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Q5DU02 (UBP22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Contains 1 USP domain.

Sequence caution

The sequence BAD90248.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Hydrolase
Protease
Thiol protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

histone deubiquitination

Inferred from electronic annotation. Source: Ensembl

histone ubiquitination

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein deubiquitination

Inferred from direct assay Ref.5. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred by curator Ref.5. Source: MGI

   Cellular_componentSAGA complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionH4 histone acetyltransferase activity

Inferred from electronic annotation. Source: Ensembl

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525Ubiquitin carboxyl-terminal hydrolase 22
PRO_0000080651

Regions

Domain176 – 520345USP
Zinc finger61 – 12161UBP-type

Sites

Active site1851Nucleophile By similarity
Active site4791Proton acceptor By similarity

Amino acid modifications

Modified residue1291N6-acetyllysine By similarity

Experimental info

Sequence conflict771L → H in BAE36137. Ref.2
Sequence conflict1881N → D in AAH80737. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q5DU02 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: C4CD69A0317CD0EF

FASTA52559,954
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS24807.1.
RefSeqNP_001004143.2. NM_001004143.4.
UniGeneMm.30602.

3D structure databases

ProteinModelPortalQ5DU02.
SMRQ5DU02. Positions 76-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ5DU02. 2 interactions.

Protein family/group databases

MEROPSC19.035.

PTM databases

PhosphoSiteQ5DU02.

Proteomic databases

PaxDbQ5DU02.
PRIDEQ5DU02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041683; ENSMUSP00000041263; ENSMUSG00000042506.
GeneID216825.
KEGGmmu:216825.
UCSCuc007jhc.2. mouse.

Organism-specific databases

CTD23326.
MGIMGI:2144157. Usp22.
RougeSearch...

Phylogenomic databases

eggNOGCOG5533.
GeneTreeENSGT00750000117288.
HOVERGENHBG058014.
InParanoidQ3U2W4.
KOK11366.
OMAYCQMCDD.
OrthoDBEOG7FR7G7.
PhylomeDBQ5DU02.
TreeFamTF323554.

Gene expression databases

BgeeQ5DU02.
CleanExMM_USP22.
GenevestigatorQ5DU02.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio375358.
PROQ5DU02.
SOURCESearch...

Entry information

Entry nameUBP22_MOUSE
AccessionPrimary (citable) accession number: Q5DU02
Secondary accession number(s): Q3TU34 expand/collapse secondary AC list , Q3U2W4, Q5SU81, Q66JV8, Q6PDX3, Q8BJG3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot