Q14997 · PSME4_HUMAN
- ProteinProteasome activator complex subunit 4
- GenePSME4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1843 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradation of histones following DNA double-strand breaks.
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 | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | spermatoproteasome complex | |
Molecular Function | lysine-acetylated histone binding | |
Molecular Function | peptidase activator activity | |
Molecular Function | proteasome binding | |
Biological Process | DNA damage response | |
Biological Process | DNA repair | |
Biological Process | proteasomal ubiquitin-independent protein catabolic process | |
Biological Process | sperm DNA condensation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProteasome activator complex 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 accessionQ14997
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in nuclear foci following treatment with ionizing radiation, but not with ultraviolet irradiation or H2O2.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031189 | 872 | in dbSNP:rs2302878 | |||
Sequence: I → V | ||||||
Natural variant | VAR_031190 | 1371 | in dbSNP:rs805408 | |||
Sequence: S → T | ||||||
Mutagenesis | 1716-1717 | Abolishes binding to acetylated histones. | ||||
Sequence: NF → TS | ||||||
Natural variant | VAR_059755 | 1825 | in dbSNP:rs35903236 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,784 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000280718 | 1-1843 | UniProt | Proteasome activator complex subunit 4 | |||
Sequence: MEPAERAGVGEPPEPGGRPEPGPRGFVPQKEIVYNKLLPYAERLDAESDLQLAQIKCNLGRAVQLQELWPGGLFWTRKLSTYIRLYGRKFSKEDHVLFIKLLYELVSIPKLEISMMQGFARLLINLLKKKELLSRADLELPWRPLYDMVERILYSKTEHLGLNWFPNSVENILKTLVKSCRPYFPADATAEMLEEWRPLMCPFDVTMQKAITYFEIFLPTSLPPELHHKGFKLWFDELIGLWVSVQNLPQWEGQLVNLFARLATDNIGYIDWDPYVPKIFTRILRSLNLPVGSSQVLVPRFLTNAYDIGHAVIWITAMMGGPSKLVQKHLAGLFNSITSFYHPSNNGRWLNKLMKLLQRLPNSVVRRLHRERYKKPSWLTPVPDSHKLTDQDVTDFVQCIIQPVLLAMFSKTGSLEAAQALQNLALMRPELVIPPVLERTYPALETLTEPHQLTATLSCVIGVARSLVSGGRWFPEGPTHMLPLLMRALPGVDPNDFSKCMITFQFIATFSTLVPLVDCSSVLQERNDLTEVERELCSATAEFEDFVLQFMDRCFGLIESSTLEQTREETETEKMTHLESLVELGLSSTFSTILTQCSKEIFMVALQKVFNFSTSHIFETRVAGRMVADMCRAAVKCCPEESLKLFVPHCCSVITQLTMNDDVLNDEELDKELLWNLQLLSEITRVDGRKLLLYREQLVKILQRTLHLTCKQGYTLSCNLLHHLLRSTTLIYPTEYCSVPGGFDKPPSEYFPIKDWGKPGDLWNLGIQWHVPSSEEVSFAFYLLDSFLQPELVKLQHCGDGKLEMSRDDILQSLTIVHNCLIGSGNLLPPLKGEPVTNLVPSMVSLEETKLYTGLEYDLSRENHREVIATVIRKLLNHILDNSEDDTKSLFLIIKIIGDLLQFQGSHKHEFDSRWKSFNLVKKSMENRLHGKKQHIRALLIDRVMLQHELRTLTVEGCEYKKIHQDMIRDLLRLSTSSYSQVRNKAQQTFFAALGAYNFCCRDIIPLVLEFLRPDRQGVTQQQFKGALYCLLGNHSGVCLANLHDWDCIVQTWPAIVSSGLSQAMSLEKPSIVRLFDDLAEKIHRQYETIGLDFTIPKSCVEIAELLQQSKNPSINQILLSPEKIKEGIKRQQEKNADALRNYENLVDTLLDGVEQRNLPWKFEHIGIGLLSLLLRDDRVLPLRAIRFFVENLNHDAIVVRKMAISAVAGILKQLKRTHKKLTINPCEISGCPKPTQIIAGDRPDNHWLHYDSKTIPRTKKEWESSCFVEKTHWGYYTWPKNMVVYAGVEEQPKLGRSREDMTEAEQIIFDHFSDPKFVEQLITFLSLEDRKGKDKFNPRRFCLFKGIFRNFDDAFLPVLKPHLEHLVADSHESTQRCVAEIIAGLIRGSKHWTFEKVEKLWELLCPLLRTALSNITVETYNDWGACIATSCESRDPRKLHWLFELLLESPLSGEGGSFVDACRLYVLQGGLAQQEWRVPELLHRLLKYLEPKLTQVYKNVRERIGSVLTYIFMIDVSLPNTTPTISPHVPEFTARILEKLKPLMDVDEEIQNHVMEENGIGEEDERTQGIKLLKTILKWLMASAGRSFSTAVTEQLQLLPLFFKIAPVENDNSYDELKRDAKLCLSLMSQGLLYPHQVPLVLQVLKQTARSSSWHARYTVLTYLQTMVFYNLFIFLNNEDAVKDIRWLVISLLEDEQLEVREMAATTLSGLLQCNFLTMDSPMQIHFEQLCKTKLPKKRKRDPGSVGDTIPSAELVKRHAGVLGLGACVLSSPYDVPTWMPQLLMNLSAHLNDPQPIEMTVKKTLSNFRRTHHDNWQEHKQQFTDDQLLVLTDLLVSPCYYA | |||||||
