| General information | | DisProt: | DP00226 | | Name: | Calcyclin-binding protein | | Synonym(s): | CYBP_MOUSE
CacyBP
Siah-interacting protein
SIP
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q9CXW3 | | UniGene: | Mm.10702 | | SwissProt: | CYBP_MOUSE | | TrEMBL: | | | NCBI (GI): | 46576641 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 229 | | Percent disordered: | 34% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS QKKPELDNEK - 60
PAAVVAPLTT GYTVKISNYG WDQSDKFVKI YITLTGVHQV PTENVQVHFT ERSFDLLVKN - 120
LNGKNYSMIV NNLLKPISVE SSSKKVKTDT VIILCRKKAE NTRWDYLTQV EKECKEKEKP - 180
SYDTEADPSE GLMNVLKKIY EDGDDDMKRT INKAWVESRE KQAREDTEF
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| Functional narrative |
"Siah-interacting protein (SIP) was identified as a novel adaptor that physically links the E3 ubiquitin ligase activity of Siah-1 with Skp1 and Ebi F-Box protein in the degradation of beta-catenin, a transcriptional activator of TCF/LEF genes.... The principal role of SIP appears to be bringing various components of the complex into physical proximity, orchestrating the correct distance and orientation of the E2 enzyme and the site on beta-catenin for ubiquitination." (Bhattacharya et al. 2005)
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| 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.
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| Region 1 | | Type: | Ordered | | Name: | SIPN Domain | | Location: | 1 - 47 | | Length: | 47 | | Region sequence: |
MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQ | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (303 K; pH: 7; NaCl 50 mM; NaPi 20 mM)
| References:
- Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. "The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies." Biochemistry. 2005; 44(27): 9462-71. PubMed: 15996101
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 48 - 73 | | Length: | 26 | | Region sequence: |
QKSQKKPELDNEKPAAVVAPLTTGYT | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (303 K; pH: 7; NaCl 50 mM; NaPi 20 mM)
| References:
- Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. "The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies." Biochemistry. 2005; 44(27): 9462-71. PubMed: 15996101
| Comments:
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| Region 3 | | Type: | Ordered | | Name: | CS Domain | | Location: | 74 - 177 | | Length: | 104 | | Region sequence: |
VKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNL
LKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | | | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (303 K; pH: 7; NaCl 50 mM; NaPi 20 mM)
| References:
- Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. "The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies." Biochemistry. 2005; 44(27): 9462-71. PubMed: 15996101
| Comments:
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| Region 4 | | Type: | Disordered | | Name: | SGS Domain | | Location: | 178 - 229 | | Length: | 52 | | Region sequence: |
EKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (303 K; pH: 7; NaCl 50 mM; NaPi 20 mM)
| References:
- Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. "The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies." Biochemistry. 2005; 44(27): 9462-71. PubMed: 15996101
| Comments:
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| References |
- Matsuzawa S, Li C, Ni CZ, Takayama S, Reed JC, Ely KR. "Structural analysis of Siah1 and its interactions with Siah-interacting protein (SIP)." J Biol Chem. 2003; 278(3): 1837-40. PubMed: 12421809
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