PCD16_HUMAN - dbPTM
PCD16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCD16_HUMAN
UniProt AC Q96JQ0
Protein Name Protocadherin-16
Gene Name DCHS1
Organism Homo sapiens (Human).
Sequence Length 3298
Subcellular Localization Cell membrane
Single-pass type I membrane protein. In the embryonic cortex, FAT4 and DCHS1 accumulated at the cell-cell boundaries located apical to the adherens junction..
Protein Description Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation. In the heart, has a critical role for proper morphogenesis of the mitral valve, acting in the regulation of cell migration involved in valve formation. [PubMed: 26258302]
Protein Sequence MQKELGIVPSCPGMKSPRPHLLLPLLLLLLLLLGAGVPGAWGQAGSLDLQIDEEQPAGTLIGDISAGLPAGTAAPLMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDREQRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQVPEHTAFGTRYPLEPARDADAGRLGTQGYALSGDGAGETFRLETRPGPDGTPVPELVVTGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGVNGAVTYEINRRQSEGDGPFSIDAHTGLLQLERPLDFEQRRVHELVVQARDGGAHPELGSAFVTVHVRDANDNQPSMTVIFLSADGSPQVSEAAPPGQLVARISVSDPDDGDFAHVNVSLEGGEGHFALSTQDSVIYLVCVARRLDREERDAYNLRVTATDSGSPPLRAEAAFVLHVTDVNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGAHTHWFSIDPTSGIITTAASLDYELEPQPQLIVVATDGGLPPLASSATVSVALQDVNDNEPQFQRTFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGSSGSPPFRIDAHSGDVCTTRTLDRDQGPSSFDFTVTAVDGGGLKSMVYVKVFLSDENDNPPQFYPREYAASISAQSPPGTAVLRLRAHDPDQGSHGRLSYHILAGNSPPLFTLDEQSGLLTVAWPLARRANSVVQLEIGAEDGGGLQAEPSARVDISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGIVQAHNPPGRLAPVTLSLSGGDPRGLFSLDAVSGLLQTLRPLDRELLGPVLELEVRAGSGVPPAFAVARVRVLLDDVNDNSPAFPAPEDTVLLPPNTAPGTPIYTLRALDPDSGVNSRVTFTLLAGGGGAFTVDPTTGHVRLMRPLGPSGGPAHELELEARDGGSPPRTSHFRLRVVVQDVGTRGLAPRFNSPTYRVDLPSGTTAGTQVLQVQAQAPDGGPITYHLAAEGASSPFGLEPQSGWLWVRAALDREAQELYILKVMAVSGSKAELGQQTGTATVRVSILNQNEHSPRLSEDPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQTGEVTTLQTLDREQQSSYQLLVQVQDGGSPPRSTTGTVHVAVLDLNDNSPTFLQASGAAGGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHSGELLTAAPLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSARLAEPPPDLAERDPAAPVPVVLTVTAAEGLRPGSLLGSVAAPEPAGVGALTYTLVGGADPEGTFALDAASGRLYLARPLDFEAGPPWRALTVRAEGPGGAGARLLRVQVQVQDENEHAPAFARDPLALALPENPEPGAALYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPALLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALHVVARDPDLGEAARVSYRLASGGDGHFRLHSSTGALSVVRPLDREQRAEHVLTVVASDHGSPPRSATQVLTVSVADVNDEAPTFQQQEYSVLLRENNPPGTSLLTLRATDPDVGANGQVTYGGVSSESFSLDPDTGVLTTLRALDREEQEEINLTVYAQDRGSPPQLTHVTVRVAVEDENDHAPTFGSAHLSLEVPEGQDPQTLTMLRASDPDVGANGQLQYRILDGDPSGAFVLDLASGEFGTMRPLDREVEPAFQLRIEARDGGQPALSATLLLTVTVLDANDHAPAFPVPAYSVEVPEDVPAGTLLLQLQAHDPDAGANGHVTYYLGAGTAGAFLLEPSSGELRTAAALDREQCPSYTFSVSAVDGAAAGPLSTTVSVTITVRDVNDHAPTFPTSPLRLRLPRPGPSFSTPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALGPRDRVLFIVATDLGRPARSATGVIIVGLQGEAERGPRFPRASSEATIRENAPPGTPIVSPRAVHAGGTNGPITYSILSGNEKGTFSIQPSTGAITVRSAEGLDFEVSPRLRLVLQAESGGAFAFTVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEADDLDQGSGGQISYSLAASQPARGLFHVDPTTGTITTTAILDREIWAETRLVLMATDRGSPALVGSATLTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQDPFSVGRYGGRVSLTGPLDFEQCDRYQLQLLAHDGPHEGRANLTVLVEDVNDNAPAFSQSLYQVMLLEHTPPGSAILSVSATDRDSGANGHISYHLASPADGFSVDPNNGTLFTIVGTVALGHDGSGAVDVVLEARDHGAPGRAARATVHVQLQDQNDHAPSFTLSHYRVAVTEDLPPGSTLLTLEATDADGSRSHAAVDYSIISGNWGRVFQLEPRLAEAGESAGPGPRALGCLVLLEPLDFESLTQYNLTVAAADRGQPPQSSVVPVTVTVLDVNDNPPVFTRASYRVTVPEDTPVGAELLHVEASDADPGPHGLVRFTVSSGDPSGLFELDESSGTLRLAHALDCETQARHQLVVQAADPAGAHFALAPVTIEVQDVNDHGPAFPLNLLSTSVAENQPPGTLVTTLHAIDGDAGAFGRLRYSLLEAGPGPEGREAFALNSSTGELRARVPFDYEHTESFRLLVGAADAGNLSASVTVSVLVTGEDEYDPVFLAPAFHFQVPEGARRGHSLGHVQATDEDGGADGLVLYSLATSSPYFGINQTTGALYLRVDSRAPGSGTATSGGGGRTRREAPRELRLEVIARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVLGLVRARSRKAEAAPGPMSQAAPLASDSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAGGPYPRGGSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDADGLSDTSCEPPAPDTWYKGRKAGLLLPGAGATLYREEGPPATATAFLGGCGLSPAPTGDYGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAHPGAKSVPPKPANTAAARAIFPPASHRSPISHEGSLSSAAMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSAESGLEPPDDTELHI
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
156PhosphorylationALQVPEHTAFGTRYP
HHCCCCCCCCCCCCC
23.2430108239
160PhosphorylationPEHTAFGTRYPLEPA
CCCCCCCCCCCCCCC
22.1530108239
162PhosphorylationHTAFGTRYPLEPARD
CCCCCCCCCCCCCCC
16.4130108239
217N-linked_GlycosylationTGELDRENRSHYMLQ
ECCCCCCCCCEEEEE
52.20UniProtKB CARBOHYD
256N-linked_GlycosylationNDHAPAFNQSRYHAV
CCCCCCCCCCCCEEE
40.81UniProtKB CARBOHYD
402N-linked_GlycosylationDGDFAHVNVSLEGGE
CCCEEEEEEEEECCC
14.06UniProtKB CARBOHYD
438PhosphorylationDREERDAYNLRVTAT
CHHHHHHCCCEEEEC
21.0122817900
584N-linked_GlycosylationQFQRTFYNASLPEGT
CHHHEEEECCCCCCC
20.89UniProtKB CARBOHYD
591O-linked_GlycosylationNASLPEGTQPGTCFL
ECCCCCCCCCCCEEE
29.90OGP
915PhosphorylationAPGTPIYTLRALDPD
CCCCCEEEEEECCCC
15.5324719451
942PhosphorylationAGGGGAFTVDPTTGH
ECCCCCEEECCCCCC
24.38-
946PhosphorylationGAFTVDPTTGHVRLM
CCEEECCCCCCEEEE
40.73-
947PhosphorylationAFTVDPTTGHVRLMR
CEEECCCCCCEEEEE
30.58-
1002PhosphorylationGLAPRFNSPTYRVDL
CCCCCCCCCEEEEEC
18.8623403867
1004PhosphorylationAPRFNSPTYRVDLPS
CCCCCCCEEEEECCC
24.6323403867
1005PhosphorylationPRFNSPTYRVDLPSG
CCCCCCEEEEECCCC
16.4223403867
1076PhosphorylationILKVMAVSGSKAELG
EEEEEEECCCHHHHC
28.01-
1078PhosphorylationKVMAVSGSKAELGQQ
EEEEECCCHHHHCCC
22.61-
1168PhosphorylationGEVTTLQTLDREQQS
CCEEEEEECCHHHHC
33.47-
1196PhosphorylationPPRSTTGTVHVAVLD
CCCCCCCEEEEEEEE
12.83-
1208PhosphorylationVLDLNDNSPTFLQAS
EEECCCCCCCCCEEC
28.34-
1210PhosphorylationDLNDNSPTFLQASGA
ECCCCCCCCCEECCC
36.48-
1234PhosphorylationPDRVPPGTLVTTLQA
CCCCCCCCEEEEEEE
