AIDA_HUMAN - dbPTM
AIDA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIDA_HUMAN
UniProt AC Q96BJ3
Protein Name Axin interactor, dorsalization-associated protein
Gene Name AIDA
Organism Homo sapiens (Human).
Sequence Length 306
Subcellular Localization
Protein Description Acts as a ventralizing factor during embryogenesis. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling (By similarity)..
Protein Sequence MSEVTRSLLQRWGASFRRGADFDSWGQLVEAIDEYQILARHLQKEAQAQHNNSEFTEEQKKTIGKIATCLELRSAALQSTQSQEEFKLEDLKKLEPILKNILTYNKEFPFDVQPVPLRRILAPGEEENLEFEEDEEEGGAGAGSPDSFPARVPGTLLPRLPSEPGMTLLTIRIEKIGLKDAGQCIDPYITVSVKDLNGIDLTPVQDTPVASRKEDTYVHFNVDIELQKHVEKLTKGAAIFFEFKHYKPKKRFTSTKCFAFMEMDEIKPGPIVIELYKKPTDFKRKKLQLLTKKPLYLHLHQTLHKE
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
15PhosphorylationLLQRWGASFRRGADF
HHHHHCCCCCCCCCC
18.4927251275
24PhosphorylationRRGADFDSWGQLVEA
CCCCCCCCHHHHHHH
32.85113330853
62PhosphorylationFTEEQKKTIGKIATC
CCHHHHHHHHHHHHH
41.8323403867
68PhosphorylationKTIGKIATCLELRSA
HHHHHHHHHHHHHHH
22.5423403867
79PhosphorylationLRSAALQSTQSQEEF
HHHHHHHCCCCCCCC
29.3027251275
80PhosphorylationRSAALQSTQSQEEFK
HHHHHHCCCCCCCCC
21.1927251275
82PhosphorylationAALQSTQSQEEFKLE
HHHHCCCCCCCCCHH
39.3826471730
144PhosphorylationEGGAGAGSPDSFPAR
CCCCCCCCCCCCCCC
25.6225159151
147PhosphorylationAGAGSPDSFPARVPG
CCCCCCCCCCCCCCC
36.1922199227
155PhosphorylationFPARVPGTLLPRLPS
CCCCCCCCCCCCCCC
21.0337604329
162PhosphorylationTLLPRLPSEPGMTLL
CCCCCCCCCCCCEEE
62.1027499020
167PhosphorylationLPSEPGMTLLTIRIE
CCCCCCCEEEEEEEE
25.2431437747
170PhosphorylationEPGMTLLTIRIEKIG
CCCCEEEEEEEEECC
16.0168716917
188PhosphorylationAGQCIDPYITVSVKD
CCCCCCCEEEEEEEC
12.8946160909
232"N6,N6-dimethyllysine"ELQKHVEKLTKGAAI
HHHHHHHHHHHCCEE
61.44-
232MethylationELQKHVEKLTKGAAI
HHHHHHHHHHHCCEE
61.44-
235AcetylationKHVEKLTKGAAIFFE
HHHHHHHHCCEEEEE
57.9220167786
276PhosphorylationGPIVIELYKKPTDFK
CCEEEEEECCCCCCC
12.2721406692
296PhosphorylationLLTKKPLYLHLHQTL
HHHCCCCCHHHHHHC
10.7068730133

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 AIDA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIDA_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 AIDA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AIDA_HUMANAIDAphysical
25416956
LNX1_HUMANLNX1physical
25416956
PKHF2_HUMANPLEKHF2physical
21516116

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND MASSSPECTROMETRY.

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