ID A0A287AS01_PIG Unreviewed; 808 AA.
AC A0A287AS01;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 3.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000256|HAMAP-Rule:MF_03062};
DE EC=3.4.19.12 {ECO:0000256|HAMAP-Rule:MF_03062};
DE AltName: Full=Deubiquitinating enzyme 16 {ECO:0000256|HAMAP-Rule:MF_03062};
DE AltName: Full=Ubiquitin thioesterase 16 {ECO:0000256|HAMAP-Rule:MF_03062};
DE AltName: Full=Ubiquitin-specific-processing protease 16 {ECO:0000256|HAMAP-Rule:MF_03062};
GN Name=USP16 {ECO:0000256|HAMAP-Rule:MF_03062,
GN ECO:0000313|Ensembl:ENSSSCP00000046693.3,
GN ECO:0000313|VGNC:VGNC:94749};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000046693.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000046693.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000046693.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000046693.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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. {ECO:0000256|HAMAP-Rule:MF_03062}.
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; Evidence={ECO:0000256|ARBA:ARBA00000707,
CC ECO:0000256|HAMAP-Rule:MF_03062, ECO:0000256|RuleBase:RU366025};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03062}.
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. {ECO:0000256|HAMAP-Rule:MF_03062}.
CC -!- PTM: Phosphorylated at the onset of mitosis and dephosphorylated during
CC the metaphase/anaphase transition. Phosphorylation by AURKB enhances
CC the deubiquitinase activity. {ECO:0000256|HAMAP-Rule:MF_03062}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03062}.
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DR AlphaFoldDB; A0A287AS01; -.
DR Ensembl; ENSSSCT00000062487.3; ENSSSCP00000046693.3; ENSSSCG00000027594.4.
DR VGNC; VGNC:94749; USP16.
DR GeneTree; ENSGT00940000156013; -.
DR OMA; MAAGHYV; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000027594; Expressed in epididymis and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287AS01; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0140014; P:mitotic nuclear division; IEA:UniProtKB-UniRule.
DR GO; GO:0051289; P:protein homotetramerization; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_03062; UBP16; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR030849; UBP16.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF12; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 16; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_03062};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03062};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|HAMAP-Rule:MF_03062};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03062};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03062};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, ECO:0000256|HAMAP-
KW Rule:MF_03062};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03062};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_03062}.
FT DOMAIN 8..127
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 180..807
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 133..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT ACT_SITE 742
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
SQ SEQUENCE 808 AA; 91451 MW; 69FBDE3B7D1F3D3C CRC64;
MGSVAVEPTC RHIRKGLEQG NLKKALVNVE WNICQDCKTD NKVKDKSEEE TENPSVWLCL
KCGHQGCGRD SQEQHALKHY MTPRSEPHCL VLSLDNWSVW CYLCDDEVQY CNSNRLGQVV
DYVRKQAGIT APKSAKDNGN IELENKKLEK ESKNEQEREK KENKAKENPS MNSASQITVK
GLSNLGNTCF FNAVMQNLSQ TPVLRELLKE VKMSGTIVKI EPPDLALTEP LEINLEPPGP
LTLAMSQFLN EMQETKKGIV TPRELFSQVC KKAVRFKGYQ QQDSQELLRY LLDGMRAEEH
QRVSKGILKA FGNSTEKLDE ELKNKVKDYE KKKSVPSFVD RIFGGELTST IMCDECRTVS
LVHESFLDLS LPVLDDQSGK KSINDKNLKK TMEDEDKDCE EEKDNDSYIK ERNDIPSGTS
KHLQKKAKKQ AKKQAKYQRR QQKIQGKVLH LNDVCAVDHP EDNECEVEAS TSEVDVKSSH
TSQEEVMHKE CCEKDLNGHE KTVESVTDNQ KSTEEGDMKI VNLDNDLEVL ASSPTECTGN
LNGAYLKAGS NGEVDISSGF KNLNLNAALE PDEINIEILN DDLTPGAKVY EVVNEDPETA
FCTLANREAF NTDECSIQHC LYQFTRNEKL RDANKLLCEV CTRRQYSGPK ANIKGERKHV
YTNAKKQMLI SLAPPVLTLH LKRFQQAGFN LRKVNKHIKF PEILDLAPFC TLKCKNVAEE
NTRVLYSLYG VVEHSGTMRS GHYTAYAKAR TANSHLSDLV LHGDIPQDFE MESTKGQWFH
ISDTHVQAVP TTKVLNSQAY LLFYERIL
//
