UniProtKB - P25789 (PSA4_HUMAN)
Proteasome subunit alpha type-4
PSMA4
Functioni
GO - Molecular functioni
- endopeptidase activity Source: GO_Central
- threonine-type endopeptidase activity Source: InterPro
GO - Biological processi
- anaphase-promoting complex-dependent catabolic process Source: Reactome
- antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
- Fc-epsilon receptor signaling pathway Source: Reactome
- interleukin-1-mediated signaling pathway Source: Reactome
- MAPK cascade Source: Reactome
- negative regulation of canonical Wnt signaling pathway Source: Reactome
- negative regulation of G2/M transition of mitotic cell cycle Source: Reactome
- NIK/NF-kappaB signaling Source: Reactome
- positive regulation of canonical Wnt signaling pathway Source: Reactome
- post-translational protein modification Source: Reactome
- pre-replicative complex assembly Source: Reactome
- proteasomal ubiquitin-independent protein catabolic process Source: GO_Central
- proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
- protein deubiquitination Source: Reactome
- protein polyubiquitination Source: Reactome
- regulation of cellular amino acid metabolic process Source: Reactome
- regulation of hematopoietic stem cell differentiation Source: Reactome
- regulation of mitotic cell cycle phase transition Source: Reactome
- regulation of mRNA stability Source: Reactome
- regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
- SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
- stimulatory C-type lectin receptor signaling pathway Source: Reactome
- T cell receptor signaling pathway Source: Reactome
- transmembrane transport Source: Reactome
- tumor necrosis factor-mediated signaling pathway Source: Reactome
- viral process Source: UniProtKB-KW
- Wnt signaling pathway, planar cell polarity pathway Source: Reactome
Keywordsi
Biological process | Host-virus interaction |
Enzyme and pathway databases
PathwayCommonsi | P25789 |
Reactomei | R-HSA-1169091, Activation of NF-kappaB in B cells R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha R-HSA-1236974, ER-Phagosome pathway R-HSA-1236978, Cross-presentation of soluble exogenous antigens (endosomes) R-HSA-174084, Autodegradation of Cdh1 by Cdh1:APC/C R-HSA-174113, SCF-beta-TrCP mediated degradation of Emi1 R-HSA-174154, APC/C:Cdc20 mediated degradation of Securin R-HSA-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 R-HSA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A R-HSA-180534, Vpu mediated degradation of CD4 R-HSA-180585, Vif-mediated degradation of APOBEC3G R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21 R-HSA-195253, Degradation of beta-catenin by the destruction complex R-HSA-202424, Downstream TCR signaling R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation R-HSA-2467813, Separation of Sister Chromatids R-HSA-2871837, FCERI mediated NF-kB activation R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1 R-HSA-350562, Regulation of ornithine decarboxylase (ODC) R-HSA-382556, ABC-family proteins mediated transport R-HSA-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-4608870, Asymmetric localization of PCP proteins R-HSA-4641257, Degradation of AXIN R-HSA-4641258, Degradation of DVL R-HSA-5358346, Hedgehog ligand biogenesis R-HSA-5362768, Hh mutants are degraded by ERAD R-HSA-5607761, Dectin-1 mediated noncanonical NF-kB signaling R-HSA-5607764, CLEC7A (Dectin-1) signaling R-HSA-5610780, Degradation of GLI1 by the proteasome R-HSA-5610783, Degradation of GLI2 by the proteasome R-HSA-5610785, GLI3 is processed to GLI3R by the proteasome R-HSA-5632684, Hedgehog 'on' state R-HSA-5658442, Regulation of RAS by GAPs R-HSA-5668541, TNFR2 non-canonical NF-kB pathway R-HSA-5676590, NIK-->noncanonical NF-kB signaling R-HSA-5678895, Defective CFTR causes cystic fibrosis R-HSA-5687128, MAPK6/MAPK4 signaling R-HSA-5689603, UCH proteinases R-HSA-5689880, Ub-specific processing proteases R-HSA-68827, CDT1 association with the CDC6:ORC:origin complex R-HSA-68949, Orc1 removal from chromatin R-HSA-69017, CDK-mediated phosphorylation and removal of Cdc6 R-HSA-69481, G2/M Checkpoints R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint R-HSA-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis R-HSA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs R-HSA-8939902, Regulation of RUNX2 expression and activity R-HSA-8941858, Regulation of RUNX3 expression and activity R-HSA-8948751, Regulation of PTEN stability and activity R-HSA-8951664, Neddylation R-HSA-9010553, Regulation of expression of SLITs and ROBOs R-HSA-9020702, Interleukin-1 signaling R-HSA-9604323, Negative regulation of NOTCH4 signaling R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation |
Protein family/group databases
MEROPSi | T01.973 |
Names & Taxonomyi
Protein namesi | Recommended name: Proteasome subunit alpha type-4Alternative name(s): Macropain subunit C9 Multicatalytic endopeptidase complex subunit C9 Proteasome component C9 Proteasome subunit L |
Gene namesi | Name:PSMA4 Synonyms:HC9, PSC9 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:9533, PSMA4 |
MIMi | 176846, gene |
neXtProti | NX_P25789 |
VEuPathDBi | HostDB:ENSG00000041357.15 |
Subcellular locationi
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: GO_Central
- intracellular membrane-bounded organelle Source: HPA
- P-body Source: UniProtKB
- proteasome complex Source: UniProtKB
- proteasome core complex Source: UniProtKB
- proteasome core complex, alpha-subunit complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Nucleus, ProteasomePathology & Biotechi
Organism-specific databases
DisGeNETi | 5685 |
OpenTargetsi | ENSG00000041357 |
PharmGKBi | PA33878 |
Miscellaneous databases
Pharosi | P25789, Tbio |
Chemistry databases
ChEMBLi | CHEMBL2364701 CHEMBL3831201 |
DrugBanki | DB08515, (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE |
Genetic variation databases
BioMutai | PSMA4 |
DMDMi | 130861 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000124103 | 1 – 261 | Proteasome subunit alpha type-4Add BLAST | 261 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 13 | PhosphoserineCombined sources | 1 | |
Modified residuei | 75 | PhosphoserineCombined sources | 1 | |
Modified residuei | 127 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 173 | PhosphoserineCombined sources | 1 | |
Modified residuei | 176 | N6-acetyllysineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | P25789 |
jPOSTi | P25789 |
MassIVEi | P25789 |
MaxQBi | P25789 |
PaxDbi | P25789 |
PeptideAtlasi | P25789 |
PRIDEi | P25789 |
ProteomicsDBi | 54292 [P25789-1] 54293 [P25789-2] |
TopDownProteomicsi | P25789-1 [P25789-1] |
2D gel databases
UCD-2DPAGEi | P25789 |
PTM databases
iPTMneti | P25789 |
MetOSitei | P25789 |
PhosphoSitePlusi | P25789 |
SwissPalmi | P25789 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSG00000041357, Expressed in monocyte and 241 other tissues |
