HAMAP rule MF_03062
General rule information
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| Accession | MF_03062 |
| Dates | 26-FEB-2009 (Created)
19-NOV-2022 (Last updated, Version 20) |
| Name | UBP16 |
| Scope(s) |
Eukaryota Vertebrata |
| Template(s) | Q9Y5T5 (UBP16_HUMAN); [ Recover all ] |
| Triggered by |
HAMAP; MF_03062 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | UBP16 |
| Protein name | RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16; EC=3.4.19.12; AltName: Full=Deubiquitinating enzyme 16; AltName: Full=Ubiquitin thioesterase 16; AltName: Full=Ubiquitin-specific-processing protease 16; |
| Gene name | Name=USP16; |
Comments
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| case <OC:Mammalia> | |
| FUNCTION | Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. |
| else | |
| FUNCTION | Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. |
| end case | |
| CATALYTIC ACTIVITY | Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; |
| SUBUNIT | Homotetramer. |
| SUBCELLULAR LOCATION | Nucleus. |
| DOMAIN | The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin. |
| case <OC:Mammalia> | |
| PTM | Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity. |
| end case | |
| SIMILARITY | Belongs to the peptidase C19 family. USP16 subfamily. |
Keywords
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| Activator |
| Cell cycle |
| Cell division |
| Chromatin regulator |
| Hydrolase |
| Metal-binding |
| Mitosis |
| Nucleus |
| Protease |
| Thiol protease |
| Transcription |
| Transcription regulation |
| Ubl conjugation pathway |
| Zinc |
| Zinc-finger |
Gene Ontology
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| GO:0005634; Cellular component:nucleus |
| GO:0004197; Molecular function:cysteine-type endopeptidase activity |
| GO:0042393; Molecular function:histone binding |
| GO:0003713; Molecular function:transcription coactivator activity |
| GO:0043130; Molecular function:ubiquitin binding |
| GO:0004843; Molecular function:cysteine-type deubiquitinase activity |
| GO:0008270; Molecular function:zinc ion binding |
| GO:0000278; Biological process:mitotic cell cycle |
| GO:0016578; Biological process:histone deubiquitination |
| GO:0140014; Biological process:mitotic nuclear division |
| GO:0045893; Biological process:positive regulation of DNA-templated transcription |
| GO:0051289; Biological process:protein homotetramerization |
Cross-references
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| PROSITE | PS00972; USP_1; 1; |
| PROSITE | PS00973; USP_2; 1; |
| PROSITE | PS50235; USP_3; 1; |
| PROSITE | PS50271; ZF_UBP; 1; |
| Pfam | PF00443; UCH; 1; |
| Pfam | PF02148; zf-UBP; 1; |
Features
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| From: UBP16_HUMAN (Q9Y5T5) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 205 | 205 | /note="Nucleophile" | C | ||||||||
| ACT_SITE | 758 | 758 | /note="Proton acceptor" | H | ||||||||
| BINDING | 24 | 24 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | ||||||||
| BINDING | 26 | 26 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
H | ||||||||
| BINDING | 48 | 48 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | ||||||||
| BINDING | 51 | 51 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | ||||||||
| BINDING | 74 | 74 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
C | ||||||||
| BINDING | 77 | 77 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
C | ||||||||
| BINDING | 82 | 82 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | ||||||||
| BINDING | 90 | 90 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
H | ||||||||
| BINDING | 94 | 94 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
H | ||||||||
| BINDING | 103 | 103 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
H | ||||||||
| BINDING | 116 | 116 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | ||||||||
| BINDING | 119 | 119 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | ||||||||
Additional information
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| Size range | 812-901 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |