PFDN5

Prefoldin subunit 5 is a protein that in humans is encoded by the PFDN5 gene.[4][5][6]

PFDN5
Identifiers
Aliases	PFDN5, MM-1, MM1, PFD5, prefoldin subunit 5
External IDs	OMIM: 604899 MGI: 1928753 HomoloGene: 1972 GeneCards: PFDN5
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.13 Start 53,295,291 bp[1] End 53,299,450 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • unfolded protein binding • GO:0001948 protein binding • GO:0001106 transcription corepressor activity Cellular component • cytoplasm • cell 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
Species	Human	Mouse
Entrez	5204	56612
Ensembl	ENSG00000123349	n/a
UniProt	Q99471	Q9WU28
RefSeq (mRNA)	NM_145897 NM_002624 NM_145896	NM_020031 NM_027044
RefSeq (protein)	NP_002615 NP_665904	NP_081320
Location (UCSC)	Chr 12: 53.3 – 53.3 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

PFDN5 has been shown to interact with Myc.[5][7]

References

1. GRCh38: Ensembl release 89: ENSG00000123349 - 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. 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.
5. 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.
6. "Entrez Gene: PFDN5 prefoldin subunit 5".
7. 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.

Further reading

• 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.
• 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.
• 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.