ExpressionAtlasi | P25789, baseline and differential |
Genevisiblei | P25789, HS |
Organism-specific databases
HPAi | ENSG00000041357, Low tissue specificity |
Interactioni
Subunit structurei
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
5 Publications(Microbial infection) Interaction with HTLV-1 TAX protein favors NFKB1 activation.
1 PublicationBinary interactionsi
Hide detailsP25789
Protein-protein interaction databases
BioGRIDi | 111658, 163 interactors |
ComplexPortali | CPX-5993, 26S Proteasome complex |
CORUMi | P25789 |
DIPi | DIP-29365N |
IntActi | P25789, 57 interactors |
MINTi | P25789 |
STRINGi | 9606.ENSP00000044462 |
Chemistry databases
BindingDBi | P25789 |
Miscellaneous databases
RNActi | P25789, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P25789 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0178, Eukaryota |
GeneTreei | ENSGT00550000074827 |
InParanoidi | P25789 |
OMAi | CNEKQRY |
OrthoDBi | 1222564at2759 |
PhylomeDBi | P25789 |
TreeFami | TF106209 |
Family and domain databases
Gene3Di | 3.60.20.10, 1 hit |
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR023332, Proteasome_alpha-type IPR000426, Proteasome_asu_N IPR016050, Proteasome_bsu_CS IPR001353, Proteasome_sua/b IPR034647, Proteasome_subunit_alpha4 |
PANTHERi | PTHR11599:SF13, PTHR11599:SF13, 1 hit |
Pfami | View protein in Pfam PF00227, Proteasome, 1 hit PF10584, Proteasome_A_N, 1 hit |
SMARTi | View protein in SMART SM00948, Proteasome_A_N, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
PROSITEi | View protein in PROSITE PS00388, PROTEASOME_ALPHA_1, 1 hit PS51475, PROTEASOME_ALPHA_2, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR
60 70 80 90 100
NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ
110 120 130 140 150
YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS
160 170 180 190 200
DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAIKVLNKT
210 220 230 240 250
MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE
260
KKEKEQKEKD K
Computationally mapped potential isoform sequencesi
There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH0YKT8 | H0YKT8_HUMAN | Proteasome subunit beta | PSMA4 | 181 | Annotation score: | ||
H0YLC2 | H0YLC2_HUMAN | Proteasome subunit alpha type | PSMA4 | 174 | Annotation score: | ||
H0YL69 | H0YL69_HUMAN | Proteasome subunit alpha type | PSMA4 | 236 | Annotation score: | ||
H0YMA1 | H0YMA1_HUMAN | Proteasome subunit alpha type | PSMA4 | 209 | Annotation score: | ||
H0YMZ1 | H0YMZ1_HUMAN | Proteasome subunit alpha type | PSMA4 | 220 | Annotation score: | ||
H0YLS6 | H0YLS6_HUMAN | Proteasome subunit alpha type | PSMA4 | 125 | Annotation score: | ||
H0YMI6 | H0YMI6_HUMAN | Proteasome subunit alpha type | PSMA4 | 183 | Annotation score: | ||
H0YN18 | H0YN18_HUMAN | Proteasome subunit alpha type-4 | PSMA4 | 230 | Annotation score: | ||
H0YKS0 | H0YKS0_HUMAN | Proteasome subunit alpha type-4 | PSMA4 | 122 | Annotation score: | ||
H0YMV3 | H0YMV3_HUMAN | Proteasome subunit alpha type-4 | PSMA4 | 86 | Annotation score: |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_043102 | 1 – 71 | Missing in isoform 2. 1 PublicationAdd BLAST | 71 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00763 mRNA Translation: BAA00660.1 BT009784 mRNA Translation: AAP88786.1 AC027228 Genomic DNA No translation available. CH471136 Genomic DNA Translation: EAW99163.1 CH471136 Genomic DNA Translation: EAW99164.1 BC005361 mRNA Translation: AAH05361.1 BC022445 mRNA Translation: AAH22445.1 BC022817 mRNA Translation: AAH22817.2 BC047667 mRNA Translation: AAH47667.1 BC093069 mRNA Translation: AAH93069.1 |
