CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012507
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
276DVPQPDEKSIITYVSubiquitination[1]
367EADKNRSKGIYQSLEubiquitination[1]
383AVQAGQLKVPPGYHPubiquitination[1]
487FNDVQTLKDGRHPQGubiquitination[1]
520TEYNLRLKAGVAAPAubiquitination[1]
700ELKEKKIKELQNAGDubiquitination[1]
798LQDAQDEKEQLNEYKubiquitination[1]
813GHLSGLAKRAKAVVQubiquitination[1]
1055QRIAEQQKAQAEVEGubiquitination[1]
1100ELELTLGKLEQVRSLubiquitination[1]
1140RAHEEQLKEAQAVPAubiquitination[1]
1300EECQRFAKQYINAIKubiquitination[1]
1317ELQLVTYKAQLEPVAubiquitination[1]
1608AEAELQSKRASFAEKubiquitination[1]
2299FLQEEAEKMKQVAEEubiquitination[1]
2821SLFQAMQKGLIVREHubiquitination[1]
3073SIYNALKKDLLPSDMubiquitination[1]
3175GGIVDPSKSHRVPLDubiquitination[1]
3206SAPRADAKAYSDPSTubiquitination[1]
3274EVPVGGFKGRTVTVWubiquitination[1]
3537ADPSDDTKGFFDPNTubiquitination[1]
3858YQRGYLNKDTHDQLSubiquitination[1]
4008GYVIDPIKGLKLTVEubiquitination[1]
4048YKDPYSGKLISLFQAubiquitination[1]
4499EAAAQSTKGYYSPYSubiquitination[1]
Reference
 [1] 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] 
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
MSGEDAEVRA VSEDVSNGSS GSPSPGDTLP WNLGKTQRSR RSGGGAGSNG SVLDPAERAV 60
IRIADERDRV QKKTFTKWVN KHLIKAQRHI SDLYEDLRDG HNLISLLEVL SGDSLPREKG 120
RMRFHKLQNV QIALDYLRHR QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG 180
QSEDMTAKEK LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ 240
TNLENLDQAF SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP RVPDVQDGVR 300
ANELQLRWQE YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE IEILWSQFLK FKEMELPAKE 360
ADKNRSKGIY QSLEGAVQAG QLKVPPGYHP LDVEKEWGKL HVAILEREKQ LRSEFERLEC 420
LQRIVTKLQM EAGLCEEQLN QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF 480
NDVQTLKDGR HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR 540
RPELEDSTLR YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ SIEEFRAKIE 600
RARSDEGQLS PATRGAYRDC LGRLDLQYAK LLNSSKARLR SLESLHSFVA AATKELMWLN 660
EKEEEEVGFD WSDRNTNMTA KKESYSALMR ELELKEKKIK ELQNAGDRLL REDHPARPTV 720
ESFQAALQTQ WSWMLQLCCC IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR 780
SATVTRLEDL LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC 840
DYKQVEVTVH KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ EAQEAVTRLE 900
AQHQALVTLW HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT FRTLKPEEQR QALHSLELHY 960
QAFLRDSQDA GGFGPEDRLM AEREYGSCSH HYQQLLQSLE QGAQEESRCQ RCISELKDIR 1020
LQLEACETRT VHRLRLPLDK EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL 1080
PEPSPAAPTL RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK 1140
EAQAVPATLP ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL QQRHGERDVE 1200
VERWRERVAQ LLERWQAVLA QTDVRQRELE QLGRQLRYYR ESADPLGAWL QDARRRQEQI 1260
QAMPLADSQA VREQLRQEQA LLEEIERHGE KVEECQRFAK QYINAIKDYE LQLVTYKAQL 1320
EPVASPAKKP KVQSGSESVI QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ 1380
QRAEERERLA EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ 1440
QKRSIQEELQ QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA TERQRGGAEG 1500
ELQALRARAE EAEAQKRQAQ EEAERLRRQV QDESQRKRQA EVELASRVKA EAEAAREKQR 1560
ALQALEELRL QAEEAERRLR QAEVERARQV QVALETAQRS AEAELQSKRA SFAEKTAQLE 1620
RSLQEEHVAV AQLREEAERR AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ 1680
QKSLAQAEAE KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ 1740
ELIRLRAETE QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE MEVLLASKAR 1800
AEEESRSTSE KSKQRLEAEA GRFRELAEEA ARLRALAEEA KRQRQLAEED AARQRAEAER 1860
