dbPTM

CTNB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CTNB1_MOUSE
UniProt AC	Q02248
Protein Name	Catenin beta-1
Gene Name	Ctnnb1
Organism	Mus musculus (Mouse).
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 . Cytoplasm
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 (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle. [PubMed: 21325504]
Protein Sequence	MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATQADLME ------CCCHHHHHH	14.39	-
19	Ubiquitination	MAMEPDRKAAVSHWQ HCCCCCHHHHHHHHH	48.34	22790023
23	O-linked_Glycosylation	PDRKAAVSHWQQQSY CCHHHHHHHHHHHHH	17.80	-
23	Phosphorylation	PDRKAAVSHWQQQSY CCHHHHHHHHHHHHH	17.80	12027456
29	Phosphorylation	VSHWQQQSYLDSGIH HHHHHHHHHHCCCCC	24.27	9233789
33	Phosphorylation	QQQSYLDSGIHSGAT HHHHHHCCCCCCCCC	36.73	19303846
37	Phosphorylation	YLDSGIHSGATTTAP HHCCCCCCCCCCCCC	28.36	15308623
40	Phosphorylation	SGIHSGATTTAPSLS CCCCCCCCCCCCCCC	28.36	29899451
41	Phosphorylation	GIHSGATTTAPSLSG CCCCCCCCCCCCCCC	22.04	19303846
45	Phosphorylation	GATTTAPSLSGKGNP CCCCCCCCCCCCCCC	32.48	9233789
47	Phosphorylation	TTTAPSLSGKGNPEE CCCCCCCCCCCCCCH	42.68	21082442
49	Acetylation	TAPSLSGKGNPEEED CCCCCCCCCCCCHHC	52.73	60093
59	Phosphorylation	PEEEDVDTSQVLYEW CCHHCCCHHHHHHHH	22.40	23649490
60	Phosphorylation	EEEDVDTSQVLYEWE CHHCCCHHHHHHHHH	17.52	23649490
64	Phosphorylation	VDTSQVLYEWEQGFS CCHHHHHHHHHHCCC	21.82	-
73	Phosphorylation	WEQGFSQSFTQEQVA HHHCCCCCCCHHHHC	29.12	23649490
86	Phosphorylation	VADIDGQYAMTRAQR HCCCCCHHHHHHHHH	12.13	22817900
133	Ubiquitination	AEPSQMLKHAVVNLI CCHHHHHHHHHHHHH	24.95	22790023
142	Phosphorylation	AVVNLINYQDDAELA HHHHHHCCCCHHHHH	13.31	22817900
158	Ubiquitination	RAIPELTKLLNDEDQ HHHHHHHHHCCCCCC	64.70	22790023
170	Ubiquitination	EDQVVVNKAAVMVHQ CCCHHHHHHHHHHHH	26.55	22790023
179	Phosphorylation	AVMVHQLSKKEASRH HHHHHHCCHHHHHHH	34.80	29472430
180	Ubiquitination	VMVHQLSKKEASRHA HHHHHCCHHHHHHHH	64.32	27667366
191	Phosphorylation	SRHAIMRSPQMVSAI HHHHHHHCHHHHHHH	11.34	25521595
194	Oxidation	AIMRSPQMVSAIVRT HHHHCHHHHHHHHHH	2.67	17242355
201	Phosphorylation	MVSAIVRTMQNTNDV HHHHHHHHHCCCCCH	16.53	30165576
205	Phosphorylation	IVRTMQNTNDVETAR HHHHHCCCCCHHHHH	18.86	30165576
210	Phosphorylation	QNTNDVETARCTAGT CCCCCHHHHHHCHHH	21.17	30165576
213	S-nitrosocysteine	NDVETARCTAGTLHN CCHHHHHHCHHHHHH	2.58	-
213	S-nitrosylation	NDVETARCTAGTLHN CCHHHHHHCHHHHHH	2.58	20925432
