MYCBP2

MYCBP2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3GBW, 3HWJ
Identifiers
Aliases	MYCBP2 , PAM, Myc-bp2, Phr, MYC binding protein 2, E3 ubiquitin protein ligase, PHR1, MYC binding protein 2
External IDs	OMIM: 610392 MGI: 2179432 HomoloGene: 9005 GeneCards: MYCBP2
Gene location (Human)
Chr.	Chromosome 13 (human) [1]
End	77,327,094 bp [1]
Gene location (Mouse)
Chr.	Chromosome 14 (mouse) [2]
End	103,346,814 bp [2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• protein binding ; • metal ion binding ; • transferase activity ; • guanyl-nucleotide exchange factor activity ; • zinc ion binding ; • Ran GTPase binding ; • protein homodimerization activity ; • ubiquitin protein ligase activity ;
Cellular component	• membrane ; • cell nucleus ; • cytoplasm ; • cytoskeleton ; • microtubule cytoskeleton ; • axon ; • cell projection ; • intracellular membrane-bounded organelle ;
Biological process	• regulation of transcription, DNA-templated ; • protein ubiquitination ; • transcription, DNA-templated ; • motor neuron axon guidance ; • branchiomotor neuron axon guidance ; • central nervous system projection neuron axonogenesis ; • regulation of protein localization ; • negative regulation of protein catabolic process ; • cell morphogenesis involved in neuron differentiation ; • neuromuscular process ; • regulation of cytoskeleton organization ; • regulation of axon guidance ; • positive regulation of protein ubiquitination ; • circadian regulation of gene expression ; • rhythmic process ;
	Sources:Amigo / QuickGO
Orthologs
	23077
	105689
	ENSG00000005810
	ENSMUSG00000033004
	O75592
	Q7TPH6
	NM_015057
	NM_207215
	NP_055872
	NP_997098
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 13, 2019

Probable E3 ubiquitin-protein ligase MYCBP2 also known as myc-binding protein 2 or protein associates with myc (PAM) is an enzyme that in humans is encoded by the MYCBP2 gene.^[5]^[6]

Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called enzymology and a new field of pseudoenzyme analysis has recently grown up, recognising that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties.

In biology, a gene is a sequence of nucleotides in DNA or RNA that encodes the synthesis of a gene product, either RNA or protein.

Structure

PAM contains a N-terminal leucine zipper, central MYC-binding, and C-terminal histone-binding protein homology domains.^[5]

The N-terminus (also known as the amino-terminus, NH₂-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide referring to the free amine group (-NH₂) located at the end of a polypeptide. Normally the amine group is bonded to another carboxylic group in a protein to make it a chain, but since the end of a protein has only 1 out of 2 areas chained, the free amine group is referred to the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right in LTR languages. This correlates the translation direction to the text direction (because when a protein is translated from messenger RNA, it is created from N-terminus to C-terminus - amino acids are added to the carbonyl end).

A leucine zipper is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The polypeptide segments containing these periodic arrays of leucine residues were proposed to exist in an alpha-helical conformation and the leucine side chains from one alpha helix interdigitate with those from the alpha helix of a second polypeptide, facilitating dimerization.

Myc is a family of regulator genes and proto-oncogenes that code for transcription factors. The Myc family consists of three related human genes: c-myc, l-myc (MYCL), and n-myc (MYCN). c-myc was the first gene to be discovered in this family, due to homology with the viral gene v-myc.

Interactions

MYCBP2 has been shown to interact with Myc.^[5]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000005810 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033004 - 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.
1 2 3 Guo Q, Xie J, Dang CV, Liu ET, Bishop JM (Sep 1998). "Identification of a large Myc-binding protein that contains RCC1-like repeats". Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9172–7. doi:10.1073/pnas.95.16.9172. PMC 21311 . PMID 9689053.
↑ "Entrez Gene: MYCBP2 MYC binding protein 2".

Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi: 10.1093/dnares/9.3.99 . PMID 12168954.
Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1998). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355–64. doi: 10.1093/dnares/5.6.355 . PMID 10048485.
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934 . PMID 11042152.
Murthy V, Han S, Beauchamp RL, Smith N, Haddad LA, Ito N, Ramesh V (2004). "Pam and its ortholog highwire interact with and may negatively regulate the TSC1.TSC2 complex". J. Biol. Chem. 279 (2): 1351–8. doi: 10.1074/jbc.M310208200 . PMID 14559897.
Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
Pierre SC, Häusler J, Birod K, Geisslinger G, Scholich K (2004). "PAM mediates sustained inhibition of cAMP signaling by sphingosine-1-phosphate". EMBO J. 23 (15): 3031–40. doi:10.1038/sj.emboj.7600321. PMC 514936 . PMID 15257286.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446 . PMID 15302935.
Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi: 10.1016/j.cub.2004.07.051 . PMID 15324660.
Gao X, Patel TB (2005). "Histidine residues 912 and 913 in protein associated with Myc are necessary for the inhibition of adenylyl cyclase activity". Mol. Pharmacol. 67 (1): 42–9. doi:10.1124/mol.104.005355. PMID 15470080.
Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi: 10.1074/mcp.M500021-MCP200 . PMID 15778465.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID 17081983.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948 . PMID 17353931.

In computing, a digital object identifier (DOI) is a persistent identifier or handle used to identify objects uniquely, standardized by the International Organization for Standardization (ISO). An implementation of the Handle System, DOIs are in wide use mainly to identify academic, professional, and government information, such as journal articles, research reports and data sets, and official publications though they also have been used to identify other types of information resources, such as commercial videos.

PubMed Central (PMC) is a free digital repository that archives publicly accessible full-text scholarly articles that have been published within the biomedical and life sciences journal literature. As one of the major research databases within the suite of resources that have been developed by the National Center for Biotechnology Information (NCBI), PubMed Central is much more than just a document repository. Submissions into PMC undergo an indexing and formatting procedure which results in enhanced metadata, medical ontology, and unique identifiers which all enrich the XML structured data for each article on deposit. Content within PMC can easily be interlinked to many other NCBI databases and accessed via Entrez search and retrieval systems, further enhancing the public's ability to freely discover, read and build upon this portfolio of biomedical knowledge.

This article on a gene on human chromosome 13 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000005810 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033004 - 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.

[pmid9689053-5] 1 2 3 Guo Q, Xie J, Dang CV, Liu ET, Bishop JM (Sep 1998). "Identification of a large Myc-binding protein that contains RCC1-like repeats". Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9172–7. doi:10.1073/pnas.95.16.9172. PMC 21311 . PMID 9689053.

[entrez-6] "Entrez Gene: MYCBP2 MYC binding protein 2".

MYCBP2

Contents

Structure

Interactions

Related Research Articles

References

Further reading