CCDSi | CCDS10303.1 [P25789-1] CCDS45319.1 [P25789-2] |
PIRi | S15972, SNHUC9 |
RefSeqi | NP_001096137.1, NM_001102667.2 [P25789-1] NP_001096138.1, NM_001102668.2 [P25789-2] NP_001317605.1, NM_001330676.1 [P25789-1] NP_002780.1, NM_002789.5 [P25789-1] |
Genome annotation databases
Ensembli | ENST00000044462; ENSP00000044462; ENSG00000041357 [P25789-1] ENST00000413382; ENSP00000402118; ENSG00000041357 [P25789-2] ENST00000559082; ENSP00000453887; ENSG00000041357 [P25789-1] |
GeneIDi | 5685 |
KEGGi | hsa:5685 |
UCSCi | uc002bdu.5, human [P25789-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00763 mRNA Translation: BAA00660.1 BT009784 mRNA Translation: AAP88786.1 AC027228 Genomic DNA No translation available. CH471136 Genomic DNA Translation: EAW99163.1 CH471136 Genomic DNA Translation: EAW99164.1 BC005361 mRNA Translation: AAH05361.1 BC022445 mRNA Translation: AAH22445.1 BC022817 mRNA Translation: AAH22817.2 BC047667 mRNA Translation: AAH47667.1 BC093069 mRNA Translation: AAH93069.1 |
CCDSi | CCDS10303.1 [P25789-1] CCDS45319.1 [P25789-2] |
PIRi | S15972, SNHUC9 |
RefSeqi | NP_001096137.1, NM_001102667.2 [P25789-1] NP_001096138.1, NM_001102668.2 [P25789-2] NP_001317605.1, NM_001330676.1 [P25789-1] NP_002780.1, NM_002789.5 [P25789-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4R3O | X-ray | 2.60 | C/Q | 2-251 | [»] | |
4R67 | X-ray | 2.89 | C/Q/e/s | 2-251 | [»] | |
5A0Q | electron microscopy | 3.50 | C/Q | 1-261 | [»] | |
5GJQ | electron microscopy | 4.50 | D/j | 1-261 | [»] | |
5GJR | electron microscopy | 3.50 | D/j | 1-261 | [»] | |
5L4G | electron microscopy | 4.02 | C/P | 1-261 | [»] | |
5LE5 | X-ray | 1.80 | B/P | 1-261 | [»] | |
5LEX | X-ray | 2.20 | B/P | 1-261 | [»] | |
5LEY | X-ray | 1.90 | B/P | 1-261 | [»] | |
5LEZ | X-ray | 2.19 | B/P | 1-261 | [»] | |
5LF0 | X-ray | 2.41 | B/P | 1-261 | [»] | |
5LF1 | X-ray | 2.00 | B/P | 1-261 | [»] | |
5LF3 | X-ray | 2.10 | B/P | 1-261 | [»] | |
5LF4 | X-ray | 1.99 | B/P | 1-261 | [»] | |
5LF6 | X-ray | 2.07 | B/P | 1-261 | [»] | |
5LF7 | X-ray | 2.00 | B/P | 1-261 | [»] | |
5LN3 | electron microscopy | 6.80 | C | 1-261 | [»] | |
5M32 | electron microscopy | 3.80 | B/P | 1-261 | [»] | |
5T0C | electron microscopy | 3.80 | AI/BI | 2-261 | [»] | |
5T0G | electron microscopy | 4.40 | I | 2-261 | [»] | |
5T0H | electron microscopy | 6.80 | I | 2-261 | [»] | |
5T0I | electron microscopy | 8.00 | I | 2-261 | [»] | |
5T0J | electron microscopy | 8.00 | I | 2-261 | [»] | |
5VFO | electron microscopy | 3.50 | I/i | 2-251 | [»] | |
5VFP | electron microscopy | 4.20 | I/i | 2-251 | [»] | |
5VFQ | electron microscopy | 4.20 | I/i | 2-251 | [»] | |
5VFR | electron microscopy | 4.90 | I/i | 2-251 | [»] | |
5VFS | electron microscopy | 3.60 | I/i | 2-251 | [»] | |
5VFT | electron microscopy | 7.00 | I/i | 2-251 | [»] | |
5VFU | electron microscopy | 5.80 | I/i | 2-251 | [»] | |
6AVO | electron microscopy | 3.80 | O/Z | 1-261 | [»] | |
6E5B | X-ray | 2.77 | B/P | 1-261 | [»] | |
6KWY | electron microscopy | 2.72 | B/P | 1-261 | [»] | |
6MSB | electron microscopy | 3.00 | I/i | 2-261 | [»] | |
