Q5DU02 (UBP22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 22
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 22
Ubiquitin thioesterase 22
Ubiquitin-specific-processing protease 22

Gene names

Name:	Usp22
Synonyms:	Kiaa1063

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression By similarity.
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Subunit structure	Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ATXN7L3, ENY2 and USP22 form a subcomplex required for histone deubiquitination. Interacts directly with ATXN7L3; leading to its recritment to the SAGA complex By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Highly expressed in brain and weakly in other organs. Ref.5
Developmental stage	Highly expressed between E10.5 and E12.5. Expressed in the midbrain, forebrain, hindbrain and dorsal root ganglia of embryos at E12.5. Ref.5
Sequence similarities	Belongs to the peptidase C19 family. UBP8 subfamily. Contains 1 UBP-type zinc finger.
Sequence caution	The sequence BAD90248.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Protease Thiol protease
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW histone deubiquitination Inferred from electronic annotation. Source: Compara histone ubiquitination Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara protein deubiquitination Inferred from direct assay Ref.5. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred by curator Ref.5. Source: MGI
Cellular_component	SAGA complex Inferred from electronic annotation. Source: Compara
Molecular_function	H4 histone acetyltransferase activity Inferred from electronic annotation. Source: Compara ligand-dependent nuclear receptor transcription coactivator activity Inferred from electronic annotation. Source: Compara ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay Ref.5. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 525	525	Ubiquitin carboxyl-terminal hydrolase 22		PRO_0000080651
Regions
	Zinc finger	61 – 121	61	UBP-type
Sites
	Active site	185	1	Nucleophile By similarity
	Active site	479	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	129	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	77	1	L → H in BAE36137. Ref.2
	Sequence conflict	188	1	N → D in AAH80737. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q5DU02 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: C4CD69A0317CD0EF	FASTA	525	59,954
	10 20 30 40 50 60 MVARPEPEVE AMDAELAVPP PGCSHLGSFK VDNWKQNLRA IYQCFVWSGT AEARKRKAKS 70 80 90 100 110 120 CVCHVCGIHL NRLHSCLYCV FFGCFTKKHI HDHAKSKRHN LAIDLMYGGI YCFLCQDYIY 130 140 150 160 170 180 DKDIEIIAKE EQRKAWKMQG VGEKFSTWEP TKRELELLKH NPKRRKITSN CTIGLRGLIN 190 200 210 220 230 240 LGNTCFMNCI VQALTHTPLL RDFFLSDRHR CEMQSPSSCL VCEMSSLFQE FYSGHRSPHI 250 260 270 280 290 300 PYKLLHLVWT HARHLAGYEQ QDAHEFLIAA LDVLHRHCKG DDNGKKANNP NHCNCIIDQI 310 320 330 340 350 360 FTGGLQSDVT CQVCHGVSTT IDPFWDISLD LPGSSTPFWP LSPGSEGSVV NGESHASGTT 370 380 390 400 410 420 TLTDCLRRFT RPEHLGSSAK IKCSGCHSYQ ESTKQLTMKK LPIVACFHLK RFEHSAKLRR 430 440 450 460 470 480 KITTYVSFPL ELDMTPFMAS SKESRMNGQY QQPLDSLNND NKYSLFAVVN HQGTLESGHY 490 500 510 520 TSFIRQHKDQ WFKCDDAIIT KASIKDVLDS EGYLLFYHKQ FLEYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Head and Spinal ganglion.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
[5]	"The expression patterns of deubiquitinating enzymes, USP22 and Usp22." Lee H.-J., Kim M.-S., Shin J.-M., Park T.-J., Chung H.-M., Baek K.-H. Gene Expr. Patterns 6:277-284(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK084022 mRNA. Translation: BAC39100.1. AK220368 mRNA. Translation: BAD90248.1. Different initiation. AK155071 mRNA. Translation: BAE33026.1. AK160992 mRNA. Translation: BAE36137.1. AL646093 Genomic DNA. Translation: CAI25897.1. BC058419 mRNA. Translation: AAH58419.1. BC080737 mRNA. Translation: AAH80737.1.
IPI	IPI00228479.
RefSeq	NP_001004143.2. NM_001004143.4.
UniGene	Mm.30602.
3D structure databases
ProteinModelPortal	Q5DU02.
SMR	Q5DU02. Positions 76-517.
ModBase	Search...
Protein family/group databases
MEROPS	C19.035.
PTM databases
PhosphoSite	Q5DU02.
Proteomic databases
PaxDb	Q5DU02.
PRIDE	Q5DU02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000041683; ENSMUSP00000041263; ENSMUSG00000042506.
GeneID	216825.
KEGG	mmu:216825.
UCSC	uc007jhc.2. mouse.
Organism-specific databases
CTD	23326.
MGI	MGI:2144157. Usp22.
Rouge	Search...
Phylogenomic databases
eggNOG	COG5533.
GeneTree	ENSGT00690000101718.
HOVERGEN	HBG058014.
InParanoid	Q3U2W4.
KO	K11366.
OMA	IHEHAKA.
OrthoDB	EOG48PMJS.
Gene expression databases
ArrayExpress	Q5DU02.
Bgee	Q5DU02.
CleanEx	MM_USP22.
Genevestigator	Q5DU02.
GermOnline	ENSMUSG00000042506. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR013083. Znf_RING/FYVE/PHD. IPR001607. Znf_UBP. [Graphical view]
Pfam	PF00443. UCH. 1 hit. PF02148. zf-UBP. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	375358.
SOURCE	Search...

Entry information

Entry name

UBP22_MOUSE

Accession

Primary (citable) accession number: Q5DU02
Secondary accession number(s): Q3TU34 , Q3U2W4, Q5SU81, Q66JV8, Q6PDX3, Q8BJG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program