CTNA2_MOUSE - dbPTM
CTNA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTNA2_MOUSE
UniProt AC Q61301
Protein Name Catenin alpha-2
Gene Name Ctnna2
Organism Mus musculus (Mouse).
Sequence Length 953
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm . Cytoplasm, cytoskeleton . Cell junction, adherens junction . Cell projection, axon . Nucleus .
Protein Description May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation..
Protein Sequence MTSATSPIILKWDPKSLEIRTLTVERLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGEQIAKESQDLKEELVAAVEDVRKQGETMRIASSEFADDPCSSVKRGTMVRAARALLSAVTRLLILADMADVMRLLSHLKIVEEALEAVKNATNEQDLANRFKEFGKEMVKLNYVAARRQQELKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGISSAAQATSPTDEAKGHTGIGELAAALNEFDNKIILDPMTFSEARFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMNNTGRKEKGDPLNIAIDKMTKKTRDLRRQLRKAVMDHISDSFLETNVPLLVLIEAAKSGNEKEVKEYAQVFREHANKLVEVANLACSISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLTEAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAEMENYEAGVYTEKVLEATKLLSETVMPRFAEQVEVAIEALSANVPQPFEENEFIDASRLVYDGVRDIRKAVLMIRTPEELEDDSDFEQEDYDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEEKAKIAEQVEIFHQEKSKLDAEVAKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVINAAKKIAEAGSRMDKLARAVADQCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELIVSGTGVQSTFTTFYEVDCDVIDGGRASQLSTHLPTCAEGAPIGSGSSDSSMLDSATSLIQAAKNLMNAVVLTVKASYVASTKYQKVYGTAAVNSPVVSWKMKAPEKKPLVKREKPEEFQTRVRRGSQKKHISPVQALSEFKAMDSF
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------MTSATSPII
------CCCCCCCEE		27.37-
2Phosphorylation------MTSATSPII
------CCCCCCCEE		27.3723527152
2 (in isoform 3)Phosphorylation-27.3720415495
3Phosphorylation-----MTSATSPIIL
-----CCCCCCCEEE		28.4023527152
5Phosphorylation---MTSATSPIILKW
---CCCCCCCEEEEC		34.5017114649
6 (in isoform 3)Phosphorylation-17.5120415495
6Phosphorylation--MTSATSPIILKWD
--CCCCCCCEEEECC		17.5123527152
7 (in isoform 3)Phosphorylation-17.1820415495
8 (in isoform 3)Phosphorylation-6.0420415495
9 (in isoform 3)Phosphorylation-3.5320415495
10 (in isoform 3)Phosphorylation-4.8020415495
11 (in isoform 3)Phosphorylation-38.8620415495
13 (in isoform 3)Phosphorylation-38.8820415495
15UbiquitinationIILKWDPKSLEIRTL
EEEECCCCCCEEEEE		66.2622790023
15 (in isoform 3)Phosphorylation-66.2620415495
15 (in isoform 3)Ubiquitination-66.2622790023
16 (in isoform 3)Phosphorylation-36.3020415495
18 (in isoform 3)Phosphorylation-37.2020415495
19 (in isoform 3)Phosphorylation-5.0320415495
28 (in isoform 3)Ubiquitination-8.80-
33PhosphorylationRLLEPLVTQVTTLVN
HHHHHHHHHHHHHHC		25.6327717184
36PhosphorylationEPLVTQVTTLVNTSN
HHHHHHHHHHHCCCC		12.4727717184
37PhosphorylationPLVTQVTTLVNTSNK
HHHHHHHHHHCCCCC		29.8327717184
41PhosphorylationQVTTLVNTSNKGPSG
HHHHHHCCCCCCCCC		26.6323984901
42PhosphorylationVTTLVNTSNKGPSGK
HHHHHCCCCCCCCCC		31.1923984901
44UbiquitinationTLVNTSNKGPSGKKK
HHHCCCCCCCCCCCC		72.4722790023
44 (in isoform 3)Ubiquitination-72.4722790023
49AcetylationSNKGPSGKKKGRSKK
CCCCCCCCCCCCCCC		56.5015618345
50AcetylationNKGPSGKKKGRSKKA
CCCCCCCCCCCCCCH		65.086569293
51AcetylationKGPSGKKKGRSKKAH
CCCCCCCCCCCCCHH		64.146568981
57 (in isoform 3)Ubiquitination-11.19-
80UbiquitinationEKGEQIAKESQDLKE
HHHHHHHHHCHHHHH		60.5722790023
80 (in isoform 3)Ubiquitination-60.5722790023
93UbiquitinationKEELVAAVEDVRKQG
HHHHHHHHHHHHHHC		4.6827667366
93 (in isoform 3)Ubiquitination-4.68-
221PhosphorylationKKNATMLYTASQAFL
HHCHHHEEEHHHHHH		6.8819854140
224PhosphorylationATMLYTASQAFLRHP
HHHEEEHHHHHHHCC		17.7819854140
255PhosphorylationQEAIAGISSAAQATS
HHHHHHHHHHHHCCC		17.0123335269
256PhosphorylationEAIAGISSAAQATSP
HHHHHHHHHHHCCCC		26.2123335269
