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 24-JAN-2024, entry version 96. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9913-ENSBTAP00000011818; -. DR Ensembl; ENSBTAT00000011818.6; ENSBTAP00000011818.5; ENSBTAG00000008978.6. 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; NVSCNCI; -. DR OrthoDB; 227085at2759; -. 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 cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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:0140950; F:histone H2A deubiquitinase activity; IEA:Ensembl. DR GO; GO:0140936; F:histone H2B deubiquitinase activity; IEA:Ensembl. DR GO; GO:0010485; F:histone H4 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:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd02660; Peptidase_C19D; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR21646:SF40; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-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 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 //