AC   MF_03062;
DC   Protein; auto
TR   HAMAP; MF_03062; -; 1; level=0
XX
Names: UBP16
XX
ID   UBP16
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 16;
DE   AltName: Full=Ubiquitin thioesterase 16;
DE   AltName: Full=Ubiquitin-specific-processing protease 16;
GN   Name=USP16;
XX
case <OC:Mammalia>
CC   -!- FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A
CC       (H2AK119Ub), a specific tag for epigenetic transcriptional repression,
CC       thereby acting as a coactivator. Deubiquitination of histone H2A is a
CC       prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3
CC       (H3S10ph), and is required for chromosome segregation when cells enter
CC       into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB
CC       leads to enhance its activity, thereby maintaining transcription in
CC       resting lymphocytes. Regulates Hox gene expression via histone H2A
CC       deubiquitination. Prefers nucleosomal substrates. Does not
CC       deubiquitinate histone H2B.
else
CC   -!- FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A
CC       (H2AK119Ub), a specific tag for epigenetic transcriptional repression,
CC       thereby acting as a coactivator. Deubiquitination of histone H2A is a
CC       prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3
CC       (H3S10ph), and is required for chromosome segregation when cells enter
CC       into mitosis. Regulates Hox gene expression via histone H2A
CC       deubiquitination. Prefers nucleosomal substrates. Does not
CC       deubiquitinate histone H2B.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions that form a pair of
CC       cross-braced ring fingers encapsulated within a third zinc finger in
CC       the primary structure. It recognizes the C-terminal tail of free
CC       ubiquitin.
case <OC:Mammalia>
CC   -!- PTM: Phosphorylated at the onset of mitosis and dephosphorylated during
CC       the metaphase/anaphase transition. Phosphorylation by AURKB enhances
CC       the deubiquitinase activity.
end case
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily.
XX
DR   PROSITE; PS00972; USP_1; 1; trigger=no
DR   PROSITE; PS00973; USP_2; 1; trigger=no
DR   PROSITE; PS50235; USP_3; 1; trigger=no
DR   PROSITE; PS50271; ZF_UBP; 1; trigger=yes
DR   Pfam; PF00443; UCH; 1; trigger=no
DR   Pfam; PF02148; zf-UBP; 1; trigger=no
XX
KW   Activator
KW   Cell cycle
KW   Cell division
KW   Chromatin regulator
KW   Hydrolase
KW   Metal-binding
KW   Mitosis
KW   Nucleus
KW   Protease
KW   Thiol protease
KW   Transcription
KW   Transcription regulation
KW   Ubl conjugation pathway
KW   Zinc
KW   Zinc-finger
XX
GO   GO:0005634; C:nucleus
GO   GO:0004197; F:cysteine-type endopeptidase activity
GO   GO:0042393; F:histone binding
GO   GO:0003713; F:transcription coactivator activity
GO   GO:0043130; F:ubiquitin binding
GO   GO:0004843; F:cysteine-type deubiquitinase activity
GO   GO:0008270; F:zinc ion binding
GO   GO:0000278; P:mitotic cell cycle
GO   GO:0016578; P:histone deubiquitination
GO   GO:0140014; P:mitotic nuclear division
GO   GO:0045893; P:positive regulation of DNA-templated transcription
GO   GO:0051289; P:protein homotetramerization
XX
FT   From: UBP16_HUMAN (Q9Y5T5)
FT   ACT_SITE        205
FT                   /note="Nucleophile"
FT   Condition: C
FT   ACT_SITE        758
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: C
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: C
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: C
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   Condition: C
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   Condition: C
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: C
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   Condition: H
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   Condition: H
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: C
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: C
XX
Size: 812-901;
Related: None;
Template: Q9Y5T5;
Scope:
 Eukaryota; Vertebrata
Fusion:
 Nter: None
 Cter: None
Duplicate: in MYOLU
Plasmid: None
Comments: None
XX
# Revision 1.20 2022/11/19
//