6MSD | electron microscopy | 3.20 | I/i | 2-261 | [»] | |
6MSE | electron microscopy | 3.30 | I/i | 2-261 | [»] | |
6MSG | electron microscopy | 3.50 | I/i | 2-261 | [»] | |
6MSH | electron microscopy | 3.60 | I/i | 2-261 | [»] | |
6MSJ | electron microscopy | 3.30 | I/i | 2-261 | [»] | |
6MSK | electron microscopy | 3.20 | I/i | 2-261 | [»] | |
6R70 | electron microscopy | 3.50 | B/P | 2-249 | [»] | |
6REY | electron microscopy | 3.00 | C/Q | 1-261 | [»] | |
6RGQ | electron microscopy | 2.60 | C/Q | 1-261 | [»] | |
6WJD | electron microscopy | 4.80 | I/i | 2-261 | [»] | |
6WJN | electron microscopy | 5.70 | I/i | 2-251 | [»] | |
6XMJ | electron microscopy | 3.00 | C | 2-251 | [»] | |
SMRi | P25789 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111658, 163 interactors |
ComplexPortali | CPX-5993, 26S Proteasome complex |
CORUMi | P25789 |
DIPi | DIP-29365N |
IntActi | P25789, 57 interactors |
MINTi | P25789 |
STRINGi | 9606.ENSP00000044462 |
Chemistry databases
BindingDBi | P25789 |
ChEMBLi | CHEMBL2364701 CHEMBL3831201 |
DrugBanki | DB08515, (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE |
Protein family/group databases
MEROPSi | T01.973 |
PTM databases
iPTMneti | P25789 |
MetOSitei | P25789 |
PhosphoSitePlusi | P25789 |
SwissPalmi | P25789 |
Genetic variation databases
BioMutai | PSMA4 |
DMDMi | 130861 |
2D gel databases
UCD-2DPAGEi | P25789 |
Proteomic databases
EPDi | P25789 |
jPOSTi | P25789 |
MassIVEi | P25789 |
MaxQBi | P25789 |
PaxDbi | P25789 |
PeptideAtlasi | P25789 |
PRIDEi | P25789 |
ProteomicsDBi | 54292 [P25789-1] 54293 [P25789-2] |
TopDownProteomicsi | P25789-1 [P25789-1] |
Protocols and materials databases
Antibodypediai | 27657, 323 antibodies |
DNASUi | 5685 |
Genome annotation databases
Ensembli | ENST00000044462; ENSP00000044462; ENSG00000041357 [P25789-1] ENST00000413382; ENSP00000402118; ENSG00000041357 [P25789-2] ENST00000559082; ENSP00000453887; ENSG00000041357 [P25789-1] |
GeneIDi | 5685 |
KEGGi | hsa:5685 |
UCSCi | uc002bdu.5, human [P25789-1] |
Organism-specific databases
CTDi | 5685 |
DisGeNETi | 5685 |
GeneCardsi | PSMA4 |
HGNCi | HGNC:9533, PSMA4 |
HPAi | ENSG00000041357, Low tissue specificity |
MIMi | 176846, gene |
neXtProti | NX_P25789 |
OpenTargetsi | ENSG00000041357 |
PharmGKBi | PA33878 |
VEuPathDBi | HostDB:ENSG00000041357.15 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0178, Eukaryota |
GeneTreei | ENSGT00550000074827 |
InParanoidi | P25789 |
OMAi | CNEKQRY |
OrthoDBi | 1222564at2759 |
PhylomeDBi | P25789 |
TreeFami | TF106209 |
Enzyme and pathway databases
PathwayCommonsi | P25789 |
Reactomei | R-HSA-1169091, Activation of NF-kappaB in B cells R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha R-HSA-1236974, ER-Phagosome pathway R-HSA-1236978, Cross-presentation of soluble exogenous antigens (endosomes) R-HSA-174084, Autodegradation of Cdh1 by Cdh1:APC/C R-HSA-174113, SCF-beta-TrCP mediated degradation of Emi1 R-HSA-174154, APC/C:Cdc20 mediated degradation of Securin R-HSA-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 R-HSA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A R-HSA-180534, Vpu mediated degradation of CD4 R-HSA-180585, Vif-mediated degradation of APOBEC3G R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21 R-HSA-195253, Degradation of beta-catenin by the destruction complex R-HSA-202424, Downstream TCR signaling