Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01204
Entry Name
UniProt Accession
Theoretical PI
5.13
Molecular Weight
122293.92
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Desmoglein-2
Protein Synonyms/Alias
Cadherin family member 5; HDGC;
Gene Name
DSG2
Gene Synonyms/Alias
CDHF5;
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
635
Canonical
VPLLLLMCHCGKGAK
[1]
S-Palmitoylation
637
Canonical
LLLLMCHCGKGAKGF
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Sequence Annotation
Topological domain: 50 609 Extracellular.
Transmembrane: 610 634 Helical.
Topological domain: 635 1118 Cytoplasmic.
Domain: 50 160 Cadherin 1.
Domain: 161 273 Cadherin 2.
Domain: 274 388 Cadherin 3.
Domain: 389 503 Cadherin 4.
Modified residue: 680 680 Phosphoserine.
Modified residue: 703 703 Phosphoserine.
Modified residue: 1118 1118 Phosphoserine.
Protein Length
1118 AA.
Protein Sequence
(Canonical)
MARSPGRAYA LLLLLICFNV GSGLHLQVLS TRNENKLLPK HPHLVRQKRA WITAPVALRE  60
GEDLSKKNPI AKIHSDLAEE RGLKITYKYT GKGITEPPFG IFVFNKDTGE LNVTSILDRE  120
ETPFFLLTGY ALDARGNNVE KPLELRIKVL DINDNEPVFT QDVFVGSVEE LSAAHTLVMK  180
INATDADEPN TLNSKISYRI VSLEPAYPPV FYLNKDTGEI YTTSVTLDRE EHSSYTLTVE  240
ARDGNGEVTD KPVKQAQVQI RILDVNDNIP VVENKVLEGM VEENQVNVEV TRIKVFDADE  300
IGSDNWLANF TFASGNEGGY FHIETDAQTN EGIVTLIKEV DYEEMKNLDF SVIVANKAAF  360
HKSIRSKYKP TPIPIKVKVK NVKEGIHFKS SVISIYVSES MDRSSKGQII GNFQAFDEDT  420
GLPAHARYVK LEDRDNWISV DSVTSEIKLA KLPDFESRYV QNGTYTVKIV AISEDYPRKT  480
ITGTVLINVE DINDNCPTLI EPVQTICHDA EYVNVTAEDL DGHPNSGPFS FSVIDKPPGM  540
AEKWKIARQE STSVLLQQSE KKLGRSEIQF LISDNQGFSC PEKQVLTLTV CECLHGSGCR  600
EAQHDSYVGL GPAAIALMIL AFLLLLLVPL LLLMCHCGKG AKGFTPIPGT IEMLHPWNNE  660
GAPPEDKVVP SFLPVDQGGS LVGRNGVGGM AKEATMKGSS SASIVKGQHE MSEMDGRWEE  720
HRSLLSGRAT QFTGATGAIM TTETTKTARA TGASRDMAGA QAAAVALNEE FLRNYFTDKA  780
ASYTEEDENH TAKDCLLVYS QEETESLNAS IGCCSFIEGE LDDRFLDDLG LKFKTLAEVC  840
LGQKIDINKE IEQRQKPATE TSMNTASHSL CEQTMVNSEN TYSSGSSFPV PKSLQEANAE  900
KVTQEIVTER SVSSRQAQKV ATPLPDPMAS RNVIATETSY VTGSTMPPTT VILGPSQPQS  960
LIVTERVYAP ASTLVDQPYA NEGTVVVTER VIQPHGGGSN PLEGTQHLQD VPYVMVRERE  1020
SFLAPSSGVQ PTLAMPNIAV GQNVTVTERV LAPASTLQSS YQIPTENSMT ARNTTVSGAG  1080
VPGPLPDFGL EESGHSNSTI TTSSTRVTKH STVQHSYS                          1118
FASTA
(Canonical)
>LipidDB-9606-01204|Q14126
MARSPGRAYALLLLLICFNVGSGLHLQVLSTRNENKLLPKHPHLVRQKRAWITAPVALRE
GEDLSKKNPIAKIHSDLAEERGLKITYKYTGKGITEPPFGIFVFNKDTGELNVTSILDRE
