ID   UBP22_MOUSE             Reviewed;         525 AA.
AC   Q5DU02; Q3TU34; Q3U2W4; Q5SU81; Q66JV8; Q6PDX3; Q8BJG3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   27-MAR-2024, entry version 154.
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; Synonyms=Kiaa1063;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16378762; DOI=10.1016/j.modgep.2005.07.007;
RA   Lee H.-J., Kim M.-S., Shin J.-M., Park T.-J., Chung H.-M., Baek K.-H.;
RT   "The expression patterns of deubiquitinating enzymes, USP22 and Usp22.";
RL   Gene Expr. Patterns 6:277-284(2006).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=27013495; DOI=10.15252/embr.201541392;
RA   Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
RT   "The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances
RT   apoptosis.";
RL   EMBO Rep. 17:724-738(2016).
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:0000269|PubMed:27013495}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and weakly in other
CC       organs. {ECO:0000269|PubMed:16378762}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed between 10.5 dpc and 12.5 dpc.
CC       Expressed in the midbrain, forebrain, hindbrain and dorsal root ganglia
CC       of embryos at 12.5 dpc. {ECO:0000269|PubMed:16378762}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90248.1; 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; AK084022; BAC39100.1; -; mRNA.
DR   EMBL; AK220368; BAD90248.1; ALT_INIT; mRNA.
DR   EMBL; AK155071; BAE33026.1; -; mRNA.
DR   EMBL; AK160992; BAE36137.1; -; mRNA.
DR   EMBL; AL646093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058419; AAH58419.1; -; mRNA.
DR   EMBL; BC080737; AAH80737.1; -; mRNA.
DR   CCDS; CCDS24807.1; -.
DR   RefSeq; NP_001004143.2; NM_001004143.4.
DR   AlphaFoldDB; Q5DU02; -.
DR   SMR; Q5DU02; -.
DR   BioGRID; 229796; 6.
DR   ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR   ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR   ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR   IntAct; Q5DU02; 2.
DR   MINT; Q5DU02; -.
DR   STRING; 10090.ENSMUSP00000041263; -.
DR   MEROPS; C19.075; -.
DR   iPTMnet; Q5DU02; -.
DR   PhosphoSitePlus; Q5DU02; -.
DR   EPD; Q5DU02; -.
DR   MaxQB; Q5DU02; -.
DR   PaxDb; 10090-ENSMUSP00000041263; -.
DR   PeptideAtlas; Q5DU02; -.
DR   ProteomicsDB; 298409; -.
DR   Pumba; Q5DU02; -.
DR   Antibodypedia; 26118; 387 antibodies from 32 providers.
DR   DNASU; 216825; -.
DR   Ensembl; ENSMUST00000041683.9; ENSMUSP00000041263.9; ENSMUSG00000042506.16.
DR   GeneID; 216825; -.
DR   KEGG; mmu:216825; -.
DR   UCSC; uc007jhc.2; mouse.
DR   AGR; MGI:2144157; -.
DR   CTD; 23326; -.
DR   MGI; MGI:2144157; Usp22.
DR   VEuPathDB; HostDB:ENSMUSG00000042506; -.
DR   eggNOG; KOG1867; Eukaryota.
DR   GeneTree; ENSGT00940000156623; -.
DR   HOGENOM; CLU_008279_11_0_1; -.
DR   InParanoid; Q5DU02; -.
DR   OMA; YGNRIFN; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; Q5DU02; -.
DR   TreeFam; TF323554; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 216825; 11 hits in 83 CRISPR screens.
DR   ChiTaRS; Usp22; mouse.
DR   PRO; PR:Q5DU02; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5DU02; Protein.
DR   Bgee; ENSMUSG00000042506; Expressed in cortical plate and 251 other cell types or tissues.
DR   ExpressionAtlas; Q5DU02; baseline and differential.
DR   GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
DR   GO; GO:0033276; C:transcription factor TFTC complex; NAS:ComplexPortal.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0140950; F:histone H2A deubiquitinase activity; ISO:MGI.
DR   GO; GO:0140936; F:histone H2B deubiquitinase activity; ISO:MGI.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal.
DR   GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:MGI.
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.
DR   Genevisible; Q5DU02; MM.
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..525
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 22"
FT                   /id="PRO_0000080651"
FT   DOMAIN          176..520
FT                   /note="USP"
FT   ZN_FING         21..138
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   ACT_SITE        185
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        479
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         66
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         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   MOD_RES         129
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPT9"
FT   CONFLICT        77
FT                   /note="L -> H (in Ref. 2; BAE36137)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="N -> D (in Ref. 4; AAH80737)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  59954 MW;  C4CD69A0317CD0EF CRC64;
     MVARPEPEVE AMDAELAVPP PGCSHLGSFK VDNWKQNLRA IYQCFVWSGT AEARKRKAKS
     CVCHVCGIHL NRLHSCLYCV FFGCFTKKHI HDHAKSKRHN LAIDLMYGGI YCFLCQDYIY
     DKDIEIIAKE EQRKAWKMQG VGEKFSTWEP TKRELELLKH NPKRRKITSN CTIGLRGLIN
     LGNTCFMNCI VQALTHTPLL RDFFLSDRHR CEMQSPSSCL VCEMSSLFQE FYSGHRSPHI
     PYKLLHLVWT HARHLAGYEQ QDAHEFLIAA LDVLHRHCKG DDNGKKANNP NHCNCIIDQI
     FTGGLQSDVT CQVCHGVSTT IDPFWDISLD LPGSSTPFWP LSPGSEGSVV NGESHASGTT
     TLTDCLRRFT RPEHLGSSAK IKCSGCHSYQ ESTKQLTMKK LPIVACFHLK RFEHSAKLRR
     KITTYVSFPL ELDMTPFMAS SKESRMNGQY QQPLDSLNND NKYSLFAVVN HQGTLESGHY
     TSFIRQHKDQ WFKCDDAIIT KASIKDVLDS EGYLLFYHKQ FLEYE
//