CTNB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CTNB1_HUMAN
• UniProt AC: P35222
• Protein Name: Catenin beta-1
• Gene Name: CTNNB1
• Organism: Homo sapiens (Human).
• 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 . Cytoplas
• 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. [PubMed: 17524503]
• Protein Sequence: MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL

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	22814378
3	Phosphorylation	-----MATQADLMEL -----CCCHHHHHHH	24.00	30576142
19	Acetylation	MAMEPDRKAAVSHWQ HCCCCCHHHHHHHHH	48.34	18987336
19	Ubiquitination	MAMEPDRKAAVSHWQ HCCCCCHHHHHHHHH	48.34	21906983
19	Ubiquitination	MAMEPDRKAAVSHWQ HCCCCCHHHHHHHHH	48.34	21890473
19 (in isoform 1)	Ubiquitination	-	48.34	21890473
23	O-linked_Glycosylation	PDRKAAVSHWQQQSY CCHHHHHHHHHHHHH	17.80	33019562
23	Phosphorylation	PDRKAAVSHWQQQSY CCHHHHHHHHHHHHH	17.80	26356563
29	Phosphorylation	VSHWQQQSYLDSGIH HHHHHHHHHHCCCCC	24.27	21712546
30	Phosphorylation	SHWQQQSYLDSGIHS HHHHHHHHHCCCCCC	15.36	21712546
33	Phosphorylation	QQQSYLDSGIHSGAT HHHHHHCCCCCCCCC	36.73	17001009
37	Phosphorylation	YLDSGIHSGATTTAP HHCCCCCCCCCCCCC	28.36	22025562
40	O-linked_Glycosylation	SGIHSGATTTAPSLS CCCCCCCCCCCCCCC	28.36	33019562
40	Phosphorylation	SGIHSGATTTAPSLS CCCCCCCCCCCCCCC	28.36	26356563
41	Phosphorylation	GIHSGATTTAPSLSG CCCCCCCCCCCCCCC	22.04	22025562
41	O-linked_Glycosylation	GIHSGATTTAPSLSG CCCCCCCCCCCCCCC	22.04	33019562
42	Phosphorylation	IHSGATTTAPSLSGK CCCCCCCCCCCCCCC	32.01	25850435
45	Phosphorylation	GATTTAPSLSGKGNP CCCCCCCCCCCCCCC	32.48	12239584
47	Phosphorylation	TTTAPSLSGKGNPEE CCCCCCCCCCCCCCH	42.68	25850435
49	Acetylation	TAPSLSGKGNPEEED CCCCCCCCCCCCHHC	52.73	11973335
49	Ubiquitination	TAPSLSGKGNPEEED CCCCCCCCCCCCHHC	52.73	49322
49	Methylation	TAPSLSGKGNPEEED CCCCCCCCCCCCHHC	52.73	24824780
59	Phosphorylation	PEEEDVDTSQVLYEW CCHHCCCHHHHHHHH	22.40	27251275
60	Phosphorylation	EEEDVDTSQVLYEWE CHHCCCHHHHHHHHH	17.52	27251275
64	Phosphorylation	VDTSQVLYEWEQGFS CCHHHHHHHHHHCCC	21.82	22817900
71	Phosphorylation	YEWEQGFSQSFTQEQ HHHHHCCCCCCCHHH	31.57	28348404
73	Phosphorylation	WEQGFSQSFTQEQVA HHHCCCCCCCHHHHC	29.12	24275569
75	Phosphorylation	QGFSQSFTQEQVADI HCCCCCCCHHHHCCC	36.12	29496963
86	Phosphorylation	VADIDGQYAMTRAQR HCCCCCHHHHHHHHH	12.13	17318191
102	Phosphorylation	RAAMFPETLDEGMQI HHHHCCCCCCCCCCC	39.48	19141652
112	Phosphorylation	EGMQIPSTQFDAAHP CCCCCCCCCCCCCCC	28.09	19141652
112	O-linked_Glycosylation	EGMQIPSTQFDAAHP CCCCCCCCCCCCCCC	28.09	33019562
120	Phosphorylation	QFDAAHPTNVQRLAE CCCCCCCCCHHHHCC	37.85	19141652
129	Phosphorylation	VQRLAEPSQMLKHAV HHHHCCHHHHHHHHH	21.52	28857561
133	Ubiquitination	AEPSQMLKHAVVNLI CCHHHHHHHHHHHHH	24.95	21906983
133	Acetylation	AEPSQMLKHAVVNLI CCHHHHHHHHHHHHH	24.95	21466224
133 (in isoform 1)	Ubiquitination	-	24.95	21890473
142	Phosphorylation	AVVNLINYQDDAELA HHHHHHCCCCHHHHH	13.31	17052462
158	Ubiquitination	RAIPELTKLLNDEDQ HHHHHHHHHCCCCCC	64.70	21906983
158	Ubiquitination	RAIPELTKLLNDEDQ HHHHHHHHHCCCCCC	64.70	21890473
158 (in isoform 1)	Ubiquitination	-	64.70	21890473
170	Ubiquitination	EDQVVVNKAAVMVHQ CCCHHHHHHHHHHHH	26.55	21906983
170	Ubiquitination	EDQVVVNKAAVMVHQ CCCHHHHHHHHHHHH	26.55	21890473
170 (in isoform 1)	Ubiquitination	-	26.55	21890473
179	Phosphorylation	AVMVHQLSKKEASRH HHHHHHCCHHHHHHH	34.80	28258704
180	Ubiquitination	VMVHQLSKKEASRHA HHHHHCCHHHHHHHH	64.32	-
180	2-Hydroxyisobutyrylation	VMVHQLSKKEASRHA HHHHHCCHHHHHHHH	64.32	-
181	Ubiquitination	MVHQLSKKEASRHAI HHHHCCHHHHHHHHH	55.95	-
184	Phosphorylation	QLSKKEASRHAIMRS HCCHHHHHHHHHHHC	26.20	27174698