R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation R-HSA-2467813, Separation of Sister Chromatids R-HSA-2871837, FCERI mediated NF-kB activation R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1 R-HSA-350562, Regulation of ornithine decarboxylase (ODC) R-HSA-382556, ABC-family proteins mediated transport R-HSA-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-4608870, Asymmetric localization of PCP proteins R-HSA-4641257, Degradation of AXIN R-HSA-4641258, Degradation of DVL R-HSA-5358346, Hedgehog ligand biogenesis R-HSA-5362768, Hh mutants are degraded by ERAD R-HSA-5607761, Dectin-1 mediated noncanonical NF-kB signaling R-HSA-5607764, CLEC7A (Dectin-1) signaling R-HSA-5610780, Degradation of GLI1 by the proteasome R-HSA-5610783, Degradation of GLI2 by the proteasome R-HSA-5610785, GLI3 is processed to GLI3R by the proteasome R-HSA-5632684, Hedgehog 'on' state R-HSA-5658442, Regulation of RAS by GAPs R-HSA-5668541, TNFR2 non-canonical NF-kB pathway R-HSA-5676590, NIK-->noncanonical NF-kB signaling R-HSA-5678895, Defective CFTR causes cystic fibrosis R-HSA-5687128, MAPK6/MAPK4 signaling R-HSA-5689603, UCH proteinases R-HSA-5689880, Ub-specific processing proteases R-HSA-68827, CDT1 association with the CDC6:ORC:origin complex R-HSA-68949, Orc1 removal from chromatin R-HSA-69017, CDK-mediated phosphorylation and removal of Cdc6 R-HSA-69481, G2/M Checkpoints R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint R-HSA-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis R-HSA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs R-HSA-8939902, Regulation of RUNX2 expression and activity R-HSA-8941858, Regulation of RUNX3 expression and activity R-HSA-8948751, Regulation of PTEN stability and activity R-HSA-8951664, Neddylation R-HSA-9010553, Regulation of expression of SLITs and ROBOs R-HSA-9020702, Interleukin-1 signaling R-HSA-9604323, Negative regulation of NOTCH4 signaling R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation |
Miscellaneous databases
BioGRID-ORCSi | 5685, 762 hits in 962 CRISPR screens |
ChiTaRSi | PSMA4, human |
GeneWikii | PSMA4 |
GenomeRNAii | 5685 |
Pharosi | P25789, Tbio |
PROi | PR:P25789 |
RNActi | P25789, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000041357, Expressed in monocyte and 241 other tissues |
ExpressionAtlasi | P25789, baseline and differential |
Genevisiblei | P25789, HS |
Family and domain databases
Gene3Di | 3.60.20.10, 1 hit |
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR023332, Proteasome_alpha-type IPR000426, Proteasome_asu_N IPR016050, Proteasome_bsu_CS IPR001353, Proteasome_sua/b IPR034647, Proteasome_subunit_alpha4 |
PANTHERi | PTHR11599:SF13, PTHR11599:SF13, 1 hit |
Pfami | View protein in Pfam PF00227, Proteasome, 1 hit PF10584, Proteasome_A_N, 1 hit |
SMARTi | View protein in SMART SM00948, Proteasome_A_N, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
PROSITEi | View protein in PROSITE PS00388, PROTEASOME_ALPHA_1, 1 hit PS51475, PROTEASOME_ALPHA_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PSA4_HUMAN | |
Accessioni | P25789Primary (citable) accession number: P25789 Secondary accession number(s): D3DW86 Q8TBD1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | May 1, 1992 | |
Last modified: | April 7, 2021 | |
This is version 222 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families