UBP22_BOVIN
ID UBP22_BOVIN Reviewed; 514 AA.
AC P0C8Z3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 22;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 22;
DE AltName: Full=Ubiquitin thioesterase 22;
DE AltName: Full=Ubiquitin-specific-processing protease 22;
GN Name=USP22;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon, Brain cortex, and Rumen;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone deubiquitinating component of the transcription
CC regulatory histone acetylation (HAT) complex SAGA. Catalyzes the
CC deubiquitination of both histones H2A and H2B, thereby acting as a
CC coactivator. Recruited to specific gene promoters by activators such as
CC MYC, where it is required for transcription. Required for nuclear
CC receptor-mediated transactivation and cell cycle progression (By
CC similarity). {ECO:0000250}.
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: Component of some SAGA transcription coactivator-HAT
CC complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H,
CC TAF10, TRRAP and USP22. Within the SAGA complex, ATXN7L3, ENY2 and
CC USP22 form a subcomplex required for histone deubiquitination.
CC Interacts directly with ATXN7L3; leading to its recruitment to the SAGA
CC complex. Interacts with ATXN7L3 and weakly with ATXN7L3B.
CC {ECO:0000250|UniProtKB:Q9UPT9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5DU02}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000305}.
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DR EMBL; EE333442; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EH202007; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EV691513; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001160039.1; NM_001166567.1.
DR AlphaFoldDB; P0C8Z3; -.
DR SMR; P0C8Z3; -.
DR STRING; 9913.ENSBTAP00000011818; -.
DR PaxDb; P0C8Z3; -.
DR PRIDE; P0C8Z3; -.
DR Ensembl; ENSBTAT00000011818; ENSBTAP00000011818; ENSBTAG00000008978.
DR GeneID; 509694; -.
DR KEGG; bta:509694; -.
DR CTD; 23326; -.
DR VEuPathDB; HostDB:ENSBTAG00000008978; -.
DR VGNC; VGNC:36716; USP22.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000156623; -.
DR HOGENOM; CLU_008279_11_0_1; -.
DR InParanoid; P0C8Z3; -.
DR OMA; FMSVILQ; -.
DR OrthoDB; 929408at2759; -.
DR TreeFam; TF323554; -.
DR Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000008978; Expressed in floor plate of diencephalon and 104 other tissues.
DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
DR GO; GO:0016574; P:histone ubiquitination; IEA:Ensembl.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
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 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 Acetylation; Activator; Cell cycle; Chromatin regulator; Hydrolase;
KW Metal-binding; Nucleus; Protease; Reference proteome; Thiol protease;
KW Transcription; Transcription regulation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..514
FT /note="Ubiquitin carboxyl-terminal hydrolase 22"
FT /id="PRO_0000367510"
FT DOMAIN 165..509
FT /note="USP"
FT ZN_FING 10..127
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT ACT_SITE 174
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPT9"
SQ SEQUENCE 514 AA; 58737 MW; D825824E36F6C7B4 CRC64;
MDAELVVTPP GCAHLGSFKV DNWKQNLRAI YQCFVWSGSA EARKRKAKSC VCHVCGLHLN
RLHSCLHCVF FGCFTKKHIH EHAKSKRHNL AIELMYGGIY CFLCQDYIYD KDIEIIAKEE
QRKAWKMQGV GEKFSTWEPT KRELELLKHN PKRRKITSNC TIGLRGLINL GNTCFMNCIV
QALTHTPLLR DFFLSDRHRC EMQSPSSCLV CEMSSLFQEF YSGHRSPHIP YKLLHLVWTH
ARHLAGYEQQ DAHEFLIAAL DVLHRHCKGD DNGKKANNPN HCNCIIDQIF TGGLQSDVTC
QVCHGVSTTI DPFWDISLDL PGSSTPFWPL SPGSESSVVN GESHVSGTTT LTDCLRRFTR
PEHLGSSAKI KCSGCHSYQE STKQLTMKKL PIVACFHLKR FEHSAKLRRK ITTYVSFPLE
LDMTPFMASS KESRMNGQYQ QPTDSLNNDN KYSLFAVVNH QGTLESGHYT SFIRQHKDQW
FKCDDAIITK ASIADVLDSE GYLLFYHKQF LEYE
