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.. |
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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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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156 | Phosphorylation | ALQVPEHTAFGTRYP HHCCCCCCCCCCCCC | 23.24 | 30108239 | |
160 | Phosphorylation | PEHTAFGTRYPLEPA CCCCCCCCCCCCCCC | 22.15 | 30108239 | |
162 | Phosphorylation | HTAFGTRYPLEPARD CCCCCCCCCCCCCCC | 16.41 | 30108239 | |
217 | N-linked_Glycosylation | TGELDRENRSHYMLQ ECCCCCCCCCEEEEE | 52.20 | UniProtKB CARBOHYD | |
256 | N-linked_Glycosylation | NDHAPAFNQSRYHAV CCCCCCCCCCCCEEE | 40.81 | UniProtKB CARBOHYD | |
402 | N-linked_Glycosylation | DGDFAHVNVSLEGGE CCCEEEEEEEEECCC | 14.06 | UniProtKB CARBOHYD | |
438 | Phosphorylation | DREERDAYNLRVTAT CHHHHHHCCCEEEEC | 21.01 | 22817900 | |
584 | N-linked_Glycosylation | QFQRTFYNASLPEGT CHHHEEEECCCCCCC | 20.89 | UniProtKB CARBOHYD | |
591 | O-linked_Glycosylation | NASLPEGTQPGTCFL ECCCCCCCCCCCEEE | 29.90 | OGP | |
915 | Phosphorylation | APGTPIYTLRALDPD CCCCCEEEEEECCCC | 15.53 | 24719451 | |
942 | Phosphorylation | AGGGGAFTVDPTTGH ECCCCCEEECCCCCC | 24.38 | - | |
946 | Phosphorylation | GAFTVDPTTGHVRLM CCEEECCCCCCEEEE | 40.73 | - | |
947 | Phosphorylation | AFTVDPTTGHVRLMR CEEECCCCCCEEEEE | 30.58 | - | |
1002 | Phosphorylation | GLAPRFNSPTYRVDL CCCCCCCCCEEEEEC | 18.86 | 23403867 | |
1004 | Phosphorylation | APRFNSPTYRVDLPS CCCCCCCEEEEECCC | 24.63 | 23403867 | |
1005 | Phosphorylation | PRFNSPTYRVDLPSG CCCCCCEEEEECCCC | 16.42 | 23403867 | |
1076 | Phosphorylation | ILKVMAVSGSKAELG EEEEEEECCCHHHHC | 28.01 | - | |
1078 | Phosphorylation | KVMAVSGSKAELGQQ EEEEECCCHHHHCCC | 22.61 | - | |
1168 | Phosphorylation | GEVTTLQTLDREQQS CCEEEEEECCHHHHC | 33.47 | - | |
1196 | Phosphorylation | PPRSTTGTVHVAVLD CCCCCCCEEEEEEEE | 12.83 | - | |
1208 | Phosphorylation | VLDLNDNSPTFLQAS EEECCCCCCCCCEEC | 28.34 | - | |
1210 | Phosphorylation | DLNDNSPTFLQASGA ECCCCCCCCCEECCC | 36.48 | - | |
1234 | Phosphorylation | PDRVPPGTLVTTLQA CCCCCCCCEEEEEEE | 24.67 | - | |
1237 | Phosphorylation | VPPGTLVTTLQAKDP CCCCCEEEEEEECCC | 25.54 | - | |
1238 | Phosphorylation | PPGTLVTTLQAKDPD CCCCEEEEEEECCCC | 14.92 | - | |
1249 | N-linked_Glycosylation | KDPDEGENGTILYTL CCCCCCCCCEEEEEE | 64.86 | UniProtKB CARBOHYD | |
1290 | Phosphorylation | ERPHYVLTLSAHDQG CCCCEEEEEEECCCC | 14.50 | 30206219 | |
1292 | Phosphorylation | PHYVLTLSAHDQGSP CCEEEEEEECCCCCC | 20.51 | 30206219 | |
1298 | Phosphorylation | LSAHDQGSPPRSASL EEECCCCCCCCCHHH | 26.54 | 30206219 | |
1496 | Phosphorylation | DARTGALSAPRGLDR ECCCCCCCCCCCCCC | 35.38 | 24719451 | |
1521 | N-linked_Glycosylation | EATDRPANASRRRAA HHCCCCCCHHHHHHH | 40.92 | UniProtKB CARBOHYD | |
1581 | Phosphorylation | LGEAARVSYRLASGG HHHHHHEEEEECCCC | 10.05 | 23828894 | |
1582 | Phosphorylation | GEAARVSYRLASGGD HHHHHEEEEECCCCC | 13.54 | - | |
