PSMA3 | ENSG00000100567 | NCBI 5684

Details for: PSMA3

Gene ID: 5684

Symbol: PSMA3

Ensembl ID: ENSG00000100567

Description: proteasome 20S subunit alpha 3

Associated with

Abc-family proteins mediated transport
(R-HSA-382556)
Abc transporter disorders
(R-HSA-5619084)
Adaptive immune system
(R-HSA-1280218)
Antigen processing-cross presentation
(R-HSA-1236975)
Apc/c-mediated degradation of cell cycle proteins
(R-HSA-174143)
Apoptosis
(R-HSA-109581)
Assembly of the pre-replicative complex
(R-HSA-68867)
Auf1 (hnrnp d0) binds and destabilizes mrna
(R-HSA-450408)
Axon guidance
(R-HSA-422475)
Beta-catenin independent wnt signaling
(R-HSA-3858494)
C-type lectin receptors (clrs)
(R-HSA-5621481)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to chemical stress
(R-HSA-9711123)
Cellular response to hypoxia
(R-HSA-1234174)
Class i mhc mediated antigen processing & presentation
(R-HSA-983169)
Clec7a (dectin-1) signaling
(R-HSA-5607764)
Cytokine signaling in immune system
(R-HSA-1280215)
Defective cftr causes cystic fibrosis
(R-HSA-5678895)
Degradation of axin
(R-HSA-4641257)
Degradation of beta-catenin by the destruction complex
(R-HSA-195253)
Degradation of dvl
(R-HSA-4641258)
Degradation of gli1 by the proteasome
(R-HSA-5610780)
Degradation of gli2 by the proteasome
(R-HSA-5610783)
Deubiquitination
(R-HSA-5688426)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Disorders of transmembrane transporters
(R-HSA-5619115)
Dna replication
(R-HSA-69306)
Dna replication pre-initiation
(R-HSA-69002)
Downstream signaling events of b cell receptor (bcr)
(R-HSA-1168372)
Downstream tcr signaling
(R-HSA-202424)
Fc epsilon receptor (fceri) signaling
(R-HSA-2454202)
Fceri mediated nf-kb activation
(R-HSA-2871837)
Formation of paraxial mesoderm
(R-HSA-9793380)
G1/s dna damage checkpoints
(R-HSA-69615)
G2/m checkpoints
(R-HSA-69481)
Gastrulation
(R-HSA-9758941)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Gli3 is processed to gli3r by the proteasome
(R-HSA-5610785)
Hedgehog 'off' state
(R-HSA-5610787)
Hedgehog 'on' state
(R-HSA-5632684)
Hedgehog ligand biogenesis
(R-HSA-5358346)
Hh mutants abrogate ligand secretion
(R-HSA-5387390)
Hh mutants are degraded by erad
(R-HSA-5362768)
Hiv infection
(R-HSA-162906)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Interleukin-1 family signaling
(R-HSA-446652)
Intracellular signaling by second messengers
(R-HSA-9006925)
Mapk1/mapk3 signaling
(R-HSA-5684996)
Mapk6/mapk4 signaling
(R-HSA-5687128)
Mapk family signaling cascades
(R-HSA-5683057)
Metabolism
(R-HSA-1430728)
Metabolism of amino acids and derivatives
(R-HSA-71291)
Metabolism of polyamines
(R-HSA-351202)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mitotic g1 phase and g1/s transition
(R-HSA-453279)
Mitotic g2-g2/m phases
(R-HSA-453274)
Mitotic metaphase and anaphase
(R-HSA-2555396)
M phase
(R-HSA-68886)
Neddylation
(R-HSA-8951664)
Nervous system development
(R-HSA-9675108)
Nik-->noncanonical nf-kb signaling
(R-HSA-5676590)
Oxygen-dependent proline hydroxylation of hypoxia-inducible factor alpha
(R-HSA-1234176)
Pcp/ce pathway
(R-HSA-4086400)
Pip3 activates akt signaling
(R-HSA-1257604)
Post-translational protein modification
(R-HSA-597592)
Programmed cell death
(R-HSA-5357801)
Proteasome assembly
(R-HSA-9907900)
Raf/map kinase cascade
(R-HSA-5673001)
Regulation of activated pak-2p34 by proteasome mediated degradation
(R-HSA-211733)
Regulation of apoptosis
(R-HSA-169911)
Regulation of mitotic cell cycle
(R-HSA-453276)
Regulation of mrna stability by proteins that bind au-rich elements
(R-HSA-450531)
Regulation of ornithine decarboxylase (odc)
(R-HSA-350562)
Rna polymerase ii transcription
(R-HSA-73857)
Signaling by hedgehog
(R-HSA-5358351)
Signaling by interleukins
(R-HSA-449147)
Signaling by notch
(R-HSA-157118)
Signaling by notch4
(R-HSA-9013694)
Signaling by robo receptors
(R-HSA-376176)
Signaling by the b cell receptor (bcr)
(R-HSA-983705)
Signaling by wnt
(R-HSA-195721)
Signal transduction
(R-HSA-162582)
S phase
(R-HSA-69242)
Tcf dependent signaling in response to wnt
(R-HSA-201681)
Tcr signaling
(R-HSA-202403)
Tnfr2 non-canonical nf-kb pathway
(R-HSA-5668541)
Transport of small molecules
(R-HSA-382551)
Ub-specific processing proteases
(R-HSA-5689880)
Uch proteinases
(R-HSA-5689603)
Viral infection pathways
(R-HSA-9824446)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 433.6359
Cell Significance Index: -67.4500
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 246.1724
Cell Significance Index: -62.4400
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 193.2042
Cell Significance Index: -79.5900
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 173.4931
Cell Significance Index: -81.9100
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 149.4600
Cell Significance Index: -76.8800
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 62.2082
Cell Significance Index: -76.7000
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 22.9351
Cell Significance Index: -61.4400
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 20.0580
Cell Significance Index: -79.1500
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 15.0613
Cell Significance Index: -46.2600
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: 2.2072
Cell Significance Index: 18.5400
Cell Name: granulosa cell (CL0000501)
Fold Change: 2.1122
Cell Significance Index: 55.5400
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 1.9538
Cell Significance Index: 91.8300
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 1.8422
Cell Significance Index: 49.1900
Cell Name: cell in vitro (CL0001034)
Fold Change: 1.5659
Cell Significance Index: 855.1700
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 1.5553
Cell Significance Index: 213.5800
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 1.5416
Cell Significance Index: 109.0300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 1.4846
Cell Significance Index: 42.5600
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 1.4817
Cell Significance Index: 40.3300
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 1.3301
Cell Significance Index: 588.0700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.2823
Cell Significance Index: 231.1600
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.2569
Cell Significance Index: 154.5500
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 1.1371
Cell Significance Index: 327.1800
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 1.0443
Cell Significance Index: 48.6900
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 1.0434
Cell Significance Index: 21.8400
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 0.9902
Cell Significance Index: 10.7700
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 0.9432
Cell Significance Index: 27.7000
Cell Name: lactocyte (CL0002325)
Fold Change: 0.9331
Cell Significance Index: 120.5500
Cell Name: odontoblast (CL0000060)
Fold Change: 0.9205
Cell Significance Index: 118.0000
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.8564
Cell Significance Index: 101.0000
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.8514
Cell Significance Index: 63.4600
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.8490
Cell Significance Index: 170.3000
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.8302
Cell Significance Index: 28.8500
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.8063
Cell Significance Index: 160.0200
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.7861
Cell Significance Index: 127.8500
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.6099
Cell Significance Index: 31.6800
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.5276
Cell Significance Index: 11.4300
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.4613
Cell Significance Index: 29.7600
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.4224
Cell Significance Index: 7.0700
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.3935
Cell Significance Index: 272.1900
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.3248
Cell Significance Index: 116.5100
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.2345
Cell Significance Index: 23.2000
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.2220
Cell Significance Index: 42.2500
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.1733
Cell Significance Index: 29.5900
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.1684
Cell Significance Index: 12.9200
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.1075
Cell Significance Index: 81.4000
Cell Name: retinal rod cell (CL0000604)
Fold Change: 0.0814
Cell Significance Index: 0.9700
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0424
Cell Significance Index: 79.8100
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.0326
Cell Significance Index: 0.9100
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.0253
Cell Significance Index: 39.0200
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0157
Cell Significance Index: 0.9900
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0120
Cell Significance Index: 22.1400
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0050
Cell Significance Index: -6.8000
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0164
Cell Significance Index: -12.0500
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0206
Cell Significance Index: -12.8900
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0224
Cell Significance Index: -14.2200
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0299
Cell Significance Index: -22.1300
Cell Name: peg cell (CL4033014)
Fold Change: -0.0511
Cell Significance Index: -1.1800
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0706
Cell Significance Index: -32.0500
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0757
Cell Significance Index: -7.7300
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0767
Cell Significance Index: -43.2300
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.1235
Cell Significance Index: -6.9300
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1630
Cell Significance Index: -34.3400
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: -0.1646
Cell Significance Index: -1.8700
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1903
Cell Significance Index: -21.8000
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.1996
Cell Significance Index: -4.2500
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.2178
Cell Significance Index: -9.8700
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.2516
Cell Significance Index: -29.3200
