CXA1_MOUSE - dbPTM
CXA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CXA1_MOUSE
UniProt AC P23242
Protein Name Gap junction alpha-1 protein
Gene Name Gja1
Organism Mus musculus (Mouse).
Sequence Length 382
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell junction, gap junction . Endoplasmic reticulum . Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65.
Protein Description Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. [PubMed: 15181016 Plays an essential role in gap junction communication in the ventricles]
Protein Sequence MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDSQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI
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
5Phosphorylation---MGDWSALGKLLD
---CCCHHHHHHHHH		20.5323737553
9UbiquitinationGDWSALGKLLDKVQA
CCHHHHHHHHHHHHH		46.88-
108UbiquitinationRKEEKLNKKEEELKV
HHHHHHCHHHHHHHH		72.50-
109UbiquitinationKEEKLNKKEEELKVA
HHHHHCHHHHHHHHH		70.10-
114UbiquitinationNKKEEELKVAQTDGV
CHHHHHHHHHHCCCC		38.51-
128UbiquitinationVNVEMHLKQIEIKKF
CCCEEEEEEEEEEEC		34.25-
133UbiquitinationHLKQIEIKKFKYGIE
EEEEEEEEECCCCHH		39.09-
136UbiquitinationQIEIKKFKYGIEEHG
EEEEEECCCCHHHCC		51.99-
137PhosphorylationIEIKKFKYGIEEHGK
EEEEECCCCHHHCCC		26.86-
144UbiquitinationYGIEEHGKVKMRGGL
CCHHHCCCEEECCHH		40.36-
244PhosphorylationKDRVKGRSDPYHATT
HHHHCCCCCCCCCCC		52.1625619855
247PhosphorylationVKGRSDPYHATTGPL
HCCCCCCCCCCCCCC		14.7427742792
250PhosphorylationRSDPYHATTGPLSPS
CCCCCCCCCCCCCCC		20.9725619855
251PhosphorylationSDPYHATTGPLSPSK
CCCCCCCCCCCCCCC		37.2725619855
255PhosphorylationHATTGPLSPSKDCGS
CCCCCCCCCCCCCCC		30.2022729691
257PhosphorylationTTGPLSPSKDCGSPK
CCCCCCCCCCCCCCC		37.4425619855
258UbiquitinationTGPLSPSKDCGSPKY
CCCCCCCCCCCCCCE		61.49-
260S-nitrosylationPLSPSKDCGSPKYAY
CCCCCCCCCCCCEEE		7.1721278135
260S-nitrosocysteinePLSPSKDCGSPKYAY
CCCCCCCCCCCCEEE		7.17-
262PhosphorylationSPSKDCGSPKYAYFN
CCCCCCCCCCEEEEC		25.2625619855
264UbiquitinationSKDCGSPKYAYFNGC
CCCCCCCCEEEECCC		44.18-
265PhosphorylationKDCGSPKYAYFNGCS
CCCCCCCEEEECCCC		15.2116857951
267PhosphorylationCGSPKYAYFNGCSSP
CCCCCEEEECCCCCC		8.4223737553
271S-nitrosocysteineKYAYFNGCSSPTAPL
CEEEECCCCCCCCCC		3.69-
271S-nitrosylationKYAYFNGCSSPTAPL
CEEEECCCCCCCCCC		3.6921071693
272PhosphorylationYAYFNGCSSPTAPLS
EEEECCCCCCCCCCC		40.5323737553
273PhosphorylationAYFNGCSSPTAPLSP
EEECCCCCCCCCCCC		30.2823737553
275PhosphorylationFNGCSSPTAPLSPMS
ECCCCCCCCCCCCCC		42.7423737553
279PhosphorylationSSPTAPLSPMSPPGY
CCCCCCCCCCCCCCC		19.9318776144
282PhosphorylationTAPLSPMSPPGYKLV
CCCCCCCCCCCCEEC		31.1818776144
286PhosphorylationSPMSPPGYKLVTGDR
CCCCCCCCEECCCCC		13.6119060867
287UbiquitinationPMSPPGYKLVTGDRN
CCCCCCCEECCCCCC		42.25-
290PhosphorylationPPGYKLVTGDRNNSS
