CACYBP

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]
End	175,012,027 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[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
	27101
	12301
	ENSG00000116161
	ENSMUSG00000014226
	Q9HB71
	Q9CXW3
	NM_014412; NM_001007214
	NM_009786
	NP_001007215; NP_055227
	NP_033916
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

GRCh38: Ensembl release 89: ENSG00000116161 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000014226 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.
"Entrez Gene: CACYBP calcyclin binding protein".
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.
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. PMID 30656909.

External links

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

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. S2CID 4427026.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000116161 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid11389839-5] 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.

[pmid12421809-6] 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.

[entrez-7] "Entrez Gene: CACYBP calcyclin binding protein".

[autogenerated1-8] 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. PMID 30656909.

CACYBP

Protein Interactions

References

External links

Further reading