PSMF1

Proteasome inhibitor PI31 subunit is a protein that in humans is encoded by the PSMF1 gene.[5][6]

PSMF1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VT8, 4OUH
Identifiers
Aliases	PSMF1, PI31, proteasome inhibitor subunit 1
External IDs	OMIM: 617858 MGI: 1346072 HomoloGene: 38231 GeneCards: PSMF1
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20p13 Start 1,113,240 bp[1] End 1,189,415 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 G3 Start 151,715,812 bp[2] End 151,744,186 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • proteasome binding • GO:0001948 protein binding • endopeptidase inhibitor activity • protein homodimerization activity • protein heterodimerization activity Cellular component • cytoplasm • cytosol • membrane • nucleoplasm • endoplasmic reticulum • proteasome complex • proteasome core complex • perinuclear region of cytoplasm Biological process • regulation of cellular amino acid metabolic process • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent • ubiquitin-dependent protein catabolic process • regulation of mRNA stability • positive regulation of canonical Wnt signaling pathway • protein polyubiquitination • stimulatory C-type lectin receptor signaling pathway • tumor necrosis factor-mediated signaling pathway • MAPK cascade • Fc-epsilon receptor signaling pathway • NIK/NF-kappaB signaling • negative regulation of proteasomal protein catabolic process • anaphase-promoting complex-dependent catabolic process • T cell receptor signaling pathway • negative regulation of canonical Wnt signaling pathway • proteasome-mediated ubiquitin-dependent protein catabolic process • Wnt signaling pathway, planar cell polarity pathway • negative regulation of endopeptidase activity • negative regulation of G2/M transition of mitotic cell cycle • protein deubiquitination • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process • transmembrane transport • regulation of transcription from RNA polymerase II promoter in response to hypoxia • post-translational modification • regulation of hematopoietic stem cell differentiation • interleukin-1-mediated signaling pathway • regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9491	228769
Ensembl	ENSG00000125818	ENSMUSG00000032869
UniProt	Q92530 Q5QPM9	Q8BHL8
RefSeq (mRNA)	NM_006814 NM_178578 NM_178579 NM_001323407 NM_001323408 NM_001323409 NM_001323410	NM_144889 NM_212446 NM_001305244
RefSeq (protein)	NP_001310336 NP_001310337 NP_001310338 NP_001310339 NP_006805 NP_848693	NP_001292173 NP_997611
Location (UCSC)	Chr 20: 1.11 – 1.19 Mb	Chr 2: 151.72 – 151.74 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a protein that inhibits the activation of the proteasome by the 11S and 19S regulators. Alternative transcript variants have been identified for this gene.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000125818 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032869 - 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.
5. Tanahashi N, Kawahara H, Murakami Y, Tanaka K (Apr 1999). "The proteasome-dependent proteolytic system". Molecular Biology Reports. 26 (1–2): 3–9. doi:10.1023/A:1006909522731. PMID 10363639.
6. "Entrez Gene: PSMF1 proteasome (prosome, macropain) inhibitor subunit 1 (PI31)".

Further reading

• Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. doi:10.1016/S0092-8674(03)00602-0. PMID 12914693.
• Minghetti L, Visentin S, Patrizio M, Franchini L, Ajmone-Cat MA, Levi G (May 2004). "Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions". Neurochemical Research. 29 (5): 965–78. doi:10.1023/B:NERE.0000021241.90133.89. PMID 15139295.
• Liou LY, Herrmann CH, Rice AP (Sep 2004). "HIV-1 infection and regulation of Tat function in macrophages". The International Journal of Biochemistry & Cell Biology. 36 (9): 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343.
• Bannwarth S, Gatignol A (Jan 2005). "HIV-1 TAR RNA: the target of molecular interactions between the virus and its host". Current HIV Research. 3 (1): 61–71. doi:10.2174/1570162052772924. PMID 15638724.
• Gibellini D, Vitone F, Schiavone P, Re MC (Apr 2005). "HIV-1 tat protein and cell proliferation and survival: a brief review". The New Microbiologica. 28 (2): 95–109. PMID 16035254.
• Hetzer C, Dormeyer W, Schnölzer M, Ott M (Oct 2005). "Decoding Tat: the biology of HIV Tat posttranslational modifications". Microbes and Infection / Institut Pasteur. 7 (13): 1364–9. doi:10.1016/j.micinf.2005.06.003. PMID 16046164.
• Peruzzi F (2006). "The multiple functions of HIV-1 Tat: proliferation versus apoptosis". Frontiers in Bioscience. 11: 708–17. doi:10.2741/1829. PMID 16146763.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Seeger M, Ferrell K, Frank R, Dubiel W (Mar 1997). "HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation". The Journal of Biological Chemistry. 272 (13): 8145–8. doi:10.1074/jbc.272.13.8145. PMID 9079628.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Madani N, Kabat D (Dec 1998). "An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein". Journal of Virology. 72 (12): 10251–5. PMC 110608. PMID 9811770.
• Simon JH, Gaddis NC, Fouchier RA, Malim MH (Dec 1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". Nature Medicine. 4 (12): 1397–400. doi:10.1038/3987. PMID 9846577.
• McCutchen-Maloney SL, Matsuda K, Shimbara N, Binns DD, Tanaka K, Slaughter CA, DeMartino GN (Jun 2000). "cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome". The Journal of Biological Chemistry. 275 (24): 18557–65. doi:10.1074/jbc.M001697200. PMID 10764772.
• Mulder LC, Muesing MA (Sep 2000). "Degradation of HIV-1 integrase by the N-end rule pathway". The Journal of Biological Chemistry. 275 (38): 29749–53. doi:10.1074/jbc.M004670200. PMID 10893419.
• Sheehy AM, Gaddis NC, Choi JD, Malim MH (Aug 2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein". Nature. 418 (6898): 646–50. Bibcode:2002Natur.418..646S. doi:10.1038/nature00939. PMID 12167863.
• Zaiss DM, Standera S, Kloetzel PM, Sijts AJ (Oct 2002). "PI31 is a modulator of proteasome formation and antigen processing". Proceedings of the National Academy of Sciences of the United States of America. 99 (22): 14344–9. Bibcode:2002PNAS...9914344Z. doi:10.1073/pnas.212257299. PMC 137886. PMID 12374861.
• Huang X, Seifert U, Salzmann U, Henklein P, Preissner R, Henke W, Sijts AJ, Kloetzel PM, Dubiel W (Nov 2002). "The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing". Journal of Molecular Biology. 323 (4): 771–82. doi:10.1016/S0022-2836(02)00998-1. PMID 12419264.