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.2792
Cell Significance Index: -14.6600
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.2906
Cell Significance Index: -2.3700
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2935
Cell Significance Index: -42.6600
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.3041
Cell Significance Index: -2.8000
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.3062
Cell Significance Index: -10.7600
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.3683
Cell Significance Index: -9.4100
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.3725
Cell Significance Index: -9.9800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.3941
Cell Significance Index: -11.3600
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.4512
Cell Significance Index: -14.4500
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.5068
Cell Significance Index: -8.9600
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.5103
Cell Significance Index: -58.2500
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.5711
Cell Significance Index: -13.9400
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.6465
Cell Significance Index: -11.0800
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -0.6525
Cell Significance Index: -12.0600
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.6908
Cell Significance Index: -54.7100
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.7182
Cell Significance Index: -74.7800
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.7337
Cell Significance Index: -10.0100
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.7362
Cell Significance Index: -49.5000
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.7505
Cell Significance Index: -46.1300
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.7649
Cell Significance Index: -20.4600
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.8250
Cell Significance Index: -12.1800
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.8855
Cell Significance Index: -5.3500
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.9572
Cell Significance Index: -48.3800
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.9707
Cell Significance Index: -28.5900
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -1.1333
Cell Significance Index: -50.1300
Cell Name: kidney cell (CL1000497)
Fold Change: -1.1385
Cell Significance Index: -9.0900
Cell Name: preadipocyte (CL0002334)
Fold Change: -1.2630
Cell Significance Index: -24.6500
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.3019
Cell Significance Index: -79.8200
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -1.3255
Cell Significance Index: -50.2000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -1.3924
Cell Significance Index: -35.7900
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: -1.3953
Cell Significance Index: -11.9900
Cell Name: medium spiny neuron (CL1001474)
Fold Change: -1.4984
Cell Significance Index: -20.2200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -1.6192
Cell Significance Index: -40.4800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** PSMA3 is a highly conserved gene, with high sequence similarity across species. The protein product of the PSMA3 gene, PSA3, is a subunit of the 20S proteasome, which is a large protein complex composed of 14 subunits. The 20S proteasome is responsible for degrading proteins on a ubiquitin-ligated chain, and PSMA3 plays a crucial role in this process. The PSMA3 gene is also highly regulated, with expression levels varying depending on the cell type and developmental stage. **Pathways and Functions** The PSMA3 gene is involved in various cellular pathways, including: 1. **Protein degradation**: PSMA3 is a subunit of the 20S proteasome, which is responsible for degrading damaged or misfolded proteins. 2. **Cell cycle regulation**: The 20S proteasome, including PSMA3, plays a crucial role in regulating the cell cycle by degrading proteins involved in cell cycle progression. 3. **Immune response**: PSMA3 is involved in the regulation of immune responses, including the presentation of antigens to T-cells. 4. **Apoptosis**: The 20S proteasome, including PSMA3, is involved in regulating apoptosis (programmed cell death). 5. **Hedgehog signaling**: PSMA3 is involved in the regulation of hedgehog signaling, a critical pathway involved in development and disease. **Clinical Significance** Abnormalities in the PSMA3 gene have been linked to various diseases, including: 1. **Cancer**: Mutations in the PSMA3 gene have been identified in certain types of cancer, including prostate cancer. 2. **Immunodeficiency disorders**: Abnormalities in the PSMA3 gene have been linked to immunodeficiency disorders, including severe combined immunodeficiency (SCID). 3. **Neurodegenerative diseases**: PSMA3 has been implicated in the pathogenesis of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. In conclusion, the PSMA3 gene plays a critical role in various cellular processes, including protein degradation, cell cycle regulation, and immune response. Abnormalities in the PSMA3 gene have been linked to various diseases, highlighting the importance of this gene in human health and disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Macropain subunit C8

