ID UB22B_XENLA Reviewed; 523 AA. AC Q6DCJ1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 2. DT 27-MAR-2024, entry version 90. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 22-B; DE EC=3.4.19.12; DE AltName: Full=Deubiquitinating enzyme 22-B; DE AltName: Full=Ubiquitin thioesterase 22-B; DE AltName: Full=Ubiquitin-specific-processing protease 22-B; GN Name=usp22-b; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUL-2004) 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, where CC it is required for transcription (By 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. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5DU02}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH78033.1; Type=Erroneous initiation; Evidence={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; BC078033; AAH78033.1; ALT_INIT; mRNA. DR RefSeq; NP_001090240.1; NM_001096771.1. DR AlphaFoldDB; Q6DCJ1; -. DR SMR; Q6DCJ1; -. DR DNASU; 779144; -. DR GeneID; 779144; -. DR KEGG; xla:779144; -. DR AGR; Xenbase:XB-GENE-6086104; -. DR CTD; 779144; -. DR Xenbase; XB-GENE-6086104; usp22.S. DR OrthoDB; 227085at2759; -. DR Proteomes; UP000186698; Chromosome 9_10S. DR Bgee; 779144; Expressed in blastula and 19 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC. 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:0006508; P:proteolysis; IEA:UniProtKB-KW. 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:SF33; 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 Activator; Cell cycle; Chromatin regulator; Hydrolase; Metal-binding; KW Nucleus; Protease; Reference proteome; Thiol protease; Transcription; KW Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..523 FT /note="Ubiquitin carboxyl-terminal hydrolase 22-B" FT /id="PRO_0000367513" FT DOMAIN 174..518 FT /note="USP" FT ZN_FING 4..121 FT /note="UBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT ACT_SITE 183 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT ACT_SITE 477 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 49 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 76 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="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" SQ SEQUENCE 523 AA; 60109 MW; C0DE1CA8DD61439D CRC64; MSPAGCSHVN SFKVENWRQN LRVIYQCFVW SGTPETRKRK AKSCVCHMCG AHLNRLHSCL YCVYFGCFTK KHIHEHAKNK RHNLAIDLLY GGIYCFMCQD YIYDKDMEQV AKEEQRKAWK LQVFSPALVS PYQYTMTGVG EKYSTWEPTK RELELLQHNP KRRKITTNCT IGLRGLINLG NTCFMNCIVQ ALTHTPLLRD FFLSDRHKCE MQSPNSCLVC EMSTLFQEFY SGHRSPHIPY RLLHLVWTHA RHLAGYEQQD AHEFLIAALD VLHRHCKGDD NGKKANNPNH CNCIIDQIFT GGLQSDVTCQ VCHGVSTTID PFWDISLDLP GSSTPFWPLS PGSDAGVVNG ESHVSGTTTL TDCLRRFTRP EHLGSSAKIK CSGCHSYQES TKQLTMKKLP IVACFHLKRF EHSAKLRRKI TTYVSFPLEL DMMPFMASSK ESRMNGQYQQ PSDSLHNDNK YSLFAVVNHQ GTLESGHYTS FIRQHKDQWF KCDDAIITKA SIKDVIDSEG YLLFYHKQFL EYE //