CTNA2_HUMAN - dbPTM
CTNA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTNA2_HUMAN
UniProt AC P26232
Protein Name Catenin alpha-2
Gene Name CTNNA2
Organism Homo sapiens (Human).
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 MTSATSPIILKWDPKSLEIRTLTVERLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGEQIAKESQDLKEELVAAVEDVRKQGETMRIASSEFADDPCSSVKRGTMVRAARALLSAVTRLLILADMADVMRLLSHLKIVEEALEAVKNATNEQDLANRFKEFGKEMVKLNYVAARRQQELKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGISNAAQATSPTDEAKGHTGIGELAAALNEFDNKIILDPMTFSEARFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMNNTGRKEKGDPLNIAIDKMTKKTRDLRRQLRKAVMDHISDSFLETNVPLLVLIEAAKSGNEKEVKEYAQVFREHANKLVEVANLACSISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLTEAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAEMENYEAGVYTEKVLEATKLLSETVMPRFAEQVEVAIEALSANVPQPFEENEFIDASRLVYDGVRDIRKAVLMIRTPEELEDDSDFEQEDYDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEEKAKIAEQVEIFHQEKSKLDAEVAKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVINAAKKIAEAGSRMDKLARAVADQCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELIVSGTGVQSTFTTFYEVDCDVIDGGRASQLSTHLPTCAEGAPIGSGSSDSSMLDSATSLIQAAKNLMNAVVLTVKASYVASTKYQKVYGTAAVNSPVVSWKMKAPEKKPLVKREKPEEFQTRVRRGSQKKHISPVQALSEFKAMDSF
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
2Phosphorylation------MTSATSPII
------CCCCCCCEE		27.3720068231
2 (in isoform 2)Phosphorylation-27.37-
3Phosphorylation-----MTSATSPIIL
-----CCCCCCCEEE		28.4020068231
3 (in isoform 2)Phosphorylation-28.40-
5Phosphorylation---MTSATSPIILKW
---CCCCCCCEEEEC		34.5020068231
6Phosphorylation--MTSATSPIILKWD
--CCCCCCCEEEECC		17.5120068231
6 (in isoform 2)Phosphorylation-17.51-
15 (in isoform 1)Ubiquitination-66.2621906983
15UbiquitinationIILKWDPKSLEIRTL
EEEECCCCCCEEEEE		66.2621890473
16PhosphorylationILKWDPKSLEIRTLT
EEECCCCCCEEEEEE		36.3024719451
33PhosphorylationRLLEPLVTQVTTLVN
HHHHHHHHHHHHHHC		25.6323403867
36PhosphorylationEPLVTQVTTLVNTSN
HHHHHHHHHHHCCCC		12.4728857561
37PhosphorylationPLVTQVTTLVNTSNK
HHHHHHHHHHCCCCC		29.8328857561
41PhosphorylationQVTTLVNTSNKGPSG
HHHHHHCCCCCCCCC		26.6323403867
42 (in isoform 2)Phosphorylation-31.1927251275
42PhosphorylationVTTLVNTSNKGPSGK
HHHHHCCCCCCCCCC		31.1925849741
49 (in isoform 2)Ubiquitination-56.5021906983
80UbiquitinationEKGEQIAKESQDLKE
HHHHHHHHHCHHHHH		60.57-
132PhosphorylationRAARALLSAVTRLLI
HHHHHHHHHHHHHHH		22.8822817900
135PhosphorylationRALLSAVTRLLILAD
HHHHHHHHHHHHHHH		18.4722817900
151PhosphorylationADVMRLLSHLKIVEE
HHHHHHHHHHHHHHH		31.2220068231
151 (in isoform 2)Phosphorylation-31.22-
218PhosphorylationGALKKNATMLYTASQ
HHHHHCHHHEEEHHH		19.6623532336
255PhosphorylationQEAIAGISNAAQATS
HHHHHHHCCHHHCCC		21.3525307156
261PhosphorylationISNAAQATSPTDEAK
HCCHHHCCCCCHHHC		24.1425072903
262 (in isoform 2)Phosphorylation-28.9024719451
262PhosphorylationSNAAQATSPTDEAKG
CCHHHCCCCCHHHCC		28.9015345747
264PhosphorylationAAQATSPTDEAKGHT
HHHCCCCCHHHCCCC		46.3625072903
302PhosphorylationSEARFRPSLEERLES
CCHHCCCCHHHHHHH		44.1220860994