222	Phosphorylation	AGTLHNLSHHREGLL HHHHHHHHHCCCCHH	23.67	-
233	Ubiquitination	EGLLAIFKSGGIPAL CCHHHHHHCCCHHHH	41.92	22790023
246	Phosphorylation	ALVKMLGSPVDSVLF HHHHHHCCCHHHHHH	20.14	-
331	Phosphorylation	LVNIMRTYTYEKLLW HHHHHHHCCHHHHHH	9.28	-
333	Phosphorylation	NIMRTYTYEKLLWTT HHHHHCCHHHHHHHH	10.72	-
381	Glutathionylation	SQRLVQNCLWTLRNL HHHHHHHHHHHHHHH	1.55	24333276
381	S-palmitoylation	SQRLVQNCLWTLRNL HHHHHHHHHHHHHHH	1.55	28526873
393	Phosphorylation	RNLSDAATKQEGMEG HHHHHHHHHHHHHHH	34.67	22817900
461	Phosphorylation	AGDREDITEPAICAL CCCCCCCCHHHHHHH	48.51	29895711
466	S-palmitoylation	DITEPAICALRHLTS CCCHHHHHHHHHHHH	2.95	28526873
489	Phosphorylation	QNAVRLHYGLPVVVK HHHHHHHHCCCEEEH	25.58	20116462
520	Glutathionylation	LIRNLALCPANHAPL HHHHHHHCCCCCHHH	2.19	24333276
520	S-palmitoylation	LIRNLALCPANHAPL HHHHHHHCCCCCHHH	2.19	28526873
547	Phosphorylation	LVRAHQDTQRRTSMG HHHHCHHHHHHHCCC	19.87	29899451
551	Phosphorylation	HQDTQRRTSMGGTQQ CHHHHHHHCCCCHHH	25.84	27087446
552	Phosphorylation	QDTQRRTSMGGTQQQ HHHHHHHCCCCHHHH	17.39	27087446
553	Oxidation	DTQRRTSMGGTQQQF HHHHHHCCCCHHHHH	5.92	17242355
556	Phosphorylation	RRTSMGGTQQQFVEG HHHCCCCHHHHHHCC	19.92	25521595
573	S-palmitoylation	MEEIVEGCTGALHIL HHHHHCHHCHHHHHH	1.69	28526873
573	Glutathionylation	MEEIVEGCTGALHIL HHHHHCHHCHHHHHH	1.69	24333276
605	Phosphorylation	LFVQLLYSPIENIQR HHHHHHHCCCHHHHH	21.26	22817900
619	S-palmitoylation	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	28526873
619	Glutathionylation	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	24333276
619	S-nitrosylation	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	20705246
619	S-nitrosocysteine	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	-
625	Ubiquitination	LCELAQDKEAAEAIE HHHHHCCHHHHHHHH	36.85	-
653	Phosphorylation	SRNEGVATYAAAVLF HCCHHHHHHHHHHHH	15.99	22817900
654	Phosphorylation	RNEGVATYAAAVLFR CCHHHHHHHHHHHHH	5.63	22203675
670	Phosphorylation	SEDKPQDYKKRLSVE CCCCCCCHHHHHHHH	17.11	29514104
671	Ubiquitination	EDKPQDYKKRLSVEL CCCCCCHHHHHHHHH	39.44	22790023
675	Phosphorylation	QDYKKRLSVELTSSL CCHHHHHHHHHHHHH	19.99	25521595
679	Phosphorylation	KRLSVELTSSLFRTE HHHHHHHHHHHHHCC	11.63	22817900
680	Phosphorylation	RLSVELTSSLFRTEP HHHHHHHHHHHHCCC	37.35	27087446
681	Phosphorylation	LSVELTSSLFRTEPM HHHHHHHHHHHCCCC	26.71	21183079
685	Phosphorylation	LTSSLFRTEPMAWNE HHHHHHHCCCCCCCC	36.79	-
693	Phosphorylation	EPMAWNETADLGLDI CCCCCCCCCCCCCCC	23.43	-