1586 | Phosphorylation | RVSYRLASGGDGHFR HEEEEECCCCCCCEE | 48.15 | - | |
1593 | Methylation | SGGDGHFRLHSSTGA CCCCCCEEEECCCCC | 26.30 | - | |
1718 | N-linked_Glycosylation | REEQEEINLTVYAQD HHHHHCCCEEEEECC | 32.70 | UniProtKB CARBOHYD | |
1959 | Phosphorylation | DVNDHAPTFPTSPLR ECCCCCCCCCCCCCE | 42.93 | 29083192 | |
1962 | Phosphorylation | DHAPTFPTSPLRLRL CCCCCCCCCCCEECC | 38.49 | 29083192 | |
1963 | Phosphorylation | HAPTFPTSPLRLRLP CCCCCCCCCCEECCC | 23.36 | 29083192 | |
1996 | N-linked_Glycosylation | EDRDAGANASILYRL HHCCCCCCCEEEHHH | 33.05 | UniProtKB CARBOHYD | |
1998 | Phosphorylation | RDAGANASILYRLAG CCCCCCCEEEHHHHC | 16.97 | 24905233 | |
2001 | Phosphorylation | GANASILYRLAGTPP CCCCEEEHHHHCCCC | 11.25 | 24905233 | |
2006 | Phosphorylation | ILYRLAGTPPPGTTV EEHHHHCCCCCCCCC | 27.32 | 24905233 | |
2011 | Phosphorylation | AGTPPPGTTVDSYTG HCCCCCCCCCCCCCC | 29.44 | 24905233 | |
2012 | Phosphorylation | GTPPPGTTVDSYTGE CCCCCCCCCCCCCCE | 28.38 | 24905233 | |
2015 | Phosphorylation | PPGTTVDSYTGEIRV CCCCCCCCCCCEEEE | 21.91 | 24905233 | |
2016 | Phosphorylation | PGTTVDSYTGEIRVA CCCCCCCCCCEEEEE | 17.82 | 24905233 | |
2017 | Phosphorylation | GTTVDSYTGEIRVAR CCCCCCCCCEEEEEC | 32.08 | 24905233 | |
2049 | Phosphorylation | DLGRPARSATGVIIV CCCCCCCCCCEEEEE | 32.08 | 24719451 | |
2361 | N-linked_Glycosylation | GPHEGRANLTVLVED CCCCCCCEEEEEEEE | 34.58 | UniProtKB CARBOHYD | |
2363 | Phosphorylation | HEGRANLTVLVEDVN CCCCCEEEEEEEECC | 16.17 | 24043423 | |
2377 | Phosphorylation | NDNAPAFSQSLYQVM CCCCHHHHHHHHHHH | 22.44 | 24043423 | |
2379 | Phosphorylation | NAPAFSQSLYQVMLL CCHHHHHHHHHHHCC | 28.04 | 24043423 | |
2381 | Phosphorylation | PAFSQSLYQVMLLEH HHHHHHHHHHHCCCC | 12.33 | 24043423 | |
2389 | Phosphorylation | QVMLLEHTPPGSAIL HHHCCCCCCCCCEEE | 23.08 | 24043423 | |
2393 | Phosphorylation | LEHTPPGSAILSVSA CCCCCCCCEEEEEEE | 20.22 | 24043423 | |
2397 | Phosphorylation | PPGSAILSVSATDRD CCCCEEEEEEEECCC | 14.12 | 24043423 | |
2399 | Phosphorylation | GSAILSVSATDRDSG CCEEEEEEEECCCCC | 23.29 | 24043423 | |
2401 | Phosphorylation | AILSVSATDRDSGAN EEEEEEEECCCCCCC | 24.86 | 24043423 | |
2428 | N-linked_Glycosylation | GFSVDPNNGTLFTIV CCEECCCCCCEEEEE | 50.65 | UniProtKB CARBOHYD | |
2512 | Phosphorylation | EATDADGSRSHAAVD EEECCCCCCCCEEEE | 31.02 | 23403867 | |
2514 | Phosphorylation | TDADGSRSHAAVDYS ECCCCCCCCEEEEEE | 21.12 | 23403867 | |
2521 | Phosphorylation | SHAAVDYSIISGNWG CCEEEEEEEECCCCC | 14.69 | 23403867 | |
2524 | Phosphorylation | AVDYSIISGNWGRVF EEEEEEECCCCCEEE | 25.14 | 23403867 | |
2569 | N-linked_Glycosylation | FESLTQYNLTVAAAD HHHHHCCEEEEEEHH | 21.30 | UniProtKB CARBOHYD | |
2761 | N-linked_Glycosylation | GREAFALNSSTGELR HHEEEEECCCCCCEE | 30.41 | UniProtKB CARBOHYD | |
2792 | N-linked_Glycosylation | VGAADAGNLSASVTV EEHHCCCCCCEEEEE | 32.32 | UniProtKB CARBOHYD | |
2862 | N-linked_Glycosylation | SSPYFGINQTTGALY CCCCCCCCCCCCEEE | 33.26 | UniProtKB CARBOHYD | |