191	Phosphorylation	SRHAIMRSPQMVSAI HHHHHHHCHHHHHHH	11.34	19664994
196	Phosphorylation	MRSPQMVSAIVRTMQ HHCHHHHHHHHHHHC	13.61	23927012
201	Phosphorylation	MVSAIVRTMQNTNDV HHHHHHHHHCCCCCH	16.53	25867546
217	Phosphorylation	TARCTAGTLHNLSHH HHHHCHHHHHHHHHC	23.52	22912867
222	Phosphorylation	AGTLHNLSHHREGLL HHHHHHHHHCCCCHH	23.67	25850435
233	Ubiquitination	EGLLAIFKSGGIPAL CCHHHHHHCCCHHHH	41.92	21906983
233	Ubiquitination	EGLLAIFKSGGIPAL CCHHHHHHCCCHHHH	41.92	21890473
233 (in isoform 1)	Ubiquitination	-	41.92	21890473
246	Phosphorylation	ALVKMLGSPVDSVLF HHHHHHCCCHHHHHH	20.14	22817900
250	Phosphorylation	MLGSPVDSVLFYAIT HHCCCHHHHHHHHHH	22.43	25404012
254	Phosphorylation	PVDSVLFYAITTLHN CHHHHHHHHHHHHHH	7.92	25404012
257	Phosphorylation	SVLFYAITTLHNLLL HHHHHHHHHHHHHHH	18.35	25404012
258	Phosphorylation	VLFYAITTLHNLLLH HHHHHHHHHHHHHHC	21.65	25404012
281	Ubiquitination	RLAGGLQKMVALLNK HHHHHHHHHHHHHHC	40.14	-
288	Ubiquitination	KMVALLNKTNVKFLA HHHHHHHCCCCCEEE	41.25	-
289	Phosphorylation	MVALLNKTNVKFLAI HHHHHHCCCCCEEEE	44.14	22210691
311	Phosphorylation	LAYGNQESKLIILAS HHHCCCCCEEEEEEC	24.01	22210691
331	Phosphorylation	LVNIMRTYTYEKLLW HHHHHHHCCHHHHHH	9.28	22817900
332	Phosphorylation	VNIMRTYTYEKLLWT HHHHHHCCHHHHHHH	25.29	-
333	Phosphorylation	NIMRTYTYEKLLWTT HHHHHCCHHHHHHHH	10.72	22056988
335	Ubiquitination	MRTYTYEKLLWTTSR HHHCCHHHHHHHHHH	38.17	21906983
335	Ubiquitination	MRTYTYEKLLWTTSR HHHCCHHHHHHHHHH	38.17	21890473
335 (in isoform 1)	Ubiquitination	-	38.17	21890473
345	Acetylation	WTTSRVLKVLSVCSS HHHHHHHHHHHHHCC	37.97	15060161
345	Ubiquitination	WTTSRVLKVLSVCSS HHHHHHHHHHHHHCC	37.97	20639865
354	Acetylation	LSVCSSNKPAIVEAG HHHHCCCCCEEEEEC	37.46	23273980
354	Ubiquitination	LSVCSSNKPAIVEAG HHHHCCCCCEEEEEC	37.46	21906983
354 (in isoform 1)	Ubiquitination	-	37.46	21890473
393	Phosphorylation	RNLSDAATKQEGMEG HHHHHHHHHHHHHHH	34.67	19565571
394	Ubiquitination	NLSDAATKQEGMEGL HHHHHHHHHHHHHHH	41.44	-
435	Acetylation	TCNNYKNKMMVCQVG CCCCCCCCEEEEECC	24.99	22368965
435	Ubiquitination	TCNNYKNKMMVCQVG CCCCCCCCEEEEECC	24.99	20639865
461	Phosphorylation	AGDREDITEPAICAL CCCCCCCCHHHHHHH	48.51	24719451
466	S-palmitoylation	DITEPAICALRHLTS CCCHHHHHHHHHHHH	2.95	26865113
472	Phosphorylation	ICALRHLTSRHQEAE HHHHHHHHHHHHHHH	20.00	22817900
473	Phosphorylation	CALRHLTSRHQEAEM HHHHHHHHHHHHHHH	33.84	22817900
489	Phosphorylation	QNAVRLHYGLPVVVK HHHHHHHHCCCEEEH	25.58	27273156
496	Ubiquitination	YGLPVVVKLLHPPSH HCCCEEEHHHCCCCH	33.45	-
508	Ubiquitination	PSHWPLIKATVGLIR CCHHHHHHHHHHHHH	45.76	21906983
508 (in isoform 1)	Ubiquitination	-	45.76	21890473
510	Phosphorylation	HWPLIKATVGLIRNL HHHHHHHHHHHHHHH	15.31	-
520	S-nitrosylation	LIRNLALCPANHAPL HHHHHHHCCCCCHHH	2.19	24105792
547	Phosphorylation	LVRAHQDTQRRTSMG HHHHCHHHHHHHCCC	19.87	26074081
551	Phosphorylation	HQDTQRRTSMGGTQQ CHHHHHHHCCCCHHH	25.84	29255136
552	Phosphorylation	QDTQRRTSMGGTQQQ HHHHHHHCCCCHHHH	17.39	29255136
553	Sulfoxidation	DTQRRTSMGGTQQQF HHHHHHCCCCHHHHH	5.92	21406390
556	Phosphorylation	RRTSMGGTQQQFVEG HHHCCCCHHHHHHCC	19.92	22167270
574	Phosphorylation	EEIVEGCTGALHILA HHHHCHHCHHHHHHH	36.02	20068231
605	Phosphorylation	LFVQLLYSPIENIQR HHHHHHHCCCHHHHH	21.26	-
619	S-nitrosocysteine	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	-
619	S-nitrosylation	RVAAGVLCELAQDKE HHHHHHHHHHHCCHH	3.61	-
625	Ubiquitination	LCELAQDKEAAEAIE HHHHHCCHHHHHHHH	36.85	21906983
625 (in isoform 1)	Ubiquitination	-	36.85	21890473
641	Phosphorylation	EGATAPLTELLHSRN CCCCCCHHHHHHHCC	24.43	22210691
646	Phosphorylation	PLTELLHSRNEGVAT CHHHHHHHCCHHHHH	36.45	-
