P55036 · PSMD4_HUMAN
- Protein26S proteasome non-ATPase regulatory subunit 4
- GenePSMD4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | proteasome accessory complex | |
Cellular Component | proteasome complex | |
Cellular Component | proteasome regulatory particle, base subcomplex | |
Molecular Function | identical protein binding | |
Molecular Function | molecular adaptor activity | |
Molecular Function | polyubiquitin modification-dependent protein binding | |
Molecular Function | RNA binding | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name26S proteasome non-ATPase regulatory subunit 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP55036
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 352 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000173828 | 1-377 | UniProt | 26S proteasome non-ATPase regulatory subunit 4 | |||
Sequence: MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATTGTEDSDDALLKMTISQQEFGRTGLPDLSSMTEEEQIAYAMQMSLQGAEFGQAESADIDASSAMDTSEPAKEEDDYDVMQDPEFLQSVLENLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEDKK | |||||||
Cross-link | 122 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 250 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 253 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 256 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 256 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 266 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 358 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 361 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases and few additional components including PSMD4 (PubMed:27342858, PubMed:27428775).
Interacts with NUB1 (PubMed:11585840).
Interacts with SQSTM1 (PubMed:15340068).
Interacts with UBQLN4 (PubMed:15280365).
Interacts with UBE3A (PubMed:22645313).
Interacts with UBQLN1 (via ubiquitin-like domain) (PubMed:15147878).
Interacts with DDI2 (PubMed:29290612).
Interacts with NUB1 (PubMed:11585840).
Interacts with SQSTM1 (PubMed:15340068).
Interacts with UBQLN4 (PubMed:15280365).
Interacts with UBE3A (PubMed:22645313).
Interacts with UBQLN1 (via ubiquitin-like domain) (PubMed:15147878).
Interacts with DDI2 (PubMed:29290612).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-188 | VWFA | ||||
Sequence: STMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPI | ||||||
Region | 197-262 | Interaction with UBQLN1 | ||||
Sequence: LGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATTGTEDSDDALLK | ||||||
Domain | 211-230 | UIM 1 | ||||
Sequence: SADPELALALRVSMEEQRQR | ||||||
Region | 216-220 | Essential for ubiquitin-binding | ||||
Sequence: LALAL | ||||||
Region | 224-255 | Disordered | ||||
Sequence: MEEQRQRQEEEARRAAAASAAEAGIATTGTED | ||||||
Compositional bias | 225-239 | Basic and acidic residues | ||||
Sequence: EEQRQRQEEEARRAA | ||||||
Domain | 282-301 | UIM 2 | ||||
Sequence: TEEEQIAYAMQMSLQGAEFG | ||||||
Region | 287-291 | Essential for ubiquitin-binding | ||||
Sequence: IAYAM | ||||||
Region | 300-327 | Disordered | ||||
Sequence: FGQAESADIDASSAMDTSEPAKEEDDYD | ||||||
Region | 341-377 | Disordered | ||||
Sequence: NLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEDKK |
Domain
The 2 UIM motifs are involved in the binding to a multi-ubiquitin chain in a cooperative way.
Sequence similarities
Belongs to the proteasome subunit S5A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
P55036-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameRpn10A
- Length377
- Mass (Da)40,737
- Last updated1996-10-01 v1
- ChecksumEC712EC4DB1CE9AB
P55036-2
- NameRpn10E
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U51007 EMBL· GenBank· DDBJ | AAC50433.1 EMBL· GenBank· DDBJ | mRNA | ||
U24704 EMBL· GenBank· DDBJ | AAB54057.1 EMBL· GenBank· DDBJ | mRNA | ||
AB033605 EMBL· GenBank· DDBJ | BAA97581.1 EMBL· GenBank· DDBJ | mRNA | ||
AL391069 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL592424 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471121 EMBL· GenBank· DDBJ | EAW53457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW53458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002365 EMBL· GenBank· DDBJ | AAH02365.1 EMBL· GenBank· DDBJ | mRNA | ||
BC072008 EMBL· GenBank· DDBJ | AAH72008.1 EMBL· GenBank· DDBJ | mRNA | ||
U72664 EMBL· GenBank· DDBJ | AAB68598.1 EMBL· GenBank· DDBJ | mRNA |