination[1]
4354DRINLAQKAFCGFEDubiquitination[1]
4376SAAQALKKGWLYYEAubiquitination[1]
4472EAAAQSTKGYYSPYSubiquitination[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
 Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofibers integrity. 
Sequence Annotation
 DOMAIN 175 400 Actin-binding.
 DOMAIN 179 282 CH 1.
 DOMAIN 295 397 CH 2.
 REPEAT 645 710 Spectrin 1.
 REPEAT 740 824 Spectrin 2.
 REPEAT 837 930 Spectrin 3.
 REPEAT 1315 1415 Spectrin 4.
 REPEAT 2826 2863 Plectin 1.
 REPEAT 2864 2901 Plectin 2.
 REPEAT 2902 2939 Plectin 3.
 REPEAT 2940 2977 Plectin 4.
 REPEAT 2981 3015 Plectin 5.
 REPEAT 3116 3153 Plectin 6.
 REPEAT 3154 3191 Plectin 7.
 REPEAT 3192 3229 Plectin 8.
 REPEAT 3230 3267 Plectin 9.
 REPEAT 3268 3305 Plectin 10.
 REPEAT 3306 3343 Plectin 11.
 REPEAT 3485 3522 Plectin 12.
 REPEAT 3523 3560 Plectin 13.
 REPEAT 3561 3598 Plectin 14.
 REPEAT 3599 3636 Plectin 15.
 REPEAT 3640 3674 Plectin 16.
 REPEAT 3820 3857 Plectin 17.
 REPEAT 3858 3895 Plectin 18.
 REPEAT 3896 3933 Plectin 19.
 REPEAT 3934 3971 Plectin 20.
 REPEAT 3975 4008 Plectin 21.
 REPEAT 4063 4100 Plectin 22.
 REPEAT 4101 4138 Plectin 23.
 REPEAT 4139 4176 Plectin 24.
 REPEAT 4177 4214 Plectin 25.
 REPEAT 4218 4252 Plectin 26.
 REPEAT 4265 4305 Plectin 27.
 REPEAT 4319 4356 Plectin 28.
 REPEAT 4408 4445 Plectin 29.
 REPEAT 4446 4483 Plectin 30.
 REPEAT 4484 4521 Plectin 31.
 REPEAT 4522 4559 Plectin 32.
 REPEAT 4560 4597 Plectin 33.
 REGION 1 1470 Globular 1.
 REGION 1471 2755 Central fibrous rod domain.
 REGION 2756 4684 Globular 2.
 REGION 4250 4300 Binding to intermediate filaments (By
 REGION 4625 4640 4 X 4 AA tandem repeats of G-S-R-X.
 MOD_RES 113 113 Phosphothreonine.
 MOD_RES 125 125 Phosphoserine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 201 201 Phosphoserine (By similarity).
 MOD_RES 720 720 Phosphoserine.
 MOD_RES 1435 1435 Phosphoserine.
 MOD_RES 1721 1721 Phosphoserine.
 MOD_RES 1732 1732 Phosphoserine.
 MOD_RES 3033 3033 Phosphotyrosine (By similarity).
 MOD_RES 3091 3091 N6-acetyllysine.
 MOD_RES 3362 3362 Phosphotyrosine (By similarity).
 MOD_RES 3420 3420 N6-acetyllysine.
 MOD_RES 4030 4030 Phosphothreonine.
 MOD_RES 4382 4382 Phosphoserine.
 MOD_RES 4384 4384 Phosphoserine (By similarity).
 MOD_RES 4385 4385 Phosphoserine.
 MOD_RES 4386 4386 Phosphoserine.
 MOD_RES 4389 4389 Phosphoserine.
 MOD_RES 4390 4390 Phosphoserine.
 MOD_RES 4391 4391 Phosphoserine.
 MOD_RES 4392 4392 Phosphoserine.
 MOD_RES 4396 4396 Phosphoserine.
 MOD_RES 4400 4400 Phosphoserine.
 MOD_RES 4411 4411 Phosphothreonine.
 MOD_RES 4539 4539 Phosphothreonine; by CDK1 (By
 MOD_RES 4613 4613 Phosphoserine.
 MOD_RES 4615 4615 Phosphotyrosine (By similarity).