24.67-
1237PhosphorylationVPPGTLVTTLQAKDP
CCCCCEEEEEEECCC
25.54-
1238PhosphorylationPPGTLVTTLQAKDPD
CCCCEEEEEEECCCC
14.92-
1249N-linked_GlycosylationKDPDEGENGTILYTL
CCCCCCCCCEEEEEE
64.86UniProtKB CARBOHYD
1290PhosphorylationERPHYVLTLSAHDQG
CCCCEEEEEEECCCC
14.5030206219
1292PhosphorylationPHYVLTLSAHDQGSP
CCEEEEEEECCCCCC
20.5130206219
1298PhosphorylationLSAHDQGSPPRSASL
EEECCCCCCCCCHHH
26.5430206219
1496PhosphorylationDARTGALSAPRGLDR
ECCCCCCCCCCCCCC
35.3824719451
1521N-linked_GlycosylationEATDRPANASRRRAA
HHCCCCCCHHHHHHH
40.92UniProtKB CARBOHYD
1581PhosphorylationLGEAARVSYRLASGG
HHHHHHEEEEECCCC
10.0523828894
1582PhosphorylationGEAARVSYRLASGGD
HHHHHEEEEECCCCC
13.54-
1586PhosphorylationRVSYRLASGGDGHFR
HEEEEECCCCCCCEE
48.15-
1593MethylationSGGDGHFRLHSSTGA
CCCCCCEEEECCCCC
26.30-
1718N-linked_GlycosylationREEQEEINLTVYAQD
HHHHHCCCEEEEECC
32.70UniProtKB CARBOHYD
1959PhosphorylationDVNDHAPTFPTSPLR
ECCCCCCCCCCCCCE
42.9329083192
1962PhosphorylationDHAPTFPTSPLRLRL
CCCCCCCCCCCEECC
38.4929083192
1963PhosphorylationHAPTFPTSPLRLRLP
CCCCCCCCCCEECCC
23.3629083192
1996N-linked_GlycosylationEDRDAGANASILYRL
HHCCCCCCCEEEHHH
33.05UniProtKB CARBOHYD
1998PhosphorylationRDAGANASILYRLAG
CCCCCCCEEEHHHHC
16.9724905233
2001PhosphorylationGANASILYRLAGTPP
CCCCEEEHHHHCCCC
11.2524905233
2006PhosphorylationILYRLAGTPPPGTTV
EEHHHHCCCCCCCCC
27.3224905233
2011PhosphorylationAGTPPPGTTVDSYTG
HCCCCCCCCCCCCCC
29.4424905233
2012PhosphorylationGTPPPGTTVDSYTGE
CCCCCCCCCCCCCCE
28.3824905233
2015PhosphorylationPPGTTVDSYTGEIRV
CCCCCCCCCCCEEEE
21.9124905233
2016PhosphorylationPGTTVDSYTGEIRVA
CCCCCCCCCCEEEEE
17.8224905233
2017PhosphorylationGTTVDSYTGEIRVAR
CCCCCCCCCEEEEEC
32.0824905233
2049PhosphorylationDLGRPARSATGVIIV
CCCCCCCCCCEEEEE
32.0824719451
2361N-linked_GlycosylationGPHEGRANLTVLVED
CCCCCCCEEEEEEEE
34.58UniProtKB CARBOHYD
2363PhosphorylationHEGRANLTVLVEDVN
CCCCCEEEEEEEECC
16.1724043423
2377PhosphorylationNDNAPAFSQSLYQVM
CCCCHHHHHHHHHHH
22.4424043423
2379PhosphorylationNAPAFSQSLYQVMLL
CCHHHHHHHHHHHCC
28.0424043423
2381PhosphorylationPAFSQSLYQVMLLEH
HHHHHHHHHHHCCCC
12.3324043423
2389PhosphorylationQVMLLEHTPPGSAIL
HHHCCCCCCCCCEEE
23.0824043423
2393PhosphorylationLEHTPPGSAILSVSA
CCCCCCCCEEEEEEE
20.2224043423
2397PhosphorylationPPGSAILSVSATDRD
CCCCEEEEEEEECCC
14.1224043423
2399PhosphorylationGSAILSVSATDRDSG
CCEEEEEEEECCCCC
23.2924043423
2401PhosphorylationAILSVSATDRDSGAN
EEEEEEEECCCCCCC
24.8624043423
2428N-linked_GlycosylationGFSVDPNNGTLFTIV
CCEECCCCCCEEEEE
50.65UniProtKB CARBOHYD
2512PhosphorylationEATDADGSRSHAAVD
EEECCCCCCCCEEEE
31.0223403867
2514PhosphorylationTDADGSRSHAAVDYS
ECCCCCCCCEEEEEE
21.1223403867
2521PhosphorylationSHAAVDYSIISGNWG
CCEEEEEEEECCCCC
14.6923403867
2524PhosphorylationAVDYSIISGNWGRVF
EEEEEEECCCCCEEE
25.1423403867
2569N-linked_GlycosylationFESLTQYNLTVAAAD
HHHHHCCEEEEEEHH
21.30UniProtKB CARBOHYD
