CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012506
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
28REGVMVAKKDRRPRSubiquitination[1]
128GPLGSPPKRGPLPTEubiquitination[2, 3]
143EQRVYRRKELEEVSPubiquitination[2, 3]
187VQKKTFTKWVNKHLIacetylation[4]
187VQKKTFTKWVNKHLIubiquitination[3]
236KGRMRFHKLQNVQIAubiquitination[3]
300EDMTAKEKLLLWSQRubiquitination[3]
338NAIIHRHKPLLIDMNubiquitination[3]
386DVPQPDEKSIITYVSubiquitination[2, 5]
462WSQFLKFKEMELPAKacetylation[6]
469KEMELPAKEADKNRSubiquitination[2]
477EADKNRSKGIYQSLEubiquitination[2]
493AVQAGQLKVPPGYHPubiquitination[2]
567VRLLAAGKVPQRAGEubiquitination[3]
581EVERDLDKADSMIRLubiquitination[2]
597FNDVQTLKDGRHPQGubiquitination[2, 3]
630TEYNLRLKAGVAAPAubiquitination[2]
740RLDLQYAKLLNSSKAubiquitination[2, 3]
810ELKEKKIKELQNAGDubiquitination[7]
908LQDAQDEKEQLNEYKacetylation[8, 9]
908LQDAQDEKEQLNEYKubiquitination[2, 7]
923GHLSGLAKRAKAVVQubiquitination[7]
1165QRIAEQQKAQAEVEGubiquitination[2, 3, 7]
1175AEVEGLGKGVARLSAubiquitination[3]
1186RLSAEAEKVLALPEPubiquitination[2]
1210ELELTLGKLEQVRSLubiquitination[1, 2, 3, 5, 7, 10, 11, 12, 13, 14]
1224LSAIYLEKLKTISLVubiquitination[3]
1250RAHEEQLKEAQAVPAubiquitination[2, 7, 11]
1266LPELEATKASLKKLRacetylation[8]
1410EECQRFAKQYINAIKubiquitination[2, 3, 7]
1417KQYINAIKDYELQLVubiquitination[2]
1427ELQLVTYKAQLEPVAubiquitination[2, 7]
1508EVEAALEKQRQLAEAubiquitination[2]
1718AEAELQSKRASFAEKubiquitination[2, 7]
1725KRASFAEKTAQLERSubiquitination[3]
1774ELERWQLKANEALRLacetylation[8]
1833LAEQELEKQRQLAEGacetylation[9]
1896ELEAELAKVRAEMEVacetylation[8]
1951RALAEEAKRQRQLAEacetylation[8]
1975AERVLAEKLAAIGEAacetylation[9]
2073ALKASFEKAAAGKAEacetylation[8]
2189KRLQAEEKAHAFAVQacetylation[9]
2379VQMEELSKLKARIEAacetylation[8]
2409FLQEEAEKMKQVAEEacetylation[9]
2409FLQEEAEKMKQVAEEubiquitination[7]
2447QQRALAEKMLKEKMQubiquitination[3]
2553QAEEIGEKLHRTELAacetylation[8]
2604EKLQQEAKLLQLKSEubiquitination[3]
2650ERFIEQEKAKLEQLFubiquitination[2]
2663LFQDEVAKAQQLREEubiquitination[2]
2761ASQVAATKTLPNGRDubiquitination[3]
2841SIAGLLLKATNEKLSacetylation[4, 8]
2903VGPELHHKLLSAERAacetylation[9]
2915ERAVTGYKDPYTGQQacetylation[9]
2931SLFQAMQKGLIVREHubiquitination[2]
2988ADPSDDTKGFFDPNTubiquitination[2]
3027PLTDKAAKGGELVYTubiquitination[2]
3053TVSAPFGKFQGKTVTacetylation[9]
3091TGRITVEKIIKIIITacetylation[4, 8, 9]
3183SIYNALKKDLLPSDMubiquitination[2, 7]
3231VGPEFHEKLLSAEKAubiquitination[3]
3285GGIVDPSKSHRVPLDubiquitination[2, 7]
3316SAPRADAKAYSDPSTubiquitination[2, 7]
3384EVPVGGFKGRTVTVWubiquitination[2, 3, 7]
3420TGKVTVEKVIKILITacetylation[4, 8]
3420TGKVTVEKVIKILITubiquitination[3]
3469RAQFEQLKDGKTTVKacetylation[8]
3476KDGKTTVKDLSELGSubiquitination[3]
3590SLFQAMQKGLVLRQHubiquitination[2, 3]
3647ADPSDDTKGFFDPNTubiquitination[2]
3968YQRGYLNKDTHDQLSacetylation[9]
3968YQRGYLNKDTHDQLSubiquitination[2, 7]
4027LTFRGLRKQITMEELubiquitination[2, 3]
4060TSIEEVTKNLQKFLEubiquitination[2, 3]
4118GYVIDPIKGLKLTVEubiquitination[2, 7]
4138GIVGPEFKDKLLSAEubiquitination[2]
4140VGPEFKDKLLSAERAubiquitination[3]
4152ERAVTGYKDPYSGKLubiquitination[2, 3]
4158YKDPYSGKLISLFQAubiquitination[2, 7]
4173MKKGLILKDHGIRLLacetylation[8]
4205LPVEVAYKRGLFDEEubiquitination[2]
4287IVDPETGKEMSVYEAubiquitination[2, 3]
4348DIDDAIAKNLIDRSAubiquitination[2, 3]
4475PVTDAVNKGLVDKIMubiquitination[2]
4480VNKGLVDKIMVDRINubiquitination[3]
4491DRINLAQKAFCGFEDubiquitination[3]
4513SAAQALKKGWLYYEAubiquitination[2, 3]
4609EAAAQSTKGYYSPYSubiquitination[1, 2, 3, 7, 11]
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] 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] 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]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [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]
 [7] 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]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] 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]
 [11] 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]
 [12] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [13] 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]
 [14] 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
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
MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLRARGL 60
VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV RRPVAMVMPA RRTPHVQAVQ 120
GPLGSPPKRG PLPTEEQRVY RRKELEEVSP ETPVVPATTQ RTLARPGPEP APATDERDRV 180
QKKTFTKWVN KHLIKAQRHI SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV 240
QIALDYLRHR QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK 300
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ TNLENLDQAF 360
SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP RVPDVQDGVR ANELQLRWQE 420
YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE IEILWSQFLK FKEMELPAKE ADKNRSKGIY 480
QSLEGAVQAG QLKVPPGYHP LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM 540
EAGLCEEQLN QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR 600
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR RPELEDSTLR 660
YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ SIEEFRAKIE RARSDEGQLS 720
PATRGAYRDC LGRLDLQYAK LLNSSKARLR SLESLHSFVA AATKELMWLN EKEEEEVGFD 780