 MOD_RES 4618 4618 Phosphoserine.
 MOD_RES 4622 4622 Phosphoserine.
 MOD_RES 4626 4626 Phosphoserine.
 MOD_RES 4642 4642 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cell junction; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Epidermolysis bullosa; Limb-girdle muscular dystrophy; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4684 AA 
Protein Sequence
MSQHQLRVPQ PEGLGRKRTS SEDNLYLAVL RASEGKKDER DRVQKKTFTK WVNKHLIKAQ 60
RHISDLYEDL RDGHNLISLL EVLSGDSLPR EKGRMRFHKL QNVQIALDYL RHRQVKLVNI 120
RNDDIADGNP KLTLGLIWTI ILHFQISDIQ VSGQSEDMTA KEKLLLWSQR MVEGYQGLRC 180
DNFTSSWRDG RLFNAIIHRH KPLLIDMNKV YRQTNLENLD QAFSVAERDL GVTRLLDPED 240
VDVPQPDEKS IITYVSSLYD AMPRVPDVQD GVRANELQLR WQEYRELVLL LLQWMRHHTA 300
AFEERRFPSS FEEIEILWSQ FLKFKEMELP AKEADKNRSK GIYQSLEGAV QAGQLKVPPG 360
YHPLDVEKEW GKLHVAILER EKQLRSEFER LECLQRIVTK LQMEAGLCEE QLNQADALLQ 420
SDVRLLAAGK VPQRAGEVER DLDKADSMIR LLFNDVQTLK DGRHPQGEQM YRRVYRLHER 480
LVAIRTEYNL RLKAGVAAPA TQVAQVTLQS VQRRPELEDS TLRYLQDLLA WVEENQHRVD 540
GAEWGVDLPS VEAQLGSHRG LHQSIEEFRA KIERARSDEG QLSPATRGAY RDCLGRLDLQ 600
YAKLLNSSKA RLRSLESLHS FVAAATKELM WLNEKEEEEV GFDWSDRNTN MTAKKESYSA 660
LMRELELKEK KIKELQNAGD RLLREDHPAR PTVESFQAAL QTQWSWMLQL CCCIEAHLKE 720
NAAYFQFFSD VREAEGQLQK LQEALRRKYS CDRSATVTRL EDLLQDAQDE KEQLNEYKGH 780
LSGLAKRAKA VVQLKPRHPA HPMRGRLPLL AVCDYKQVEV TVHKGDECQL VGPAQPSHWK 840
VLSSSGSEAA VPSVCFLVPP PNQEAQEAVT RLEAQHQALV TLWHQLHVDM KSLLAWQSLR 900
RDVQLIRSWS LATFRTLKPE EQRQALHSLE LHYQAFLRDS QDAGGFGPED RLMAEREYGS 960
CSHHYQQLLQ SLEQGAQEES RCQRCISELK DIRLQLEACE TRTVHRLRLP LDKEPARECA 1020
QRIAEQQKAQ AEVEGLGKGV ARLSAEAEKV LALPEPSPAA PTLRSELELT LGKLEQVRSL 1080
SAIYLEKLKT ISLVIRGTQG AEEVLRAHEE QLKEAQAVPA TLPELEATKA SLKKLRAQAE 1140
AQQPTFDALR DELRGAQEVG ERLQQRHGER DVEVERWRER VAQLLERWQA VLAQTDVRQR 1200
ELEQLGRQLR YYRESADPLG AWLQDARRRQ EQIQAMPLAD SQAVREQLRQ EQALLEEIER 1260
HGEKVEECQR FAKQYINAIK DYELQLVTYK AQLEPVASPA KKPKVQSGSE SVIQEYVDLR 1320
THYSELTTLT SQYIKFISET LRRMEEEERL AEQQRAEERE RLAEVEAALE KQRQLAEAHA 1380
QAKAQAEREA KELQQRMQEE VVRREEAAVD AQQQKRSIQE ELQQLRQSSE AEIQAKARQA 1440
EAAERSRLRI EEEIRVVRLQ LEATERQRGG AEGELQALRA RAEEAEAQKR QAQEEAERLR 1500
