P35222

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession CTNB1_HUMAN; P35222;
Entrez ID 1499
GenBank Protein ID
GenBank Nucleotide ID
Protein Name Catenin beta-1 (Beta-catenin)
Gene Name CTNNB1; CTNNB; OK/SW-cl.35; PRO2286
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionKey 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)
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 GAQGEPLGYR QDDPSYRSFH 720
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD 780
L 782

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1PhosphorylationProstate cancer/carcinoma/adenocarcinomaP24088787
[Reference]: Similarly, AR79 inhibited -catenin phosphorylation, increased nuclear -catenin accumulation in prostate cancer and osteoblast cell lines, and increased proliferation of prostate cancer cells in vitro through -catenin
2Serine PhosphorylationPrimary hyperparathyroidismDS3322576020
[Reference]: Taking also previous studies into account we conclude that activating mutations of the regulatory GSK3? phosphorylation sites serine 33 and 37, encoded by CTNNB1 exon 3, rarely occur in parathyroid adenomas from patients with pHP
3Serine PhosphorylationMelanomaUS3317001009
[Reference]: Identification of class I MHC-associated phosphopeptides as targets for cancer immunotherapy.
4Serine PhosphorylationPrimary hyperparathyroidismDS3722576020
[Reference]: Taking also previous studies into account we conclude that activating mutations of the regulatory GSK3? phosphorylation sites serine 33 and 37, encoded by CTNNB1 exon 3, rarely occur in parathyroid adenomas from patients with pHP
5Serine PhosphorylationNephroblastomaNS4512239584
[Reference]: Frequent beta-catenin mutations preferentially occurring at codon 45 most likely indicate special importance of this codon for the development of WT and existence of an underlying mechanism causing such a tissue-specific mutational pattern.
6Serine PhosphorylationCutaneous malignant melanomaNS4511351304
[Reference]: Mutations altering the GSK-3beta phosphorylation sites lead to cellular accumulation of beta-catenin and constitutive transcription of Tcf/Lef target genes.
7Threonine PhosphorylationProstate cancer/carcinoma/adenocarcinomaLNCaPDT12022511927
[Reference]: Beta-catenin phosphorylated at threonine 120 antagonizes generation of active beta-catenin by spatial localization in trans-Golgi network
8Tyrosine PhosphorylationGlioblastomaUY33322056988
[Reference]: In addition, positive correlations have been identified between c-Src activity, ?-catenin Y333 phosphorylation and PKM2 nuclear accumulation in human glioblastoma specimens.?
9Serine PhosphorylationColitisUS55220580720
[Reference]: Biochemical analyses indicated that PI3K-Akt signaling increased nuclear total beta-catenin and P-beta-catenin(552) levels and reduced N-terminal beta-catenin phosphorylation, which is associated with degradation.?
10Tyrosine PhosphorylationIntestinal cancerPY65421307168
[Reference]: B-catenin tyrosine 654 phosphorylation increases Wnt signalling and intestinal tumorigenesis

※ Disease Cross-ref Annotation

DatabaseAnnotation
Cancer Gene Census
colorectal, ovarian, hepatoblastoma, pleomorphic salivary gland adenoma, other tumour types
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
DisGeNet (Curated)
(count: 106)
(view all)
C0000737; Abdominal Pain
C0001418; Adenocarcinoma
C0001430; Adenoma
C0001624; Adrenal Gland Neoplasms
C0007134; Renal Cell Carcinoma
C0007528; Cecal Neoplasms
HGMD
(count: 1)
CM043757; Colorectal adenoma?; Missense/nonsense
GWASdb
(count: 1)
rs13072632; Multiple complex diseases; Null