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	Q9WV60	Uniprot
29	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
33	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
33	S	Phosphorylation	Kinase	HIPK2	Q9QZR5	Uniprot
33	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
37	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
37	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
37	S	Phosphorylation	Kinase	HIPK2	Q9QZR5	Uniprot
41	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
41	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
41	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
45	S	Phosphorylation	Kinase	PRKCZ	Q02956	GPS
45	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
45	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
45	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
45	S	Phosphorylation	Kinase	CSNK1A1	Q8BK63	GPS
45	S	Phosphorylation	Kinase	CK1D	Q9DC28	PSP
47	S	Phosphorylation	Kinase	CK1D	Q9DC28	PSP
47	S	Phosphorylation	Kinase	CK1D	P48730	PSP
64	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
86	Y	Phosphorylation	Kinase	CSK	P41241	Uniprot
86	Y	Phosphorylation	Kinase	SRC	P05480	PSP
120	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
142	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
142	Y	Phosphorylation	Kinase	FYN	P39688	Uniprot
142	Y	Phosphorylation	Kinase	FYN	P06241	PSP
142	Y	Phosphorylation	Kinase	FER	P70451	PSP
142	Y	Phosphorylation	Kinase	FER	P16591	PSP
191	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
191	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
246	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
552	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
552	S	Phosphorylation	Kinase	AKT1	P31749	PSP
552	S	Phosphorylation	Kinase	AMPK	-	Uniprot
552	S	Phosphorylation	Kinase	AKT1	P31750	PSP
605	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
605	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
654	Y	Phosphorylation	Kinase	SRC	P12931	PSP
654	Y	Phosphorylation	Kinase	SRC	P05480	PSP
675	S	Phosphorylation	Kinase	MAP3K2	Q61083	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	Btrc	Q3ULA2	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxw11	Q5SRY7	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Neurl2	Q9D0S4	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Siah1a	P61092	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Skp2	Q9Z0Z3	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Smurf2	A2A5Z6	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Tbl1x	Q9QXE7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	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	20307497
Phosphorylated on Ser-33 and Ser-37 by HIPK2.
33	S	Phosphorylation	20307497
Phosphorylation proceeds then from Thr-41 to Ser-33.
37	S	Phosphorylation	20307497
Phosphorylated on Ser-33 and Ser-37 by HIPK2.
41	T	Phosphorylation	-
Phosphorylation proceeds then from Thr-41 to Ser-33.
45	S	Phosphorylation	21183079
Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase.
49	K	Acetylation	-
Deacetylated at Lys-49 by SIRT1.
191	S	Phosphorylation	17242355
Phosphorylation on Ser-191 and Ser-246 by CDK5.
246	S	Phosphorylation	-
Phosphorylation on Ser-191 and Ser-246 by CDK5.
552	S	Phosphorylation	17242355
Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription.
619	C	S-nitrosylation	20705246
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CTNB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSN1_HUMAN	PSEN1	physical	12070348
RHG32_MOUSE	Arhgap32	physical	12531901
TF7L2_MOUSE	Tcf7l2	physical	19805521
CTNB1_MOUSE	Ctnnb1	physical	20211142
ITF2_MOUSE	Tcf4	genetic	16478791
CBY1_MOUSE	Cby1	genetic	16678101
CNBP1_MOUSE	Ctnnbip1	genetic	16678101
LEF1_MOUSE	Lef1	genetic	16678101
SOX2_MOUSE	Sox2	genetic	15781477
SOX2_MOUSE	Sox2	physical	15781477
CCND1_MOUSE	Ccnd1	genetic	15314168
ITF2_MOUSE	Tcf4	physical	16007074
CADH1_MOUSE	Cdh1	physical	16368433
HNF1A_MOUSE	Hnf1a	genetic	15866165
TF7L2_MOUSE	Tcf7l2	genetic	15778706
SMCA4_MOUSE	Smarca4	physical	15525990
AXIN2_MOUSE	Axin2	physical	9554852
AXIN1_MOUSE	Axin1	physical	10318824
GSK3B_MOUSE	Gsk3b	physical	10318824
ITF2_MOUSE	Tcf4	physical	12874278
GSK3B_MOUSE	Gsk3b	physical	12874278
CNBP1_MOUSE	Ctnnbip1	physical	12874278
CADH1_MOUSE	Cdh1	physical	12874278
TX1B3_MOUSE	Tax1bp3	physical	12874278
TX1B3_MOUSE	Tax1bp3	genetic	12874278
CADH1_MOUSE	Cdh1	physical	15057752
KIFA3_MOUSE	Kifap3	physical	15834408
KIF3B_MOUSE	Kif3b	physical	15834408
CADH2_MOUSE	Cdh2	physical	15834408
CTND1_MOUSE	Ctnnd1	physical	15834408
TF7L2_MOUSE	Tcf7l2	physical	17053159
LEF1_MOUSE	Lef1	physical	18202148
TF7L1_MOUSE	Tcf7l1	physical	18202148
ESR1_MOUSE	Esr1	physical	18202148
FBW1A_HUMAN	BTRC	physical	12417018
AXIN1_HUMAN	AXIN1	physical	12417018
CADH1_MOUSE	Cdh1	physical	11953314
BCL9_HUMAN	BCL9	physical	17113272
BCL9L_HUMAN	BCL9L	physical	17113272
CTNA1_MOUSE	Ctnna1	physical	17113272
BCL9_DROME	lgs	physical	17113272
CTNA_DROME	alpha-Cat	physical	17113272
PANG1_DROME	pan	physical	17113272
PANG2_DROME	pan	physical	17113272
PO5F1_MOUSE	Pou5f1	physical	23444350
NANOG_MOUSE	Nanog	physical	23444350
CADH1_MOUSE	Cdh1	physical	23444350
TF7L2_HUMAN	TCF7L2	physical	12417018

Drug and Disease Associations

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

Regulatory Network of CTNB1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"AMP-activated protein kinase (AMPK) cross-talks with canonical Wntsignaling via phosphorylation of beta-catenin at Ser 552."; Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.; Biochem. Biophys. Res. Commun. 395:146-151(2010). Cited for: PHOSPHORYLATION AT SER-552, AND MUTAGENESIS OF SER-552.	20361929 [Abstract]
"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-cateninfor phosphorylation and proteasomal degradation."; Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.; Biochem. Biophys. Res. Commun. 394:966-971(2010). Cited for: PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND MUTAGENESIS OFSER-33 AND SER-37.	20307497 [Abstract]
"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-675, AND MASSSPECTROMETRY.	19131326 [Abstract]
"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-552 AND SER-675, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"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-551; SER-552 ANDTHR-556, AND MASS SPECTROMETRY.	17242355 [Abstract]
"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-551 AND THR-556, ANDMASS SPECTROMETRY.	17114649 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-654, AND MASSSPECTROMETRY.	18034455 [Abstract]

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