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Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity3 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator
Biological processCell adhesion, Neurogenesis, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-196299 Beta-catenin phosphorylation cascade
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-3134973 LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-351906 Apoptotic cleavage of cell adhesion proteins
R-MMU-375170 CDO in myogenesis
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-4086398 Ca2+ pathway
R-MMU-418990 Adherens junctions interactions
R-MMU-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-8951430 RUNX3 regulates WNT signaling

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:Ctnnb1
Synonyms:Catnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88276 Ctnnb1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Synapse

Pathology & Biotechi

Disruption phenotypei

Sympathetic ganglia-specific conditional knockout mice lead to a reduction in sympathetic ganglia size and in progenitor cell number, but does not alter sympathetic innervation of peripheral target organs.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi8M → P: Loss of interaction with VCL. 1 Publication1
Mutagenesisi33S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication1
Mutagenesisi37S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication1
Mutagenesisi552S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000642722 – 781Catenin beta-1Add BLAST780

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei23Phosphoserine; by GSK3-beta; alternateBy similarity1
Glycosylationi23O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei29Phosphoserine; by GSK3-betaBy similarity1
Modified residuei33Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei37Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei41Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei49N6-acetyllysineBy similarity1
Modified residuei64Phosphotyrosine; by PTK6By similarity1
Modified residuei86Phosphotyrosine; by CSKBy similarity1
Modified residuei142Phosphotyrosine; by FYN and PTK61 Publication1
Modified residuei191PhosphoserineCombined sources1
Modified residuei246Phosphoserine; by CDK5By similarity1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei333PhosphotyrosineBy similarity1
Modified residuei552Phosphoserine; by AMPKCombined sources1 Publication1
Modified residuei556PhosphothreonineBy similarity1
Modified residuei619S-nitrosocysteine1 Publication1
Modified residuei654PhosphotyrosineBy similarity1
Modified residuei675PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding (By similarity). Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization (By similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity (By similarity).By similarity
Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity).By similarity
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.1 Publication
O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.By similarity
Deacetylated at Lys-49 by SIRT1.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiQ02248
PaxDbiQ02248
PeptideAtlasiQ02248
PRIDEiQ02248

PTM databases

iPTMnetiQ02248
PhosphoSitePlusiQ02248
SwissPalmiQ02248

Miscellaneous databases

PMAP-CutDBiQ02248

Expressioni

Tissue specificityi

Expressed in cerebellar granule neurons (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000006932 Expressed in 363 organ(s), highest expression level in olfactory bulb
CleanExiMM_CTNNB1
ExpressionAtlasiQ02248 baseline and differential
GenevisibleiQ02248 MM

Interactioni

Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Binds SLC9A3R1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with PTPRJ. Interacts with PKT7. Interacts with FAT1 (via the cytoplasmic domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts with NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6. Interacts with RAPGEF2. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. Interacts with FERMT2. Identified in a complex with TCF4 and FERMT2. Another cytoplasmic pool is part of a large complex containing 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. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1 and CTNNA3. Interacts with TRPV4; the TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. The CTNNB1 and TCF4 complex interacts with PML. Interacts with XIRP1. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with GLIS2. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with SLC30A9. Interacts with RORA. May interact with P-cadherin/CDH3. Interacts with RNF220 (By similarity). Interacts with CTNND2 (By similarity). Interacts (via the C-terminal region) with CBY1 (By similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity). Interacts with DLG5 (PubMed:25232112). Interacts with FAM53B; promoting translocation to the nucleus. Interacts with TMEM170B (By similarity). Interacts with AHI1 (By similarity). Interacts with GID8 (By similarity). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity).By similarity21 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198512, 88 interactors
ComplexPortaliCPX-318 beta1-catenin - LEF1 complex
CPX-86 Beta-catenin-ICAT complex
CORUMiQ02248
DIPiDIP-31560N
IntActiQ02248, 75 interactors
MINTiQ02248
STRINGi10090.ENSMUSP00000007130

Structurei

Secondary structure

1781
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00341
ProteinModelPortaliQ02248
SMRiQ02248
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02248

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati151 – 191ARM 1Add BLAST41
Repeati193 – 234ARM 2Add BLAST42
Repeati235 – 276ARM 3Add BLAST42
Repeati277 – 318ARM 4Add BLAST42
Repeati319 – 360ARM 5Add BLAST42
Repeati361 – 389ARM 6Add BLAST29
Repeati400 – 441ARM 7Add BLAST42
Repeati442 – 484ARM 8Add BLAST43
Repeati489 – 530ARM 9Add BLAST42
Repeati531 – 571ARM 10Add BLAST41
Repeati594 – 636ARM 11Add BLAST43
Repeati637 – 666ARM 12Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 23Interaction with VCL1 PublicationAdd BLAST22
Regioni156 – 178Interaction with BCL9By similarityAdd BLAST23
Regioni772 – 781Interaction with SCRIB1 Publication10

Sequence similaritiesi

Belongs to the beta-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4203 Eukaryota
COG0035 LUCA
GeneTreeiENSGT00730000110821
HOGENOMiHOG000230958
HOVERGENiHBG000919
InParanoidiQ02248
KOiK02105
OMAiFNQNFSQ
OrthoDBiEOG091G03A5
PhylomeDBiQ02248
TreeFamiTF317997

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR013284 Beta-catenin
PfamiView protein in Pfam
PF00514 Arm, 4 hits
PRINTSiPR01869 BCATNINFAMLY
SMARTiView protein in SMART
SM00185 ARM, 12 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 9 hits