261PhosphorylationISSAAQATSPTDEAK
HHHHHHCCCCCCHHC		24.1425521595
262PhosphorylationSSAAQATSPTDEAKG
HHHHHCCCCCCHHCC		28.9025521595
264PhosphorylationAAQATSPTDEAKGHT
HHHCCCCCCHHCCCC		46.3625521595
271PhosphorylationTDEAKGHTGIGELAA
CCHHCCCCCHHHHHH		38.8829899451
302PhosphorylationSEARFRPSLEERLES
CCHHCCCCHHHHHHH		44.1222802335
321PhosphorylationAALMADSSCTRDDRR
HHHHCCCCCCCCHHH		21.7629899451
358UbiquitinationNNTGRKEKGDPLNIA
HHCCCCCCCCHHHHH		72.2022790023
358 (in isoform 3)Ubiquitination-72.2022790023
371UbiquitinationIAIDKMTKKTRDLRR
HHHHHHCHHHHHHHH		48.9627667366
371 (in isoform 3)Ubiquitination-48.96-
415UbiquitinationSGNEKEVKEYAQVFR
CCCHHHHHHHHHHHH		46.2127667366
417PhosphorylationNEKEVKEYAQVFREH
CHHHHHHHHHHHHHH		9.1622499769
428UbiquitinationFREHANKLVEVANLA
HHHHHHHHHHHHHHH		3.8927667366
476UbiquitinationLAARPQSKVAQDNMD
HHHCCCCHHHHCCHH		36.0227667366
489UbiquitinationMDVFKDQWEKQVRVL
HHHHHHHHHHHHHHH		25.5327667366
632PhosphorylationKAVLMIRTPEELEDD
HHHHCCCCHHHHCCC		24.9124925903
640PhosphorylationPEELEDDSDFEQEDY
HHHHCCCCCCCHHHC		57.4225521595
647PhosphorylationSDFEQEDYDVRSRTS
CCCCHHHCCHHCCCC		18.6529899451
651PhosphorylationQEDYDVRSRTSVQTE
HHHCCHHCCCCEECC		39.4925521595
653PhosphorylationDYDVRSRTSVQTEDD
HCCHHCCCCEECCCC		34.2024925903
654PhosphorylationYDVRSRTSVQTEDDQ
CCHHCCCCEECCCCC		15.8924925903
657PhosphorylationRSRTSVQTEDDQLIA
HCCCCEECCCCCCCC		38.9524925903
667PhosphorylationDQLIAGQSARAIMAQ
CCCCCHHHHHHHHHC		20.8525619855
719S-palmitoylationIVLAKQMCMIMMEMT
HHHHHHHHHHHHHHC		1.2228680068
757UbiquitinationEAGSRMDKLARAVAD
HHHHHHHHHHHHHHH		34.4027667366
769PhosphorylationVADQCPDSACKQDLL
HHHHCCCCHHHHHHH		22.2525521595
770UbiquitinationADQCPDSACKQDLLA
HHHCCCCHHHHHHHH		16.3527667366
778PhosphorylationCKQDLLAYLQRIALY
HHHHHHHHHHHHHHH		11.8822668510
785PhosphorylationYLQRIALYCHQLNIC
HHHHHHHHHHHHCCH		4.4722668510
796 (in isoform 3)Ubiquitination-42.4322790023
796 (in isoform 2)Ubiquitination-42.43-
796UbiquitinationLNICSKVKAEVQNLG
HCCHHHHHHHHHHCC		42.4322790023
809 (in isoform 3)Ubiquitination-24.52-
889UbiquitinationASYVASTKYQKVYGT
HHHHHCCCCEEEECC		43.09-
889AcetylationASYVASTKYQKVYGT
HHHHHCCCCEEEECC		43.0922826441
894PhosphorylationSTKYQKVYGTAAVNS
CCCCEEEECCCCCCC		18.7819367708
896PhosphorylationKYQKVYGTAAVNSPV
CCEEEECCCCCCCCE		8.1819367708
901PhosphorylationYGTAAVNSPVVSWKM
ECCCCCCCCEEECCC		16.6925521595
905PhosphorylationAVNSPVVSWKMKAPE
CCCCCEEECCCCCCC		22.6319367708
927PhosphorylationEKPEEFQTRVRRGSQ
CCHHHHHHHHHCCCC		36.1319854140
933PhosphorylationQTRVRRGSQKKHISP
HHHHHCCCCCCCCCH		36.69-
939PhosphorylationGSQKKHISPVQALSE
CCCCCCCCHHHHHHH		20.8125521595
945PhosphorylationISPVQALSEFKAMDS
CCHHHHHHHHHHHCC		43.9624925903
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 CTNA2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTNA2_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 CTNA2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CTNA2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTNA2_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION AT SER-6;SER-640; SER-654 AND THR-657, AND MASS SPECTROMETRY.
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-654, 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-654 AND THR-657, ANDMASS 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 THR-5; THR-261; SER-640 ANDSER-901, AND MASS SPECTROMETRY.
"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 THR-653 AND SER-654, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION AT SER-6;SER-640; SER-654 AND THR-657, AND MASS 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-262; SER-640 ANDSER-901, AND MASS SPECTROMETRY.

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