Genular Protein ID: 4282489683

Symbol: PSA3_HUMAN

Name: Macropain subunit C8

UniProtKB Accession Codes:

P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70

Database IDs:

Citations:

PubMed ID: 2025653

Title: Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes).

PubMed ID: 2025653

DOI: 10.1016/0167-4781(91)90090-9

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7811265

Title: Human proteasome subunits from 2-dimensional gels identified by partial sequencing.

PubMed ID: 7811265

DOI: 10.1006/bbrc.1994.2876

PubMed ID: 8610016

Title: A role for the proteasome regulator PA28alpha in antigen presentation.

PubMed ID: 8610016

DOI: 10.1038/381166a0

PubMed ID: 11521686

Title: Gene expression induced by BO-653, probucol and BHQ in human endothelial cells.

PubMed ID: 11521686

DOI: 10.5551/jat1994.7.223

PubMed ID: 11350925

Title: A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome.

PubMed ID: 11350925

DOI: 10.1093/emboj/20.10.2367

PubMed ID: 12181345

Title: Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome.

PubMed ID: 12181345

DOI: 10.1091/mbc.e02-03-0122

PubMed ID: 12376572

Title: Mapping and structural dissection of human 20 s proteasome using proteomic approaches.

PubMed ID: 12376572

DOI: 10.1074/mcp.m200030-mcp200

PubMed ID: 12472671

Title: Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes.

PubMed ID: 12472671

DOI: 10.1046/j.1365-3083.2002.01179.x

PubMed ID: 14550573

Title: Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits.

PubMed ID: 14550573

DOI: 10.1016/s0014-5793(03)01025-1

PubMed ID: 14674694

Title: Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner.

PubMed ID: 14674694

DOI: 10.1023/a:1027317014159

PubMed ID: 15244466

Title: 20S proteasome prevents aggregation of heat-denatured proteins without PA700 regulatory subcomplex like a molecular chaperone.

PubMed ID: 15244466

DOI: 10.1021/bm049957a

PubMed ID: 15936278

Title: HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome.

PubMed ID: 15936278

DOI: 10.1016/j.cub.2005.04.058

PubMed ID: 15831937

Title: Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells.

PubMed ID: 15831937

DOI: 10.1099/vir.0.80763-0

PubMed ID: 16337594

Title: MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein.

PubMed ID: 16337594

DOI: 10.1016/j.molcel.2005.10.017

PubMed ID: 15592455

Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

PubMed ID: 15592455

DOI: 10.1038/nbt1046

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16298756

Title: Chemical structure-dependent gene expression of proteasome subunits via regulation of the antioxidant response element.

PubMed ID: 16298756

DOI: 10.1080/10715760500354430

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17323924

Title: Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.

PubMed ID: 17323924

DOI: 10.1021/bi061994u

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 17499743

Title: Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes.

PubMed ID: 17499743

DOI: 10.1016/j.prostaglandins.2006.12.001

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 18971267

Title: Ubiquitin-independent degradation of hepatitis C virus F protein.

PubMed ID: 18971267

DOI: 10.1128/jvi.00832-08

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23495936

Title: Molecular architecture and assembly of the eukaryotic proteasome.

