PCDH1_HUMAN - dbPTM
PCDH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCDH1_HUMAN
UniProt AC Q08174
Protein Name Protocadherin-1
Gene Name PCDH1
Organism Homo sapiens (Human).
Sequence Length 1060
Subcellular Localization Cell junction. Cell membrane
Single-pass type I membrane protein . Found at cell-cell boundaries and probably at cell-matrix boundaries.
Protein Description May be involved in cell-cell interaction processes and in cell adhesion..
Protein Sequence MDSGAGGRRCPEAALLILGPPRMEHLRHSPGPGGQRLLLPSMLLALLLLLAPSPGHATRVVYKVPEEQPPNTLIGSLAADYGFPDVGHLYKLEVGAPYLRVDGKTGDIFTTETSIDREGLRECQNQLPGDPCILEFEVSITDLVQNGSPRLLEGQIEVQDINDNTPNFASPVITLAIPENTNIGSLFPIPLASDRDAGPNGVASYELQAGPEAQELFGLQVAEDQEEKQPQLIVMGNLDRERWDSYDLTIKVQDGGSPPRASSALLRVTVLDTNDNAPKFERPSYEAELSENSPIGHSVIQVKANDSDQGANAEIEYTFHQAPEVVRRLLRLDRNTGLITVQGPVDREDLSTLRFSVLAKDRGTNPKSARAQVVVTVKDMNDNAPTIEIRGIGLVTHQDGMANISEDVAEETAVALVQVSDRDEGENAAVTCVVAGDVPFQLRQASETGSDSKKKYFLQTTTPLDYEKVKDYTIEIVAVDSGNPPLSSTNSLKVQVVDVNDNAPVFTQSVTEVAFPENNKPGEVIAEITASDADSGSNAELVYSLEPEPAAKGLFTISPETGEIQVKTSLDREQRESYELKVVAADRGSPSLQGTATVLVNVLDCNDNDPKFMLSGYNFSVMENMPALSPVGMVTVIDGDKGENAQVQLSVEQDNGDFVIQNGTGTILSSLSFDREQQSTYTFQLKAVDGGVPPRSAYVGVTINVLDENDNAPYITAPSNTSHKLLTPQTRLGETVSQVAAEDFDSGVNAELIYSIAGGNPYGLFQIGSHSGAITLEKEIERRHHGLHRLVVKVSDRGKPPRYGTALVHLYVNETLANRTLLETLLGHSLDTPLDIDIAGDPEYERSKQRGNILFGVVAGVVAVALLIALAVLVRYCRQREAKSGYQAGKKETKDLYAPKPSGKASKGNKSKGKKSKSPKPVKPVEDEDEAGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQVGQPFQLSTPQPLPHPYHGAIWTEVWE
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
72PhosphorylationPEEQPPNTLIGSLAA
CCCCCCCCEEHHHHH		26.0622210691
76PhosphorylationPPNTLIGSLAADYGF
CCCCEEHHHHHHHCC		14.0822210691
81PhosphorylationIGSLAADYGFPDVGH
EHHHHHHHCCCCCCE		18.8819690332
90PhosphorylationFPDVGHLYKLEVGAP
CCCCCEEEEEEECCC		14.0919690332
98PhosphorylationKLEVGAPYLRVDGKT
EEEECCCEEEECCCC		13.4522210691
111PhosphorylationKTGDIFTTETSIDRE
CCCCEEEECCCCCHH		26.90-
113PhosphorylationGDIFTTETSIDREGL
CCEEEECCCCCHHHH		28.96-
114PhosphorylationDIFTTETSIDREGLR
CEEEECCCCCHHHHH		19.09-
249PhosphorylationRWDSYDLTIKVQDGG
HCCCCEEEEEEECCC		18.82-
262PhosphorylationGGSPPRASSALLRVT
CCCCCCCCEEEEEEE		19.88-
305N-linked_GlycosylationSVIQVKANDSDQGAN
EEEEEEECCCCCCCC		43.5319159218
403N-linked_GlycosylationTHQDGMANISEDVAE
ECCCCCCCCCHHHHH		29.44UniProtKB CARBOHYD
446PhosphorylationPFQLRQASETGSDSK
CEEEEECHHCCCCCC		27.61-
450PhosphorylationRQASETGSDSKKKYF
EECHHCCCCCCCEEE		46.24-
456PhosphorylationGSDSKKKYFLQTTTP
CCCCCCEEEEEECCC		20.5719702290
531PhosphorylationVIAEITASDADSGSN
EEEEEEECCCCCCCC		25.3623401153
537PhosphorylationASDADSGSNAELVYS
ECCCCCCCCEEEEEE		36.50-
544PhosphorylationSNAELVYSLEPEPAA
CCEEEEEECCCCCCC		20.83-
577PhosphorylationLDREQRESYELKVVA
CCHHHHHHEEEEEEE		26.5430576142
618N-linked_GlycosylationKFMLSGYNFSVMENM
