PCD19_HUMAN - dbPTM
PCD19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCD19_HUMAN
UniProt AC Q8TAB3
Protein Name Protocadherin-19
Gene Name PCDH19
Organism Homo sapiens (Human).
Sequence Length 1148
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Potential calcium-dependent cell-adhesion protein..
Protein Sequence MESLLLPVLLLLAILWTQAAALINLKYSVEEEQRAGTVIANVAKDAREAGFALDPRQASAFRVVSNSAPHLVDINPSSGLLVTKQKIDRDLLCRQSPKCIISLEVMSSSMEICVIKVEIKDLNDNAPSFPAAQIELEISEAASPGTRIPLDSAYDPDSGSFGVQTYELTPNELFGLEIKTRGDGSRFAELVVEKSLDRETQSHYSFRITALDGGDPPRLGTVGLSIKVTDSNDNNPVFSESTYAVSVPENSPPNTPVIRLNASDPDEGTNGQVVYSFYGYVNDRTRELFQIDPHSGLVTVTGALDYEEGHVYELDVQAKDLGPNSIPAHCKVTVSVLDTNDNPPVINLLSVNSELVEVSESAPPGYVIALVRVSDRDSGLNGRVQCRLLGNVPFRLQEYESFSTILVDGRLDREQHDQYNLTIQARDGGVPMLQSAKSFTVLITDENDNHPHFSKPYYQVIVQENNTPGAYLLSVSARDPDLGLNGSVSYQIVPSQVRDMPVFTYVSINPNSGDIYALRSFNHEQTKAFEFKVLAKDGGLPSLQSNATVRVIILDVNDNTPVITAPPLINGTAEVYIPRNSGIGYLVTVVKAEDYDEGENGRVTYDMTEGDRGFFEIDQVNGEVRTTRTFGESSKSSYELIVVAHDHGKTSLSASALVLIYLSPALDAQESMGSVNLSLIFIIALGSIAGILFVTMIFVAIKCKRDNKEIRTYNCSNCLTITCLLGCFIKGQNSKCLHCISVSPISEEQDKKTEEKVSLRGKRIAEYSYGHQKKSSKKKKISKNDIRLVPRDVEETDKMNVVSCSSLTSSLNYFDYHQQTLPLGCRRSESTFLNVENQNTRNTSANHIYHHSFNSQGPQQPDLIINGVPLPETENYSFDSNYVNSRAHLIKSSSTFKDLEGNSLKDSGHEESDQTDSEHDVQRSLYCDTAVNDVLNTSVTSMGSQMPDHDQNEGFHCREECRILGHSDRCWMPRNPMPIRSKSPEHVRNIIALSIEATAADVEAYDDCGPTKRTFATFGKDVSDHPAEERPTLKGKRTVDVTICSPKVNSVIREAGNGCEAISPVTSPLHLKSSLPTKPSVSYTIALAPPARDLEQYVNNVNNGPTRPSEAEPRGADSEKVMHEVSPILKEGRNKESPGVKRLKDIVL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
27PhosphorylationAALINLKYSVEEEQR
HHHHHCCCCHHHHHH		22.55-
37PhosphorylationEEEQRAGTVIANVAK
HHHHHHCEEEEHHHH		14.0419413330
261N-linked_GlycosylationNTPVIRLNASDPDEG
CCCEEECCCCCCCCC		27.78UniProtKB CARBOHYD
420N-linked_GlycosylationREQHDQYNLTIQARD
HHHHHCEEEEEEECC		25.69UniProtKB CARBOHYD
485N-linked_GlycosylationRDPDLGLNGSVSYQI
CCCCCCCCCCEEEEE		38.61UniProtKB CARBOHYD
542PhosphorylationAKDGGLPSLQSNATV
EECCCCCCCCCCCEE		44.0523909892
545PhosphorylationGGLPSLQSNATVRVI
CCCCCCCCCCEEEEE		33.4523909892
546N-linked_GlycosylationGLPSLQSNATVRVII
CCCCCCCCCEEEEEE		27.03UniProtKB CARBOHYD
548PhosphorylationPSLQSNATVRVIILD
CCCCCCCEEEEEEEE		17.0723909892
570N-linked_GlycosylationITAPPLINGTAEVYI
EECCCCCCCEEEEEE		49.82UniProtKB CARBOHYD
604PhosphorylationEGENGRVTYDMTEGD
CCCCCEEEEECCCCC		16.6726503514
605PhosphorylationGENGRVTYDMTEGDR
CCCCEEEEECCCCCC		10.8126503514
608PhosphorylationGRVTYDMTEGDRGFF
CEEEEECCCCCCCEE		33.6426503514
676N-linked_GlycosylationQESMGSVNLSLIFII
HHHCCCCCHHHHHHH		26.13UniProtKB CARBOHYD
752AcetylationISEEQDKKTEEKVSL
CCHHHHCCHHHCHHH		70.2524471213
