CAD89_DROME - dbPTM
CAD89_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAD89_DROME
UniProt AC Q9VEU1
Protein Name Cadherin-89D
Gene Name Cad89D
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2240
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 MDSEAYPMKSSVKISQKKKASQDMAVICVWVMPLAVFGLIAIGQAAKTGQVQASSGSCAFHTLDGVAAESEGVRFIRLREDAQVGKEILRLQAYPRSTAALKGADASGDHKYFNLTEHNATTLVVSLARSLERLVDRDVPRNLLKFRILCAGKQEKLEEGSYLSITVYIEDVNDNAPEFLNVPYVVDVDENTSIESIIFEGVQAFDRDKPNTPNSEVHFSMSTVPEQLSADGSPYFALKSPHRPLLILKRELDFDNGIRQFKLPIFAWDRGTPANQANTTITINVRDVDDLPPKFTEGVYRTRINEFYPMTGVPIRIPLYFAPPIMAFDQDSLNASLVYDIISGNERQLFRVNPHNGVMYLQKEIDLEEESLPGNTFVLQLEARQKDNPLKKALARIEVEVLDLNDNVPEFEADYYNISIVENLPTGFSVLQVNAVDRDQGENSEFLYNLVETKDAAGAFRIDSRTGWITVRDDRLLDREQRRSIQLNVEALERNPSYLDDKHLKKPGPSKVQVEITLLDTNDNTPKFEHGNLYEFKVPINAPTGYVIGQVVAHDPDEGPNGHLLYELQRPKGSGYIPFRLDNKNGTIYVGGPLRRGRIAVFVEATDQPTNPSERRFSLAVITIEVYATIDDQAIDFVGAPYEFWVGANTPLGTSVGQVRTTLIYEGGDEIMYDLLHTYSEGVPFAIEERSGIITVIRELSEFKRKVYQFEAVANYLFANSSQSLVMSRSSSPLTTIASPAELSDEGVLITNLTIHIVNKPEQKVPLRPVIEEINMNVIHFHVEENVVGGIIGQLLYKNGINLVNNELGTYREMPSEPTSRNITMGSRFRSRNRSRSSKSKRRLPRRLVGDANIKLRYIIANQQEVVNKISITEDGTLLTLTGLDREQQPSYELTVIVEYSTGLVSGAGIYQVNIKVDDVNDNAPKFNALTYVGLINENCVVGTELSMNHAILIQDADEGPNAEFRVQLQGDYSDEFSIEYVNGTSSENSTHHKMPSTTGAFNIFNLTDQWNDEFKYQELHTTFMQTNFKLSSGPYFRISYTGKRGLDREKQQLYNLKIIAADTGGLSGYAHLTVLVADVNDNAPMFERISVFKDSRLEIREYTTDMEIYFVESSSGMTAPQATAAMMLAPPPYHIPGSPRFNVDRERSVGAGLGVVARAKSRRRMVRALTTKCPLFAIYEDTPVGTKVLQLSASDEDFGKNALLHYELQGEQVERTPGMPMLRVHGVKYFAIDKLSGELSVNYPLSANIEIMLNLTVTDIDGLKDSTCLRFTVMDVNNHAPTFKKSWYSFDTPEGEYKDSVLGQLTAIDMDFGENANITYTLSDSHLPFTIKPASGVLKIGGQLDRELKDKYSFQVIATDNAPVMQRMSSSVDVEVNVLDINDNRPEFIGYDDQTKAVKFIPSVADRTLMLPVYKAYLDRSTQPGTFVRQLTAIDKDNVGNGNGLVLYSIRHQEMQAPLFQIDSRDGTISTISRINGYNDYEHLNVSVIASDVGSPALSATAIVIVNLQGQAVTDPPKSTPKPEPPANVTVFQHAYYEVKLTENNEAPIEVMRLNLSAGLNPENYRWSLWLEEGLDETDAHPPFEYDAKNMLLYALKPFDREHISRYQLRIRADRLSREARNYARVSYPVVDERIEGLSLNECRILVHIADENDNAPKFRGNGQPIVAVLPQSASFGYPVTRVEANDLDEGLNAEIRYRLLNEPARLFGIDELSGNIRLLGELSRTEHIYGFDVKATDRMGADDGRSGIVNVFVYIINEAKQVRLVVAGMPVEVERRIEGLMEALSDAIGKDVRVRLLEPYSGGLEPATNAYIYAVDPHTNSIMEMEQLQDALAGLQLDALQLQQQKLDGGKPMPRILELAEFGQLARPAHASASSFMGGLEFVTVVLLALISLGALIAACCYVCMRQKRRLWSQRDFSASDAGLTYTIAGIGSPRGQKQRRQRQQRHTQRCSKGSTGSQRPTSAFMPESVCSSAQTQSTATATEKLEQQLHHHHQQQAMATQQQHHQYLNEQQRQQKREYIDVPLPKSIAKAAAVTSGGDGAVGVGSTPFVLKYNACQPVNNLNNYETSLFSLHSTGQDSGVEFLSSRELYETSPDSFQHGGSKRGNNTEVLCPRHAKAHLELRQPNTDSSDTYEDSLKTDEPLVAHNCRSANCEHRQHQQHPSHHPHYQNTRFEKRSCVRHSFSGVKDDLMQQSPQISLRPRGHALRNSMNDLEQRLHNLEQSFRRPLEFSKSNSLF
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
114N-linked_GlycosylationSGDHKYFNLTEHNAT
CCCCCCEECCCCCHH
42.85-
119N-linked_GlycosylationYFNLTEHNATTLVVS
CEECCCCCHHHHHHH
32.52-
191N-linked_GlycosylationYVVDVDENTSIESII
EEEECCCCCCEEEEE
34.36-
278N-linked_GlycosylationGTPANQANTTITINV
CCCCCCCCCEEEEEE
28.17-
334N-linked_GlycosylationAFDQDSLNASLVYDI
ECCCCCCCEEEEEEH
31.28-
417N-linked_GlycosylationEFEADYYNISIVENL
CCCCEEECEEEEECC
18.46-
585N-linked_GlycosylationPFRLDNKNGTIYVGG
CEEEECCCCEEEECC
60.12-
720N-linked_GlycosylationVANYLFANSSQSLVM
HHHHHHCCCCCEEEE
34.55-
752N-linked_GlycosylationDEGVLITNLTIHIVN
CCCEEEEEEEEEEEC
28.35-
822N-linked_GlycosylationPSEPTSRNITMGSRF
CCCCCCCCCCCCHHH
33.57-
833N-linked_GlycosylationGSRFRSRNRSRSSKS
CHHHHHCCCCCCCCC
47.75-
983N-linked_GlycosylationEFSIEYVNGTSSENS
CEEEEEECCCCCCCC
47.31-
989N-linked_GlycosylationVNGTSSENSTHHKMP
ECCCCCCCCCCCCCC
54.90-
1006N-linked_GlycosylationTGAFNIFNLTDQWND
CCCEEEECCCCCCCC
37.93-
1255N-linked_GlycosylationANIEIMLNLTVTDID
CCEEEEEECEEECCC
19.11-
1318N-linked_GlycosylationMDFGENANITYTLSD
CCCCCCCEEEEEECC
38.42-
1486N-linked_GlycosylationYNDYEHLNVSVIASD
CCCCCCEEEEEEEEC
26.40-
1529N-linked_GlycosylationPKPEPPANVTVFQHA
CCCCCCCCEEEEEEE
35.45-
1556N-linked_GlycosylationPIEVMRLNLSAGLNP
CEEEEEEEECCCCCH
22.91-

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 CAD89_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAD89_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 CAD89_DROME !!

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

Oops, there are no PPI records of CAD89_DROME !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAD89_DROME

loading...

Related Literatures of Post-Translational Modification

TOP