653	Phosphorylation	SRNEGVATYAAAVLF HCCHHHHHHHHHHHH	15.99	28152594
654	Phosphorylation	RNEGVATYAAAVLFR CCHHHHHHHHHHHHH	5.63	17318191
666	Ubiquitination	LFRMSEDKPQDYKKR HHHCCCCCCCCHHHH	40.29	-
670	Phosphorylation	SEDKPQDYKKRLSVE CCCCCCCHHHHHHHH	17.11	21423209
671	Ubiquitination	EDKPQDYKKRLSVEL CCCCCCHHHHHHHHH	39.44	21906983
671 (in isoform 1)	Ubiquitination	-	39.44	21890473
675	Phosphorylation	QDYKKRLSVELTSSL CCHHHHHHHHHHHHH	19.99	29255136
679	Phosphorylation	KRLSVELTSSLFRTE HHHHHHHHHHHHHCC	11.63	23927012
680	Phosphorylation	RLSVELTSSLFRTEP HHHHHHHHHHHHCCC	37.35	23927012
681	Phosphorylation	LSVELTSSLFRTEPM HHHHHHHHHHHCCCC	26.71	23927012
715	Phosphorylation	GYRQDDPSYRSFHSG CCCCCCCCCCCCCCC	39.92	28152594
716	Phosphorylation	YRQDDPSYRSFHSGG CCCCCCCCCCCCCCC	18.70	28152594
718	Phosphorylation	QDDPSYRSFHSGGYG CCCCCCCCCCCCCCC	21.05	19001871
721	Phosphorylation	PSYRSFHSGGYGQDA CCCCCCCCCCCCCCC	31.72	24275569
724	Phosphorylation	RSFHSGGYGQDALGM CCCCCCCCCCCCCCC	18.35	24275569
748	Phosphorylation	GHHPGADYPVDGLPD CCCCCCCCCCCCCCC	12.48	-

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	GSK3B	P49841	GPS
29	S	Phosphorylation	Kinase	GSK3B	P49841	GPS
29	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
29	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
30	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
33	S	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
33	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
33	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
33	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
33	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
33	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
33	S	Phosphorylation	Kinase	CHUK	O15111	GPS
37	S	Phosphorylation	Kinase	CHUK	O15111	GPS
37	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
37	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
37	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
37	S	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
37	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
37	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
41	T	Phosphorylation	Kinase	CHUK	O15111	GPS
41	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
41	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
41	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
41	T	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
41	T	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
45	S	Phosphorylation	Kinase	CHUK	O15111	GPS
45	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS
45	S	Phosphorylation	Kinase	CK1A	P97633	PSP
45	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
45	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
45	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
45	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
45	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
45	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
64	Y	Phosphorylation	Kinase	BRK	Q13882	PSP
64	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
64	Y	Phosphorylation	Kinase	PTK6	Q64434	GPS
86	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
86	Y	Phosphorylation	Kinase	SRC	P12931	GPS
86	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
86	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
86	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
102	T	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
102	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
102	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
112	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
