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)
End	175,012,027 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	160,040,445 bp
RNA expression pattern
	Top expressed in
	endothelial cell; ; pons; ; postcentral gyrus; ; entorhinal cortex; ; superior frontal gyrus; ; middle temporal gyrus; ; Brodmann area 46; ; Brodmann area 23; ; orbitofrontal cortex; ; superior vestibular nucleus;
	Top expressed in
	primitive streak; ; abdominal wall; ; maxillary prominence; ; somite; ; yolk sac; ; arcuate nucleus; ; dorsomedial hypothalamic nucleus; ; dermis; ; medial vestibular nucleus; ; paraventricular nucleus of hypothalamus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	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; nucleus; nucleoplasm; neuron projection; cell body; cytoplasm; cytosol; SCF ubiquitin ligase complex;
Biological process	cardiac muscle cell differentiation; positive regulation of DNA replication; human ageing; 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[edit]

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[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116161 – Ensembl, May 2017
^ ^a ^b ^c 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.
^ ^a ^b 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.
^ ^a ^b "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[edit]

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

Further reading[edit]

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.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[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.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]