Q02248

※ Protein Information

Tag	Content
UniProt Accession	CTNB1_MOUSE; Q02248;
Entrez ID	12387
GenBank Protein ID	NM_001165902.1; NM_007614.3;
GenBank Nucleotide ID	NP_001159374.1; NP_031640.1;
Protein Name	Catenin beta-1 (Beta-catenin)
Gene Name	Ctnnb1; Catnb
Organism	Mus musculus
NCBI Taxa ID	10090
Functional 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 adh(view all) Functional 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).
Sequence (Fasta)	MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS 60 QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT 120 NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK 180 KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL 240 VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC 300 LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA 360 GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA 420 AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM 480 AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL 540 VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV 600 QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF 660 RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEALGYR QDDPSYRSFH 720 SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD 780 L 782 Fasta Sequence >Q02248\|Ctnnb1; Catnb\|Mus musculus (Mouse) MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL

※ PTM-Disease Association

Num	PTM	Disease	Type	PTM Site	PMID
1	Serine Phosphorylation	Acute myeloid leukaemia/Acute myelogenous leukemia	P	S37	21156284
1	[Reference]: The development of LSCs led to decreased nuclear phosphorylation of beta-catenin S37 and T41.
2	Threonine Phosphorylation	Acute myeloid leukaemia/Acute myelogenous leukemia	P	T41	21156284
2	[Reference]: The development of LSCs led to decreased nuclear phosphorylation of beta-catenin S37 and T41.

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 42) (view all)	MESH:D058739 ; Aberrant Crypt Foci MESH:D000015 ; Abnormalities, Multiple MESH:D000230 ; Adenocarcinoma MESH:D000236 ; Adenoma MESH:D018248 ; Adenoma, Liver Cell MESH:D000310 ; Adrenal Gland Neoplasms MESH:D018268 ; Adrenocortical Carcinoma MESH:D001943 ; Breast Neoplasms MESH:D006528 ; Carcinoma, Hepatocellular MESH:D002430 ; Cecal Neoplasms MESH:D056486 ; Chemical and Drug Induced Liver Injury MESH:D003110 ; Colonic Neoplasms MESH:D015179 ; Colorectal Neoplasms MESH:D019465 ; Craniofacial Abnormalities MESH:D003397 ; Craniopharyngioma MESH:D018450 ; Disease Progression MESH:D006394 ; Hemangiosarcoma MESH:D018197 ; Hepatoblastoma MESH:D007414 ; Intestinal Neoplasms MESH:D008103 ; Liver Cirrhosis MESH:D008113 ; Liver Neoplasms MESH:D008114 ; Liver Neoplasms, Experimental MESH:D008175 ; Lung Neoplasms MESH:D020522 ; Lymphoma, Mantle-Cell MESH:D008527 ; Medulloblastoma OMIM:615075 ; MENTAL RETARDATION, AUTOSOMAL DOMINANT 19 MESH:C562839 ; Mesothelioma, Malignant MESH:D009133 ; Muscular Atrophy MESH:D009361 ; Neoplasm Invasiveness MESH:D009362 ; Neoplasm Metastasis MESH:D009410 ; Nerve Degeneration MESH:D065886 ; Neurodevelopmental Disorders MESH:D054318 ; No-Reflow Phenomenon MESH:D010051 ; Ovarian Neoplasms MESH:D010190 ; Pancreatic Neoplasms MESH:D010534 ; Peritoneal Neoplasms MESH:D018296 ; Pilomatrixoma MESH:D011471 ; Prostatic Neoplasms MESH:D013262 ; Stevens-Johnson Syndrome MESH:D002583 ; Uterine Cervical Neoplasms MESH:D061205 ; Vascular Calcification MESH:D009396 ; Wilms Tumor

Database

Annotation

CTD (Curated)
(count: 42)
(view all)

MESH:D058739 ; Aberrant Crypt Foci
MESH:D000015 ; Abnormalities, Multiple
MESH:D000230 ; Adenocarcinoma
MESH:D000236 ; Adenoma
MESH:D018248 ; Adenoma, Liver Cell
MESH:D000310 ; Adrenal Gland Neoplasms

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 25) (view all)	142 AVVNLINYQDDAELA dbPAF 179 AVMVHQLSKKEASRH dbPAF 191 SRHAIMRSPQMVSAI dbPAF 23 PDRKAAVSHWQQQSY dbPAF 29 VSHWQQQSYLDSGIH dbPAF 33 QQQSYLDSGIHSGAT dbPAF 37 YLDSGIHSGATTTAP dbPAF 393 RNLSDAATKQEGMEG dbPAF 41 GIHSGATTTAPSLSG dbPAF 45 GATTTAPSLSGKGNP dbPAF 47 TTTAPSLSGKGNPEE dbPAF 489 QNAVRLHYGLPVVVK dbPAF 551 HQDTQRRTSMGGTQQ dbPAF 552 QDTQRRTSMGGTQQQ dbPAF 556 RRTSMGGTQQQFVEG dbPAF 605 LFVQLLYSPIENIQR dbPAF 653 SRNEGVATYAAAVLF dbPAF 654 RNEGVATYAAAVLFR dbPAF 675 QDYKKRLSVELTSSL dbPAF 679 KRLSVELTSSLFRTE dbPAF 680 RLSVELTSSLFRTEP dbPAF 681 LSVELTSSLFRTEPM dbPAF 685 LTSSLFRTEPMAWNE dbPAF 693 EPMAWNETADLGLDI dbPAF 86 VADIDGQYAMTRAQR dbPAF
Ubiquitination (count: 6)	133 AEPSQMLKHAVVNLI PLMD 158 RAIPELTKLLNDEDQ PLMD 170 EDQVVVNKAAVMVHQ PLMD 19 MAMEPDRKAAVSHWQ PLMD 233 EGLLAIFKSGGIPAL PLMD 671 EDKPQDYKKRLSVEL PLMD

PTM

Modification Sites

Phosphorylation
(count: 25)
(view all)

142       AVVNLINYQDDAELA     dbPAF
179       AVMVHQLSKKEASRH     dbPAF
191       SRHAIMRSPQMVSAI     dbPAF
23        PDRKAAVSHWQQQSY     dbPAF
29        VSHWQQQSYLDSGIH     dbPAF
33        QQQSYLDSGIHSGAT     dbPAF

Ubiquitination
(count: 6)

133       AEPSQMLKHAVVNLI     PLMD
158       RAIPELTKLLNDEDQ     PLMD
170       EDQVVVNKAAVMVHQ     PLMD
19        MAMEPDRKAAVSHWQ     PLMD
233       EGLLAIFKSGGIPAL     PLMD
671       EDKPQDYKKRLSVEL     PLMD

※ Protein-Protein Interaction

Network

Interaction

Source

P25799	Q02248	MINT
Q01097	Q02248	IntAct
Q02248	Q61029	MINT
Q02248	Q9WV60	MINT

PTMD Annotation Information

※ Protein Information

Functional Description

Fasta Sequence

※ PTM-Disease Association

※ Disease Cross-ref Annotation

※ PTM Sites

※ Protein-Protein Interaction