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All

Q02248-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,471
Last modified:July 1, 1993 - v1
Checksum:iD708F170A3FBED6E
GO

Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q6A9E9Q6A9_MOUSE
Catenin beta-1
Ctnnb1
607Annotation score:
F7BAC9F7BAC9_MOUSE
Catenin beta-1
Ctnnb1
169Annotation score:
D3YUH4D3YUH4_MOUSE
Catenin beta-1
Ctnnb1
174Annotation score:
F7CRC6F7CRC6_MOUSE
Catenin beta-1
Ctnnb1
174Annotation score:
F6QZ47F6QZ47_MOUSE
Catenin beta-1
Ctnnb1
145Annotation score:
D3Z7S6D3Z7S6_MOUSE
Catenin beta-1
Ctnnb1
42Annotation score:
D3Z5Q1D3Z5Q1_MOUSE
Catenin beta-1
Ctnnb1
83Annotation score:
E9PW26E9PW26_MOUSE
Catenin beta-1
Ctnnb1
90Annotation score:

Sequence cautioni

The sequence AAH06739 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti371T → I in BAB31250 (PubMed:16141072).Curated1
Sequence conflicti478A → T in BAB31250 (PubMed:16141072).Curated1
Sequence conflicti487L → F in BAB31250 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA Translation: AAA37280.1
AK035311 mRNA Translation: BAC29027.1
AK018515 mRNA Translation: BAB31250.1
BC006739 mRNA Translation: AAH06739.1 Different initiation.
BC048153 mRNA Translation: AAH48153.1
BC053065 mRNA Translation: AAH53065.1
CCDSiCCDS23630.1
PIRiS35091
RefSeqiNP_001159374.1, NM_001165902.1
NP_031640.1, NM_007614.3
UniGeneiMm.291928

Genome annotation databases

EnsembliENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932
GeneIDi12387
KEGGimmu:12387
UCSCiuc009scu.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA Translation: AAA37280.1
AK035311 mRNA Translation: BAC29027.1
AK018515 mRNA Translation: BAB31250.1
BC006739 mRNA Translation: AAH06739.1 Different initiation.
BC048153 mRNA Translation: AAH48153.1
BC053065 mRNA Translation: AAH53065.1
CCDSiCCDS23630.1
PIRiS35091
RefSeqiNP_001159374.1, NM_001165902.1
NP_031640.1, NM_007614.3
UniGeneiMm.291928

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DOWX-ray1.80B118-149[»]
1I7WX-ray2.00A/C134-671[»]
1I7XX-ray3.00A/C134-671[»]
1JPPX-ray3.10A/B134-671[»]
1M1EX-ray2.10A134-671[»]
1V18X-ray2.10A134-671[»]
2BCTX-ray2.90A150-665[»]
3BCTX-ray2.10A193-661[»]
3OUWX-ray2.91A134-671[»]
3OUXX-ray2.40A134-671[»]
4EV8X-ray1.90A134-671[»]
4EV9X-ray2.10A134-671[»]
4EVAX-ray2.00A/C134-671[»]
4EVPX-ray2.26A134-671[»]
4EVTX-ray2.34A134-671[»]
4ONSX-ray2.80B/D78-151[»]
DisProtiDP00341
ProteinModelPortaliQ02248
SMRiQ02248
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198512, 88 interactors
ComplexPortaliCPX-318 beta1-catenin - LEF1 complex
CPX-86 Beta-catenin-ICAT complex
CORUMiQ02248
DIPiDIP-31560N
IntActiQ02248, 75 interactors
MINTiQ02248
STRINGi10090.ENSMUSP00000007130

PTM databases

iPTMnetiQ02248
PhosphoSitePlusiQ02248
SwissPalmiQ02248

Proteomic databases

MaxQBiQ02248
PaxDbiQ02248
PeptideAtlasiQ02248
PRIDEiQ02248

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932
GeneIDi12387
KEGGimmu:12387
UCSCiuc009scu.2 mouse

Organism-specific databases

CTDi1499
MGIiMGI:88276 Ctnnb1

Phylogenomic databases

eggNOGiKOG4203 Eukaryota
COG0035 LUCA
GeneTreeiENSGT00730000110821
HOGENOMiHOG000230958
HOVERGENiHBG000919
InParanoidiQ02248
KOiK02105
OMAiFNQNFSQ
OrthoDBiEOG091G03A5
PhylomeDBiQ02248
TreeFamiTF317997

Enzyme and pathway databases

ReactomeiR-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-196299 Beta-catenin phosphorylation cascade
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-3134973 LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-351906 Apoptotic cleavage of cell adhesion proteins
R-MMU-375170 CDO in myogenesis
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-4086398 Ca2+ pathway
R-MMU-418990 Adherens junctions interactions
R-MMU-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-8951430 RUNX3 regulates WNT signaling

Miscellaneous databases

ChiTaRSiCtnnb1 mouse
EvolutionaryTraceiQ02248
PMAP-CutDBiQ02248
PROiPR:Q02248
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000006932 Expressed in 363 organ(s), highest expression level in olfactory bulb
CleanExiMM_CTNNB1
ExpressionAtlasiQ02248 baseline and differential
GenevisibleiQ02248 MM

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR013284 Beta-catenin
PfamiView protein in Pfam
PF00514 Arm, 4 hits
PRINTSiPR01869 BCATNINFAMLY
SMARTiView protein in SMART
SM00185 ARM, 12 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 9 hits
ProtoNetiSearch...

Entry informationi

Entry nameiCTNB1_MOUSE
AccessioniPrimary (citable) accession number: Q02248
Secondary accession number(s): Q922W1, Q9D335
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 7, 2018
This is version 218 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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