PSMF1

Protein found in humans
PSMF1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2VT8, 4OUH

Identifiers
AliasesPSMF1, PI31, proteasome inhibitor subunit 1
External IDsOMIM: 617858; MGI: 1346072; HomoloGene: 38231; GeneCards: PSMF1; OMA:PSMF1 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for PSMF1
Genomic location for PSMF1
Band20p13Start1,113,240 bp[1]
End1,189,415 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for PSMF1
Genomic location for PSMF1
Band2|2 G3Start151,557,732 bp[2]
End151,586,106 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • sperm

  • blood

  • gastrocnemius muscle

  • popliteal artery

  • monocyte

  • islet of Langerhans

  • right coronary artery

  • stromal cell of endometrium

  • ganglionic eminence

  • bone marrow cells
Top expressed in
  • seminiferous tubule

  • spermatid

  • secondary oocyte

  • blood

  • sciatic nerve

  • interventricular septum

  • spermatocyte

  • proximal tubule

  • islet of Langerhans

  • spleen
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • proteasome binding
  • 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 protein modification
  • regulation of hematopoietic stem cell differentiation
  • interleukin-1-mediated signaling pathway
  • regulation of mitotic cell cycle phase transition
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 2: 151.56 – 151.59 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000125818 – Ensembl, May 2017
  2. ^ a b c 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. S2CID 38305744.
  6. ^ a b "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. S2CID 16340355.
  • 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. S2CID 25323034.
  • 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. doi:10.1128/JVI.72.12.10251-10255.1998. 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. S2CID 25235070.
  • 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. S2CID 4403228.
  • 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.


  • v
  • t
  • e
A (alpha subunits)B (beta subunits)C (ATPases)D (non-ATPases)E (activator subunits)F (inhibitor subunit)
  • PSMF1
Stub icon

This article on a gene on human chromosome 20 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e