CEEEECCCEEHHHCC		26.66UniProtKB CARBOHYD
662N-linked_GlycosylationNGDFVIQNGTGTILS
CCCEEEECCCEEEEE		38.58UniProtKB CARBOHYD
795PhosphorylationHRLVVKVSDRGKPPR
EEEEEEECCCCCCCC		18.8430576142
813N-linked_GlycosylationALVHLYVNETLANRT
EEEEHHHCHHHHCHH		23.9919159218
818N-linked_GlycosylationYVNETLANRTLLETL
HHCHHHHCHHHHHHH		40.3519159218
886PhosphorylationQREAKSGYQAGKKET
HHHHHCCCCCCCCCC		11.4118083107
891AcetylationSGYQAGKKETKDLYA
CCCCCCCCCCCCCCC		70.477364235
894UbiquitinationQAGKKETKDLYAPKP
CCCCCCCCCCCCCCC		46.9921906983
894 (in isoform 1)Ubiquitination-46.9921906983
894 (in isoform 2)Ubiquitination-46.9921906983
897PhosphorylationKKETKDLYAPKPSGK
CCCCCCCCCCCCCCC		30.8725884760
900UbiquitinationTKDLYAPKPSGKASK
CCCCCCCCCCCCCCC		43.5821906983
900 (in isoform 1)Ubiquitination-43.5821906983
900 (in isoform 2)Ubiquitination-43.5821906983
902PhosphorylationDLYAPKPSGKASKGN
CCCCCCCCCCCCCCC		60.0828152594
906PhosphorylationPKPSGKASKGNKSKG
CCCCCCCCCCCCCCC		44.5829507054
914AcetylationKGNKSKGKKSKSPKP
CCCCCCCCCCCCCCC		58.577369475
915PhosphorylationGNKSKGKKSKSPKPV
CCCCCCCCCCCCCCC		72.3118669648
915 (in isoform 2)Phosphorylation-72.3118669648
916PhosphorylationNKSKGKKSKSPKPVK
CCCCCCCCCCCCCCC		41.6827174698
917AcetylationKSKGKKSKSPKPVKP
CCCCCCCCCCCCCCC		78.607369491
918PhosphorylationSKGKKSKSPKPVKPV
CCCCCCCCCCCCCCC		45.2923403867
920UbiquitinationGKKSKSPKPVKPVED
CCCCCCCCCCCCCCC		70.3221906983
920 (in isoform 1)Ubiquitination-70.3221906983
920 (in isoform 2)Ubiquitination-70.3221906983
923UbiquitinationSKSPKPVKPVEDEDE
CCCCCCCCCCCCCCH		52.4521906983
923 (in isoform 1)Ubiquitination-52.4521906983
923 (in isoform 2)Ubiquitination-52.4521906983
928PhosphorylationPVKPVEDEDEAGLQK
CCCCCCCCCHHHHHH		44.2218669648
928 (in isoform 2)Phosphorylation-44.2218669648
935UbiquitinationEDEAGLQKSLKFNLM
CCHHHHHHHHEEECC		63.9021906983
935 (in isoform 1)Ubiquitination-63.9021906983
935 (in isoform 2)Ubiquitination-63.9021906983
936PhosphorylationDEAGLQKSLKFNLMS
CHHHHHHHHEEECCC		24.6728258704
938AcetylationAGLQKSLKFNLMSDA
HHHHHHHEEECCCCC		39.027363925
938UbiquitinationAGLQKSLKFNLMSDA
HHHHHHHEEECCCCC		39.022190698
938 (in isoform 1)Ubiquitination-39.0221906983
938 (in isoform 2)Ubiquitination-39.0221906983
943PhosphorylationSLKFNLMSDAPGDSP
HHEEECCCCCCCCCC		33.5129255136
949PhosphorylationMSDAPGDSPRIHLPL
CCCCCCCCCCEECCC		23.2229255136
958PhosphorylationRIHLPLNYPPGSPDL
CEECCCCCCCCCCCC		20.6330266825
962PhosphorylationPLNYPPGSPDLGRHY
CCCCCCCCCCCCCCC		22.4830266825
969PhosphorylationSPDLGRHYRSNSPLP
CCCCCCCCCCCCCCC		17.8627259358
971PhosphorylationDLGRHYRSNSPLPSI
CCCCCCCCCCCCCCC		34.2028355574
973PhosphorylationGRHYRSNSPLPSIQL
CCCCCCCCCCCCCCC		29.1228355574
977PhosphorylationRSNSPLPSIQLQPQS
CCCCCCCCCCCCCCC		30.5630278072
984PhosphorylationSIQLQPQSPSASKKH