VLAEKLAAIG EATRLKTEAE IALKEKEAEN ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE 1920
RLAQLRKASD SELERQKGLV EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS 1980
NAEDTLRSKE QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER 2040
LKAKVEEARR LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ ELQQTLQQEQ 2100
SVLDQLRGEA EAARRAAEEA EEARVQAERE AAQSRRQVEE AERLKQSAEE QAQARAQAQA 2160
AAEKLRKEAE QEAARRAQAE QAALRQKQAA DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL 2220
QLEETDHQKN LLDEELQRLK AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA 2280
LILRDKDNTQ RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK 2340
EKMQAVQEAT RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG FQRTLEAERQ 2400
RQLEMSAEAE RLKLRVAEMS RAQARAEEDA QRFRKQAEEI GEKLHRTELA TQEKVTLVQT 2460
LEIQRQQSDH DAERLREAIA ELEREKEKLQ QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ 2520
SFLSEKDSLL QRERFIEQEK AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME 2580
EARRRQHEAE EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE 2640
EVTASQVAAT KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI LSAEELQRLA 2700
QGHTTVDELA RREDVRHYLQ GRSSIAGLLL KATNEKLSVY AALQRQLLSP GTALILLEAQ 2760
AASGFLLDPV RNRRLTVNEA VKEGVVGPEL HHKLLSAERA VTGYKDPYTG QQISLFQAMQ 2820
KGLIVREHGI RLLEAQIATG GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF 2880
FDPNTHENLT YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP 2940
FGKFQGKTVT IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV EEQEQKGRLC 3000
FEGLRSLVPA AELLESRVID RELYQQLQRG ERSVRDVAEV DTVRRALRGA NVIAGVWLEE 3060
AGQKLSIYNA LKKDLLPSDM AVALLEAQAG TGHIIDPATS ARLTVDEAVR AGLVGPEFHE 3120
KLLSAEKAVT GYRDPYTGQS VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP 3180
LDVACARGCL DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS 3240
EKAARARQEE LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT AEQRQELLRQ 3300
FRTGKVTVEK VIKILITIVE EVETLRQERL SFSGLRAPVP ASELLASGVL SRAQFEQLKD 3360
GKTTVKDLSE LGSVRTLLQG SGCLAGIYLE DTKEKVSIYE AMRRGLLRAT TAALLLEAQA 3420
ATGFLVDPVR NQRLYVHEAV KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK 3480
GLVLRQHGIR LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF 3540
DPNTHENLTY RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET RRAFEETQID 3600
IPGGGSHGGS TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV TKERMIIIII EIIEKTEIIR 3660
QQGLASYDYV RRRLTAEDLF EARIISLETY NLLREGTRSL REALEAESAW CYLYGTGSVA 3720
GVYLPGSRQT LSIYQALKKG LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV 3780
GPELHDRLLS AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR 3840
LGFHLPLEVA YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR CRRDDGTGQL 3900
LLPLSDARKL TFRGLRKQIT MEELVRSQVM DEATALQLRE GLTSIEEVTK NLQKFLEGTS 3960
CIAGVFVDAT KERLSVYQAM KKGIIRPGTA FELLEAQAAT GYVIDPIKGL KLTVEEAVRM 4020
GIVGPEFKDK LLSAERAVTG YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII 4080
DPEESHRLPV EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ 4140
TGLCLLPLKE KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI DHQTYLELSE 4200
QECEWEEITI SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL IDRSALDQYR AGTLSITEFA 4260
DMLSGNAGGF RSRSSSVGSS SSYPISPAVS RTQLASWSDP TEETGPVAGI LDTETLEKVS 4320
ITEAMHRNLV DNITGQRLLE AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ 4380
KAFCGFEDPR TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ 4440
RGTVDARTAQ KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL LEAAAQSTKG 4500
YYSPYSVSGS GSTAGSRTGS RTGSRAGSRR GSFDATGSGF SMTFSSSSYS SSGYGRRYAS 4560
GSSASLGGPE SAVA 4574 
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