2967 | Ubiquitination | LVRARSRKAEAAPGP HHHHHHCCCCCCCCC | 52.40 | 32142685 | |
2976 | Phosphorylation | EAAPGPMSQAAPLAS CCCCCCHHHHHHHCC | 21.57 | 22210691 | |
2983 | Phosphorylation | SQAAPLASDSLQKLG HHHHHHCCHHHHHCC | 35.10 | 30266825 | |
2985 | Phosphorylation | AAPLASDSLQKLGRE HHHHCCHHHHHCCCC | 30.15 | 30266825 | |
2988 | Ubiquitination | LASDSLQKLGREPPS HCCHHHHHCCCCCCC | 59.19 | 32142685 | |
2995 | Phosphorylation | KLGREPPSPPPSEHL HCCCCCCCCCCCHHH | 61.83 | 24719451 | |
2999 | Phosphorylation | EPPSPPPSEHLYHQT CCCCCCCCHHHCCCC | 43.34 | 25002506 | |
3003 | Phosphorylation | PPPSEHLYHQTLPSY CCCCHHHCCCCCCCC | 8.19 | 25002506 | |
3006 | Phosphorylation | SEHLYHQTLPSYGGP CHHHCCCCCCCCCCC | 27.59 | 25002506 | |
3009 | Phosphorylation | LYHQTLPSYGGPGAG HCCCCCCCCCCCCCC | 39.25 | 25884760 | |
3010 | Phosphorylation | YHQTLPSYGGPGAGG CCCCCCCCCCCCCCC | 24.94 | 28348404 | |
3024 | Phosphorylation | GPYPRGGSLDPSHSS CCCCCCCCCCCCCCC | 32.21 | 26699800 | |
3028 | Phosphorylation | RGGSLDPSHSSGRGS CCCCCCCCCCCCCCC | 35.35 | 26699800 | |
3030 | Phosphorylation | GSLDPSHSSGRGSAE CCCCCCCCCCCCCCC | 38.53 | 26699800 | |
3031 | Phosphorylation | SLDPSHSSGRGSAEA CCCCCCCCCCCCCCH | 27.38 | 26699800 | |
3035 | Phosphorylation | SHSSGRGSAEAAEDD CCCCCCCCCCHHCCH | 22.90 | 26699800 | |
3055 | Phosphorylation | NEFPRVASVASSLAA CCCHHHHHHHHHHHH | 18.50 | 30266825 | |
3058 | Phosphorylation | PRVASVASSLAARGP HHHHHHHHHHHHHCC | 24.59 | 30266825 | |
3059 | Phosphorylation | RVASVASSLAARGPD HHHHHHHHHHHHCCC | 16.58 | 30266825 | |
3094 | Ubiquitination | DTWYKGRKAGLLLPG CCCCCCCEEEEEECC | 56.31 | 32142685 | |
3107 | Phosphorylation | PGAGATLYREEGPPA CCCCCEEECCCCCCC | 16.18 | 25884760 | |
3237 | Phosphorylation | FPPASHRSPISHEGS CCCCCCCCCCCCCCC | 22.59 | 27732954 | |
3240 | Phosphorylation | ASHRSPISHEGSLSS CCCCCCCCCCCCCCC | 20.90 | 27732954 | |
3244 | Phosphorylation | SPISHEGSLSSAAMS CCCCCCCCCCCCCCC | 23.30 | 27732954 | |
3246 | Phosphorylation | ISHEGSLSSAAMSPS CCCCCCCCCCCCCCC | 21.45 | 27732954 | |
3247 | Phosphorylation | SHEGSLSSAAMSPSF CCCCCCCCCCCCCCC | 25.91 | 27732954 | |
3251 | Phosphorylation | SLSSAAMSPSFSPSL CCCCCCCCCCCCCCC | 16.80 | 27732954 | |
3253 | Phosphorylation | SSAAMSPSFSPSLSP CCCCCCCCCCCCCCH | 30.92 | 27732954 | |
3255 | Phosphorylation | AAMSPSFSPSLSPLA CCCCCCCCCCCCHHH | 20.23 | 27732954 | |
3257 | Phosphorylation | MSPSFSPSLSPLAAR CCCCCCCCCCHHHHC | 40.04 | 27732954 | |
3259 | Phosphorylation | PSFSPSLSPLAARSP CCCCCCCCHHHHCCC | 23.39 | 27732954 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of PCD16_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of PCD16_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Oops, there are no PPI records of PCD16_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
601390 | Van Maldergem syndrome 1 (VMLDS1) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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