ID A0A1U7RYS3_ALLSI Unreviewed; 825 AA.
AC A0A1U7RYS3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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|RefSeq:XP_006021446.1, ECO:0000313|RefSeq:XP_025057119.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|RefSeq:XP_006021446.1};
RN [1] {ECO:0000313|RefSeq:XP_006021446.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
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. {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 -!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03062}.
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DR RefSeq; XP_006021446.1; XM_006021384.3.
DR RefSeq; XP_006021447.1; XM_006021385.2.
DR RefSeq; XP_006021448.1; XM_006021386.2.
DR RefSeq; XP_006021449.1; XM_006021387.2.
DR RefSeq; XP_025057119.1; XM_025201334.1.
DR STRING; 38654.A0A1U7RYS3; -.
DR GeneID; 102369463; -.
DR KEGG; asn:102369463; -.
DR CTD; 10600; -.
DR eggNOG; KOG1873; Eukaryota.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000189705; Unplaced.
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|HAMAP-Rule:MF_03062, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Thiol protease {ECO:0000256|HAMAP-Rule:MF_03062,
KW ECO:0000256|RuleBase:RU366025};
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 22..142
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 196..824
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 145..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..452
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT ACT_SITE 759
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03062"
SQ SEQUENCE 825 AA; 93900 MW; 1454F5CC37CC1FB9 CRC64;
MGKKRTKGKT AQTDETLDIQ EPVCKHIRKG VEHGLLKKAL LNVEWNVCED CRTDNKAQDK
SQEETDESPS IWLCLKCGHR GCGRNSQEQH ALKHHTTPRS DPHCLVLSLD NWSVWCYLCD
NEVPYSSSTR LGQLVDNVRK ACADTPHTAS EHQESQDFEN KKTEKDNRNE QEKEKREGMI
KEETSYPNTN AEVIVKGLSN LGNTCFFNAV MQNLSQTPVL RELLKEAKMP GTTVKIEPPD
FSTEPLVIQL EQPGPLTLAM CQFLTEMQET KKGTVTPKEL FAQVCKKAIR FKGYQQQDSQ
ELLRYLLDGM RAEEIQRVSV GLLKMLNVSD RQNEELKKKI KEYEKKKGIQ TFVDRIFGGE
LTSTIMCEEC RTVSLVHESF LDLSLPVLDD QSTKSTKERN AKKAKEKETD EEEDDDKHND
SYMKEREDPG ASKHHQKKAK KQAKKQAKNQ RRQQKLQGKV LQLTEVCVTE ESEENLETNK
ETKAEEMNSE VTDLKQEEEP SNQCKELYLN QKDLNNKENC TDTQSEHENI GNPEQECLEN
ENNVADPLGN LISTAECISG LEDLPFEEDD HVEDEALATS MSKLQLDAAS DIDMDTLDEF
DTAQTKICEV VNEDPETAFC TLANREDLNI EEGSIHLCLY QFTRNEELSE TNKLLCDVCT
ERQYGPTNNG KSEKKPVYTN AKKQMLISLA PPILTLHLKR FQQAGFNLRK VNRHIKFPEV
IDLAPFCTVK CKNVAEGNSR VLYSLYGVVE HSGTMRSGHY TAYAKMRAMN NHLSDLVLHG
EVPQASETES AKGQWFHISD THVQAVSTSK VLSSQAYLLF YERLL
//