112	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
112	T	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
112	T	Phosphorylation	Kinase	PRKD1	Q15139	PSP
120	T	Phosphorylation	Kinase	PRKD1	Q15139	PSP
142	Y	Phosphorylation	Kinase	FGFR2	P21802	PSP
142	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
142	Y	Phosphorylation	Kinase	NTRK1	P04629	GPS
142	Y	Phosphorylation	Kinase	FGFR3	P22607	PSP
142	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot
142	Y	Phosphorylation	Kinase	BRK	Q13882	PSP
191	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
246	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
331	Y	Phosphorylation	Kinase	BRK	Q13882	PSP
332	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
333	Y	Phosphorylation	Kinase	SRC	P12931	PSP
333	Y	Phosphorylation	Kinase	BRK	Q13882	PSP
393	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
393	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
393	T	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
472	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
489	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
552	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
552	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
552	S	Phosphorylation	Kinase	AKT1	P31749	PSP
552	S	Phosphorylation	Kinase	AKT2	P31751	PSP
552	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
605	S	Phosphorylation	Kinase	MAPK12	P53778	GPS
654	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
654	Y	Phosphorylation	Kinase	SRC	P12931	PSP
654	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
654	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
654	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
654	Y	Phosphorylation	Kinase	ERBB2	P04626	GPS
675	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
675	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
675	S	Phosphorylation	Kinase	MAP3K2	Q9Y2U5	GPS
675	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
675	S	Phosphorylation	Kinase	PAK4	O96013	PSP
715	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
718	S	Phosphorylation	Kinase	PLK1	P53350	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:23744067
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM33	Q9UPN9	PMID:25639486
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:10023660
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:11389839
-	K	Ubiquitination	E3 ubiquitin ligase	NEURL2	Q9BR09	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW11	Q9UKB1	PMID:10321728
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	TBL1X	O60907	PMID:20181957
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	CDC34	P49427	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	FANCL	Q9NW38	PMID:22653977
-	K	Ubiquitination	E3 ubiquitin ligase	COP1	Q8NHY2	PMID:25311538
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:30806153

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.	12027456
33	S	Phosphorylation	Phosphorylated on Ser-33 and Ser-37 by HIPK2 and GSK3B, this phosphorylation triggers proteasomal degradation.	20307497
33	S	Phosphorylation	Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33.	20307497
37	S	Phosphorylation	Phosphorylated on Ser-33 and Ser-37 by HIPK2 and GSK3B, this phosphorylation triggers proteasomal degradation.	20307497
37	S	Phosphorylation	Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33.	20307497
41	T	Phosphorylation	Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33.	12027456
45	S	Phosphorylation	Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase.	12051714