2761N-linked_GlycosylationGREAFALNSSTGELR
HHEEEEECCCCCCEE
30.41UniProtKB CARBOHYD
2792N-linked_GlycosylationVGAADAGNLSASVTV
EEHHCCCCCCEEEEE
32.32UniProtKB CARBOHYD
2862N-linked_GlycosylationSSPYFGINQTTGALY
CCCCCCCCCCCCEEE
33.26UniProtKB CARBOHYD
2967UbiquitinationLVRARSRKAEAAPGP
HHHHHHCCCCCCCCC
52.4032142685
2976PhosphorylationEAAPGPMSQAAPLAS
CCCCCCHHHHHHHCC
21.5722210691
2983PhosphorylationSQAAPLASDSLQKLG
HHHHHHCCHHHHHCC
35.1030266825
2985PhosphorylationAAPLASDSLQKLGRE
HHHHCCHHHHHCCCC
30.1530266825
2988UbiquitinationLASDSLQKLGREPPS
HCCHHHHHCCCCCCC
59.1932142685
2995PhosphorylationKLGREPPSPPPSEHL
HCCCCCCCCCCCHHH
61.8324719451
2999PhosphorylationEPPSPPPSEHLYHQT
CCCCCCCCHHHCCCC
43.3425002506
3003PhosphorylationPPPSEHLYHQTLPSY
CCCCHHHCCCCCCCC
8.1925002506
3006PhosphorylationSEHLYHQTLPSYGGP
CHHHCCCCCCCCCCC
27.5925002506
3009PhosphorylationLYHQTLPSYGGPGAG
HCCCCCCCCCCCCCC
39.2525884760
3010PhosphorylationYHQTLPSYGGPGAGG
CCCCCCCCCCCCCCC
24.9428348404
3024PhosphorylationGPYPRGGSLDPSHSS
CCCCCCCCCCCCCCC
32.2126699800
3028PhosphorylationRGGSLDPSHSSGRGS
CCCCCCCCCCCCCCC
35.3526699800
3030PhosphorylationGSLDPSHSSGRGSAE
CCCCCCCCCCCCCCC
38.5326699800
3031PhosphorylationSLDPSHSSGRGSAEA
CCCCCCCCCCCCCCH
27.3826699800
3035PhosphorylationSHSSGRGSAEAAEDD
CCCCCCCCCCHHCCH
22.9026699800
3055PhosphorylationNEFPRVASVASSLAA
CCCHHHHHHHHHHHH
18.5030266825
3058PhosphorylationPRVASVASSLAARGP
HHHHHHHHHHHHHCC
24.5930266825
3059PhosphorylationRVASVASSLAARGPD
HHHHHHHHHHHHCCC
16.5830266825
3094UbiquitinationDTWYKGRKAGLLLPG
CCCCCCCEEEEEECC
56.3132142685
3107PhosphorylationPGAGATLYREEGPPA
CCCCCEEECCCCCCC
16.1825884760
3237PhosphorylationFPPASHRSPISHEGS
CCCCCCCCCCCCCCC
22.5927732954
3240PhosphorylationASHRSPISHEGSLSS
CCCCCCCCCCCCCCC
20.9027732954
3244PhosphorylationSPISHEGSLSSAAMS
CCCCCCCCCCCCCCC
23.3027732954
3246PhosphorylationISHEGSLSSAAMSPS
CCCCCCCCCCCCCCC
21.4527732954
3247PhosphorylationSHEGSLSSAAMSPSF
CCCCCCCCCCCCCCC
25.9127732954
3251PhosphorylationSLSSAAMSPSFSPSL
CCCCCCCCCCCCCCC
16.8027732954
3253PhosphorylationSSAAMSPSFSPSLSP
CCCCCCCCCCCCCCH
30.9227732954
3255PhosphorylationAAMSPSFSPSLSPLA
CCCCCCCCCCCCHHH
20.2327732954
3257PhosphorylationMSPSFSPSLSPLAAR
CCCCCCCCCCHHHHC
40.0427732954
3259PhosphorylationPSFSPSLSPLAARSP
CCCCCCCCHHHHCCC
23.3927732954

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 PCD16_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCD16_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 PCD16_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PCD16_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601390Van Maldergem syndrome 1 (VMLDS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCD16_HUMAN

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Related Literatures of Post-Translational Modification

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