AJUBA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AJUBA_MOUSE
• UniProt AC: Q91XC0
• Protein Name: LIM domain-containing protein ajuba
• Gene Name: Ajuba
• Organism: Mus musculus (Mouse).
• Sequence Length: 547
• Subcellular Localization: Cytoplasm, cytoskeleton. Cell membrane. Cell junction. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, P-body. Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase (By simi
• Protein Description: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell-cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1..
• Protein Sequence: MERLGEKASRLLEKLRLSDSGSAKFGRRKGEASRSGSDGTPGAGKGRLSGLGGPRKSGHRGANGGPGDEPLEPAREQGPLDAERNARGSFEAQRFEGSFPGGPPPTRALPLPLSSPPDFRLETTAPALSPRSSFASSSASDASKPSSPRGSLLLDGAGASGAGGSRPCSNRTSGISMGYDQRHGSPLPAGPCLFGLPLTTAPAGYPGGAPSAYPELHAALDRLCAHRSVGFGCQESRHSYPPALGSPGALTGAVVGTAGPLERRGAQPGRHSVTGYGDCAAGARYQDELTALLRLTVATGGREAGARGEPSGIEPSGLEESPGPFVPEASRSRIREPEAREDYFGTCIKCNKGIYGQSNACQALDSLYHTQCFVCCSCGRTLRCKAFYSVNGSVYCEEDYLFSGFQEAAEKCCVCGHLILEKILQAMGKSYHPGCFRCIVCNKCLDGVPFTVDFSNQVYCVTDYHKNYAPKCAACGQPILPSEGCEDIVRVISMDRDYHFECYHCEDCRMQLSDEEGCCCFPLDGHLLCHGCHMQRLSARQPSTNYI

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
9	Phosphorylation	ERLGEKASRLLEKLR HHHHHHHHHHHHHHC	34.23	22324799
18	Phosphorylation	LLEKLRLSDSGSAKF HHHHHCCCCCCCCCC	24.24	29514104
22	Phosphorylation	LRLSDSGSAKFGRRK HCCCCCCCCCCCCCC	32.03	29514104
89	Phosphorylation	AERNARGSFEAQRFE HHHHHCCCHHHHHCC	17.85	30352176
98	Phosphorylation	EAQRFEGSFPGGPPP HHHHCCCCCCCCCCC	22.52	25168779
114	Phosphorylation	RALPLPLSSPPDFRL CCCCCCCCCCCCCEE	38.57	26643407
115	Phosphorylation	ALPLPLSSPPDFRLE CCCCCCCCCCCCEEE	48.40	26643407
123	Phosphorylation	PPDFRLETTAPALSP CCCCEEEECCCCCCC	32.61	26643407
124	Phosphorylation	PDFRLETTAPALSPR CCCEEEECCCCCCCC	22.67	28507225
129	Phosphorylation	ETTAPALSPRSSFAS EECCCCCCCCHHCCC	22.00	26824392
132	Phosphorylation	APALSPRSSFASSSA CCCCCCCHHCCCCCC	32.94	25619855
133	Phosphorylation	PALSPRSSFASSSAS CCCCCCHHCCCCCCC	26.55	25619855
137	Phosphorylation	PRSSFASSSASDASK CCHHCCCCCCCCCCC	26.88	25619855
138	Phosphorylation	RSSFASSSASDASKP CHHCCCCCCCCCCCC	29.33	25619855
140	Phosphorylation	SFASSSASDASKPSS HCCCCCCCCCCCCCC	35.34	25619855
143	Phosphorylation	SSSASDASKPSSPRG CCCCCCCCCCCCCCC	50.52	25619855
146	Phosphorylation	ASDASKPSSPRGSLL CCCCCCCCCCCCCEE	57.63	27087446
147	Phosphorylation	SDASKPSSPRGSLLL CCCCCCCCCCCCEEE	27.43	25521595
160	Phosphorylation	LLDGAGASGAGGSRP EECCCCCCCCCCCCC	28.40	25338131
165	Phosphorylation	GASGAGGSRPCSNRT CCCCCCCCCCCCCCC	31.93	25338131
169	Phosphorylation	AGGSRPCSNRTSGIS CCCCCCCCCCCCCCC	31.84	25338131
172	Phosphorylation	SRPCSNRTSGISMGY CCCCCCCCCCCCCCC	35.24	-
185	Phosphorylation	GYDQRHGSPLPAGPC CCCCCCCCCCCCCCE	19.69	26824392
199	Phosphorylation	CLFGLPLTTAPAGYP EEECCCCCCCCCCCC	20.97	26160508
200	Phosphorylation	LFGLPLTTAPAGYPG EECCCCCCCCCCCCC	38.02	26160508
228	Phosphorylation	DRLCAHRSVGFGCQE HHHHHHCCCCCCCCC	19.41	23984901
236	Phosphorylation	VGFGCQESRHSYPPA CCCCCCCCCCCCCCC	14.93	23984901
239	Phosphorylation	GCQESRHSYPPALGS CCCCCCCCCCCCCCC	37.92	26824392
240	Phosphorylation	CQESRHSYPPALGSP CCCCCCCCCCCCCCC	13.70	23984901
246	Phosphorylation	SYPPALGSPGALTGA CCCCCCCCCCHHCCC	22.47	26824392
251	Phosphorylation	LGSPGALTGAVVGTA CCCCCHHCCCEEECC	23.66	23984901
257	Phosphorylation	LTGAVVGTAGPLERR HCCCEEECCCCCHHC	19.48	23984901
272	Phosphorylation	GAQPGRHSVTGYGDC CCCCCCCCCCCCCCC	21.73	25521595
274	Phosphorylation	QPGRHSVTGYGDCAA CCCCCCCCCCCCCCC	27.92	24899341
276	Phosphorylation	GRHSVTGYGDCAAGA CCCCCCCCCCCCCCC	10.63	25777480
321	Phosphorylation	EPSGLEESPGPFVPE CCCCCCCCCCCCCCH	26.28	26824392

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
172	T	Phosphorylation	Kinase	PAK1	Q13153	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AJUBA_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AJUBA_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of AJUBA_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.