49	K	Acetylation	Deacetylated at Lys-49 by SIRT1.	24824780
191	S	Phosphorylation	Phosphorylation on Ser-191 and Ser-246 by CDK5.	17009320
246	S	Phosphorylation	Phosphorylation on Ser-191 and Ser-246 by CDK5.	17009320
552	S	Phosphorylation	Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription (By similarity).	21406692
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTND1_HUMAN	CTNND1	physical	9535896
PLAK_HUMAN	JUP	physical	9535896
P85A_HUMAN	PIK3R1	physical	10477752
AXIN1_HUMAN	AXIN1	physical	9734785
ANDR_HUMAN	AR	physical	11792709
GSK3B_HUMAN	GSK3B	physical	11251183
CADH1_HUMAN	CDH1	physical	11712088
CTNA1_HUMAN	CTNNA1	physical	7954478
CADH1_HUMAN	CDH1	physical	7954478
VINC_HUMAN	VCL	physical	9405455
APC_HUMAN	APC	physical	11712088
PIN1_HUMAN	PIN1	physical	11533658
ITF2_HUMAN	TCF4	physical	12657632
APC_HUMAN	APC	physical	12628243
BCL9L_MOUSE	Bcl9l	physical	15574752
CBP_HUMAN	CREBBP	genetic	15782138
MUC1_HUMAN	MUC1	physical	12618757
LEF1_HUMAN	LEF1	physical	15684397
APC_HUMAN	APC	physical	11251183
APC_HUMAN	APC	physical	11533658
ANDR_HUMAN	AR	physical	12944908
CTND1_HUMAN	CTNND1	physical	11712088
ERBB2_HUMAN	ERBB2	physical	11950845
ESR1_HUMAN	ESR1	physical	15304487
PLAK_HUMAN	JUP	physical	11712088
PPAC_HUMAN	ACP1	physical	12438242
HNF4A_HUMAN	HNF4A	physical	12944908
CADH1_HUMAN	CDH1	physical	15023525
NHRF1_HUMAN	SLC9A3R1	physical	12830000
CADH1_HUMAN	CDH1	physical	12830000
PTN14_HUMAN	PTPN14	physical	12808048
LEF1_HUMAN	LEF1	physical	12748295
CBY1_HUMAN	CBY1	physical	12712206
CTNA1_HUMAN	CTNNA1	physical	12640114
CADH1_HUMAN	CDH1	physical	12640114
RUVB1_HUMAN	RUVBL1	physical	9843967
SMCA4_HUMAN	SMARCA4	physical	11532957
LEF1_HUMAN	LEF1	physical	8757136
APCL_HUMAN	APC2	physical	9823329
FHL2_HUMAN	FHL2	physical	12466281
ERBB2_HUMAN	ERBB2	physical	7702605
TGFR2_HUMAN	TGFBR2	physical	12000714
USP9X_HUMAN	USP9X	physical	10620020
CADH1_HUMAN	CDH1	physical	10772923
CADH1_HUMAN	CDH1	physical	11113628
CAD11_HUMAN	CDH11	physical	10029089
IKKA_HUMAN	CHUK	physical	11527961
IKKB_HUMAN	IKBKB	physical	11527961
APC_HUMAN	APC	physical	11707392
CADH6_HUMAN	CDH6	physical	10207020
CAD18_HUMAN	CDH18	physical	10207020
CYBP_HUMAN	CACYBP	physical	11389839
SKP1_HUMAN	SKP1	physical	11389839
CADH1_HUMAN	CDH1	physical	12169098
MUC1_HUMAN	MUC1	physical	11152665
TF7L1_HUMAN	TCF7L1	physical	11136974
PSN1_HUMAN	PSEN1	physical	9738936
CADH9_HUMAN	CDH9	physical	10861224
CAD10_HUMAN	CDH10	physical	10861224
CADH7_HUMAN	CDH7	physical	10861224
CADH3_HUMAN	CDH3	physical	10381631
CADH1_HUMAN	CDH1	physical	10381631
MUC1_HUMAN	MUC1	physical	11483589
CD5R1_HUMAN	CDK5R1	physical	11168528
EZRI_HUMAN	EZR	physical	10462524
PTPRU_HUMAN	PTPRU	physical	12501215
KAT2B_HUMAN	KAT2B	physical	18987336
JADE1_HUMAN	JADE1	physical	18806787
CADH1_HUMAN	CDH1	physical	18593907
TRRAP_HUMAN	TRRAP	physical	18347063
CBP_HUMAN	CREBBP	physical	18347063
CHD8_HUMAN	CHD8	physical	18378692
PSN1_HUMAN	PSEN1	physical	17360711
HDAC7_HUMAN	HDAC7	physical	20224040
CADH5_HUMAN	CDH5	physical	20224040
FBW1A_HUMAN	BTRC	physical	16798748
TRRAP_HUMAN	TRRAP	physical	16510874
EP400_HUMAN	EP400	physical	16510874
KMT2A_HUMAN	KMT2A	physical	16510874
SMCA5_HUMAN	SMARCA5	physical	16510874
RUVB1_HUMAN	RUVBL1	physical	16510874
ASH2L_HUMAN	ASH2L	physical	16510874
KMT2D_HUMAN	KMT2D	physical	16510874
MEN1_HUMAN	MEN1	physical	16510874
RBBP5_HUMAN	RBBP5	physical	16510874
KAT2A_HUMAN	KAT2A	physical	16510874
FOXO3_HUMAN	FOXO3	physical	15905404
PSN1_HUMAN	PSEN1	physical	16126725
EZH2_HUMAN	EZH2	physical	19661437
TRRAP_HUMAN	TRRAP	physical	16510875
