General information | DisProt: | DP00709 | Name: | Protein chibby homolog 1 | Synonym(s): | CBY1_HUMAN
ARPP-binding protein
Cytosolic leucine-rich protein
PIGEA-14
PKD2 interactor, Golgi and endoplasmic reticulum-associated 1
Chibby
Cby
| First appeared in release: | Release 5.7 (02/28/2011) | UniProt: | Q9Y3M2 | UniGene: | | SwissProt: | CBY1_HUMAN | TrEMBL: | | NCBI (GI): | | Source organism: | Homo sapiens (Human) | Sequence length: | 126 | Percent disordered: | 50% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MPFFGNTFSP KKTPPRKSAS LSNLHSLDRS TREVELGLEY GSPTMNLAGQ SLKFENGQWI - 60 AETGVSGGVD RREVQRLRRR NQQLEEENNL LRLKVDILLD MLSESTAESH LMEKELDELR - 120 ISRKRK
|
Functional narrative |
Function: Inhibits the Wnt/Wingless pathway by binding to beta- catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation.
SUBUNIT: Homodimer. Interacts with polycystin-2/PKD2 and GM130. Interacts with the C-terminal region of beta-catenin.
Subcellular Location: Nucleus speckle. Golgi apparatus, trans- Golgi network. Note=Nuclear, in a punctate manner. Also found in the trans-Golgi.
TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in heart, skeletal muscle, kidney and placenta. Also found in brain, lung, liver and testis. Significantly down-regulated in thyroid and metastatic uterine tumors.
MISCELLANEOUS: \'Chibby\' is Japanese for \'small\'; the gene was so named for the RNAi phenotype seen in flies.
SIMILARITY: Belongs to the chibby family. -----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
|
Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
Region 1 | Type: | Disordered w/ Residual Structure | Name: | N-terminal segment | Location: | 1 - 19 | Length: | 19 | Region sequence: |
MPFFGNTFSPKKTPPRKSA | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Nuclear localization
Protein-protein binding
Phosphorylation
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 5; Cby (250-300 uM); sodium acetate 10 mM; urea (varying concentrations))
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; 14-3-3-zeta (protein interaction partner) 600 uM; DTT 1 mM; EDTA 1 mM; NaOH 50 mM; N-Cby(S20D) (to simulate phoshorylated-Cby) 200 uM; sodium acetate (buffer) 10 mM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; at various pH levels; Cby 40 uM; sodium acetate 10 mM; urea (or various other additives))
- Dynamic light scattering (298 K; pH: 5; Cby (concentrations of 50 uM and above) 50 uM; sodium acetate 10 mM)
| References:
- Mokhtarzada S, Yu C, Brickenden A, Choy WY. "Structural Characterization of Partially Disordered Human Chibby: Insights into Its Function in the Wnt-Signaling Pathway." 2011. PubMed: 21182262
| Comments:Mokhtarzada et al (2010) describe the N-terminal of Chibby (N-Cby) as overall intrinsically disordered with "mild helical propensity" at aa 20-50, while the rest of N-Cby "adopts transient beta-strand structure." Additionally, N-Cby contains a binding motif for 14-3-3 proteins at aa 16-22, and a nuclear export signal at aa 21-29.
|
Region 2 | Type: | Disordered w/ Residual Structure | Name: | N-terminal segment | Location: | 20 - 50 | Length: | 31 | Region sequence: |
SLSNLHSLDRSTREVELGLEYGSPTMNLAGQ | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Nuclear localization
Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 5; Cby (250-300 uM); sodium acetate (buffer) 10 mM; urea (varying concentrations))
- Nuclear magnetic resonance (NMR) (298 K; pH: 5; 14-3-3-zeta (protein interaction partner) 600 uM; DTT (buffer) 1 mM; EDTA (buffer) 1 mM; NaOH 50 mM; N-Cby(S20D) (to simulate phoshorylated-Cby) 200 uM; sodium acetate (buffer) 10 mM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; at various pH levels; Cby 40 uM; sodium acetate (buffer) 10 mM; urea (or various other additives))
- Dynamic light scattering (298 K; pH: 5; Cby (concentrations of 50 uM and above); sodium acetate (buffer))
| References:
- Mokhtarzada S, Yu C, Brickenden A, Choy WY. "Structural Characterization of Partially Disordered Human Chibby: Insights into Its Function in the Wnt-Signaling Pathway." 2011. PubMed: 21182262
| Comments:Mokhtarzada et al (2010) describe the N-terminal of Chibby (N-Cby) as overall intrinsically disordered with "mild helical propensity" at aa 20-50, while the rest of N-Cby "adopts transient beta-strand structure." Additionally, N-Cby contains a binding motif for 14-3-3 proteins at aa 16-22, and a nuclear export signal at aa 21-29.
|
Region 3 | Type: | Disordered w/ Residual Structure | Name: | N-terminal segment | Location: | 51 - 63 | Length: | 13 | Region sequence: |
SLKFENGQWIAET | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Nuclear localization
Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 5; Cby (250-300 uM); sodium acetate 10 mM; urea (varying concentrations))
- Circular dichroism (CD) spectroscopy, far-UV (298 K; at various pH levels; Cby 40 uM; sodium acetate 10 mM; urea (or various other additives))
- Dynamic light scattering (298 K; pH: 5; Cby (concentrations of 50 uM and above) 50 uM; sodium acetate 10 mM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 5; 14-3-3-zeta (protein interaction partner) 600 uM; DTT 1 mM; EDTA 1 mM; NaOH 50 mM; N-Cby(S20D) (to simulate phoshorylated-Cby) 200 uM; sodium acetate (buffer) 10 mM)
| References:
- Mokhtarzada S, Yu C, Brickenden A, Choy WY. "Structural Characterization of Partially Disordered Human Chibby: Insights into Its Function in the Wnt-Signaling Pathway." 2011. PubMed: 21182262
| Comments:Mokhtarzada et al (2010) describe the N-terminal of Chibby (N-Cby) as overall intrinsically disordered with "mild helical propensity" at aa 20-50, while the rest of N-Cby "adopts transient beta-strand structure." Additionally, N-Cby contains a binding motif for 14-3-3 proteins at aa 16-22, and a nuclear export signal at aa 21-29.
|
Region 4 | Type: | Ordered | Name: | C-terminal region | Location: | 64 - 126 | Length: | 63 | Region sequence: |
GVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISR KRK | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises from the ordered state | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Intraprotein interaction
Nuclear localization
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 5; Cby (250-300 uM); sodium acetate 10 mM; urea (varying concentrations))
- Circular dichroism (CD) spectroscopy, far-UV (298 K; at various pH levels; Cby 40 uM; sodium acetate 10 mM; urea (or various other additives))
- Dynamic light scattering (298 K; pH: 5; Cby (concentrations of 50 uM and above) 50 uM; sodium acetate 10 mM)
| References:
- Mokhtarzada S, Yu C, Brickenden A, Choy WY. "Structural Characterization of Partially Disordered Human Chibby: Insights into Its Function in the Wnt-Signaling Pathway." 2011. PubMed: 21182262
| Comments:According to Mokhtarzada et al (2010), the C-terminal of Chibby is "strongly alpha-helical...with a stable four-heptad repeat coiled-coil" at aa 73-100.
|
References |
- Mokhtarzada S, Yu C, Brickenden A, Choy WY. "Structural Characterization of Partially Disordered Human Chibby: Insights into Its Function in the Wnt-Signaling Pathway." 2011. PubMed: 21182262
|
Comments |
Author Verified 1-31-2011 (PubMed: 21182262)
|
If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|