Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01242
Entry Name
UniProt Accession
Theoretical PI
9.39
Molecular Weight
97414.85
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Plakophilin-2
Protein Synonyms/Alias
Gene Name
PKP2
Gene Synonyms/Alias
Created Date
23-JAN-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
603
Isoform 2
DNNKSIGCFGSRSRK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Roberts BJ, Johnson KE, McGuinn KP, Saowapa J, Svoboda RA, Mahoney MG, JohnsonKR, Wahl JK 3rd. Palmitoylation of plakophilin is required for desmosomeassembly. J Cell Sci. 2014 Sep 1;127(Pt 17):3782-93. doi: 10.1242/jcs.149849.Epub 2014 Jul 7.[PMID:25002405]
Functional Description
May play a role in junctional plaques.
Sequence Annotation
Modified residue: 44 44 Phosphoserine.
Modified residue: 132 132 Phosphoserine.
Modified residue: 151 151 Phosphoserine.
Modified residue: 154 154 Phosphoserine.
Modified residue: 155 155 Phosphoserine.
Modified residue: 169 169 Phosphoserine.
Modified residue: 197 197 Phosphoserine.
Modified residue: 251 251 Phosphoserine.
Modified residue: 329 329 Phosphoserine.
Protein Length
881 AA.
Protein Sequence
(Isoform 2)
MAAPGAPAEY GYIRTVLGQQ ILGQLDSSSL ALPSEAKLKL AGSSGRGGQT VKSLRIQEQV  60
QQTLARKGRS SVGNGNLHRT SSVPEYVYNL HLVENDFVGG RSPVPKTYDM LKAGTTATYE  120
GRWGRGTAQY SSQKSVEERS LRHPLRRLEI SPDSSPERAH YTHSDYQYSQ RSQAGHTLHH  180
QESRRAALLV PPRYARSEIV GVSRAGTTSR QRHFDTYHRQ YQHGSVSDTV FDSIPANPAL  240
LTYPRPGTSR SMGNLLEKEN YLTAGLTVGQ VRPLVPLQPV TQNRASRSSW HQSSFHSTRT  300
LREAGPSVAV DSSGRRAHLT VGQAAAGGSG NLLTERSTFT DSQLGNADME MTLERAVSML  360
EADHMLPSRI SAAATFIQHE CFQKSEARKR VNQLRGILKL LQLLKVQNED VQRAVCGALR  420
NLVFEDNDNK LEVAELNGVP RLLQVLKQTR DLETKKQITG LLWNLSSNDK LKNLMITEAL  480
LTLTENIIIP FSGWPEGDYP KANGLLDFDI FYNVTGCLRN MSSAGADGRK AMRRCDGLID  540
SLVHYVRGTI ADYQPDDKAT ENCVCILHNL SYQLEAELPE KYSQNIYIQN RNIQTDNNKS  600
IGCFGSRSRK VKEQYQDVPM PEEKSNPKGV EWLWHSIVIR MYLSLIAKSV RNYTQEASLG  660
ALQNLTAGSG PMPTSVAQTV VQKESGLQHT RKMLHVGDPS VKKTAISLLR NLSRNLSLQN  720
EIAKETLPDL VSIIPDTVPS TDLLIETTAS ACYTLNNIIQ NSYQNARDLL NTGGIQKIMA  780
ISAGDAYASN KASKAASVLL YSLWAHTELH HAYKKAQFKK TDFVNSRTAK AYHSLKD     837
FASTA
(Isoform 2)
>LipidDB-9606-01242|Q99959-2
MAAPGAPAEYGYIRTVLGQQILGQLDSSSLALPSEAKLKLAGSSGRGGQTVKSLRIQEQV
QQTLARKGRSSVGNGNLHRTSSVPEYVYNLHLVENDFVGGRSPVPKTYDMLKAGTTATYE
GRWGRGTAQYSSQKSVEERSLRHPLRRLEISPDSSPERAHYTHSDYQYSQRSQAGHTLHH
QESRRAALLVPPRYARSEIVGVSRAGTTSRQRHFDTYHRQYQHGSVSDTVFDSIPANPAL
LTYPRPGTSRSMGNLLEKENYLTAGLTVGQVRPLVPLQPVTQNRASRSSWHQSSFHSTRT
LREAGPSVAVDSSGRRAHLTVGQAAAGGSGNLLTERSTFTDSQLGNADMEMTLERAVSML
