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PAAF1
Identifiers
Aliases	PAAF1, PAAF, Rpn14, WDR71, proteasomal ATPase associated factor 1
External IDs	HomoloGene: 49821; GeneCards: PAAF1; OMA:PAAF1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.4 Start 73,876,699 bp End 73,931,114 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in C1 segment substantia nigra internal globus pallidus Amygdala external globus pallidus putamen pars reticulata nucleus accumbens inferior olivary nucleus caudate nucleus n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component proteasome complex Biological process viral process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 80227 n/a Ensembl ENSG00000175575 n/a UniProt Q9BRP4 n/a RefSeq (mRNA) NM_001267803 NM_001267804 NM_001267805 NM_001267806 NM_025155 NM_001363556 n/a RefSeq (protein) NP_001254732 NP_001254733 NP_001254734 NP_001254735 NP_079431 NP_001350485 n/a Location (UCSC) Chr 11: 73.88 – 73.93 Mb n/a PubMed search n/a
Wikidata
View/Edit Human

Proteasomal ATPase-associated factor 1 is an enzyme that in humans is encoded by the PAAF1 gene.

Interactions

PAAF1 has been shown to interact with PSMD10.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000175575 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Park Y, Hwang YP, Lee JS, Seo SH, Yoon SK, Yoon JB (May 2005). "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases". Molecular and Cellular Biology. 25 (9): 3842–53. doi:10.1128/MCB.25.9.3842-3853.2005. PMC 1084299. PMID 15831487.
4. Ponnappan S, Ovaa H, Ponnappan U (Mar 2007). "Lower expression of catalytic and structural subunits of the proteasome contributes to decreased proteolysis in peripheral blood T lymphocytes during aging". The International Journal of Biochemistry & Cell Biology. 39 (4): 799–809. doi:10.1016/j.biocel.2007.01.002. PMID 17317272.
5. Lassot I, Latreille D, Rousset E, Sourisseau M, Linares LK, Chable-Bessia C, Coux O, Benkirane M, Kiernan RE (Feb 2007). "The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms". Molecular Cell. 25 (3): 369–83. doi:10.1016/j.molcel.2006.12.020. PMID 17289585.
6. "Entrez Gene: WDR71 WD repeat domain 71".
7. 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". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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