RQVQDESQRK RQAEVELASR VKAEAEAARE KQRALQALEE LRLQAEEAER RLRQAEVERA 1560
RQVQVALETA QRSAEAELQS KRASFAEKTA QLERSLQEEH VAVAQLREEA ERRAQQQAEA 1620
ERAREEAERE LERWQLKANE ALRLRLQAEE VAQQKSLAQA EAEKQKEEAE REARRRGKAE 1680
EQAVRQRELA EQELEKQRQL AEGTAQQRLA AEQELIRLRA ETEQGEQQRQ LLEEELARLQ 1740
REAAAATQKR QELEAELAKV RAEMEVLLAS KARAEEESRS TSEKSKQRLE AEAGRFRELA 1800
EEAARLRALA EEAKRQRQLA EEDAARQRAE AERVLAEKLA AIGEATRLKT EAEIALKEKE 1860
AENERLRRLA EDEAFQRRRL EEQAAQHKAD IEERLAQLRK ASDSELERQK GLVEDTLRQR 1920
RQVEEEILAL KASFEKAAAG KAELELELGR IRSNAEDTLR SKEQAELEAA RQRQLAAEEE 1980
RRRREAEERV QKSLAAEEEA ARQRKAALEE VERLKAKVEE ARRLRERAEQ ESARQLQLAQ 2040
EAAQKRLQAE EKAHAFAVQQ KEQELQQTLQ QEQSVLDQLR GEAEAARRAA EEAEEARVQA 2100
EREAAQSRRQ VEEAERLKQS AEEQAQARAQ AQAAAEKLRK EAEQEAARRA QAEQAALRQK 2160
QAADAEMEKH KKFAEQTLRQ KAQVEQELTT LRLQLEETDH QKNLLDEELQ RLKAEATEAA 2220
RQRSQVEEEL FSVRVQMEEL SKLKARIEAE NRALILRDKD NTQRFLQEEA EKMKQVAEEA 2280
ARLSVAAQEA ARLRQLAEED LAQQRALAEK MLKEKMQAVQ EATRLKAEAE LLQQQKELAQ 2340
EQARRLQEDK EQMAQQLAEE TQGFQRTLEA ERQRQLEMSA EAERLKLRVA EMSRAQARAE 2400
EDAQRFRKQA EEIGEKLHRT ELATQEKVTL VQTLEIQRQQ SDHDAERLRE AIAELEREKE 2460
KLQQEAKLLQ LKSEEMQTVQ QEQLLQETQA LQQSFLSEKD SLLQRERFIE QEKAKLEQLF 2520
QDEVAKAQQL REEQQRQQQQ MEQERQRLVA SMEEARRRQH EAEEGVRRKQ EELQQLEQQR 2580
RQQEELLAEE NQRLREQLQL LEEQHRAALA HSEEVTASQV AATKTLPNGR DALDGPAAEA 2640
EPEHSFDGLR RKVSAQRLQE AGILSAEELQ RLAQGHTTVD ELARREDVRH YLQGRSSIAG 2700
LLLKATNEKL SVYAALQRQL LSPGTALILL EAQAASGFLL DPVRNRRLTV NEAVKEGVVG 2760
PELHHKLLSA ERAVTGYKDP YTGQQISLFQ AMQKGLIVRE HGIRLLEAQI ATGGVIDPVH 2820
SHRVPVDVAY RRGYFDEEMN RVLADPSDDT KGFFDPNTHE NLTYLQLLER CVEDPETGLC 2880
LLPLTDKAAK GGELVYTDSE ARDVFEKATV SAPFGKFQGK TVTIWEIINS EYFTAEQRRD 2940
LLRQFRTGRI TVEKIIKIII TVVEEQEQKG RLCFEGLRSL VPAAELLESR VIDRELYQQL 3000
QRGERSVRDV AEVDTVRRAL RGANVIAGVW LEEAGQKLSI YNALKKDLLP SDMAVALLEA 3060
QAGTGHIIDP ATSARLTVDE AVRAGLVGPE FHEKLLSAEK AVTGYRDPYT GQSVSLFQAL 3120
KKGLIPREQG LRLLDAQLST GGIVDPSKSH RVPLDVACAR GCLDEETSRA LSAPRADAKA 3180
YSDPSTGEPA TYGELQQRCR PDQLTGLSLL PLSEKAARAR QEELYSELQA RETFEKTPVE 3240
VPVGGFKGRT VTVWELISSE YFTAEQRQEL LRQFRTGKVT VEKVIKILIT IVEEVETLRQ 3300
ERLSFSGLRA PVPASELLAS GVLSRAQFEQ LKDGKTTVKD LSELGSVRTL LQGSGCLAGI 3360
YLEDTKEKVS IYEAMRRGLL RATTAALLLE AQAATGFLVD PVRNQRLYVH EAVKAGVVGP 3420
ELHEQLLSAE KAVTGYRDPY SGSTISLFQA MQKGLVLRQH GIRLLEAQIA TGGIIDPVHS 3480
HRVPVDVAYQ RGYFSEEMNR VLADPSDDTK GFFDPNTHEN LTYRQLLERC VEDPETGLRL 3540
LPLKGAEKAE VVETTQVYTE EETRRAFEET QIDIPGGGSH GGSTMSLWEV MQSDLIPEEQ 3600
RAQLMADFQA GRVTKERMII IIIEIIEKTE IIRQQGLASY DYVRRRLTAE DLFEARIISL 3660
ETYNLLREGT RSLREALEAE SAWCYLYGTG SVAGVYLPGS RQTLSIYQAL KKGLLSAEVA 3720
RLLLEAQAAT GFLLDPVKGE RLTVDEAVRK GLVGPELHDR LLSAERAVTG YRDPYTEQTI 3780
SLFQAMKKEL IPTEEALRLL DAQLATGGIV DPRLGFHLPL EVAYQRGYLN KDTHDQLSEP 3840
SEVRSYVDPS TDERLSYTQL LRRCRRDDGT GQLLLPLSDA RKLTFRGLRK QITMEELVRS 3900
QVMDEATALQ LREGLTSIEE VTKNLQKFLE GTSCIAGVFV DATKERLSVY QAMKKGIIRP 3960
GTAFELLEAQ AATGYVIDPI KGLKLTVEEA VRMGIVGPEF KDKLLSAERA VTGYKDPYSG 4020
KLISLFQAMK KGLILKDHGI RLLEAQIATG GIIDPEESHR LPVEVAYKRG LFDEEMNEIL 4080
TDPSDDTKGF FDPNTEENLT YLQLMERCIT DPQTGLCLLP LKEKKRERKT SSKSSVRKRR 4140
VVIVDPETGK EMSVYEAYRK GLIDHQTYLE LSEQECEWEE ITISSSDGVV KSMIIDRRSG 4200
RQYDIDDAIA KNLIDRSALD QYRAGTLSIT EFADMLSGNA GGFRSRSSSV GSSSSYPISP 4260
AVSRTQLASW SDPTEETGPV AGILDTETLE KVSITEAMHR NLVDNITGQR LLEAQACTGG 4320
IIDPSTGERF PVTDAVNKGL VDKIMVDRIN LAQKAFCGFE DPRTKTKMSA AQALKKGWLY 4380
YEAGQRFLEV QYLTGGLIEP DTPGRVPLDE ALQRGTVDAR TAQKLRDVGA YSKYLTCPKT 4440
KLKISYKDAL DRSMVEEGTG LRLLEAAAQS TKGYYSPYSV SGSGSTAGSR TGSRTGSRAG 4500
SRRGSFDATG SGFSMTFSSS SYSSSGYGRR YASGSSASLG GPESAVA 4547 
Gene Ontology
 GO:0043034; C:costamere; TAS:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005925; C:focal adhesion; IDA:HPA.
 GO:0030056; C:hemidesmosome; IDA:UniProtKB.
 GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
 GO:0042383; C:sarcolemma; IDA:UniProtKB.
 GO:0016528; C:sarcoplasm; ISS:BHF-UCL.
 GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR001101; Plectin_repeat.
 IPR005326; S10_plectin_N.
 IPR018159; Spectrin/alpha-actinin. 
Pfam
 PF00307; CH
 PF00681; Plectin
 PF03501; S10_plectin 
SMART
 SM00033; CH
 SM00250; PLEC
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH 
PRINTS