CCCCCCCCCCCCCCC		27.7523927012
986PhosphorylationQLQPQSPSASKKHQV
CCCCCCCCCCCCCEE		50.8830278072
988PhosphorylationQPQSPSASKKHQVVQ
CCCCCCCCCCCEEEC		46.7230278072
1014PhosphorylationGDTTSTGSEQYSDYS
CCCCCCCCHHCCCCC		22.93-
1017PhosphorylationTSTGSEQYSDYSYRT
CCCCCHHCCCCCCCC		10.2320736484
1018PhosphorylationSTGSEQYSDYSYRTN
CCCCHHCCCCCCCCC		29.7527259358
1020PhosphorylationGSEQYSDYSYRTNPP
CCHHCCCCCCCCCCC		11.1420736484
1021PhosphorylationSEQYSDYSYRTNPPK
CHHCCCCCCCCCCCC		17.0924719451
1022PhosphorylationEQYSDYSYRTNPPKY
HHCCCCCCCCCCCCC		18.4115592455
1029PhosphorylationYRTNPPKYPSKQVGQ
CCCCCCCCCCCCCCC		20.65-
1031PhosphorylationTNPPKYPSKQVGQPF
CCCCCCCCCCCCCCE		32.4128348404
1040 (in isoform 2)Phosphorylation-6.6928348404
1041PhosphorylationVGQPFQLSTPQPLPH
CCCCEECCCCCCCCC		27.5324719451
1042PhosphorylationGQPFQLSTPQPLPHP
CCCEECCCCCCCCCC		34.2428348404
1042 (in isoform 2)Phosphorylation-34.2428348404
1044 (in isoform 2)Phosphorylation-52.8528348404
1045 (in isoform 2)Phosphorylation-49.4128348404
1050PhosphorylationPQPLPHPYHGAIWTE
CCCCCCCCCCCCEEE		15.17-
1056PhosphorylationPYHGAIWTEVWE---
CCCCCCEEECCC---		17.9728348404
1057 (in isoform 2)Phosphorylation-30.5425884760
1058 (in isoform 2)Phosphorylation-5.6425884760
1059 (in isoform 2)Phosphorylation-10.19-
1061 (in isoform 2)Phosphorylation--
1068 (in isoform 2)Phosphorylation--
1089 (in isoform 2)Phosphorylation-25884760
1092 (in isoform 2)Phosphorylation-24719451
1093 (in isoform 2)Phosphorylation-28348404
1097 (in isoform 2)Phosphorylation-26657352
1130 (in isoform 2)Phosphorylation-23927012
1132 (in isoform 2)Phosphorylation-26657352
1139 (in isoform 2)Phosphorylation-25849741
1140 (in isoform 2)Phosphorylation-26657352
1142 (in isoform 2)Phosphorylation-25850435
1158 (in isoform 2)Phosphorylation-25884760
1171 (in isoform 2)Phosphorylation-23927012
1173 (in isoform 2)Phosphorylation-19664994
1180 (in isoform 2)Phosphorylation-28102081
1191 (in isoform 2)Phosphorylation-27259358
1192 (in isoform 2)Phosphorylation-25884760
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 PCDH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCDH1_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 PCDH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABCA2_HUMANABCA2physical
26496610
ACBP_HUMANDBIphysical
26496610
SSFA2_HUMANSSFA2physical
26496610
TF3C3_HUMANGTF3C3physical
26496610
TRIB1_HUMANTRIB1physical
26496610
ZNFX1_HUMANZNFX1physical
26496610
C19L2_HUMANCWF19L2physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCDH1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-813 AND ASN-818,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-962, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1017 AND TYR-1022, ANDMASS SPECTROMETRY.

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