PFDN5

PFDN5
Identifiers
Aliases	PFDN5, MM-1, MM1, PFD5, prefoldin subunit 5
External IDs	OMIM: 604899; MGI: 1928753; HomoloGene: 1972; GeneCards: PFDN5; OMA:PFDN5 - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	53,299,452 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	102,240,308 bp
RNA expression pattern
	Top expressed in
	pituitary gland; ; anterior pituitary; ; granulocyte; ; left testis; ; right testis; ; canal of the cervix; ; hypothalamus; ; nucleus accumbens; ; amygdala; ; substantia nigra;
	Top expressed in
	arcuate nucleus; ; endocardial cushion; ; mesenteric lymph nodes; ; transitional epithelium of urinary bladder; ; mammillary body; ; paraventricular nucleus of hypothalamus; ; globus pallidus; ; lateral septal nucleus; ; medial ganglionic eminence; ; lateral hypothalamus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	unfolded protein binding; protein binding; transcription corepressor activity;
Cellular component	cytoplasm; nucleus; prefoldin complex;
Biological process	negative regulation of transcription, DNA-templated; regulation of transcription, DNA-templated; retina development in camera-type eye; negative regulation of canonical Wnt signaling pathway; protein folding;
	Sources:Amigo / QuickGO
Orthologs
	5204
	56612
	ENSG00000123349
	ENSMUSG00000001289
	Q99471
	Q9WU28
	NM_145897; NM_002624; NM_145896
	NM_020031; NM_027044
	NP_002615; NP_665904
	NP_081320
	Wikidata
View/Edit Human	View/Edit Mouse

Prefoldin subunit 5 is a protein that in humans is encoded by the PFDN5 gene.^[5]^[6]^[7]

This gene encodes a member of the prefoldin alpha subunit family. The encoded protein is one of six subunits of prefoldin, a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thereby allowing them to fold correctly. The complex, consisting of two alpha and four beta subunits, forms a double beta barrel assembly with six protruding coiled-coils. The encoded protein may also repress the transcriptional activity of the proto-oncogene c-Myc. Alternatively spliced transcript variants encoding different isoforms have been described.^[7]

Interactions

PFDN5 has been shown to interact with Myc.^[6]^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000123349 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001289 – 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.
^ Vainberg IE, Lewis SA, Rommelaere H, Ampe C, Vandekerckhove J, Klein HL, Cowan NJ (May 1998). "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin". Cell. 93 (5): 863–73. doi:10.1016/S0092-8674(00)81446-4. PMID 9630229. S2CID 16011829.
^ ^a ^b Mori K, Maeda Y, Kitaura H, Taira T, Iguchi-Ariga SM, Ariga H (November 1998). "MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc". The Journal of Biological Chemistry. 273 (45): 29794–800. doi:10.1074/jbc.273.45.29794. PMID 9792694.
^ ^a ^b "Entrez Gene: PFDN5 prefoldin subunit 5".
^ Fujioka Y, Taira T, Maeda Y, Tanaka S, Nishihara H, Iguchi-Ariga SM, Nagashima K, Ariga H (November 2001). "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer". The Journal of Biological Chemistry. 276 (48): 45137–44. doi:10.1074/jbc.M106127200. PMID 11567024.

Hansen WJ, Cowan NJ, Welch WJ (April 1999). "Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins". The Journal of Cell Biology. 145 (2): 265–77. doi:10.1083/jcb.145.2.265. PMC 2133115. PMID 10209023.
Cowan NJ, Lewis SA (November 1999). "A chaperone with a hydrophilic surface". Nature Structural Biology. 6 (11): 990–1. doi:10.1038/14870. PMID 10542082. S2CID 22081346.
Rommelaere H, De Neve M, Neirynck K, Peelaers D, Waterschoot D, Goethals M, Fraeyman N, Vandekerckhove J, Ampe C (November 2001). "Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families". The Journal of Biological Chemistry. 276 (44): 41023–8. doi:10.1074/jbc.M106591200. PMID 11535601.
Fujioka Y, Taira T, Maeda Y, Tanaka S, Nishihara H, Iguchi-Ariga SM, Nagashima K, Ariga H (November 2001). "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer". The Journal of Biological Chemistry. 276 (48): 45137–44. doi:10.1074/jbc.M106127200. PMID 11567024.
Watanabe K, Ozaki T, Nakagawa T, Miyazaki K, Takahashi M, Hosoda M, Hayashi S, Todo S, Nakagawara A (April 2002). "Physical interaction of p73 with c-Myc and MM1, a c-Myc-binding protein, and modulation of the p73 function". The Journal of Biological Chemistry. 277 (17): 15113–23. doi:10.1074/jbc.M111281200. PMID 11844794.
Simons CT, Staes A, Rommelaere H, Ampe C, Lewis SA, Cowan NJ (February 2004). "Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding". The Journal of Biological Chemistry. 279 (6): 4196–203. doi:10.1074/jbc.M306053200. PMID 14634002.
Bruneel A, Labas V, Mailloux A, Sharma S, Royer N, Vinh J, Pernet P, Vaubourdolle M, Baudin B (October 2005). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis". Proteomics. 5 (15): 3876–84. doi:10.1002/pmic.200401239. PMID 16130169. S2CID 26007149.
Hagio Y, Kimura Y, Taira T, Fujioka Y, Iguchi-Ariga SM, Ariga H (January 2006). "Distinct localizations and repression activities of MM-1 isoforms toward c-Myc". Journal of Cellular Biochemistry. 97 (1): 145–55. doi:10.1002/jcb.20619. PMID 16173081. S2CID 6803370.

This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000123349 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000001289 – 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.

[pmid9630229-5] Vainberg IE, Lewis SA, Rommelaere H, Ampe C, Vandekerckhove J, Klein HL, Cowan NJ (May 1998). "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin". Cell. 93 (5): 863–73. doi:10.1016/S0092-8674(00)81446-4. PMID 9630229. S2CID 16011829.

[pmid9792694-6] Mori K, Maeda Y, Kitaura H, Taira T, Iguchi-Ariga SM, Ariga H (November 1998). "MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc". The Journal of Biological Chemistry. 273 (45): 29794–800. doi:10.1074/jbc.273.45.29794. PMID 9792694.

[entrez-7] "Entrez Gene: PFDN5 prefoldin subunit 5".

[pmid11567024-8] Fujioka Y, Taira T, Maeda Y, Tanaka S, Nishihara H, Iguchi-Ariga SM, Nagashima K, Ariga H (November 2001). "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer". The Journal of Biological Chemistry. 276 (48): 45137–44. doi:10.1074/jbc.M106127200. PMID 11567024.

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PFDN5

PFDN5

PFDN5

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Root Wikipedia Article

PFDN5

Interactions

References

Further reading