PROML_DROME - dbPTM
PROML_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PROML_DROME
UniProt AC P82295
Protein Name Prominin-like protein
Gene Name prominin-like
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1013
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MGEVAATVEPLAAVKSKSMRSRKRRQRRRRQIAYLAICGLSVAIFGFALATLIRPTTAQADADPGSWRKGYVGHGTTHEQLGQPHWPPVQYTVYRPTTNYTKAPPPPTSAMNPIFNFTHFLYDKVLYRDEPIPEGYIVVKNSDTLSLGPKVEENDWRDLLAHYWMVLIWVVILVVLIIVIPFIAVCYCCFCCCRRCRQGCPPCTSKQDAQRRFCCGICLLILIIGLIFGIIIAFVTNKMIDSGFAETSETMKRGSEDTCTYLKDVADHVHHLMMYNYEEMETHVLDQLTHAHRHIFLDLSDTSESNSLAEMERVLENMPEALELMRQVEKMEKDLRFYGSQLRDGVRGIKRDVNFAVANLCQLQMCQKFLISSNIEHIDSSQCLHFDNLPNTKEFVEGMENIVASEYYAIPQRGLSRLKKVSDKVKTQLSFVVPPMMRDLTKGRTIFREHATNVRNIVEGVLSDIHIKTLHSTKSFEDVYERFGHDRNVVSLIVCLLILLVLFILIFALLCGCFGRRRTGYGDECCSKSTGATCLLLAILLIFCVFSFIALVGLFYFMLGMVTYQGACAPLRDQENNTLFRQLDASIDLNHYLPPSESNKEVVQPLKMSSAIKACHANQTIFDMMRQHNIYDINDLTRIKVMSHSQENTDSIKVFDEDLSTVVLLTKEERDELKTAGESKLAKYHSSLYMPSLCTQFTPMNLNALSEQLYKLSNDLEYPAYGWAKVSFWNEGLNTKAFYRNFVPKLTSLVEKMKANLKKIDELISYENHDFTNTIKILTATAINSEQFIQTRGKDYINALGGNLTNSIDQMIDDYIDMIIKEANESVGHCAPLSYIYYRGVDLICHRIVDPINGFWVGILLCALLFLPILFVAHRLMCLYKKIYPYLATVGAAGVVEGGSDYLYDAYSERDREHVPLANVPKKRRKAYERRREQQDYFEDASPSVSRGNRSGGDRGGGGGDGAPGSSSMRYNDMAPTHWDHEPPRYHNPPAAPPSSEYERPPPYYYPGASEQD
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
99N-linked_GlycosylationTVYRPTTNYTKAPPP
EEECCCCCCCCCCCC
44.9819349973
116N-linked_GlycosylationSAMNPIFNFTHFLYD
CCCCCCCCHHHHHHC
41.44-
576N-linked_GlycosylationAPLRDQENNTLFRQL
CCCCCCCCCCHHHHH
40.9519349973
618N-linked_GlycosylationAIKACHANQTIFDMM
HHHHHHCCCHHHHHH
18.83-
803N-linked_GlycosylationYINALGGNLTNSIDQ
HHHHCCCHHCHHHHH
41.72-
824N-linked_GlycosylationDMIIKEANESVGHCA
HHHHHHHHHCCCCCC
43.07-
937PhosphorylationRRREQQDYFEDASPS
HHHHHHHHHCCCCCC
12.4418281928
942PhosphorylationQDYFEDASPSVSRGN
HHHHCCCCCCCCCCC
29.9925749252
949N-linked_GlycosylationSPSVSRGNRSGGDRG
CCCCCCCCCCCCCCC
33.56-
968PhosphorylationDGAPGSSSMRYNDMA
CCCCCCCCCCCCCCC
14.6927626673

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 PROML_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PROML_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 PROML_DROME !!

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

Oops, there are no PPI records of PROML_DROME !!

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99 AND ASN-576, AND MASSSPECTROMETRY.

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