CTNA1_MOUSE - dbPTM
CTNA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTNA1_MOUSE
UniProt AC P26231
Protein Name Catenin alpha-1
Gene Name Ctnna1
Organism Mus musculus (Mouse).
Sequence Length 906
Subcellular Localization Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cell junction. Found at cell-cell boundaries and probably at cell-matrix boundaries.
Protein Description Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation..
Protein Sequence MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVVAVEDVRKQGDLMKSAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGNRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDAAQHQGGSGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
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
2Acetylation------MTAVHAGNI
------CCCEECCCC		37.07-
2Phosphorylation------MTAVHAGNI
------CCCEECCCC		37.0728576409
12UbiquitinationHAGNINFKWDPKSLE
ECCCCCCCCCCCCHH		46.3122790023
16UbiquitinationINFKWDPKSLEIRTL
CCCCCCCCCHHHHHH		66.2622790023
34PhosphorylationRLLEPLVTQVTTLVN
HHHHHHHHHHHHHHC		25.6327717184
37PhosphorylationEPLVTQVTTLVNTNS
HHHHHHHHHHHCCCC		12.4727717184
38PhosphorylationPLVTQVTTLVNTNSK
HHHHHHHHHHCCCCC		29.8327717184
42PhosphorylationQVTTLVNTNSKGPSN
HHHHHHCCCCCCCCC		33.1329514104
44PhosphorylationTTLVNTNSKGPSNKK
HHHHCCCCCCCCCCC		36.6328978645
45UbiquitinationTLVNTNSKGPSNKKR
HHHCCCCCCCCCCCC		76.5322790023
48PhosphorylationNTNSKGPSNKKRGRS
CCCCCCCCCCCCCCC		70.7029514104
50UbiquitinationNSKGPSNKKRGRSKK
CCCCCCCCCCCCCCH		48.46-
57UbiquitinationKKRGRSKKAHVLAAS
CCCCCCCHHHHHHHH		45.0022790023
75UbiquitinationATENFLEKGDKIAKE
HHHHHHHHHHHHHHH		74.6522790023
81UbiquitinationEKGDKIAKESQFLKE
HHHHHHHHHHHHHHH		62.4622790023
116S-palmitoylationGEFADDPCSSVKRGN
CCCCCCCCHHHHHHH		6.4428526873
117PhosphorylationEFADDPCSSVKRGNM
CCCCCCCHHHHHHHH		43.4825338131
118PhosphorylationFADDPCSSVKRGNMV
CCCCCCHHHHHHHHH		38.0725195567
163UbiquitinationVVEDGILKLRNAGNE
CCCCCEEEECCCCCC		43.4022790023
177PhosphorylationEQDLGIQYKALKPEV
CCCCCCCHHHHCHHH		9.0525619855
178UbiquitinationQDLGIQYKALKPEVD
CCCCCCHHHHCHHHH		30.7622790023
181UbiquitinationGIQYKALKPEVDKLN
CCCHHHHCHHHHHHH		43.9522790023
186AcetylationALKPEVDKLNIMAAK
HHCHHHHHHHHHHHH		48.9223864654
193AcetylationKLNIMAAKRQQELKD
HHHHHHHHHHHHHHC		41.0023236377
193UbiquitinationKLNIMAAKRQQELKD
HHHHHHHHHHHHHHC		41.0022790023
216UbiquitinationAARGILQKNVPILYT
HHHHHHHHCCCEEEE		57.3722790023
225PhosphorylationVPILYTASQACLQHP
CCEEEECCHHHHHCC		15.5430352176
245PhosphorylationKANRDLIYKQLQQAV
HHCHHHHHHHHHHHH		10.4429514104
264PhosphorylationNAAQATASDDAAQHQ
HHHHHHCCCHHHHHC		31.5030352176
274PhosphorylationAAQHQGGSGGELAYA
HHHHCCCCHHHHHHH		50.9130352176
280PhosphorylationGSGGELAYALNNFDK
CCHHHHHHHHCCCCC		25.0126824392
295PhosphorylationQIIVDPLSFSEERFR
CEEECCCCCCHHHHC		31.9230352176
297PhosphorylationIVDPLSFSEERFRPS
EECCCCCCHHHHCCC		34.8630352176
304PhosphorylationSEERFRPSLEERLES
CHHHHCCCHHHHHHH		44.1222802335
323PhosphorylationAALMADSSCTRDDRR
HHHHCCCCCCCCHHH		21.7629899451
337GlutathionylationRERIVAECNAVRQAL
HHHHHHHHHHHHHHH		2.6024333276
391PhosphorylationKAVMDHVSDSFLETN
HHHHHHCCHHHHHCC		24.9023984901
393PhosphorylationVMDHVSDSFLETNVP
HHHHCCHHHHHCCCC		24.9923984901
397PhosphorylationVSDSFLETNVPLLVL
CCHHHHHCCCCEEHH		43.6023984901
417UbiquitinationNGNEKEVKEYAQVFR
CCCHHHHHHHHHHHH		46.2122790023
419PhosphorylationNEKEVKEYAQVFREH
CHHHHHHHHHHHHHH		9.1622499769
438GlutathionylationIEVANLACSISNNEE
HHHHHHHHHCCCCHH		4.1224333276
439PhosphorylationEVANLACSISNNEEG
HHHHHHHHCCCCHHH		24.3626824392
453PhosphorylationGVKLVRMSASQLEAL
