MYCBP

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; OMA:MYCBP - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	38,873,368 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	123,806,062 bp
RNA expression pattern
	Top expressed in
	monocyte; ; rectum; ; right uterine tube; ; body of pancreas; ; islet of Langerhans; ; right adrenal gland; ; left adrenal gland; ; body of stomach; ; minor salivary glands; ; oocyte;
	Top expressed in
	secondary oocyte; ; olfactory epithelium; ; seminiferous tubule; ; yolk sac; ; morula; ; conjunctival fornix; ; primitive streak; ; ureter; ; medullary collecting duct; ; spermatid;
	More reference expression data
	n/a
Gene ontology
Molecular function	transcription coactivator activity; protein binding;
Cellular component	cytoplasm; nucleus; mitochondrion;
Biological process	regulation of transcription, DNA-templated; transcription, DNA-templated; spermatogenesis; positive regulation of nucleic acid-templated transcription;
	Sources:Amigo / QuickGO
Orthologs
	26292
	56309
	ENSG00000214114
	ENSMUSG00000028647
	Q99417
	Q9EQS3
	NM_012333
	NM_019660
	NP_036465
	NP_062634
	Wikidata
View/Edit Human	View/Edit Mouse

C-Myc-binding protein is a protein that in humans is encoded by the MYCBP gene.^[5]^[6]

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]^[6]

Interactions

MYCBP has been shown to interact with AKAP1,^[7]^[8] C3orf15^[7] and Myc.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000214114 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028647 – 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 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.
^ ^a ^b "Entrez Gene: MYCBP c-myc binding protein".
^ ^a ^b 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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. 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000214114 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028647 – 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.

[pmid9797456-5] 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.

[entrez-6] "Entrez Gene: MYCBP c-myc binding protein".

[pmid12223483-7] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid11483602-8] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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[4]

[5]

[6]

[7]

[8]

Function

Interactions

References

Further reading