CTNA3_HUMAN - dbPTM
CTNA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTNA3_HUMAN
UniProt AC Q9UI47
Protein Name Catenin alpha-3
Gene Name CTNNA3 {ECO:0000312|EMBL:AAF21801.1, ECO:0000312|HGNC:HGNC:2511}
Organism Homo sapiens (Human).
Sequence Length 895
Subcellular Localization Cytoplasm, cytoskeleton . Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2.
Protein Description May be involved in formation of stretch-resistant cell-cell adhesion complexes..
Protein Sequence MSAETPITLNIDPQDLQVQTFTVEKLLEPLIIQVTTLVNCPQNPSSRKKGRSKRASVLLASVEEATWNLLDKGEKIAQEATVLKDELTASLEEVRKESEALKVSAERFTDDPCFLPKREAVVQAARALLAAVTRLLILADMIDVMCLLQHVSAFQRTFESLKNVANKSDLQKTYQKLGKELENLDYLAFKRQQDLKSPNQRDEIAGARASLKENSPLLHSICSACLEHSDVASLKASKDTVCEEIQNALNVISNASQGIQNMTTPPEPQAATLGSALDELENLIVLNPLTVTEEEIRPSLEKRLEAIISGAALLADSSCTRDLHRERIIAECNAIRQALQDLLSEYMNNAGKKERSNTLNIALDNMCKKTRDLRRQLRKAIIDHVSDSFLDTTVPLLVLIEAAKNGREKEIKEYAAIFHEHTSRLVEVANLACSMSTNEDGIKIVKIAANHLETLCPQIINAALALAARPKSQAVKNTMEMYKRTWENHIHVLTEAVDDITSIDDFLAVSESHILEDVNKCIIALRDQDADNLDRAAGAIRGRAARVAHIVTGEMDSYEPGAYTEGVMRNVNFLTSTVIPEFVTQVNVALEALSKSSLNVLDDNQFVDISKKIYDTIHDIRCSVMMIRTPEELEDVSDLEEEHEVRSHTSIQTEGKTDRAKMTQLPEAEKEKIAEQVADFKKVKSKLDAEIEIWDDTSNDIIVLAKNMCMIMMEMTDFTRGKGPLKHTTDVIYAAKMISESGSRMDVLARQIANQCPDPSCKQDLLAYLEQIKFYSHQLKICSQVKAEIQNLGGELIMSALDSVTSLIQAAKNLMNAVVQTVKMSYIASTKIIRIQSPAGPRHPVVMWRMKAPAKKPLIKREKPEETCAAVRRGSAKKKIHPLQVMSEFRGRQIY
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
56PhosphorylationKGRSKRASVLLASVE
CCCCHHHHHHHHHHH		19.8224275569
117AcetylationDDPCFLPKREAVVQA
CCCCCCCHHHHHHHH		66.0830587927
160PhosphorylationAFQRTFESLKNVANK
HHHHHHHHHHHHCCH		40.22-
174PhosphorylationKSDLQKTYQKLGKEL
HHHHHHHHHHHHHHH		15.6418452278
186PhosphorylationKELENLDYLAFKRQQ
HHHHHHHHHHHHCHH		11.77-
190AcetylationNLDYLAFKRQQDLKS
HHHHHHHHCHHCCCC		43.6330587933
356PhosphorylationNAGKKERSNTLNIAL
HCCHHHHHCHHHHHH		34.9518491316
502PhosphorylationEAVDDITSIDDFLAV
HHHCCCCCHHHHHHC		25.1024275569
552PhosphorylationARVAHIVTGEMDSYE
HHEEEHHHCCCCCCC		27.16-
614PhosphorylationVDISKKIYDTIHDIR
CCHHHHHHHHHHHHH		18.86-
629PhosphorylationCSVMMIRTPEELEDV
CEEEEECCHHHHCCC		24.9126437602
637PhosphorylationPEELEDVSDLEEEHE
HHHHCCCCCCCHHHH		49.1228348404
647PhosphorylationEEEHEVRSHTSIQTE
CHHHHHHCCCCCCCC		35.9723312004
649PhosphorylationEHEVRSHTSIQTEGK
HHHHHCCCCCCCCCC		28.8623312004
650PhosphorylationHEVRSHTSIQTEGKT
HHHHCCCCCCCCCCC		13.7922798277
653PhosphorylationRSHTSIQTEGKTDRA
HCCCCCCCCCCCCHH		45.0623312004
657PhosphorylationSIQTEGKTDRAKMTQ
CCCCCCCCCHHHHHC		41.39-
663PhosphorylationKTDRAKMTQLPEAEK
CCCHHHHHCCCHHHH		26.67-
681AcetylationAEQVADFKKVKSKLD
HHHHHCHHHHHHHCC		58.1530587945
682AcetylationEQVADFKKVKSKLDA
HHHHCHHHHHHHCCC		55.6930587939
739O-linked_GlycosylationIYAAKMISESGSRMD
HHHHHHHHCCCCHHH		23.3930379171
783PhosphorylationSHQLKICSQVKAEIQ
HHHHHHHHHHHHHHH		41.2926091039
799PhosphorylationLGGELIMSALDSVTS
CCHHHHHHHHHHHHH		20.7722210691
803PhosphorylationLIMSALDSVTSLIQA
HHHHHHHHHHHHHHH		28.3022210691
837PhosphorylationTKIIRIQSPAGPRHP
CEEEEECCCCCCCCC		17.8526437602
860AcetylationPAKKPLIKREKPEET
CCCCCCCCCCCHHHH		63.2991121
867PhosphorylationKREKPEETCAAVRRG
CCCCHHHHHHHHHCC		13.0420068231
895PhosphorylationEFRGRQIY-------
HHCCCCCC-------		12.26-
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 CTNA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTNA3_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 CTNA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
11590244
CTNA1_HUMANCTNNA1physical
23718855
PLAK_HUMANJUPphysical
23718855
EPS8_HUMANEPS8physical
21988832
CTNB1_HUMANCTNNB1physical
25241761
CADH3_HUMANCDH3physical
28514442
CAD12_HUMANCDH12physical
28514442
CADH1_HUMANCDH1physical
28514442
APC_HUMANAPCphysical
28514442
CAD24_HUMANCDH24physical
28514442
GO45_HUMANBLZF1physical
28514442
CAD10_HUMANCDH10physical
28514442
ARVC_HUMANARVCFphysical
28514442
PKP4_HUMANPKP4physical
28514442
CADH4_HUMANCDH4physical
28514442
CNBP1_HUMANCTNNBIP1physical
28514442
OSBL1_HUMANOSBPL1Aphysical
28514442
CTNB1_HUMANCTNNB1physical
28514442
VMA21_HUMANVMA21physical
28514442
RELL1_HUMANRELL1physical
28514442
CADH2_HUMANCDH2physical
28514442
GIMA8_HUMANGIMAP8physical
28514442
CTND1_HUMANCTNND1physical
28514442
AMER1_HUMANAMER1physical
28514442
F162A_HUMANFAM162Aphysical
28514442
AAPK2_HUMANPRKAA2physical
28514442
MYCB2_HUMANMYCBP2physical
28514442
ATPB_HUMANATP5Bphysical
28514442
TPD52_HUMANTPD52physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615616Arrhythmogenic right ventricular dysplasia, familial, 13 (ARVD13)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTNA3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, 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 THR-867, AND MASSSPECTROMETRY.

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