HHEEEEECHHHHHHH		17.7626160508
455PhosphorylationKLVRMSASQLEALCP
EEEEECHHHHHHHHH		28.1726160508
461GlutathionylationASQLEALCPQVINAA
HHHHHHHHHHHHHHH		2.6024333276
478UbiquitinationLAAKPQSKLAQENMD
HHHCCHHHHHHHCHH		42.4622790023
499PhosphorylationEKQVRVLTDAVDDIT
HHHHHHHHHCCCCCC		21.0326239621
506PhosphorylationTDAVDDITSIDDFLA
HHCCCCCCCHHHHHH		26.9923984901
507PhosphorylationDAVDDITSIDDFLAV
HCCCCCCCHHHHHHH		25.1026824392
515PhosphorylationIDDFLAVSENHILED
HHHHHHHCCHHHHHH		27.3726370283
571UbiquitinationEPGVYTEKVLEATKL
CCCCCHHHHHHHHHH		44.3022790023
576PhosphorylationTEKVLEATKLLSNTV
HHHHHHHHHHHCCCC		16.9228059163
577UbiquitinationEKVLEATKLLSNTVM
HHHHHHHHHHCCCCC		55.2522790023
619PhosphorylationIDASRLVYDGIRDIR
CCHHHHHHHHHHHHH		17.0325263469
634PhosphorylationKAVLMIRTPEELDDS
HHHHCCCCHHHCCCC		24.9125521595
641PhosphorylationTPEELDDSDFETEDF
CHHHCCCCCCCCCCC		43.8127087446
645PhosphorylationLDDSDFETEDFDVRS
CCCCCCCCCCCCCCC		40.6324925903
652PhosphorylationTEDFDVRSRTSVQTE
CCCCCCCCCCCEECC		39.4927087446
654PhosphorylationDFDVRSRTSVQTEDD
CCCCCCCCCEECCCC		34.2027087446
655PhosphorylationFDVRSRTSVQTEDDQ
CCCCCCCCEECCCCC		15.8927087446
658PhosphorylationRSRTSVQTEDDQLIA
CCCCCEECCCCCCCC		38.9524925903
668PhosphorylationDQLIAGQSARAIMAQ
CCCCCHHHHHHHHHC		20.8525619855
681UbiquitinationAQLPQEQKAKIAEQV
HCCCHHHHHHHHHHH		51.3922790023
683UbiquitinationLPQEQKAKIAEQVAS
CCHHHHHHHHHHHHH		49.8622790023
690PhosphorylationKIAEQVASFQEEKSK
HHHHHHHHHHHHHHH		28.7130352176
695UbiquitinationVASFQEEKSKLDAEV
HHHHHHHHHHHHHHH		52.7322790023
695AcetylationVASFQEEKSKLDAEV
HHHHHHHHHHHHHHH		52.7323236377
697UbiquitinationSFQEEKSKLDAEVSK
HHHHHHHHHHHHHHH		62.5522790023
704UbiquitinationKLDAEVSKWDDSGND
HHHHHHHHCCCCCCH		60.8722790023
720S-palmitoylationIVLAKQMCMIMMEMT
HHHHHHHHHHHHHHC		1.2228680068
737UbiquitinationTRGKGPLKNTSDVIS
CCCCCCCCCHHHHHH		62.4022790023
747MalonylationSDVISAAKKIAEAGS
HHHHHHHHHHHHHHH		44.4126320211
747SuccinylationSDVISAAKKIAEAGS
HHHHHHHHHHHHHHH		44.4123954790
779PhosphorylationCKQDLLAYLQRIALY
HHHHHHHHHHHHHHH		11.8822668510
786PhosphorylationYLQRIALYCHQLNIC
HHHHHHHHHHHHCCH		4.4722668510
797UbiquitinationLNICSKVKAEVQNLG
HCCHHHHHHHHHHCC		42.4322790023
842UbiquitinationASYVASTKYQKSQGM
HHHHHCCCCCCCCCC		43.09-
842AcetylationASYVASTKYQKSQGM
HHHHHCCCCCCCCCC		43.0922647165
842MalonylationASYVASTKYQKSQGM
HHHHHCCCCCCCCCC		43.0926320211
845UbiquitinationVASTKYQKSQGMASL
HHCCCCCCCCCCCCC		41.4722790023
851PhosphorylationQKSQGMASLNLPAVS
CCCCCCCCCCCCHHC		14.65-
858PhosphorylationSLNLPAVSWKMKAPE
CCCCCHHCCCCCCCC		24.08-
860UbiquitinationNLPAVSWKMKAPEKK
CCCHHCCCCCCCCCC		24.0222790023
886PhosphorylationQTKIKRASQKKHVNP
HHHHHHHHHCCCCCH		46.71-
898PhosphorylationVNPVQALSEFKAMDS
CCHHHHHHHHHHHCC		43.9619367708
905PhosphorylationSEFKAMDSI------
HHHHHHCCC------		19.6727357545
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 CTNA1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTNA1_MOUSE !!
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 CTNA1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_MOUSECtnnb1physical
12695331
FMN1_MOUSEFmn1physical
14647292
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTNA1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-654; SER-655 ANDTHR-658, AND MASS SPECTROMETRY.
"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-641, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 AND SER-655, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; THR-654 ANDTHR-658, AND MASS SPECTROMETRY.

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