EP400_HUMAN	EP400	physical	16510875
KMT2A_HUMAN	KMT2A	physical	16510875
SMCA5_HUMAN	SMARCA5	physical	16510875
RUVB1_HUMAN	RUVBL1	physical	16510875
KMT2D_HUMAN	KMT2D	physical	16510875
MEN1_HUMAN	MEN1	physical	16510875
ASH2L_HUMAN	ASH2L	physical	16510875
RBBP5_HUMAN	RBBP5	physical	16510875
HDAC1_HUMAN	HDAC1	physical	16204248
LEF1_HUMAN	LEF1	physical	16204248
IFRD1_HUMAN	IFRD1	physical	16204248
HDAC4_HUMAN	HDAC4	physical	16204248
PITX2_HUMAN	PITX2	physical	12464179
CARM1_HUMAN	CARM1	physical	11983685
HDAC1_HUMAN	HDAC1	physical	10958684
LEF1_HUMAN	LEF1	physical	10958684
LEF1_HUMAN	LEF1	physical	11835406
SOX6_HUMAN	SOX6	physical	17412698
HDAC1_HUMAN	HDAC1	physical	17412698
EP300_HUMAN	EP300	genetic	12861022
CUL1_HUMAN	CUL1	physical	10713156
SIR1_HUMAN	SIRT1	physical	20439735
FBW1A_HUMAN	BTRC	physical	10228155
AXIN1_HUMAN	AXIN1	physical	10228155
SATB1_HUMAN	SATB1	physical	20126258
ITF2_HUMAN	TCF4	physical	20126258
KAT2A_HUMAN	KAT2A	physical	20937768
RBBP5_HUMAN	RBBP5	physical	20937768
NOTC1_HUMAN	NOTCH1	physical	19000719
FBW1A_HUMAN	BTRC	physical	10074433
FOXO4_HUMAN	FOXO4	physical	20874444
NR4A1_HUMAN	NR4A1	physical	21986938
CSN3_HUMAN	COPS3	physical	19576224
GSK3B_HUMAN	GSK3B	physical	19576224
APC_HUMAN	APC	physical	19576224
CSN5_HUMAN	COPS5	physical	19576224
CSN8_HUMAN	COPS8	physical	19576224
FBW1A_HUMAN	BTRC	physical	9990852
SKP1_HUMAN	SKP1	physical	9990852
CHD8_HUMAN	CHD8	physical	22083958
CADH1_HUMAN	CDH1	physical	17220478
NDRG1_HUMAN	NDRG1	physical	17220478
RUVB2_HUMAN	RUVBL2	physical	15829968
LEF1_HUMAN	LEF1	physical	11751639
FANCC_HUMAN	FANCC	physical	22653977
HINT1_HUMAN	HINT1	physical	22647378
ITF2_HUMAN	TCF4	physical	22080605
RBP2_HUMAN	RANBP2	physical	22110128
HDAC7_HUMAN	HDAC7	physical	21836063
FBW1A_HUMAN	BTRC	physical	17053147
UBE2B_HUMAN	UBE2B	physical	22705350
ARMC8_HUMAN	ARMC8	physical	18215130
LEF1_HUMAN	LEF1	physical	12077367
AXIN1_HUMAN	AXIN1	physical	20531388
FBW1A_HUMAN	BTRC	physical	20531388
FBW1A_HUMAN	BTRC	physical	18354482
CNBP1_MOUSE	Ctnnbip1	physical	12408824
TFE2_XENLA	tcf3	physical	12408824
CADHB_XENLA	cdh3-b	physical	12408824
FBW1A_HUMAN	BTRC	physical	18851830
UB2D1_HUMAN	UBE2D1	physical	18851830
FBW1A_HUMAN	BTRC	physical	22912335
1433Z_HUMAN	YWHAZ	physical	22912335
ISG15_HUMAN	ISG15	physical	20581239
HERC5_HUMAN	HERC5	physical	20581239
KAISO_HUMAN	ZBTB33	physical	21670201
TF7L2_HUMAN	TCF7L2	physical	21670201
FBW1A_HUMAN	BTRC	physical	19150432
TBL1R_HUMAN	TBL1XR1	physical	18193033
TBL1X_HUMAN	TBL1X	physical	18193033
SKP1_HUMAN	SKP1	physical	21466614
FBW1A_HUMAN	BTRC	physical	21466614
CYBP_HUMAN	CACYBP	physical	21466614
LEF1_HUMAN	LEF1	physical	15768032
CADH1_HUMAN	CDH1	physical	16125672
CTNA1_HUMAN	CTNNA1	physical	17072306
ITF2_HUMAN	TCF4	physical	17072306
CNBP1_HUMAN	CTNNBIP1	physical	17072306
RBCC1_HUMAN	RB1CC1	physical	22751121
BRCA1_HUMAN	BRCA1	physical	20215423
APC_HUMAN	APC	physical	15327769
MK08_HUMAN	MAPK8	physical	19667122
MK09_HUMAN	MAPK9	physical	19667122
LEF1_HUMAN	LEF1	physical	9419974
A4_HUMAN	APP	physical	21832049
PTPRU_HUMAN	PTPRU	physical	9054423
CDC73_HUMAN	CDC73	physical	16630820
HINT1_HUMAN	HINT1	physical	16014379
FHIT_HUMAN	FHIT	physical	18077326
CTNA1_HUMAN	CTNNA1	physical	15492215
TBA1A_HUMAN	TUBA1A	physical	15492215
1433Z_HUMAN	YWHAZ	physical	15492215
BTF3_HUMAN	BTF3	physical	15492215
PAIRB_HUMAN	SERBP1	physical	15492215
HSP7C_HUMAN	HSPA8	physical	15492215
HS90B_HUMAN	HSP90AB1	physical	15492215
LDHB_HUMAN	LDHB	physical	15492215
RLA2_HUMAN	RPLP2	physical	15492215
ROA1_HUMAN	HNRNPA1	physical	15492215
RSSA_HUMAN	RPSA	physical	15492215
