AJUBA_HUMAN - dbPTM
AJUBA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AJUBA_HUMAN
UniProt AC Q96IF1
Protein Name LIM domain-containing protein ajuba
Gene Name AJUBA
Organism Homo sapiens (Human).
Sequence Length 538
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. Prefere
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 MERLGEKASRLLEKFGRRKGESSRSGSDGTPGPGKGRLSGLGGPRKSGPRGATGGPGDEPLEPAREQGSLDAERNQRGSFEAPRYEGSFPAGPPPTRALPLPQSLPPDFRLEPTAPALSPRSSFASSSASDASKPSSPRGSLLLDGAGAGGAGGSRPCSNRTSGISMGYDQRHGSPLPAGPCLFGPPLAGAPAGYSPGGVPSAYPELHAALDRLYAQRPAGFGCQESRHSYPPALGSPGALAGAGVGAAGPLERRGAQPGRHSVTGYGDCAVGARYQDELTALLRLTVGTGGREAGARGEPSGIEPSGLEEPPGPFVPEAARARMREPEAREDYFGTCIKCNKGIYGQSNACQALDSLYHTQCFVCCSCGRTLRCKAFYSVNGSVYCEEDYLFSGFQEAAEKCCVCGHLILEKILQAMGKSYHPGCFRCIVCNKCLDGIPFTVDFSNQVYCVTDYHKNYAPKCAACGQPILPSEGCEDIVRVISMDRDYHFECYHCEDCRMQLSDEEGCCCFPLDGHLLCHGCHMQRLNARQPPANYI
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
7Methylation-MERLGEKASRLLEK
-CHHHHHHHHHHHHH		50.27-
14UbiquitinationKASRLLEKFGRRKGE
HHHHHHHHHCCCCCC		53.7633845483
30PhosphorylationSRSGSDGTPGPGKGR
CCCCCCCCCCCCCCC		30.0228985074
39PhosphorylationGPGKGRLSGLGGPRK
CCCCCCCCCCCCCCC		30.5220068231
53PhosphorylationKSGPRGATGGPGDEP
CCCCCCCCCCCCCCC		45.5628674419
69PhosphorylationEPAREQGSLDAERNQ
HHHHHHCCCCCHHHH		23.8321815630
79PhosphorylationAERNQRGSFEAPRYE
CHHHHCCCCCCCCCC		23.3121945579
85PhosphorylationGSFEAPRYEGSFPAG
CCCCCCCCCCCCCCC		24.4721945579
88PhosphorylationEAPRYEGSFPAGPPP
CCCCCCCCCCCCCCC		19.0021945579
104PhosphorylationRALPLPQSLPPDFRL
CCCCCCCCCCCCCCC		40.6930266825
114PhosphorylationPDFRLEPTAPALSPR
CCCCCCCCCCCCCCC		35.5829255136
119PhosphorylationEPTAPALSPRSSFAS
CCCCCCCCCCHHCCC		22.0019664994
122PhosphorylationAPALSPRSSFASSSA
CCCCCCCHHCCCCCC		32.9423927012
123PhosphorylationPALSPRSSFASSSAS
CCCCCCHHCCCCCCC		26.5523927012
126PhosphorylationSPRSSFASSSASDAS
CCCHHCCCCCCCCCC		23.8623927012
127PhosphorylationPRSSFASSSASDASK
CCHHCCCCCCCCCCC		26.8830278072
128PhosphorylationRSSFASSSASDASKP
CHHCCCCCCCCCCCC		29.3323927012
130PhosphorylationSFASSSASDASKPSS
HCCCCCCCCCCCCCC		35.3423927012
133PhosphorylationSSSASDASKPSSPRG
CCCCCCCCCCCCCCC		50.5222167270
136PhosphorylationASDASKPSSPRGSLL
CCCCCCCCCCCCCEE		57.6322167270
137PhosphorylationSDASKPSSPRGSLLL
CCCCCCCCCCCCEEE		27.4322167270
141PhosphorylationKPSSPRGSLLLDGAG
CCCCCCCCEEECCCC		19.6830266825
155PhosphorylationGAGGAGGSRPCSNRT
CCCCCCCCCCCCCCC		31.9330266825
159PhosphorylationAGGSRPCSNRTSGIS
CCCCCCCCCCCCCCC		31.8430266825
163PhosphorylationRPCSNRTSGISMGYD
CCCCCCCCCCCCCCC		30.7821815630
166PhosphorylationSNRTSGISMGYDQRH
CCCCCCCCCCCCCCC		15.0727251275
169PhosphorylationTSGISMGYDQRHGSP
CCCCCCCCCCCCCCC		10.5621552520
175PhosphorylationGYDQRHGSPLPAGPC
CCCCCCCCCCCCCCC		19.6928731282
195PhosphorylationLAGAPAGYSPGGVPS
CCCCCCCCCCCCCCC		17.5022199227
196PhosphorylationAGAPAGYSPGGVPSA
CCCCCCCCCCCCCCH		19.0225394399
202PhosphorylationYSPGGVPSAYPELHA
CCCCCCCCHHHHHHH		37.7227542207
204PhosphorylationPGGVPSAYPELHAAL
CCCCCCHHHHHHHHH		11.1124211406
215PhosphorylationHAALDRLYAQRPAGF
HHHHHHHHHCCCCCC		11.1128152594
227PhosphorylationAGFGCQESRHSYPPA
CCCCCCCCCCCCCCC		14.9328152594
230PhosphorylationGCQESRHSYPPALGS
CCCCCCCCCCCCCCC		37.9230266825
231PhosphorylationCQESRHSYPPALGSP
CCCCCCCCCCCCCCC		13.7030266825
237PhosphorylationSYPPALGSPGALAGA
CCCCCCCCCCHHCCC		22.4730266825
263PhosphorylationGAQPGRHSVTGYGDC
CCCCCCCCCCCCCCC		21.7323927012
265PhosphorylationQPGRHSVTGYGDCAV
CCCCCCCCCCCCCCC		27.9230266825
267PhosphorylationGRHSVTGYGDCAVGA
CCCCCCCCCCCCCCC		10.6323927012
276PhosphorylationDCAVGARYQDELTAL
CCCCCCHHHHHHHHH		21.5627642862
340UbiquitinationDYFGTCIKCNKGIYG
CCCCCCEECCCCCCC		33.6229967540
346PhosphorylationIKCNKGIYGQSNACQ
EECCCCCCCCCCHHH		20.13-
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
119SPhosphorylationKinaseCDK1P06493
PSP
175SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AJUBA_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 AJUBA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EAA2_HUMANSLC1A2physical
11860269
RARA_HUMANRARAphysical
20133701
RARG_HUMANRARGphysical
20133701
RXRG_HUMANRXRGphysical
20133701
ANM5_HUMANPRMT5physical
18347060
SNAI1_HUMANSNAI1physical
18347060
EGLN2_HUMANEGLN2physical
22286099
EGLN3_HUMANEGLN3physical
22286099
VHL_HUMANVHLphysical
22286099
BUB1B_HUMANBUB1Bphysical
18710370
AURKB_HUMANAURKBphysical
18710370
LATS2_HUMANLATS2physical
16413547
LCK_HUMANLCKphysical
15870274
SQSTM_HUMANSQSTM1physical
15870274
KPCZ_HUMANPRKCZphysical
15870274
TRAF6_HUMANTRAF6physical
15870274
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 AJUBA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, ANDMASS SPECTROMETRY.
"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-119, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.

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