782PhosphorylationSSKKKKISKNDIRLV
CCCCCCCCHHHCEEC		34.0024719451
805PhosphorylationKMNVVSCSSLTSSLN
CCCEEEHHHCCCCCC		22.3728348404
806PhosphorylationMNVVSCSSLTSSLNY
CCEEEHHHCCCCCCC		39.7428348404
808PhosphorylationVVSCSSLTSSLNYFD
EEEHHHCCCCCCCCC		20.4428348404
809PhosphorylationVSCSSLTSSLNYFDY
EEHHHCCCCCCCCCC		37.8128348404
828PhosphorylationLPLGCRRSESTFLNV
CCCCCCCCCCEEEEE		19.2929449344
830PhosphorylationLGCRRSESTFLNVEN
CCCCCCCCEEEEEEC		26.2127470641
831PhosphorylationGCRRSESTFLNVENQ
CCCCCCCEEEEEECC		28.2626471730
903PhosphorylationFKDLEGNSLKDSGHE
CCCCCCCCCCCCCCC		47.8828348404
907PhosphorylationEGNSLKDSGHEESDQ
CCCCCCCCCCCCCCC		40.2324719451
912PhosphorylationKDSGHEESDQTDSEH
CCCCCCCCCCCCCHH		31.8424719451
915PhosphorylationGHEESDQTDSEHDVQ
CCCCCCCCCCHHHHH		46.6229449344
917PhosphorylationEESDQTDSEHDVQRS
CCCCCCCCHHHHHHH		39.9729449344
937PhosphorylationAVNDVLNTSVTSMGS
HHHHHHCCCCCCCCC		22.0328348404
938PhosphorylationVNDVLNTSVTSMGSQ
HHHHHCCCCCCCCCC		23.4828348404
940PhosphorylationDVLNTSVTSMGSQMP
HHHCCCCCCCCCCCC		16.8628348404
941PhosphorylationVLNTSVTSMGSQMPD
HHCCCCCCCCCCCCC		20.9928348404
944PhosphorylationTSVTSMGSQMPDHDQ
CCCCCCCCCCCCCCC		18.0528348404
967PhosphorylationECRILGHSDRCWMPR
HHHCCCCCCCCCCCC		25.5929449344
981PhosphorylationRNPMPIRSKSPEHVR
CCCCCCCCCCHHHHH		37.9024719451
983PhosphorylationPMPIRSKSPEHVRNI
CCCCCCCCHHHHHHH		36.4528348404
1042PhosphorylationGKRTVDVTICSPKVN
CCCEEEEEEECHHHH		16.2929449344
1045PhosphorylationTVDVTICSPKVNSVI
EEEEEEECHHHHHHH		24.7322617229
1063PhosphorylationGNGCEAISPVTSPLH
CCCCCEECCCCCCCE		21.9923312004
1066PhosphorylationCEAISPVTSPLHLKS
CCEECCCCCCCEECC		28.1924719451
1067PhosphorylationEAISPVTSPLHLKSS
CEECCCCCCCEECCC		26.2121712546
1097PhosphorylationPARDLEQYVNNVNNG
CCCCHHHHHHHCCCC		8.8625884760
1126PhosphorylationEKVMHEVSPILKEGR
HHHHHHHHHHHHCCC		11.8422617229
1137PhosphorylationKEGRNKESPGVKRLK
HCCCCCCCCCCCCHH		28.6727470641
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PCD19_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCD19_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PCD19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PCD19_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00577 Syndromic X-linked mental retardation with epilepsy or seizures, including: West syndrome (WS); Part
H00606 Early infantile epileptic encephalopathy; Ohtahara syndrome
OMIM Disease
300088Epileptic encephalopathy, early infantile, 9 (EIEE9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCD19_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37, AND MASSSPECTROMETRY.

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