UBP22_DANRE
ID UBP22_DANRE Reviewed; 506 AA.
AC A6H8I0; Q1JQ28;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, 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; ORFNames=zgc:136342;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6H8I0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6H8I0-2; Sequence=VSP_036726, VSP_036727;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC116508; AAI16509.1; -; mRNA.
DR EMBL; BC146618; AAI46619.1; -; mRNA.
DR RefSeq; NP_001038713.1; NM_001045248.1.
DR AlphaFoldDB; A6H8I0; -.
DR SMR; A6H8I0; -.
DR STRING; 7955.ENSDARP00000126663; -.
DR PaxDb; A6H8I0; -.
DR Ensembl; ENSDART00000059143; ENSDARP00000059142; ENSDARG00000040407. [A6H8I0-1]
DR Ensembl; ENSDART00000183637; ENSDARP00000149572; ENSDARG00000040407. [A6H8I0-2]
DR GeneID; 692275; -.
DR KEGG; dre:692275; -.
DR CTD; 23326; -.
DR ZFIN; ZDB-GENE-060512-211; usp22.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000156623; -.
DR InParanoid; A6H8I0; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; A6H8I0; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR PRO; PR:A6H8I0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000040407; Expressed in tail and 21 other tissues.
DR ExpressionAtlas; A6H8I0; baseline and differential.
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; Alternative splicing; Cell cycle; Chromatin regulator;
KW Hydrolase; Metal-binding; Nucleus; Protease; Reference proteome;
KW Thiol protease; Transcription; Transcription regulation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..506
FT /note="Ubiquitin carboxyl-terminal hydrolase 22"
FT /id="PRO_0000367511"
FT DOMAIN 159..501
FT /note="USP"
FT ZN_FING 4..121
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 460
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"
FT VAR_SEQ 261
FT /note="K -> KG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036726"
FT VAR_SEQ 392..506
FT /note="RFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPVDSLNNDNK
FT YSLFAVVNHQGTLESGHYTTFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQF
FT LEYE -> VRAELLLSVLIFQHPLNVFVCFSAV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036727"
FT CONFLICT 90
FT /note="Y -> H (in Ref. 1; AAI16509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 58120 MW; D749E025E4A15C03 CRC64;
MSPAGCSHVN GFKVDNWKQN LRVIYQCFVW SGSAETRKRK AKSCICHMCG AHLNRLHSCL
HCVFFGCFSK KHIHEHAKNK RHNLAIDLLY GGIYCFVCQD YIYDKDMEQI AKEEQRKAWK
LQGIGEKYSM WEPTKRELEL LRHNPKRRKI TANCTIGLRG LINLGNTCFM NCIVQALTHT
PLLRDFFLSD RHKCEMQSNS CLVCEMSQLF QEFYSGHRSP HIPFRLLHLV WTHARHLAGY
EQQDAHEFLI AALDVLHRHC KDDNGKKANN PNHCNCIIDQ IFTGGLQSDV TCQVCHGVST
TIDPFWDISL DLPGSSTPFW PLSPGSDGSV VNGDSHPSGA TTLTDCLRRF TRPEHLGSSA
KIKCSGCHSY QESTKQLTMK RLPIVACFHL KRFEHSAKLR RKITTYVSFP LELDMTPFMA
SSKESRMNGQ YQQPVDSLNN DNKYSLFAVV NHQGTLESGH YTTFIRQHKD QWFKCDDAII
TKASIKDVLD SEGYLLFYHK QFLEYE
