PCDH7_HUMAN - dbPTM
PCDH7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCDH7_HUMAN
UniProt AC O60245
Protein Name Protocadherin-7
Gene Name PCDH7
Organism Homo sapiens (Human).
Sequence Length 1069
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description
Protein Sequence MLRMRTAGWARGWCLGCCLLLPLSLSLAAAKQLLRYRLAEEGPADVRIGNVASDLGIVTGSGEVTFSLESGSEYLKIDNLTGELSTSERRIDREKLPQCQMIFDENECFLDFEVSVIGPSQSWVDLFEGQVIVLDINDNTPTFPSPVLTLTVEENRPVGTLYLLPTATDRDFGRNGIERYELLQEPGGGGSGGESRRAGAADSAPYPGGGGNGASGGGSGGSKRRLDASEGGGGTNPGGRSSVFELQVADTPDGEKQPQLIVKGALDREQRDSYELTLRVRDGGDPPRSSQAILRVLITDVNDNSPRFEKSVYEADLAENSAPGTPILQLRAADLDVGVNGQIEYVFGAATESVRRLLRLDETSGWLSVLHRIDREEVNQLRFTVMARDRGQPPKTDKATVVLNIKDENDNVPSIEIRKIGRIPLKDGVANVAEDVLVDTPIALVQVSDRDQGENGVVTCTVVGDVPFQLKPASDTEGDQNKKKYFLHTSTPLDYEATREFNVVIVAVDSGSPSLSSNNSLIVKVGDTNDNPPMFGQSVVEVYFPENNIPGERVATVLATDADSGKNAEIAYSLDSSVMGIFAIDPDSGDILVNTVLDREQTDRYEFKVNAKDKGIPVLQGSTTVIVQVADKNDNDPKFMQDVFTFYVKENLQPNSPVGMVTVMDADKGRNAEMSLYIEENNNIFSIENDTGTIYSTMSFDREHQTTYTFRVKAVDGGDPPRSATATVSLFVMDENDNAPTVTLPKNISYTLLPPSSNVRTVVATVLATDSDDGINADLNYSIVGGNPFKLFEIDPTSGVVSLVGKLTQKHYGLHRLVVQVNDSGQPSQSTTTLVHVFVNESVSNATAIDSQIARSLHIPLTQDIAGDPSYEISKQRLSIVIGVVAGIMTVILIILIVVMARYCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTNNKYSKQMRLHPYITVFG
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
79N-linked_GlycosylationSEYLKIDNLTGELST
CCEEEEECCCCCCCC		42.87UniProtKB CARBOHYD
81PhosphorylationYLKIDNLTGELSTSE
EEEEECCCCCCCCCC		34.5616674116
85PhosphorylationDNLTGELSTSERRID
ECCCCCCCCCCHHCC		26.1116674116
180PhosphorylationGRNGIERYELLQEPG
CCCCCEEEEEECCCC		9.7220068231
191PhosphorylationQEPGGGGSGGESRRA
CCCCCCCCCCCCCCC		47.0720068231
195PhosphorylationGGGSGGESRRAGAAD
CCCCCCCCCCCCCCC		30.2720068231
206PhosphorylationGAADSAPYPGGGGNG
CCCCCCCCCCCCCCC		17.7718083107
215PhosphorylationGGGGNGASGGGSGGS
CCCCCCCCCCCCCCC		39.0928857561
219PhosphorylationNGASGGGSGGSKRRL
CCCCCCCCCCCCCCC		43.1628857561
277PhosphorylationQRDSYELTLRVRDGG
HHCEEEEEEEEECCC		10.6923403867
325PhosphorylationAENSAPGTPILQLRA
HCCCCCCCCEEEEEE		13.19-
414PhosphorylationDENDNVPSIEIRKIG
CCCCCCCEEEEEEEC		28.6823322592
512PhosphorylationIVAVDSGSPSLSSNN
EEEECCCCCCCCCCC		18.4421406692
514PhosphorylationAVDSGSPSLSSNNSL
EECCCCCCCCCCCEE		42.45-
556PhosphorylationIPGERVATVLATDAD
CCCCEEEEEEEEECC		17.13-
689N-linked_GlycosylationNNIFSIENDTGTIYS
CEEEEEECCCCCEEE		50.93UniProtKB CARBOHYD
713AcetylationTTYTFRVKAVDGGDP
EEEEEEEEECCCCCC		38.1430591153
747N-linked_GlycosylationPTVTLPKNISYTLLP
CEEECCCCEEEEECC		26.88UniProtKB CARBOHYD
780N-linked_GlycosylationDGINADLNYSIVGGN
CCCCEECCEEEECCC		29.11UniProtKB CARBOHYD
822N-linked_GlycosylationHRLVVQVNDSGQPSQ
EEEEEEECCCCCCCC		22.19UniProtKB CARBOHYD
840N-linked_GlycosylationTLVHVFVNESVSNAT
EEEEEEECCCCCCCH		25.10UniProtKB CARBOHYD
845N-linked_GlycosylationFVNESVSNATAIDSQ
EECCCCCCCHHHCHH		38.87UniProtKB CARBOHYD
879PhosphorylationEISKQRLSIVIGVVA
HHHHHHHHHHHHHHH		19.5922210691
890PhosphorylationGVVAGIMTVILIILI
HHHHHHHHHHHHHHH		11.5022210691
903PhosphorylationLIVVMARYCRSKNKN
HHHHHHHHHHHCCCC		5.2322210691
906PhosphorylationVMARYCRSKNKNGYE
HHHHHHHHCCCCCCC		36.7022210691
909AcetylationRYCRSKNKNGYEAGK
HHHHHCCCCCCCCCC		56.337973143
917AcetylationNGYEAGKKDHEDFFT
CCCCCCCCCHHCCCC		64.507973157