309PhosphorylationSLEERLESIISGAAL
CHHHHHHHHHHHHHH		29.7927251275
320PhosphorylationGAALMADSSCTRDDR
HHHHHCCCCCCCCHH		20.1325850435
321PhosphorylationAALMADSSCTRDDRR
HHHHCCCCCCCCHHH		21.7625850435
322GlutathionylationALMADSSCTRDDRRE
HHHCCCCCCCCHHHH		4.1322555962
323PhosphorylationLMADSSCTRDDRRER
HHCCCCCCCCHHHHH		38.8025850435
415MalonylationSGNEKEVKEYAQVFR
CCCHHHHHHHHHHHH		46.2126320211
415UbiquitinationSGNEKEVKEYAQVFR
CCCHHHHHHHHHHHH		46.21-
417PhosphorylationNEKEVKEYAQVFREH
CHHHHHHHHHHHHHH		9.1628152594
437PhosphorylationEVANLACSISNNEEG
HHHHHHHHCCCCHHH		24.36-
475PhosphorylationTLAARPQSKVAQDNM
HHHHCCCCHHHHCCH		31.6024076635
535PhosphorylationLQEGDVDTLDRTAGA
ECCCCCHHHHHHHHH		30.3324117733
578PhosphorylationLEATKLLSETVMPRF
HHHHHHHCCCCHHHH		41.4825599653
580PhosphorylationATKLLSETVMPRFAE
HHHHHCCCCHHHHHH		20.8025599653
621MethylationRLVYDGVRDIRKAVL
HHHHHHHHHHHHHHH		38.89-
632PhosphorylationKAVLMIRTPEELEDD
HHHHCCCCHHHHCCC		24.9125072903
640 (in isoform 2)Phosphorylation-57.4224719451
640PhosphorylationPEELEDDSDFEQEDY
HHHHCCCCCCCHHHC		57.4222617229
647PhosphorylationSDFEQEDYDVRSRTS
CCCCHHHCCHHCCCC		18.6530177828
651PhosphorylationQEDYDVRSRTSVQTE
HHHCCHHCCCCEECC		39.4919664994
653 (in isoform 2)Phosphorylation-34.20-
653PhosphorylationDYDVRSRTSVQTEDD
HCCHHCCCCEECCCC		34.2029255136
654 (in isoform 2)Phosphorylation-15.89-
654PhosphorylationYDVRSRTSVQTEDDQ
CCHHCCCCEECCCCC		15.8919664994
657PhosphorylationRSRTSVQTEDDQLIA
HCCCCEECCCCCCCC		38.9519664994
667PhosphorylationDQLIAGQSARAIMAQ
CCCCCHHHHHHHHHC		20.8523927012
696UbiquitinationIFHQEKSKLDAEVAK
HHHHHHHHHHHHHHH		62.55-
726PhosphorylationCMIMMEMTDFTRGKG
HHHHHHHCCCCCCCC		18.0424043423
729PhosphorylationMMEMTDFTRGKGPLK
HHHHCCCCCCCCCCC		41.1224043423
738PhosphorylationGKGPLKNTSDVINAA
CCCCCCCHHHHHHHH		25.39-
739PhosphorylationKGPLKNTSDVINAAK
CCCCCCHHHHHHHHH		38.99-
753PhosphorylationKKIAEAGSRMDKLAR
HHHHHHHHHHHHHHH		31.3221406692
768 (in isoform 3)Phosphorylation-57.4022210691
770 (in isoform 3)Phosphorylation-16.3522210691
771 (in isoform 3)Phosphorylation-4.7522210691
778PhosphorylationCKQDLLAYLQRIALY
HHHHHHHHHHHHHHH		11.88-
786 (in isoform 3)Phosphorylation-1.3922210691
853 (in isoform 2)Phosphorylation-32.44-
853PhosphorylationGAPIGSGSSDSSMLD
CCCCCCCCCCHHHHH		32.4415345747
889UbiquitinationASYVASTKYQKVYGT
HHHHHCCCCEEEECC		43.09-
889AcetylationASYVASTKYQKVYGT
HHHHHCCCCEEEECC		43.0919608861
891 (in isoform 2)Phosphorylation-30.2324719451
901PhosphorylationYGTAAVNSPVVSWKM
ECCCCCCCCEEECCC		16.6915345747
939PhosphorylationGSQKKHISPVQALSE
CCCCCCCCHHHHHHH		20.8120886841
945PhosphorylationISPVQALSEFKAMDS
CCHHHHHHHHHHHCC		43.9620860994
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTNA2_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 CTNA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
26344197
PLAK_HUMANJUPphysical
26344197
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 CTNA2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-889, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory