PFDN4

PFDN4
Identifiers
Aliases	PFDN4, C1, PFD4, prefoldin subunit 4
External IDs	MGI: 1923512 HomoloGene: 37645 GeneCards: PFDN4
Gene ontology Molecular function • chaperone binding • unfolded protein binding • protein binding Cellular component • cytosol • nucleus • cytoplasm • prefoldin complex • mitochondrion Biological process • protein folding Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5203	109054
Ensembl	ENSG00000101132	ENSMUSG00000052033
UniProt	Q9NQP4	n/a
RefSeq (mRNA)	NM_002623	NM_001013369 NM_001110152 NM_001199902
RefSeq (protein)	NP_002614.2	n/a
Location (UCSC)	Chr 20: 54.21 – 54.23 Mb	Chr 2: 170.5 – 170.52 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Prefoldin subunit 4 is a protein that in humans is encoded by the PFDN4 gene.^[3][4][5]

Function

This gene encodes a member of the prefoldin beta 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.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. Iijima M, Kano Y, Nohno T, Namba M (Apr 1996). "Cloning of cDNA with possible transcription factor activity at the G1-S phase transition in human fibroblast cell lines". Acta Medica Okayama. 50 (2): 73–7. PMID 8744932.
5. Coraboeuf E, Deroubaix E, Hoerter J (May 1976). "Control of ionic permeabilities in normal and ischemic heart". Circulation Research. 38 (5 Suppl 1): I92–8. PMID 5203.

Further reading

• Hartl FU, Hayer-Hartl M (Mar 2002). "Molecular chaperones in the cytosol: from nascent chain to folded protein". Science. 295 (5561): 1852–8. doi:10.1126/science.1068408. PMID 11884745.
• Hansen WJ, Cowan NJ, Welch WJ (Apr 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 (Nov 1999). "A chaperone with a hydrophilic surface". Nature Structural Biology. 6 (11): 990–1. doi:10.1038/14870. PMID 10542082.
• Collins C, Volik S, Kowbel D, Ginzinger D, Ylstra B, Cloutier T, Hawkins T, Predki P, Martin C, Wernick M, Kuo WL, Alberts A, Gray JW (Jun 2001). "Comprehensive genome sequence analysis of a breast cancer amplicon". Genome Research. 11 (6): 1034–42. doi:10.1101/gr.174301. PMC 311107. PMID 11381030.
• Martín-Benito J, Boskovic J, Gómez-Puertas P, Carrascosa JL, Simons CT, Lewis SA, Bartolini F, Cowan NJ, Valpuesta JM (Dec 2002). "Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT". The EMBO Journal. 21 (23): 6377–86. doi:10.1093/emboj/cdf640. PMC 136944. PMID 12456645.
• Gstaiger M, Luke B, Hess D, Oakeley EJ, Wirbelauer C, Blondel M, Vigneron M, Peter M, Krek W (Nov 2003). "Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI". Science. 302 (5648): 1208–12. doi:10.1126/science.1088401. PMID 14615539.
• Simons CT, Staes A, Rommelaere H, Ampe C, Lewis SA, Cowan NJ (Feb 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.