UBP22_MOUSE
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 03-AUG-2022, entry version 145.
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};
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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; 4.
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; Q5DU02; -.
DR PeptideAtlas; Q5DU02; -.
DR PRIDE; Q5DU02; -.
DR ProteomicsDB; 298409; -.
DR Antibodypedia; 26118; 345 antibodies from 32 providers.
DR DNASU; 216825; -.
DR Ensembl; ENSMUST00000041683; ENSMUSP00000041263; ENSMUSG00000042506.
DR GeneID; 216825; -.
DR KEGG; mmu:216825; -.
DR UCSC; uc007jhc.2; mouse.
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; LNNDNXY; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; Q5DU02; -.
DR TreeFam; TF323554; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 216825; 11 hits in 77 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 248 other tissues.
DR ExpressionAtlas; Q5DU02; baseline and differential.
DR Genevisible; Q5DU02; MM.
DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:MGI.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0016574; P:histone ubiquitination; ISO:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC: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 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 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
