CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018831
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Envoplakin 
Protein Synonyms/Alias
 210 kDa cornified envelope precursor protein; 210 kDa paraneoplastic pemphigus antigen; p210 
Gene Name
 EVPL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
383QQLEAEEKRLAVTERubiquitination[1, 2]
500ATVQSRLKASAVESLubiquitination[1, 2]
1451LRIQELEKRPPTVQEubiquitination[3]
1467IIMEEVVKLEKDPDLubiquitination[4, 5]
1500TELNRECKNLQVQIDubiquitination[2]
1511VQIDVLQKAKSQEKTubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [5] 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
Functional Description
 Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. 
Sequence Annotation
 REPEAT 229 330 Spectrin.
 REPEAT 1185 1226 Plectin 1.
 REPEAT 1678 1713 Plectin 2.
 REPEAT 1818 1855 Plectin 3.
 REPEAT 1856 1893 Plectin 4.
 REPEAT 1894 1931 Plectin 5.
 REPEAT 1932 1969 Plectin 6.
 REPEAT 1970 2007 Plectin 7.
 REGION 1 841 Globular 1.
 REGION 12 28 4 X 4 AA tandem repeats of K-G-S-P.
 REGION 842 1673 Central fibrous rod domain.
 REGION 1674 2033 Globular 2.
 MOD_RES 1799 1799 Phosphoserine.
 LIPID 657 657 Omega-hydroxyceramide glutamate ester
 LIPID 871 871 Omega-hydroxyceramide glutamate ester
 LIPID 1607 1607 Omega-hydroxyceramide glutamate ester
 CROSSLNK 1467 1467 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Cell junction; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Keratinization; Lipoprotein; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2033 AA 
Protein Sequence
MFKGLSKGSQ GKGSPKGSPA KGSPKGSPSR HSRAATQELA LLISRMQANA DQVERDILET 60
QKRLQQDRLN SEQSQALQHQ QETGRSLKEA EVLLKDLFLD VDKARRLKHP QAEEIEKDIK 120
QLHERVTQEC AEYRALYEKM VLPPDVGPRV DWARVLEQKQ KQVCAGQYGP GMAELEQQIA 180
EHNILQKEID AYGQQLRSLV GPDAATIRSQ YRDLLKAASW RGQSLGSLYT HLQGCTRQLS 240
ALAEQQRRIL QQDWSDLMAD PAGVRREYEH FKQHELLSQE QSVNQLEDDG ERMVELRHPA 300
VGPIQAHQEA LKMEWQNFLN LCICQETQLQ HVEDYRRFQE EADSVSQTLA KLNSNLDAKY 360
SPAPGGPPGA PTELLQQLEA EEKRLAVTER ATGDLQRRSR DVAPLPQRRN PPQQPLHVDS 420
ICDWDSGEVQ LLQGERYKLV DNTDPHAWVV QGPGGETKRA PAACFCIPAP DPDAVARASR 480
LASELQALKQ KLATVQSRLK ASAVESLRPS QQAPSGSDLA NPQAQKLLTQ MTRLDGDLGQ 540
IERQVLAWAR APLSRPTPLE DLEGRIHSHE GTAQRLQSLG TEKETAQKEC EAFLSTRPVG 600
PAALQLPVAL NSVKNKFSDV QVLCSLYGEK AKAALDLERQ IQDADRVIRG FEATLVQEAP 660
IPAEPGALQE RVSELQRQRR ELLEQQTCVL RLHRALKASE HACAALQNNF QEFCQDLPRQ 720
QRQVRALTDR YHAVGDQLDL REKVVQDAAL TYQQFKNCKD NLSSWLEHLP RSQVRPSDGP 780
SQIAYKLQAQ KRLTQEIQSR ERDRATASHL SQALQAALQD YELQADTYRC SLEPTLAVSA 840
PKRPRVAPLQ ESIQAQEKNL AKAYTEVAAA QQQLLQQLEF ARKMLEKKEL SEDIRRTHDA 900
KQGSESPAQA GRESEALKAQ LEEERKRVAR VQHELEAQRS QLLQLRTQRP LERLEEKEVV 960
EFYRDPQLEG SLSRVKAQVE EEGKRRAGLQ ADLEVAAQKV VQLESKRKTM QPHLLTKEVT 1020
QVERDPGLDS QAAQLRIQIQ QLRGEDAVIS ARLEGLKKEL LALEKREVDV KEKVVVKEVV 1080
KVEKNLEMVK AAQALRLQME EDAARRKQAE EAVAKLQARI EDLERAISSV EPKVIVKEVK 1140
KVEQDPGLLQ ESSRLRSLLE EERTKNATLA RELSDLHSKY SVVEKQRPKV QLQERVHEIF 1200
QVDPETEQEI TRLKAKLQEM AGKRSGVEKE VEKLLPDLEV LRAQKPTVEY KEVTQEVVRH 1260
ERSPEVLREI DRLKAQLNEL VNSHGRSQEQ LIRLQGERDE WRRERAKVET KTVSKEVVRH 1320
EKDPVLEKEA ERLRQEVREA AQKRRAAEDA VYELQSKRLL LERRKPEEKV VVQEVVVTQK 1380
DPKLREEHSR LSGSLDEEVG RRRQLELEVQ QLRAGVEEQE GLLSFQEDRS KKLAVERELR 1440
QLTLRIQELE KRPPTVQEKI IMEEVVKLEK DPDLEKSTEA LRWDLDQEKT QVTELNRECK 1500
NLQVQIDVLQ KAKSQEKTIY KEVIRVQKDR VLEDERARVW EMLNRERTAR QAREEEARRL 1560
RERIDRAETL GRTWSREESE LQRARDQADQ ECGRLQQELR ALERQKQQQT LQLQEESKLL 1620
SQKTESERQK AAQRGQELSR LEAAILREKD QIYEKERTLR DLHAKVSREE LSQETQTRET 1680
NLSTKISILE PETGKDMSPY EAYKRGIIDR GQYLQLQELE CDWEEVTTSG PCGEESVLLD 1740
RKSGKQYSIE AALRCRRISK EEYHLYKDGH LPISEFALLV AGETKPSSSL SIGSIISKSP 1800
LASPAPQSTS FFSPSFSLGL GDDSFPIAGI YDTTTDNKCS IKTAVAKNML DPITGQKLLE 1860
AQAATGGIVD LLSRERYSVH KAMERGLIEN TSTQRLLNAQ KAFTGIEDPV TKKRLSVGEA 1920
VQKGWMPRES VLPHLQVQHL TGGLIDPKRT GRIPIQQALL SGMISEELAQ LLQDESSYEK 1980
DLTDPISKER LSYKEAMGRC RKDPLSGLLL LPAALEGYRC YRSASPTVPR SLR 2033 
Gene Ontology
 GO:0001533; C:cornified envelope; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
 GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
 GO:0005198; F:structural molecule activity; IDA:UniProtKB.
 GO:0031424; P:keratinization; IEA:UniProtKB-KW.
 GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
 GO:0018149; P:peptide cross-linking; IDA:UniProtKB. 
Interpro
 IPR001101; Plectin_repeat.
 IPR018159; Spectrin/alpha-actinin. 
Pfam
 PF00681; Plectin 
SMART
 SM00250; PLEC
 SM00150; SPEC 
PROSITE
  
PRINTS