UBP16_MACFA
ID UBP16_MACFA Reviewed; 826 AA.
AC Q4R6X7; Q4R6G7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000255|HAMAP-Rule:MF_03062};
DE EC=3.4.19.12 {ECO:0000255|HAMAP-Rule:MF_03062};
DE AltName: Full=Deubiquitinating enzyme 16 {ECO:0000255|HAMAP-Rule:MF_03062};
DE AltName: Full=Ubiquitin thioesterase 16 {ECO:0000255|HAMAP-Rule:MF_03062};
DE AltName: Full=Ubiquitin-specific-processing protease 16 {ECO:0000255|HAMAP-Rule:MF_03062};
GN Name=USP16 {ECO:0000255|HAMAP-Rule:MF_03062};
GN ORFNames=QtsA-16913, QtsA-18064;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_03062};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4R6X7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R6X7-2; Sequence=VSP_036723, VSP_036724;
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:0000255|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:0000255|HAMAP-Rule:MF_03062}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03062}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01308.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB169053; BAE01147.1; -; mRNA.
DR EMBL; AB169216; BAE01308.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q4R6X7; -.
DR BMRB; Q4R6X7; -.
DR STRING; 9541.XP_005548926.1; -.
DR PRIDE; Q4R6X7; -.
DR eggNOG; KOG1873; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0140014; P:mitotic nuclear division; IEA:UniProtKB-UniRule.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045901; P:positive regulation of translational elongation; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 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 Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 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 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cell cycle; Cell division;
KW Chromatin regulator; Hydrolase; Isopeptide bond; Metal-binding; Mitosis;
KW Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..826
FT /note="Ubiquitin carboxyl-terminal hydrolase 16"
FT /id="PRO_0000367502"
FT DOMAIN 196..825
FT /note="USP"
FT ZN_FING 22..142
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 146..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03062"
FT ACT_SITE 761
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03062"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5"
FT VAR_SEQ 150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036723"
FT VAR_SEQ 735..826
FT /note="NVAEENTRVLYSLYGVVEHSGTMRSGHYTAYAKARTANSHLSNLVLHGDIPQ
FT DFEMESKGQWFHISDTHVQAVPTTKVLNSQAYLLFYERIL -> ILKWNQKGSGFTSAT
FT HMCKLCLQLKY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036724"
FT CONFLICT 55
FT /note="N -> D (in Ref. 1; BAE01308)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="S -> P (in Ref. 1; BAE01308)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="D -> E (in Ref. 1; BAE01308)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="S -> G (in Ref. 1; BAE01147)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="N -> D (in Ref. 1; BAE01308)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="P -> S (in Ref. 1; BAE01147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 94059 MW; EEBDB3D17A4CD634 CRC64;
MGKKRTKGKT VPIDDSSETL EPMCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK
AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS EPHCLVLSLD NWSVWCYICD
NEVQYCSSNQ LGQVVDYVRK QASITTPKPA EKDNGNIELE NKKLEKESKN EQEREKKENM
AKENPPMNSP SQITVKGLSN LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD
LALTEPLEIN LEPPGPLTLA MSQFLNEMQE TKKGIVTPKE LFSQVCKKAV RFKGYQQQDS
QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS IPSFVDRIFG
GELTSTIMCD QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN DKNLKKTMED EDQDSEEEKD
NDSYIKERSD IPSGTSKHLQ KKAKKQAKKQ AKNQRRQQKI QGKVLHLNDI CTIDHPEDNE
YEAEMSLQGE VNIKSNHISQ EGVMHKEYCV NQKDLNGQEK MIESVTDNQK PTEEVDMKNI
NMDNDLEVLT SSPTECTRNL NGAYLTEASN GEVDISNGFK NLNLNAALHP DEINIEILND
SHTPGTKVYE VVNEDPETAF CTLANREVFN TDECSIQHCL YQFTRNEKLR DANKLLCEVC
TRRQCNGPKA NMKGERKHVY TNAKKQMLIS LAPPVLTLHL KRFQQAGFNL RKVNKHIKFP
EILDLAPFCT LKCKNVAEEN TRVLYSLYGV VEHSGTMRSG HYTAYAKART ANSHLSNLVL
HGDIPQDFEM ESKGQWFHIS DTHVQAVPTT KVLNSQAYLL FYERIL
