CTNB1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CTNB1_RAT
• UniProt AC: Q9WU82
• Protein Name: Catenin beta-1
• Gene Name: Ctnnb1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 781
• Subcellular Localization: Cytoplasm . Nucleus . Cytoplasm, cytoskeleton . Cell junction, adherens junction . Cell junction . Cell membrane . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cell junction, synapse . Cytopl
• Protein Description: Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity)..
• Protein Sequence: MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGPHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL

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
2	Acetylation	------MATQADLME ------CCCHHHHHH	14.39	-
23	O-linked_Glycosylation	PDRKAAVSHWQQQSY CCHHHHHHHHHHHHH	17.80	-
23	Phosphorylation	PDRKAAVSHWQQQSY CCHHHHHHHHHHHHH	17.80	-
29	Phosphorylation	VSHWQQQSYLDSGIH HHHHHHHHHHCCCCC	24.27	-
33	Phosphorylation	QQQSYLDSGIHSGAT HHHHHHCCCCCCCCC	36.73	15064718
37	Phosphorylation	YLDSGIHSGATTTAP HHCCCCCCCCCCCCC	28.36	15064718
40	Phosphorylation	SGIHSGATTTAPSLS CCCCCCCCCCCCCCC	28.36	30181290
41	Phosphorylation	GIHSGATTTAPSLSG CCCCCCCCCCCCCCC	22.04	15064718
42	Phosphorylation	IHSGATTTAPSLSGK CCCCCCCCCCCCCCC	32.01	28432305
45	Phosphorylation	GATTTAPSLSGKGNP CCCCCCCCCCCCCCC	32.48	15064718
47	Phosphorylation	TTTAPSLSGKGNPEE CCCCCCCCCCCCCCH	42.68	28432305
49	Acetylation	TAPSLSGKGNPEEED CCCCCCCCCCCCHHC	52.73	-
64	Phosphorylation	VDTSQVLYEWEQGFS CCHHHHHHHHHHCCC	21.82	-
86	Phosphorylation	VADIDGQYAMTRAQR HCCCCCHHHHHHHHH	12.13	-
142	Phosphorylation	AVVNLINYQDDAELA HHHHHHCCCCHHHHH	13.31	22817900
179	Phosphorylation	AVMVHQLSKKEASRH HHHHHHCCHHHHHHH	34.80	27097102
191	Phosphorylation	SRHAIMRSPQMVSAI HHHHHHHCHHHHHHH	11.34	23712012
196	Phosphorylation	MRSPQMVSAIVRTMQ HHCHHHHHHHHHHHC	13.61	25575281
246	Phosphorylation	ALVKMLGSPVDSVLF HHHHHHCCCHHHHHH	20.14	-
331	Phosphorylation	LVNIMRTYTYEKLLW HHHHHHHCCHHHHHH	9.28	-
333	Phosphorylation	NIMRTYTYEKLLWTT HHHHHCCHHHHHHHH	10.72	24972320
489	Phosphorylation	QNAVRLHYGLPVVVK HHHHHHHHCCCEEEH	25.58	-
551	Phosphorylation	HQDTQRRTSMGGTQQ CHHHHHHHCCCCHHH	25.84	23712012
552	Phosphorylation	QDTQRRTSMGGTQQQ HHHHHHHCCCCHHHH	17.39	23712012
556	Phosphorylation	RRTSMGGTQQQFVEG HHHCCCCHHHHHHCC	19.92	23712012
619	S-nitrosocysteine	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	-
619	S-nitrosylation	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	-
654	Phosphorylation	RNEGVATYAAAVLFR CCHHHHHHHHHHHHH	5.63	12123611
675	Phosphorylation	QDYKKRLSVELTSSL CCHHHHHHHHHHHHH	19.99	23712012
679	Phosphorylation	KRLSVELTSSLFRTE HHHHHHHHHHHHHCC	11.63	22108457
680	Phosphorylation	RLSVELTSSLFRTEP HHHHHHHHHHHHCCC	37.35	22108457
681	Phosphorylation	LSVELTSSLFRTEPM HHHHHHHHHHHCCCC	26.71	22108457

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
23	S	Phosphorylation	Kinase	GSK3-BETA	P18266	Uniprot
29	S	Phosphorylation	Kinase	GSK3-BETA	P18266	Uniprot
33	S	Phosphorylation	Kinase	CDK2	P24941	PSP
33	S	Phosphorylation	Kinase	HIPK2	-	Uniprot
33	S	Phosphorylation	Kinase	GSK3B	P18266	PSP
33	S	Phosphorylation	Kinase	CDK2	P97377	PSP
37	S	Phosphorylation	Kinase	CDK2	P97377	PSP
37	S	Phosphorylation	Kinase	HIPK2	-	Uniprot
37	S	Phosphorylation	Kinase	CDK2	P24941	PSP
37	S	Phosphorylation	Kinase	GSK3B	P18266	PSP
41	T	Phosphorylation	Kinase	CDK2	P97377	PSP
41	T	Phosphorylation	Kinase	CDK2	P24941	PSP
41	T	Phosphorylation	Kinase	GSK3B	P18266	PSP
45	S	Phosphorylation	Kinase	CDK2	P24941	PSP
45	S	Phosphorylation	Kinase	CDK2	P97377	PSP
45	S	Phosphorylation	Kinase	GSK3B	P18266	PSP
45	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
64	Y	Phosphorylation	Kinase	PTK6	-	Uniprot
86	Y	Phosphorylation	Kinase	CSK	P32577	Uniprot
142	Y	Phosphorylation	Kinase	PTK6	-	Uniprot
142	Y	Phosphorylation	Kinase	FYN	Q62844	Uniprot
246	S	Phosphorylation	Kinase	CDK5	Q03114	Uniprot
654	Y	Phosphorylation	Kinase	CSK	P32577	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
23	S	Glycosylation	O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.	-
33	S	Phosphorylation	Phosphorylated on Ser-33 and Ser-37 by HIPK2; this phosphorylation triggers proteasomal degradation.	-
33	S	Phosphorylation	Phosphorylation proceeds then from Thr-41 to Ser-33.	-
37	S	Phosphorylation	Phosphorylated on Ser-33 and Ser-37 by HIPK2; this phosphorylation triggers proteasomal degradation.	-
41	T	Phosphorylation	Phosphorylation proceeds then from Thr-41 to Ser-33.	-
45	S	Phosphorylation	Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase.	-
49	K	Acetylation	Deacetylated at Lys-49 by SIRT1.	-
191	S	Phosphorylation	Phosphorylation on Ser-191 and Ser-246 by CDK5.	22673903
246	S	Phosphorylation	Phosphorylation on Ser-191 and Ser-246 by CDK5.	-
552	S	Phosphorylation	Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription.	22673903
619	C	S-nitrosylation	S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CTNB1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APC_RAT	Apc	physical	20623542
UBC_RAT	Ubc	physical	15371442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-675, ANDMASS SPECTROMETRY.
PubMed: 16396499