917UbiquitinationNGYEAGKKDHEDFFT
CCCCCCCCCHHCCCC		64.5029967540
924PhosphorylationKDHEDFFTPQQHDKS
CCHHCCCCCCCCCCC		21.8530576142
930UbiquitinationFTPQQHDKSKKPKKD
CCCCCCCCCCCCCCC		63.1529967540
931PhosphorylationTPQQHDKSKKPKKDK
CCCCCCCCCCCCCCC		52.5526055452
943PhosphorylationKDKKNKKSKQPLYSS
CCCCCCCCCCCCEEE		37.8326356563
948PhosphorylationKKSKQPLYSSIVTVE
CCCCCCCEEEEEEEE		13.6825159151
949PhosphorylationKSKQPLYSSIVTVEA
CCCCCCEEEEEEEEE		22.6725106551
950PhosphorylationSKQPLYSSIVTVEAS
CCCCCEEEEEEEEEC		13.9225106551
953PhosphorylationPLYSSIVTVEASKPN
CCEEEEEEEEECCCC		15.8026356563
964PhosphorylationSKPNGQRYDSVNEKL
CCCCCCCCCCCCHHC		12.5127134283
966PhosphorylationPNGQRYDSVNEKLSD
CCCCCCCCCCHHCCC		20.2220639409
970 (in isoform 2)Ubiquitination-48.35-
970UbiquitinationRYDSVNEKLSDSPSM
CCCCCCHHCCCCCCC		48.3523503661
972PhosphorylationDSVNEKLSDSPSMGR
CCCCHHCCCCCCCCC		47.3025159151
974PhosphorylationVNEKLSDSPSMGRYR
CCHHCCCCCCCCCCC		18.5929255136
976PhosphorylationEKLSDSPSMGRYRSV
HHCCCCCCCCCCCCC		37.5126846344
980PhosphorylationDSPSMGRYRSVNGGP
CCCCCCCCCCCCCCC		11.0823403867
982PhosphorylationPSMGRYRSVNGGPGS
CCCCCCCCCCCCCCC		15.8221955146
989PhosphorylationSVNGGPGSPDLARHY
CCCCCCCCHHHHHHH		20.5519664994
997UbiquitinationPDLARHYKSSSPLPT
HHHHHHHCCCCCCCC		37.4229967540
998PhosphorylationDLARHYKSSSPLPTV
HHHHHHCCCCCCCCE		28.9623927012
999PhosphorylationLARHYKSSSPLPTVQ
HHHHHCCCCCCCCEE		31.6523927012
1000PhosphorylationARHYKSSSPLPTVQL
HHHHCCCCCCCCEEE		37.2323927012
1004PhosphorylationKSSSPLPTVQLHPQS
CCCCCCCCEEECCCC		28.6823927012
1011PhosphorylationTVQLHPQSPTAGKKH
CEEECCCCCCCCCCC		28.7730266825
1013PhosphorylationQLHPQSPTAGKKHQA
EECCCCCCCCCCCCC		53.9730266825
1029PhosphorylationQDLPPANTFVGAGDN
CCCCCCCCEECCCCC		23.0829449344
1038PhosphorylationVGAGDNISIGSDHCS
ECCCCCCEECCCCCC		27.4427422710
1041PhosphorylationGDNISIGSDHCSEYS
CCCCEECCCCCCCCC		23.6327422710
1045PhosphorylationSIGSDHCSEYSCQTN
EECCCCCCCCCCCCC		35.8329449344
1047PhosphorylationGSDHCSEYSCQTNNK
CCCCCCCCCCCCCCC		9.8429449344
1048PhosphorylationSDHCSEYSCQTNNKY
CCCCCCCCCCCCCCC		8.8330576142
1051PhosphorylationCSEYSCQTNNKYSKQ
CCCCCCCCCCCCCCE		45.1229449344
1064PhosphorylationKQMRLHPYITVFG--
CEEECCCEEEECC--		9.8528152594
1066PhosphorylationMRLHPYITVFG----
EECCCEEEECC----		12.1628152594
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 PCDH7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCDH7_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 PCDH7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
PSMD5_HUMANPSMD5physical
26496610
R113A_HUMANRNF113Aphysical
26496610
ABCG2_HUMANABCG2physical
26496610
CE350_HUMANCEP350physical
26496610
HNRPQ_HUMANSYNCRIPphysical
26496610
TUT7_HUMANZCCHC6physical
26496610
CYBR1_HUMANCYBRD1physical
26496610
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCDH7_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 SER-974; SER-1000 ANDSER-1011, AND MASS SPECTROMETRY.
"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-982; SER-989; SER-1000AND SER-1011, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000 AND SER-1011, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY.
"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-948, AND MASSSPECTROMETRY.

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