UB22A_XENLA
ID UB22A_XENLA Reviewed; 523 AA.
AC Q6GNI6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 22-A;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 22-A;
DE AltName: Full=Ubiquitin thioesterase 22-A;
DE AltName: Full=Ubiquitin-specific-processing protease 22-A;
GN Name=usp22-a;
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=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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}.
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DR EMBL; BC073524; AAH73524.1; -; mRNA.
DR RefSeq; NP_001085912.1; NM_001092443.1.
DR AlphaFoldDB; Q6GNI6; -.
DR SMR; Q6GNI6; -.
DR DNASU; 444339; -.
DR GeneID; 444339; -.
DR KEGG; xla:444339; -.
DR CTD; 444339; -.
DR Xenbase; XB-GENE-5806563; usp22.L.
DR OrthoDB; 929408at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 444339; Expressed in blastula and 19 other 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:0016579; P:protein deubiquitination; IEA:InterPro.
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 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-A"
FT /id="PRO_0000367512"
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; 60049 MW; 731A0AE1C2E67D61 CRC64;
MSPAGCSHVN SFKVENWKQN LRVIYQCFVW SGTPETRKRK AKSCICHMCG AHLNRLHSCL
YCVFFGCFTK 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 DMTPFMASSK ESRMNGQYQQ PSDSLHNDNK YSLFAVVNHQ GTLESGHYTS
FIRQHKDQWF KCDDAIITKA SIKDVLDSEG YLLFYHKQFL EYE
