MYCBP

C-Myc-binding protein is a protein that in humans is encoded by the MYCBP gene.[4][5]

MYCBP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2YY0
Identifiers
Aliases	MYCBP, AMY-1, MYC binding protein
External IDs	OMIM: 606535 MGI: 1891750 HomoloGene: 49312 GeneCards: MYCBP
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p34.3 Start 38,862,493 bp[1] End 38,873,368 bp[1]
Gene ontology Molecular function • GO:0001105 transcription coactivator activity • GO:0001948 protein binding Cellular component • cytoplasm • cell nucleus • mitochondrion Biological process • regulation of transcription, DNA-templated • transcription, DNA-templated • spermatogenesis • positive regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	26292	56309
Ensembl	ENSG00000214114	n/a
UniProt	Q99417	Q9EQS3
RefSeq (mRNA)	NM_012333	NM_019660
RefSeq (protein)	NP_036465	NP_062634
Location (UCSC)	Chr 1: 38.86 – 38.87 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Function

The MYCBP gene encodes a protein that binds to the N-terminal region of MYC (MIM 190080) and stimulates the activation of E box-dependent transcription by MYC.[supplied by OMIM][5]

Interactions

MYCBP has been shown to interact with AKAP1,[6][7] C3orf15[6] and Myc.[4]

References

1. GRCh38: Ensembl release 89: ENSG00000214114 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Taira T, Maëda J, Onishi T, Kitaura H, Yoshida S, Kato H, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H (Aug 1998). "AMY-1, a novel C-MYC binding protein that stimulates transcription activity of C-MYC". Genes to Cells. 3 (8): 549–65. doi:10.1046/j.1365-2443.1998.00206.x. PMID 9797456.
5. "Entrez Gene: MYCBP c-myc binding protein".
6. Yukitake H, Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (Nov 2002). "AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase". The Journal of Biological Chemistry. 277 (47): 45480–92. doi:10.1074/jbc.M206201200. PMID 12223483.
7. Furusawa M, Ohnishi T, Taira T, Iguchi-Ariga SM, Ariga H (Sep 2001). "AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm by association with S-AKAP84, an anchor protein of cAMP-dependent protein kinase". The Journal of Biological Chemistry. 276 (39): 36647–51. doi:10.1074/jbc.M103885200. PMID 11483602.

Further reading

• Furusawa M, Ohnishi T, Taira T, Iguchi-Ariga SM, Ariga H (Sep 2001). "AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm by association with S-AKAP84, an anchor protein of cAMP-dependent protein kinase". The Journal of Biological Chemistry. 276 (39): 36647–51. doi:10.1074/jbc.M103885200. PMID 11483602.
• Yukitake H, Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (Aug 2002). "AMAP-1, a novel testis-specific AMY-1-binding protein, is differentially expressed during the course of spermatogenesis". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1577 (1): 126–32. doi:10.1016/s0167-4781(02)00411-6. PMID 12151104.
• Yukitake H, Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (Nov 2002). "AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase". The Journal of Biological Chemistry. 277 (47): 45480–92. doi:10.1074/jbc.M206201200. PMID 12223483.
• Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (Dec 2002). "AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex". The Journal of Biological Chemistry. 277 (52): 50885–92. doi:10.1074/jbc.M206387200. PMID 12414807.
• Tomsig JL, Snyder SL, Creutz CE (Mar 2003). "Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif". The Journal of Biological Chemistry. 278 (12): 10048–54. doi:10.1074/jbc.M212632200. PMID 12522145.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 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.
• Ishizaki R, Shin HW, Iguchi-Ariga SM, Ariga H, Nakayama K (Aug 2006). "AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors". Genes to Cells. 11 (8): 949–59. doi:10.1111/j.1365-2443.2006.00991.x. PMID 16866877.
• Sedoris KC, Thomas SD, Miller DM (Jul 2007). "c-myc promoter binding protein regulates the cellular response to an altered glucose concentration". Biochemistry. 46 (29): 8659–68. doi:10.1021/bi7003558. PMID 17595061.