WSDRNTNMTA KKESYSALMR ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ 840
WSWMLQLCCC IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL 900
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC DYKQVEVTVH 960
KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ EAQEAVTRLE AQHQALVTLW 1020
HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT FRTLKPEEQR QALHSLELHY QAFLRDSQDA 1080
GGFGPEDRLM AEREYGSCSH HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT 1140
VHRLRLPLDK EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL 1200
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK EAQAVPATLP 1260
ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL QQRHGERDVE VERWRERVAQ 1320
LLERWQAVLA QTDVRQRELE QLGRQLRYYR ESADPLGAWL QDARRRQEQI QAMPLADSQA 1380
VREQLRQEQA LLEEIERHGE KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP 1440
KVQSGSESVI QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA 1500
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ QKRSIQEELQ 1560
QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA TERQRGGAEG ELQALRARAE 1620
EAEAQKRQAQ EEAERLRRQV QDESQRKRQA EVELASRVKA EAEAAREKQR ALQALEELRL 1680
QAEEAERRLR QAEVERARQV QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV 1740
AQLREEAERR AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE 1800
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ ELIRLRAETE 1860
QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE MEVLLASKAR AEEESRSTSE 1920
KSKQRLEAEA GRFRELAEEA ARLRALAEEA KRQRQLAEED AARQRAEAER VLAEKLAAIG 1980
EATRLKTEAE IALKEKEAEN ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD 2040
SELERQKGLV EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE 2100
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER LKAKVEEARR 2160
LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ ELQQTLQQEQ SVLDQLRGEA 2220
EAARRAAEEA EEARVQAERE AAQSRRQVEE AERLKQSAEE QAQARAQAQA AAEKLRKEAE 2280
QEAARRAQAE QAALRQKQAA DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN 2340
LLDEELQRLK AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ 2400
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK EKMQAVQEAT 2460
RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG FQRTLEAERQ RQLEMSAEAE 2520
RLKLRVAEMS RAQARAEEDA QRFRKQAEEI GEKLHRTELA TQEKVTLVQT LEIQRQQSDH 2580
DAERLREAIA ELEREKEKLQ QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL 2640
QRERFIEQEK AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE 2700
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE EVTASQVAAT 2760
KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI LSAEELQRLA QGHTTVDELA 2820
RREDVRHYLQ GRSSIAGLLL KATNEKLSVY AALQRQLLSP GTALILLEAQ AASGFLLDPV 2880
RNRRLTVNEA VKEGVVGPEL HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI 2940
RLLEAQIATG GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT 3000
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP FGKFQGKTVT 3060
IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV EEQEQKGRLC FEGLRSLVPA 3120
AELLESRVID RELYQQLQRG ERSVRDVAEV DTVRRALRGA NVIAGVWLEE AGQKLSIYNA 3180
LKKDLLPSDM AVALLEAQAG TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT 3240
GYRDPYTGQS VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL 3300
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS EKAARARQEE 3360
LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT AEQRQELLRQ FRTGKVTVEK 3420
VIKILITIVE EVETLRQERL SFSGLRAPVP ASELLASGVL SRAQFEQLKD GKTTVKDLSE 3480
LGSVRTLLQG SGCLAGIYLE DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR 3540
NQRLYVHEAV KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR 3600
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF DPNTHENLTY 3660
RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET RRAFEETQID IPGGGSHGGS 3720
TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV TKERMIIIII EIIEKTEIIR QQGLASYDYV 3780
RRRLTAEDLF EARIISLETY NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT 3840
LSIYQALKKG LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS 3900
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR LGFHLPLEVA 3960
YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR CRRDDGTGQL LLPLSDARKL 4020
TFRGLRKQIT MEELVRSQVM DEATALQLRE GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT 4080
KERLSVYQAM KKGIIRPGTA FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK 4140
LLSAERAVTG YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV 4200
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ TGLCLLPLKE 4260
KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI DHQTYLELSE QECEWEEITI 4320
SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL IDRSALDQYR AGTLSITEFA DMLSGNAGGF 4380
RSRSSSVGSS SSYPISPAVS RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV 4440
DNITGQRLLE AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR 4500
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ RGTVDARTAQ 4560
KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL LEAAAQSTKG YYSPYSVSGS 4620
GSTAGSRTGS RTGSRAGSRR GSFDATGSGF SMTFSSSSYS SSGYGRRYAS GSSASLGGPE 4680
SAVA 4684 
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