PFDN5

PFDN5

Identifiers

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)^[1]

Band	12q13.13	Start	53,295,291 bp^[1]
Band	12q13.13	End	53,299,452 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15 F2\|15 57.48 cM	Start	102,234,551 bp^[2]
Band	15 F2\|15 57.48 cM	End	102,240,308 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

pituitary gland

anterior pituitary

canal of the cervix

hypothalamus

nucleus accumbens

amygdala

substantia nigra

right uterine tube

Achilles tendon

monocyte

Top expressed in

arcuate nucleus

endocardial cushion

mammillary body

paraventricular nucleus of hypothalamus

globus pallidus

medial ganglionic eminence

lateral hypothalamus

seminal vesicula

median eminence

ventromedial nucleus

More reference expression data

BioGPS


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

Species

Human

Mouse

Entrez


5204


56612

Ensembl


ENSG00000123349


ENSMUSG00000001289

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

Chr 15: 102.23 – 102.24 Mb

PubMed search

^[3]

^[4]

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.

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This page was last edited on 4 March 2023, at 01:08

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Interactions

References

Further reading