Modified residue | 1121 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1614 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1746 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1746 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1750 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer. Interacts with the 20S and 26S proteasomes. Component of the spermatoproteasome, a form of the proteasome specifically found in testis.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14997 | CALCOCO2 Q13137 | 3 | EBI-1236916, EBI-739580 | |
BINARY | Q14997 | NUTM1 Q86Y26 | 3 | EBI-1236916, EBI-10178410 | |
BINARY | Q14997 | PSMC6 P62333 | 2 | EBI-1236916, EBI-357669 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MEPAERAGVGEPPEPGGRPEPGPRG | ||||||
Repeat | 475-519 | HEAT 1 | ||||
Sequence: PEGPTHMLPLLMRALPGVDPNDFSKCMITFQFIATFSTLVPLVDC | ||||||
Repeat | 998-1037 | HEAT 2 | ||||
Sequence: NFCCRDIIPLVLEFLRPDRQGVTQQQFKGALYCLLGNHSG | ||||||
Repeat | 1179-1217 | HEAT 3 | ||||
Sequence: RVLPLRAIRFFVENLNHDAIVVRKMAISAVAGILKQLKR | ||||||
Repeat | 1354-1392 | HEAT 4 | ||||
Sequence: DAFLPVLKPHLEHLVADSHESTQRCVAEIIAGLIRGSKH | ||||||
Repeat | 1636-1674 | HEAT 5 | ||||
Sequence: PHQVPLVLQVLKQTARSSSWHARYTVLTYLQTMVFYNLF | ||||||
Region | 1650-1738 | Bromodomain-like (BRDL) | ||||
Sequence: ARSSSWHARYTVLTYLQTMVFYNLFIFLNNEDAVKDIRWLVISLLEDEQLEVREMAATTLSGLLQCNFLTMDSPMQIHFEQLCKTKLPK | ||||||
Repeat | 1680-1718 | HEAT 6 | ||||
Sequence: EDAVKDIRWLVISLLEDEQLEVREMAATTLSGLLQCNFL |
Domain
The bromodomain-like (BRDL) region specifically recognizes and binds acetylated histones.
Sequence similarities
Belongs to the BLM10 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q14997-1
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.
- Name1
- Length1,843
- Mass (Da)211,334
- Last updated2007-03-20 v2
- Checksum2D2C3A594E4FA4E7
Q14997-2
- Name2
- Differences from canonical
- 1-625: Missing
Q14997-3
- Name3
Q14997-4
- Name4
- Differences from canonical
- 1-1628: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WBH5 | F8WBH5_HUMAN | PSME4 | 571 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023878 | 1-625 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023877 | 1-856 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023876 | 1-1628 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 217 | in Ref. 1; AAX83871 | ||||
Sequence: F → V | ||||||
Sequence conflict | 710 | in Ref. 1; AAX83871 | ||||
Sequence: C → R | ||||||
Alternative sequence | VSP_023879 | 857-871 | in isoform 3 | |||
Sequence: YDLSRENHREVIATV → MGENLAKKIMFFLLI | ||||||
Sequence conflict | 984 | in Ref. 1; AAX83871 | ||||
Sequence: N → S | ||||||
Sequence conflict | 1401 | in Ref. 2; AAH43602 | ||||
Sequence: L → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY894754 EMBL· GenBank· DDBJ | AAX83869.1 EMBL· GenBank· DDBJ | mRNA | ||
AY894755 EMBL· GenBank· DDBJ | AAX83870.1 EMBL· GenBank· DDBJ | mRNA | ||
AY894756 EMBL· GenBank· DDBJ | AAX83871.1 EMBL· GenBank· DDBJ | mRNA | ||
BC043602 EMBL· GenBank· DDBJ | AAH43602.1 EMBL· GenBank· DDBJ | mRNA | ||
BC071768 EMBL· GenBank· DDBJ | AAH71768.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112169 EMBL· GenBank· DDBJ | AAI12170.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC113668 EMBL· GenBank· DDBJ | AAI13669.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
D38521 EMBL· GenBank· DDBJ | BAA07526.1 EMBL· GenBank· DDBJ | mRNA |