PubMed ID: 23495936

DOI: 10.1146/annurev-biochem-060410-150257

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 27176742

Title: Human 20S proteasome activity towards fluorogenic peptides of various chain lengths.

PubMed ID: 27176742

DOI: 10.1515/hsz-2016-0176

PubMed ID: 26133119

Title: Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.

PubMed ID: 26133119

DOI: 10.1038/ncomms8573

PubMed ID: 26657688

Title: Disassembly of the self-assembled, double-ring structure of proteasome alpha7 homo-tetradecamer by alpha6.

PubMed ID: 26657688

DOI: 10.1038/srep18167

PubMed ID: 25599644

Title: Crystal structure of the human 20S proteasome in complex with carfilzomib.

PubMed ID: 25599644

DOI: 10.1016/j.str.2014.11.017

PubMed ID: 27428775

Title: An atomic structure of the human 26S proteasome.

PubMed ID: 27428775

DOI: 10.1038/nsmb.3273

PubMed ID: 27342858

Title: Structure of the human 26S proteasome at a resolution of 3.9 Aa.

PubMed ID: 27342858

DOI: 10.1073/pnas.1608050113

PubMed ID: 27493187

Title: The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design.

PubMed ID: 27493187

DOI: 10.1126/science.aaf8993

PubMed ID: 34711951

Title: AKIRIN2 controls the nuclear import of proteasomes in vertebrates.

PubMed ID: 34711951

DOI: 10.1038/s41586-021-04035-8

PubMed ID: 26524591

Title: Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type I IFN production.

PubMed ID: 26524591

DOI: 10.1172/jci81260

Sequence Information:

Length: 255
Mass: 28433
Checksum: A1854ED3C0650FB1
Sequence:

MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE 
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV 
HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL 
QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA 
KESLKEEDES DDDNM

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: PSMA3

Associated with

Cells (max top 100)

Other Information

Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes). PubMed ID: 2025653

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Human proteasome subunits from 2-dimensional gels identified by partial sequencing. PubMed ID: 7811265

A role for the proteasome regulator PA28alpha in antigen presentation. PubMed ID: 8610016

Gene expression induced by BO-653, probucol and BHQ in human endothelial cells. PubMed ID: 11521686

A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. PubMed ID: 11350925

Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome. PubMed ID: 12181345

Mapping and structural dissection of human 20 s proteasome using proteomic approaches. PubMed ID: 12376572

Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes. PubMed ID: 12472671

Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits. PubMed ID: 14550573

Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner. PubMed ID: 14674694

20S proteasome prevents aggregation of heat-denatured proteins without PA700 regulatory subcomplex like a molecular chaperone. PubMed ID: 15244466

HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. PubMed ID: 15936278

Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells. PubMed ID: 15831937

MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein. PubMed ID: 16337594

Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. PubMed ID: 15592455

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Chemical structure-dependent gene expression of proteasome subunits via regulation of the antioxidant response element. PubMed ID: 16298756

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. PubMed ID: 17323924

Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. PubMed ID: 17487921

Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes. PubMed ID: 17499743

Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. PubMed ID: 19367720

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. PubMed ID: 18318008

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Ubiquitin-independent degradation of hepatitis C virus F protein. PubMed ID: 18971267

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Molecular architecture and assembly of the eukaryotic proteasome. PubMed ID: 23495936

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Human 20S proteasome activity towards fluorogenic peptides of various chain lengths. PubMed ID: 27176742

Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core. PubMed ID: 26133119

Disassembly of the self-assembled, double-ring structure of proteasome alpha7 homo-tetradecamer by alpha6. PubMed ID: 26657688

Crystal structure of the human 20S proteasome in complex with carfilzomib. PubMed ID: 25599644

An atomic structure of the human 26S proteasome. PubMed ID: 27428775

Structure of the human 26S proteasome at a resolution of 3.9 Aa. PubMed ID: 27342858

The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design. PubMed ID: 27493187

AKIRIN2 controls the nuclear import of proteasomes in vertebrates. PubMed ID: 34711951

Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type I IFN production. PubMed ID: 26524591