SMD1_HUMAN	SNRPD1	physical	15492215
ITF2_HUMAN	TCF4	physical	15525529
EMD_HUMAN	EMD	physical	16858403
FBW1A_HUMAN	BTRC	physical	22682247
CADH1_HUMAN	CDH1	physical	22158051
CRYAB_HUMAN	CRYAB	physical	22158051
EZH2_HUMAN	EZH2	physical	17502350
FUS_HUMAN	FUS	physical	16230076
TOP2A_HUMAN	TOP2A	physical	16230076
GEMI5_HUMAN	GEMIN5	physical	16230076
DHX9_HUMAN	DHX9	physical	16230076
PARP1_HUMAN	PARP1	physical	16230076
PRP6_HUMAN	PRPF6	physical	16230076
DDX1_HUMAN	DDX1	physical	16230076
HNRPM_HUMAN	HNRNPM	physical	16230076
DDX5_HUMAN	DDX5	physical	16230076
NONO_HUMAN	NONO	physical	16230076
RBMX_HUMAN	RBMX	physical	16230076
ROA2_HUMAN	HNRNPA2B1	physical	16230076
ROA1_HUMAN	HNRNPA1	physical	16230076
HNRPK_HUMAN	HNRNPK	physical	16230076
CCNA2_HUMAN	CCNA2	physical	14985333
CCNE1_HUMAN	CCNE1	physical	14985333
CDK2_HUMAN	CDK2	physical	14985333
LEF1_HUMAN	LEF1	physical	15728254
CTNA3_HUMAN	CTNNA3	physical	23718855
PTPRU_HUMAN	PTPRU	physical	16574648
CADH1_HUMAN	CDH1	physical	16574648
CBL_HUMAN	CBL	physical	23744067
ABL1_HUMAN	ABL1	physical	23950177
ELAV1_HUMAN	ELAVL1	physical	22544606
PGH2_HUMAN	PTGS2	physical	22544606
NEK2_HUMAN	NEK2	physical	24501426
FBW1A_HUMAN	BTRC	physical	24501426
FBW1A_HUMAN	BTRC	physical	24451375
KCTD1_HUMAN	KCTD1	genetic	24736394
KCTD1_HUMAN	KCTD1	physical	24736394
CADH1_HUMAN	CDH1	physical	24798214
ITF2_HUMAN	TCF4	physical	24798214
SP1_HUMAN	SP1	physical	24798214
ITF2_HUMAN	TCF4	physical	23449499
RNF14_HUMAN	RNF14	physical	23449499
FBW1A_HUMAN	BTRC	physical	23514615
CSN5_HUMAN	COPS5	physical	24882689
SIAH1_HUMAN	SIAH1	physical	24882689
RN220_HUMAN	RNF220	physical	25266658
ITF2_HUMAN	TCF4	physical	12727872
SOX1_HUMAN	SOX1	physical	22767186
PPARG_HUMAN	PPARG	physical	24735796
LATS2_HUMAN	LATS2	physical	24360964
CITE1_HUMAN	CITED1	physical	15843474
ITF2_HUMAN	TCF4	physical	15060161
ANDR_HUMAN	AR	physical	15060161
HIF1A_HUMAN	HIF1A	physical	24650032
PPARG_HUMAN	PPARG	physical	19495794
PSN1_HUMAN	PSEN1	physical	16306047
FANCA_HUMAN	FANCA	physical	22653977
FANCG_HUMAN	FANCG	physical	22653977
BCL6_HUMAN	BCL6	physical	25402006
ITF2_HUMAN	TCF4	physical	25402006
ZIC3_HUMAN	ZIC3	physical	25402006
PTEN_HUMAN	PTEN	physical	20372837
PO5F1_HUMAN	POU5F1	physical	23539445
SOX2_HUMAN	SOX2	physical	23539445
HDAC6_HUMAN	HDAC6	physical	18356165
LRRF1_MOUSE	Lrrfip1	physical	16990252
TF7L2_MOUSE	Tcf7l2	genetic	12861022
TF7L2_MOUSE	Tcf7l2	physical	12861022
CEBPA_MOUSE	Cebpa	physical	12861022
SMUF1_HUMAN	SMURF1	physical	26015066
ITF2_HUMAN	TCF4	physical	24876153
TF7L2_HUMAN	TCF7L2	physical	22155184
TF7L2_HUMAN	TCF7L2	physical	11713475
TF7L2_HUMAN	TCF7L2	physical	16230076
KLF5_HUMAN	KLF5	physical	19435907
PKD1_HUMAN	PKD1	physical	11113628
PRKN_HUMAN	PARK2	physical	25877876
TF7L1_HUMAN	TCF7L1	physical	15327769
APC_HUMAN	APC	physical	26496610
CAD10_HUMAN	CDH10	physical	26496610
CTNA1_HUMAN	CTNNA1	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
AMER1_HUMAN	AMER1	physical	26496610
TRAF4_HUMAN	TRAF4	physical	24990246
FBW1A_HUMAN	BTRC	physical	26506240
TRI33_HUMAN	TRIM33	physical	25639486
UBP4_HUMAN	USP4	physical	26189775
FBW1A_HUMAN	BTRC	physical	20851351
M3K2_HUMAN	MAP3K2	physical	26884171
UBP15_HUMAN	USP15	physical	26884171
EGR1_HUMAN	EGR1	physical	21743491
ITF2_HUMAN	TCF4	physical	21743491
LEF1_HUMAN	LEF1	physical	21743491
GSK3B_HUMAN	GSK3B	physical	21743491
CADH1_HUMAN	CDH1	physical	17909039
ITF2_HUMAN	TCF4	physical	17909039
CNBP1_HUMAN	CTNNBIP1	physical	26912724
FOXM1_HUMAN	FOXM1	physical	26912724
LMNB1_HUMAN	LMNB1	physical	26912724
KPYM_HUMAN	PKM	physical	27485204
CTNA1_HUMAN	CTNNA1	physical	19941816