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 49)
(view all)
102       RAAMFPETLDEGMQI     dbPAF
112       EGMQIPSTQFDAAHP     dbPAF
120       QFDAAHPTNVQRLAE     dbPAF
142       AVVNLINYQDDAELA     dbPAF
179       AVMVHQLSKKEASRH     dbPAF
191       SRHAIMRSPQMVSAI     dbPAF
Acetylation
(count: 5)
133       AEPSQMLKHAVVNLI     PLMD
19        MAMEPDRKAAVSHWQ     PLMD
345       WTTSRVLKVLSVCSS     PLMD
354       LSVCSSNKPAIVEAG     PLMD
49        TAPSLSGKGNPEEED     PLMD
Ubiquitination
(count: 17)
(view all)
133       AEPSQMLKHAVVNLI     PLMD
158       RAIPELTKLLNDEDQ     PLMD
170       EDQVVVNKAAVMVHQ     PLMD
180       VMVHQLSKKEASRHA     PLMD
181       MVHQLSKKEASRHAI     PLMD
19        MAMEPDRKAAVSHWQ     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource
A7KAX9P35222HPRD
E9PH57P35222HPRD
F5GWR8P35222HPRD
F5GYI6P35222HPRD
F8W742P35222MINT
F8WA38P35222HPRD
G3V0F8P35222HPRD
H3BM20P35222MINT
H3BVI7P35222MINT
O00512P35222HPRD; IntAct
O00570P35222HPRD
O14617P35222IntAct
O14640P35222HPRD
O14745P35222HPRD
O14907P35222HPRD
O14920P35222HPRD
O15105P35222HPRD
O15111P35222HPRD
O15169P35222HPRD; IntAct; MINT
O15399P35222HPRD
O43707P35222IntAct
O60907P35222HPRD
O75030P35222HPRD
O75309P35222HPRD
O75564P35222MINT
O75937P35222IntAct
O95405P35222HPRD; MINT
O95996P35222HPRD
P00519P35222MINT
P00533P35222HPRD
P03372P35222HPRD
P04626P35222HPRD
P05549P35222HPRD
P06241P35222HPRD; MINT
P07947P35222MINT
P08575P35222IntAct; MINT
P08581P35222HPRD
P09496P35222IntAct
P10275P35222HPRD; IntAct; MINT
P10586P35222HPRD
P11362P35222IntAct
P11388P35222IntAct
P12830P35222DIP; IntAct; MINT
P12931P35222HPRD; MINT
P15311P35222HPRD
P15884P35222DIP; IntAct; MINT
P15923P35222HPRD
P15941P35222HPRD
P16150P35222HPRD
P16284P35222HPRD; IntAct
P16591P35222HPRD; MINT
P17948P35222HPRD
P18031P35222HPRD
P19022P35222HPRD; DIP; IntAct; MINT
P19793P35222HPRD
P19838P35222MINT;HPRD
P20749P35222HPRD
P20823P35222HPRD
P22223P35222HPRD
P22314P35222IntAct
P23467P35222IntAct
P23470P35222IntAct; MINT
P23471P35222HPRD
P24385P35222HPRD
P24666P35222HPRD
P25054P35222HPRD; IntAct; MINT
P27986P35222HPRD
P29317P35222DIP
P33151P35222HPRD; IntAct; MINT
P35221P35222HPRD; DIP; MINT
P35222P35240HPRD
P35222P35813HPRD; MINT
P35222P35869DIP
P35222P35968HPRD
P35222P36402MINT
P35222P36897HPRD
P35222P37173HPRD
P35222P37198BioGRID
P35222P39687IntAct
P35222P42167MINT
P35222P42574HPRD