EADHMLPSRISAAATFIQHECFQKSEARKRVNQLRGILKLLQLLKVQNEDVQRAVCGALR
NLVFEDNDNKLEVAELNGVPRLLQVLKQTRDLETKKQITGLLWNLSSNDKLKNLMITEAL
LTLTENIIIPFSGWPEGDYPKANGLLDFDIFYNVTGCLRNMSSAGADGRKAMRRCDGLID
SLVHYVRGTIADYQPDDKATENCVCILHNLSYQLEAELPEKYSQNIYIQNRNIQTDNNKS
IGCFGSRSRKVKEQYQDVPMPEEKSNPKGVEWLWHSIVIRMYLSLIAKSVRNYTQEASLG
ALQNLTAGSGPMPTSVAQTVVQKESGLQHTRKMLHVGDPSVKKTAISLLRNLSRNLSLQN
EIAKETLPDLVSIIPDTVPSTDLLIETTASACYTLNNIIQNSYQNARDLLNTGGIQKIMA
ISAGDAYASNKASKAASVLLYSLWAHTELHHAYKKAQFKKTDFVNSRTAKAYHSLKD
Gene Ontology
GO:0005912; C:adherens junction; ISS:BHF-UCL
GO:0030054; C:cell junction; IDA:HPA
GO:0005911; C:cell-cell junction; ISS:BHF-UCL
GO:0030057; C:desmosome; NAS:UniProtKB
GO:0016021; C:integral component of membrane; TAS:ProtInc
GO:0014704; C:intercalated disc; ISS:BHF-UCL
GO:0005882; C:intermediate filament; ISS:BHF-UCL
GO:0005634; C:nucleus; NAS:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProt
GO:0019215; F:intermediate filament binding; IDA:BHF-UCL
GO:0044325; F:ion channel binding; ISS:BHF-UCL
GO:0032947; F:protein complex scaffold; IMP:BHF-UCL
GO:0005080; F:protein kinase C binding; IPI:BHF-UCL
GO:0017080; F:sodium channel regulator activity; ISS:BHF-UCL
GO:0034334; P:adherens junction maintenance; ISS:BHF-UCL
GO:0086069; P:bundle of His cell to Purkinje myocyte communication; IMP:BHF-UCL
GO:0086001; P:cardiac muscle cell action potential; ISS:BHF-UCL
GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL
GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; ISS:BHF-UCL
GO:0086019; P:cell-cell signaling involved in cardiac conduction; IMP:BHF-UCL
GO:0002159; P:desmosome assembly; IMP:BHF-UCL
GO:0016264; P:gap junction assembly; ISS:BHF-UCL
GO:0007507; P:heart development; ISS:BHF-UCL
GO:0045110; P:intermediate filament bundle assembly; IMP:BHF-UCL
GO:0055088; P:lipid homeostasis; ISS:BHF-UCL
GO:0048496; P:maintenance of organ identity; IMP:BHF-UCL
GO:0030336; P:negative regulation of cell migration; ISS:BHF-UCL
GO:0008285; P:negative regulation of cell proliferation; ISS:BHF-UCL
GO:0010765; P:positive regulation of sodium ion transport; ISS:BHF-UCL
GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL
GO:2000810; P:regulation of tight junction assembly; ISS:BHF-UCL
GO:0016337; P:single organismal cell-cell adhesion; NAS:UniProtKB
GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL
GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL
Interpro
InterPro; IPR011989; ARM-like
InterPro; IPR016024; ARM-type_fold
InterPro; IPR000225; Armadillo
InterPro; IPR028435; Plakophilin/d_Catenin
Pfam
Pfam; PF00514; Arm;
SMART
SMART; SM00185; ARM;
PROSITE
PROSITE; PS50176; ARM_REPEAT;
PRINTS