CCCCEECCCCCCCHH		43.7423737553
296PhosphorylationVTGDRNNSSCRNYNK
CCCCCCCHHCCCCCH		34.0726824392
297PhosphorylationTGDRNNSSCRNYNKQ
CCCCCCHHCCCCCHH		21.1522942356
301PhosphorylationNNSSCRNYNKQASEQ
CCHHCCCCCHHHHHC		12.3723737553
303UbiquitinationSSCRNYNKQASEQNW
HHCCCCCHHHHHCHH		36.56-
306PhosphorylationRNYNKQASEQNWANY
CCCCHHHHHCHHHHH		36.9025521595
313PhosphorylationSEQNWANYSAEQNRM
HHCHHHHHHHHHHCC		11.0820116462
314PhosphorylationEQNWANYSAEQNRMG
HCHHHHHHHHHHCCC		25.7425521595
325PhosphorylationNRMGQAGSTISNSHA
HCCCCCCCCCCCCCC		26.1125521595
326PhosphorylationRMGQAGSTISNSHAQ
CCCCCCCCCCCCCCC		27.7525521595
328PhosphorylationGQAGSTISNSHAQPF
CCCCCCCCCCCCCCC		32.1625521595
330PhosphorylationAGSTISNSHAQPFDF
CCCCCCCCCCCCCCC		17.2625521595
341PhosphorylationPFDFPDDSQNAKKVA
CCCCCCCCCCHHHHH		32.4925619855
345UbiquitinationPDDSQNAKKVAAGHE
CCCCCCHHHHHCCCC		56.16-
346UbiquitinationDDSQNAKKVAAGHEL
CCCCCHHHHHCCCCC		34.39-
364PhosphorylationAIVDQRPSSRASSRA
EEECCCCCCCHHHCC		34.3525521595
365PhosphorylationIVDQRPSSRASSRAS
EECCCCCCCHHHCCC		34.2525521595
368PhosphorylationQRPSSRASSRASSRP
CCCCCCHHHCCCCCC		21.1725521595
369PhosphorylationRPSSRASSRASSRPR
CCCCCHHHCCCCCCC		30.7725521595
372PhosphorylationSRASSRASSRPRPDD
CCHHHCCCCCCCCCC		26.2724925903
373PhosphorylationRASSRASSRPRPDDL
CHHHCCCCCCCCCCC		45.3725263469
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
255SPhosphorylationKinaseMAPK1P63085
GPS
279SPhosphorylationKinaseCDK5Q00535
PSP
279SPhosphorylationKinaseCDK5P49615
PSP
279SPhosphorylationKinaseERK2P63085
PSP
279SPhosphorylationKinaseERK1Q63844
PSP
282SPhosphorylationKinaseCDK5Q00535
PSP
282SPhosphorylationKinaseCDK5P49615
PSP
282SPhosphorylationKinaseERK2P63085
PSP
282SPhosphorylationKinaseERK1Q63844
PSP
328SPhosphorylationKinaseCK1-FAMILY-GPS
330SPhosphorylationKinaseCK1-FAMILY-GPS
368SPhosphorylationKinasePRKCDP28867
Uniprot
368SPhosphorylationKinasePRKCGP63318
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
271CS-nitrosylation

21071693
325SPhosphorylation

21183079
328SPhosphorylation

21183079
330SPhosphorylation

21183079
368SPhosphorylation

21183079
368SPhosphorylation

21183079
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 CXA1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_MOUSETsg101physical
19210987
MLP3A_MOUSEMap1lc3aphysical
25605500
NBR1_MOUSENbr1physical
25605500
SQSTM_MOUSESqstm1physical
25605500
EPS15_MOUSEEps15physical
25605500
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CXA1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-314; THR-326;SER-328 AND SER-330, AND MASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247 AND TYR-313, ANDMASS SPECTROMETRY.

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