P35222P42858MINT
P35222P46778IntAct
P35222P46937IntAct
P35222P46940HPRD
P35222P48729HPRD
P35222P48730HPRD
P35222P49715HPRD
P35222P49768HPRD; IntAct
P35222P49789DIP
P35222P49810HPRD
P35222P49841IntAct; MINT;HPRD
P35222P50402MINT
P35222P50748BioGRID
P35222P53350HPRD
P35222P55197DIP
P35222P55286HPRD
P35222P55287HPRD
P35222P55291HPRD
P35222P62837IntAct
P35222P62877IntAct
P35222P62945IntAct
P35222P63208IntAct
P35222P68400HPRD
P35222P84022HPRD
P35222P98161HPRD
P35222P98164IntAct
P35222P98177HPRD
P35222Q00534HPRD
P35222Q01826DIP
P35222Q02952IntAct
P35222Q05209IntAct
P35222Q05586HPRD
P35222Q08050IntAct
P35222Q09472HPRD
P35222Q12778HPRD
P35222Q12913HPRD; IntAct; MINT
P35222Q12923HPRD
P35222Q13002HPRD
P35222Q13285HPRD
P35222Q13308MINT
P35222Q13485HPRD
P35222Q13526HPRD
P35222Q13547MINT
P35222Q13616IntAct
P35222Q13761IntAct
P35222Q14192HPRD
P35222Q14344HPRD
P35222Q14498IntAct
P35222Q14526MINT
P35222Q14574HPRD
P35222Q14790HPRD
P35222Q15078HPRD
P35222Q15262HPRD
P35222Q15596HPRD; MINT
P35222Q15642HPRD
P35222Q15678HPRD
P35222Q15796HPRD
P35222Q16531DIP
P35222Q16658HPRD
P35222Q16665HPRD
P35222Q16790HPRD
P35222Q16827IntAct
P35222Q17RP2MINT
P35222Q2LD37IntAct
P35222Q4KMG0HPRD
P35222Q4LDE5BioGRID
P35222Q4LE28HPRD; MINT
P35222Q4LE39IntAct
P35222Q5SRQ6HPRD
P35222Q5VTL8IntAct
P35222Q6P1J9HPRD; IntAct
P35222Q86UL8HPRD
P35222Q86UP0HPRD
P35222Q86UU0HPRD
P35222Q8CIW2MINT
P35222Q8TAM6IntAct
P35222Q8TDM6HPRD
P35222Q8TDN6IntAct
P35222Q8TEK3DIP
P35222Q8TEW0MINT
P35222Q8WVC0HPRD; IntAct
P35222Q8WYP5IntAct
P35222Q92597HPRD; IntAct;IntAct
P35222Q92729HPRD
P35222Q92731IntAct
P35222Q92793IntAct
P35222Q93008HPRD
P35222Q96B97IntAct
P35222Q96JM7IntAct
P35222Q96PU4IntAct
P35222Q96QZ7HPRD
P35222Q99623IntAct
P35222Q99697HPRD
P35222Q99959HPRD
P35222Q9BR09HPRD
P35222Q9BVG4IntAct
P35222Q9BWV1HPRD
P35222Q9BZE0HPRD; MINT
P35222Q9H6I2HPRD
P35222Q9HBD4HPRD
P35222Q9HCK8HPRD
P35222Q9HCS4HPRD
P35222Q9NQB0DIP; IntAct; MINT;HPRD
P35222Q9NRD5HPRD
P35222Q9NSA3HPRD; IntAct; MINT
P35222Q9NSC2HPRD
P35222Q9NZI8HPRD
P35222Q9P287IntAct
P35222Q9UEW8IntAct
P35222Q9UGN5MINT
P35222Q9UI47HPRD
P35222Q9UJU2HPRD; DIP
P35222Q9UKB5HPRD
P35222Q9UKE5MINT
P35222Q9UKG1IntAct
P35222Q9ULB4HPRD
P35222Q9ULB5HPRD
P35222Q9UPQ9IntAct
P35222Q9UQB3HPRD
P35222Q9Y230HPRD
P35222Q9Y265HPRD; DIP
P35222Q9Y297HPRD; IntAct; MINT
P35222Q9Y2T1HPRD
P35222Q9Y3M2HPRD; DIP
P35222Q9Y3Y4HPRD
P35222Q9Y4G8HPRD