ETPFFLLTGYALDARGNNVEKPLELRIKVLDINDNEPVFTQDVFVGSVEELSAAHTLVMK
INATDADEPNTLNSKISYRIVSLEPAYPPVFYLNKDTGEIYTTSVTLDREEHSSYTLTVE
ARDGNGEVTDKPVKQAQVQIRILDVNDNIPVVENKVLEGMVEENQVNVEVTRIKVFDADE
IGSDNWLANFTFASGNEGGYFHIETDAQTNEGIVTLIKEVDYEEMKNLDFSVIVANKAAF
HKSIRSKYKPTPIPIKVKVKNVKEGIHFKSSVISIYVSESMDRSSKGQIIGNFQAFDEDT
GLPAHARYVKLEDRDNWISVDSVTSEIKLAKLPDFESRYVQNGTYTVKIVAISEDYPRKT
ITGTVLINVEDINDNCPTLIEPVQTICHDAEYVNVTAEDLDGHPNSGPFSFSVIDKPPGM
AEKWKIARQESTSVLLQQSEKKLGRSEIQFLISDNQGFSCPEKQVLTLTVCECLHGSGCR
EAQHDSYVGLGPAAIALMILAFLLLLLVPLLLLMCHCGKGAKGFTPIPGTIEMLHPWNNE
GAPPEDKVVPSFLPVDQGGSLVGRNGVGGMAKEATMKGSSSASIVKGQHEMSEMDGRWEE
HRSLLSGRATQFTGATGAIMTTETTKTARATGASRDMAGAQAAAVALNEEFLRNYFTDKA
ASYTEEDENHTAKDCLLVYSQEETESLNASIGCCSFIEGELDDRFLDDLGLKFKTLAEVC
LGQKIDINKEIEQRQKPATETSMNTASHSLCEQTMVNSENTYSSGSSFPVPKSLQEANAE
KVTQEIVTERSVSSRQAQKVATPLPDPMASRNVIATETSYVTGSTMPPTTVILGPSQPQS
LIVTERVYAPASTLVDQPYANEGTVVVTERVIQPHGGGSNPLEGTQHLQDVPYVMVRERE
SFLAPSSGVQPTLAMPNIAVGQNVTVTERVLAPASTLQSSYQIPTENSMTARNTTVSGAG
VPGPLPDFGLEESGHSNSTITTSSTRVTKHSTVQHSYS
Gene Ontology
GO:0016324; C:apical plasma membrane; IEA:Ensembl
GO:0009986; C:cell surface; IDA:UniProtKB
GO:0005911; C:cell-cell junction; TAS:ProtInc
GO:0030057; C:desmosome; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016328; C:lateral plasma membrane; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:UniProt
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0006915; P:apoptotic process; TAS:Reactome
GO:0086069; P:bundle of His cell to Purkinje myocyte communication; IMP:BHF-UCL
GO:0007155; P:cell adhesion; IDA:UniProtKB
GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome
GO:0007156; P:homophilic cell adhesion; IEA:InterPro
GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl
GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL
GO:0032570; P:response to progesterone; IEA:Ensembl
GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL
Interpro
InterPro; IPR002126; Cadherin
InterPro; IPR015919; Cadherin-like
InterPro; IPR020894; Cadherin_CS
InterPro; IPR000233; Cadherin_cytoplasmic-dom
InterPro; IPR027397; Catenin_binding_dom
InterPro; IPR009123; Desmoglein
InterPro; IPR009122; Desmosomal_cadherin
Pfam
Pfam; PF00028; Cadherin;
Pfam; PF01049; Cadherin_C;
SMART
SMART; SM00112; CA;
PROSITE
PROSITE; PS00232; CADHERIN_1;
PROSITE; PS50268; CADHERIN_2;
PRINTS
PRINTS; PR00205; CADHERIN;
PRINTS; PR01818; DESMOCADHERN;
PRINTS; PR01819; DESMOGLEIN;