USP9X_HUMAN	USP9X	physical	27783990
UBE3A_HUMAN	UBE3A	physical	27902311
TF7L2_HUMAN	TCF7L2	physical	27902311
GSK3B_HUMAN	GSK3B	physical	27902311
APC_HUMAN	APC	physical	27902311
AXIN1_HUMAN	AXIN1	physical	27902311
SIAH1_HUMAN	SIAH1	physical	27871173
FBXW7_HUMAN	FBXW7	physical	27485116
FBW1A_HUMAN	BTRC	physical	28018973
CADH5_HUMAN	CDH5	physical	22720799
VINC_HUMAN	VCL	physical	22720799
ACTB_HUMAN	ACTB	physical	22720799
FANCA_HUMAN	FANCA	physical	24469828
FANCC_HUMAN	FANCC	physical	24469828
FANCE_HUMAN	FANCE	physical	24469828
FANCF_HUMAN	FANCF	physical	24469828
CTBP1_HUMAN	CTBP1	physical	24469828
UBP7_HUMAN	USP7	physical	29045831
GSK3B_HUMAN	GSK3B	physical	29045831

Drug and Disease Associations

• Kegg Disease
• H00018: Gastric cancer
• H00020: Colorectal cancer
• H00026: Endometrial Cancer
• H00032: Thyroid cancer
• H00048: Hepatocellular carcinoma
• H00947: Pilomatricoma; Epithelioma calcificans of Malherbe
• OMIM Disease
• 114500: Colorectal cancer (CRC)
• : Note=Activating mutations in CTNNB1 have oncogenic activity resulting in tumor development. Somatic mutations are found in various tumor types, including colon cancers, ovarian and prostate carcinomas, hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant embryonal tumors mainly affecting young children in the first three years of life.
• 132600:
• 155255: Medulloblastoma (MDB)
• 167000: Ovarian cancer (OC)
• : Note=A chromosomal aberration involving CTNNB1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3
• : 8)(p21
• : q12) with PLAG1.
• 156240:
• 615075: Mental retardation, autosomal dominant 19 (MRD19)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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.
PubMed: 20307497

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552; THR-556AND SER-675, AND MASS SPECTROMETRY.
PubMed: 18220336

"cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronalcells.";
Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B.;
J. Cell. Biochem. 100:738-749(2007).
Cited for: PHOSPHORYLATION AT SER-191 AND SER-246, INTERACTION WITH CDK5,SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed: 17009320

"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 SER-675, AND MASSSPECTROMETRY.
PubMed: 17081983

"Characterisation of the phosphorylation of beta-catenin at the GSK-3priming site Ser45.";
Hagen T., Vidal-Puig A.;
Biochem. Biophys. Res. Commun. 294:324-328(2002).
Cited for: PHOSPHORYLATION AT SER-45, CHARACTERIZATION OF VARIANT HEPATOCELLULARCARCINOMA ALA-41, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41,AND CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
PubMed: 12051714

"Identification of beta-catenin as a target of the intracellulartyrosine kinase PTK6.";
Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y.,Asara J.M., Tyner A.L.;
J. Cell Sci. 123:236-245(2010).
Cited for: PHOSPHORYLATION AT TYR-64; TYR-142; TYR-331 AND TYR-333, INTERACTIONWITH PTK6, AND MUTAGENESIS OF TYR-64.
PubMed: 20026641

"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-cateninInteraction.";
Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,Garcia de Herreros A., Dunach M.;
Mol. Cell. Biol. 23:2287-2297(2003).
Cited for: PHOSPHORYLATION AT TYR-142 BY FYN.
PubMed: 12640114

"Regulation of beta-catenin structure and activity by tyrosinephosphorylation.";
Piedra J., Martinez D., Castano J., Miravet S., Dunach M.,de Herreros A.G.;
J. Biol. Chem. 276:20436-20443(2001).
Cited for: PHOSPHORYLATION AT TYR-86 AND TYR-654, INTERACTION WITH TBP, ANDMUTAGENESIS OF TYR-654.
PubMed: 11279024