CACYBP

Calcyclin-binding protein is a protein that in humans is encoded by the CACYBP gene.[5][6][7]

CACYBP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X5M, 2A25, 2A26
Identifiers
Aliases	CACYBP, GIG5, S100A6BP, SIP, PNAS-107, calcyclin binding protein
External IDs	OMIM: 606186 MGI: 1270839 HomoloGene: 7649 GeneCards: CACYBP
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q25.1 Start 174,999,163 bp[1] End 175,012,027 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H2.1 Start 160,202,367 bp[2] End 160,212,875 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • protein homodimerization activity • protein domain specific binding • ubiquitin protein ligase binding • tubulin binding • S100 protein binding Cellular component • nuclear envelope lumen • extracellular exosome • beta-catenin destruction complex • cell nucleus • nucleoplasm • neuron projection • cell body • cytoplasm • cytosol • SCF ubiquitin ligase complex Biological process • cardiac muscle cell differentiation • positive regulation of DNA replication • aging • negative regulation of cell death • cellular response to calcium ion • heart development • response to growth hormone • cellular response to leukemia inhibitory factor Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27101	12301
Ensembl	ENSG00000116161	ENSMUSG00000014226
UniProt	Q9HB71	Q9CXW3
RefSeq (mRNA)	NM_014412 NM_001007214	NM_009786
RefSeq (protein)	NP_001007215 NP_055227	NP_033916
Location (UCSC)	Chr 1: 175 – 175.01 Mb	Chr 1: 160.2 – 160.21 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene is a calcyclin binding protein. It may be involved in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. It probably serves as a molecular bridge in ubiquitin E3 complexes and participates in the ubiquitin-mediated degradation of beta-catenin. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.[7]

Protein Interactions

CACYBP has been shown to interact with SKP1A[8] and SIAH1.[5]

The CacyBP/SIP complex instead, is known to be a part of stress respons, since it interacts with chaperone HSP90[9].

References

1. GRCh38: Ensembl release 89: ENSG00000116161 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000014226 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Matsuzawa SI, Reed JC (May 2001). "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses". Molecular Cell. 7 (5): 915–26. doi:10.1016/S1097-2765(01)00242-8. PMID 11389839.
6. Matsuzawa S, Li C, Ni CZ, Takayama S, Reed JC, Ely KR (January 2003). "Structural analysis of Siah1 and its interactions with Siah-interacting protein (SIP)". The Journal of Biological Chemistry. 278 (3): 1837–40. doi:10.1074/jbc.M210263200. PMID 12421809.
7. "Entrez Gene: CACYBP calcyclin binding protein".
8. Matsuzawa SI, Reed JC (May 2001). "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses". Molecular Cell. 7 (5): 915–26. doi:10.1016/S1097-2765(01)00242-8. PMID 11389839.
9. Filipek, Anna; Leśniak, Wiesława (2018-12-29). "Aktualny pogląd na komórkową funkcję S100A6 i jego ligandów, CacyBP/SIP i Sgt1". Postępy Biochemii (in Polish). 64 (3): 242–252. doi:10.18388/pb.2018_136. ISSN 0032-5422.

External links

• Human CACYBP genome location and CACYBP gene details page in the UCSC Genome Browser.

Further reading

• Filipek A, Jastrzebska B, Nowotny M, Kwiatkowska K, Hetman M, Surmacz L, et al. (June 2002). "Ca2+-dependent translocation of the calcyclin-binding protein in neurons and neuroblastoma NB-2a cells". The Journal of Biological Chemistry. 277 (23): 21103–9. doi:10.1074/jbc.M111010200. PMID 11927578.
• Liu WX, Wu J, Zhao Z, Zhou Y, Peng XZ, Yuan JG, Qiang BQ (March 2002). "[Cloning and expression of human calcyclin binding protein (hCacyBP) gene]". Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica et Biophysica Sinica. 34 (2): 181–6. PMID 12006993.
• Filipek A, Jastrzebska B, Nowotny M, Kuznicki J (August 2002). "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family". The Journal of Biological Chemistry. 277 (32): 28848–52. doi:10.1074/jbc.M203602200. PMID 12042313.
• Wu J, Tan X, Peng X, Yuan J, Qiang B (July 2003). "Translocation and phosphorylation of calcyclin binding protein during retinoic acid-induced neuronal differentiation of neuroblastoma SH-SY5Y cells". Journal of Biochemistry and Molecular Biology. 36 (4): 354–8. doi:10.5483/bmbrep.2003.36.4.354. PMID 12895292.
• Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, et al. (October 2005). "Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex". The Journal of Biological Chemistry. 280 (40): 34278–87. doi:10.1074/jbc.M506707200. PMID 16085652.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Sun S, Ning X, Liu J, Liu L, Chen Y, Han S, et al. (May 2007). "Overexpressed CacyBP/SIP leads to the suppression of growth in renal cell carcinoma". Biochemical and Biophysical Research Communications. 356 (4): 864–71. doi:10.1016/j.bbrc.2007.03.080. PMID 17400182.