CAD87_DROME - dbPTM
CAD87_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAD87_DROME
UniProt AC Q9VGG5
Protein Name Cadherin-87A
Gene Name Cad87A
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1975
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells (By similarity)..
Protein Sequence MKLPLGLLMICLGLTLAKGETNLPPVFTQTLNNIILYENVTVGTVVFRLEAYDPEGSPVTYGAIGADHFSVDPVSGNITLIKPLDREEKDTLKFLVSIRDRVDPEGESERDNVVEVPITFIILDLNDNPPEFQNTPYEADVNEDAAVGTTIFDKITVKDRDIVGESLDLKCLPQQQSPEACRKFRLHIIKRDATILEAAVVLNDTLNYNQRMVYHFQIEATDGPHKTQTTFEARVKDVQDKPPVFQGSLSTVIDEDSPINTLVLTVHARDGDTGEPRKIVYDLRTNPNDYFLLDAQTGELRTAKPLDREALEDSTGIISLVIRARELVNGVPSDDPLTSATAKATVTIRDVNDSPPVFNHKEYSVSLLENTLPGTPLALDMSVSDADVGINSKFALRLDDVSGVFDVEPKLVTGYSQVNIRVANGTLDYENPNQRKFIVLVVAEETDTNPRLSSTATITVSVLDANDNKPVFEQESYSASVSEAALPGQYIATITARDVDSGSYGDSGIRYSLSGTGAELFHVNEQTGVISLANCHDNGESNRRERRDLNEDEHVEEDDGEGHLEMLSMEAATREIGTEPTVQYTLITQAPEEQASSVPLPAPVPHAAPSGVPAATANDDKAPQTCLDYESETTYFLSYKATDDNGRGSASVVSLRISVTDANDSPPVCESPLYRASVDEGAVVFDSPLIVKARDADTMSRISYRIRGSEQVESIFDIDRETGQIIIRPNATLDVTNLNSDQLIFAVEANDGLFTAHCGVNITVRDVNNHVPNFEQQSYSAVVEENSEIGTSVERVHATDLDTGKNAELRYRIQQGSFDDFGIVETTGEVFVSRKLDFDRRNTYQLQIQASDQGTPSLTGTATLTINVQNSNDKDPYFVPATQHAEVRADAPPGQLVYTLIALDPDVANHNALEFAGTDDITAIDKEGKELPHYDQFKEYFKISRNGKVSVNKQLDRNLFAVMRINVLVTDSTAPNVQQGRGLLIIQIIDVNKNPPRFNAPWSVEQPQIKLQMVEEQPVGTVLTTLQANDEDSSIGEFNISDNDYFAINQTSGMIYTIARLDYEVVKEVKFQVTVSDTGVPALTATADVVVDIINLNDNDPKFSQSDYYFNVTENSPRGTVAGKVEAHDGDVGVFGEITYTLIGENNKYFSIDAYTGNVMVANSSILDREQIKELTLSVVAQDKAPAAVQKSATATIHINILDVNDNAPVFTRDVYNSTVAENAAYQPPAALLQVQAIDQDEGLYGDVRYIITAGNEMGLFKLDAQSGIVYPAQSLSGKHGAYELTISARDTQGSGTMESTTKAIITVLRVNRHKPEFVIPALSNATIEIPGDIVQPDYLLLTVRAMDNDTEENGKVSYHLQVNNRNEQQTGEFKIDEVTGELRAKTQLNRKNRANYDIILVARDAGNPPFESLRLLSVSIVDANENRPEFPDASNPYKVSINENSGRDVKIGHIQAASRSKHNRDIFYYMLLGNEDGAFYVDKLTGDIYTNKSLDREETDVYTLYILASIKADLHISEEERASFSIKTLNRDNTVAKVAITVLDVNDNPPVFEKPIYYAGVNANAKMGAAITLVNATDADQGKNAKIEFMIVASNLYKFGATKSTGSIVPSPFAISQDGRISANTIMAEYNQDRFELEIVARELEQPQSSASTKVNIWVFDGTQLVRVILSRPPEEVYQEQEEIIAELRNATQHRIIVDEIRFHLDSIGRIRMDWCDLYFHAVDPQTQQIAPVDEILKDIDRNYDYLKDYYAGFAIENVVPAYIAIVQDEFDLAVAGLVALVIVLFVGVISFIVLCCCLKHWNLSVPVETRRKEALIKKQIIEDLNTTENPLWIEQKLKLYEEQELTMQVFSEPDHISNSEAPGHLDHRSSLEQVHHVGQTVDNTYATIQPRNNQNRLTGGGGAGGGSMRSGGGASAGGVGGAGLLLARVDPHMNEFADYATLRNNRAPSLYEFTGSTFQAPIRDGDDAVAELI
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
39N-linked_GlycosylationNNIILYENVTVGTVV
CCEEEEECCEEEEEE		22.62-
77N-linked_GlycosylationSVDPVSGNITLIKPL
EECCCCCCEEEEEEC		19.30-
203N-linked_GlycosylationLEAAVVLNDTLNYNQ
HHHHHHHCCCCCCCC		28.72-
424N-linked_GlycosylationQVNIRVANGTLDYEN
EEEEEEECCEECCCC		40.9217893096
671PhosphorylationDSPPVCESPLYRASV
CCCCCCCCCCEEEEC		18.3222817900
674PhosphorylationPVCESPLYRASVDEG
CCCCCCCEEEECCCC		13.9122817900
730N-linked_GlycosylationGQIIIRPNATLDVTN
CCEEECCCCEEEEEC		35.39-
761N-linked_GlycosylationFTAHCGVNITVRDVN
EEEECCEEEEEEECC		14.97-
1039N-linked_GlycosylationDSSIGEFNISDNDYF
CCCCEEEECCCCCEE		28.66-
1049N-linked_GlycosylationDNDYFAINQTSGMIY
CCCEEEEECCCCCEE		35.33-
1111N-linked_GlycosylationSQSDYYFNVTENSPR
CCCCEEEEEECCCCC		24.55-
1163N-linked_GlycosylationTGNVMVANSSILDRE
CCCEEEECCCCCCHH		25.53-
1217N-linked_GlycosylationVFTRDVYNSTVAENA
EEEHHHCCCCHHCCC		30.93-
1325N-linked_GlycosylationFVIPALSNATIEIPG
CEEECCCCCEEECCC		41.79-
1349N-linked_GlycosylationLTVRAMDNDTEENGK
EEEEECCCCCCCCCE		45.05-
1492N-linked_GlycosylationLTGDIYTNKSLDREE
CCCCEECCCCCCCCC		18.23-
1576N-linked_GlycosylationGAAITLVNATDADQG
CCEEEEEECCCCCCC		39.9917893096
1691N-linked_GlycosylationEIIAELRNATQHRII
HHHHHHHHHHCCEEE		61.02-
1871PhosphorylationPGHLDHRSSLEQVHH
CCCCCCCCCHHHHCC		35.5419429919
1872PhosphorylationGHLDHRSSLEQVHHV
CCCCCCCCHHHHCCC		35.5619429919
1882PhosphorylationQVHHVGQTVDNTYAT
HHCCCCCCCCCCCEE		24.7319429919
1886PhosphorylationVGQTVDNTYATIQPR
CCCCCCCCCEECCCC		15.2919429919
1887PhosphorylationGQTVDNTYATIQPRN
CCCCCCCCEECCCCC		14.1719429919
1889PhosphorylationTVDNTYATIQPRNNQ
CCCCCCEECCCCCCC		15.1019429919
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 CAD87_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAD87_DROME !!
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 CAD87_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAD87_DROME !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAD87_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-424 AND ASN-1576, AND MASSSPECTROMETRY.

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