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Q9UPT9

- UBP22_HUMAN

UniProt

Q9UPT9 - UBP22_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 22

Gene

USP22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Catalytic activityi

    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).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei185 – 1851NucleophilePROSITE-ProRule annotation
    Active sitei479 – 4791Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri61 – 12161UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. enzyme binding Source: UniProt
    2. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. chromatin organization Source: Reactome
    3. embryo development Source: UniProtKB
    4. histone deubiquitination Source: UniProtKB
    5. histone H4 acetylation Source: GOC
    6. histone ubiquitination Source: UniProtKB
    7. positive regulation of mitotic cell cycle Source: UniProtKB
    8. positive regulation of transcription, DNA-templated Source: UniProtKB
    9. protein deubiquitination Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Protein family/group databases

    MEROPSiC19.035.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:USP22
    Synonyms:KIAA1063, USP3L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12621. USP22.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. SAGA complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi471 – 4711H → A: Impairs its function as a positive modulator of androgen receptor transactivation; when associated with A-479. 1 Publication
    Mutagenesisi479 – 4791H → A: Impairs its function as a positive modulator of androgen receptor transactivation; when associated with A-471. 1 Publication

    Organism-specific databases

    PharmGKBiPA37247.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 525525Ubiquitin carboxyl-terminal hydrolase 22PRO_0000080650Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei129 – 1291N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UPT9.
    PaxDbiQ9UPT9.
    PRIDEiQ9UPT9.

    PTM databases

    PhosphoSiteiQ9UPT9.

    Expressioni

    Tissue specificityi

    Moderately expressed in various tissues including heart and skeletal muscle, and weakly expressed in lung and liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9UPT9.
    BgeeiQ9UPT9.
    CleanExiHS_USP22.
    GenevestigatoriQ9UPT9.

    Organism-specific databases

    HPAiHPA044980.

    Interactioni

    Subunit structurei

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FUBP1Q96AE43EBI-723510,EBI-711404
    NFATC2Q134692EBI-723510,EBI-716258

    Protein-protein interaction databases

    BioGridi116914. 42 interactions.
    IntActiQ9UPT9. 35 interactions.
    MINTiMINT-1390273.
    STRINGi9606.ENSP00000261497.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UPT9.
    SMRiQ9UPT9. Positions 76-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini176 – 520345USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. UBP8 subfamily.Curated
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri61 – 12161UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5533.
    HOGENOMiHOG000007260.
    HOVERGENiHBG058014.
    InParanoidiQ9UPT9.
    KOiK11366.
    OMAiYCQMCDD.
    OrthoDBiEOG7FR7G7.
    PhylomeDBiQ9UPT9.
    TreeFamiTF323554.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UPT9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVSRPEPEGE AMDAELAVAP PGCSHLGSFK VDNWKQNLRA IYQCFVWSGT    50
    AEARKRKAKS CICHVCGVHL NRLHSCLYCV FFGCFTKKHI HEHAKAKRHN 100
    LAIDLMYGGI YCFLCQDYIY DKDMEIIAKE EQRKAWKMQG VGEKFSTWEP 150
    TKRELELLKH NPKRRKITSN CTIGLRGLIN LGNTCFMNCI VQALTHTPLL 200
    RDFFLSDRHR CEMQSPSSCL VCEMSSLFQE FYSGHRSPHI PYKLLHLVWT 250
    HARHLAGYEQ QDAHEFLIAA LDVLHRHCKG DDNGKKANNP NHCNCIIDQI 300
    FTGGLQSDVT CQVCHGVSTT IDPFWDISLD LPGSSTPFWP LSPGSEGNVV 350
    NGESHVSGTT TLTDCLRRFT RPEHLGSSAK IKCSGCHSYQ ESTKQLTMKK 400
    LPIVACFHLK RFEHSAKLRR KITTYVSFPL ELDMTPFMAS SKESRMNGQY 450
    QQPTDSLNND NKYSLFAVVN HQGTLESGHY TSFIRQHKDQ WFKCDDAIIT 500
    KASIKDVLDS EGYLLFYHKQ FLEYE 525
    Length:525
    Mass (Da):59,961
    Last modified:September 13, 2005 - v2
    Checksum:iD18BFE84BE8E5915
    GO
    Isoform 2 (identifier: Q9UPT9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-57: MVSRPEPEGE...SGTAEARKRK → MAPGWPSLSA...RATALQGPSQ

    Show »
    Length:513
    Mass (Da):58,179
    Checksum:i79C5E8674661256E
    GO

    Sequence cautioni

    The sequence AAH25317.1 differs from that shown. Reason: Frameshift at position 355.
    Isoform 2 : The sequence AAI10500.1 differs from that shown. Reason: Frameshift at position 3.
    The sequence BAA83015.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti85 – 851F → L in AAI26899. (PubMed:15489334)Curated
    Sequence conflicti380 – 3801K → T in CAE45893. (PubMed:17974005)Curated
    Sequence conflicti496 – 4961D → V in AAH25317. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5757MVSRP…ARKRK → MAPGWPSLSAGSRQEAPQLA AGGSAYQAVGRQFQPRATAL QGPSQ in isoform 2. 1 PublicationVSP_036720Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028986 mRNA. Translation: BAA83015.1. Different initiation.
    BC007196 mRNA. Translation: AAH07196.1.
    BC025317 mRNA. Translation: AAH25317.1. Frameshift.
    BC110499 mRNA. Translation: AAI10500.1. Frameshift.
    BC126898 mRNA. Translation: AAI26899.1.
    BX640815 mRNA. Translation: CAE45893.1.
    CCDSiCCDS42285.1. [Q9UPT9-1]
    RefSeqiNP_056091.1. NM_015276.1. [Q9UPT9-1]
    UniGeneiHs.462492.

    Genome annotation databases

    EnsembliENST00000261497; ENSP00000261497; ENSG00000124422. [Q9UPT9-1]
    ENST00000537526; ENSP00000440950; ENSG00000124422. [Q9UPT9-2]
    GeneIDi23326.
    KEGGihsa:23326.
    UCSCiuc002gyl.4. human. [Q9UPT9-1]
    uc002gyn.4. human. [Q9UPT9-2]

    Polymorphism databases

    DMDMi78103328.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028986 mRNA. Translation: BAA83015.1 . Different initiation.
    BC007196 mRNA. Translation: AAH07196.1 .
    BC025317 mRNA. Translation: AAH25317.1 . Frameshift.
    BC110499 mRNA. Translation: AAI10500.1 . Frameshift.
    BC126898 mRNA. Translation: AAI26899.1 .
    BX640815 mRNA. Translation: CAE45893.1 .
    CCDSi CCDS42285.1. [Q9UPT9-1 ]
    RefSeqi NP_056091.1. NM_015276.1. [Q9UPT9-1 ]
    UniGenei Hs.462492.

    3D structure databases

    ProteinModelPortali Q9UPT9.
    SMRi Q9UPT9. Positions 76-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116914. 42 interactions.
    IntActi Q9UPT9. 35 interactions.
    MINTi MINT-1390273.
    STRINGi 9606.ENSP00000261497.

    Protein family/group databases

    MEROPSi C19.035.

    PTM databases

    PhosphoSitei Q9UPT9.

    Polymorphism databases

    DMDMi 78103328.

    Proteomic databases

    MaxQBi Q9UPT9.
    PaxDbi Q9UPT9.
    PRIDEi Q9UPT9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261497 ; ENSP00000261497 ; ENSG00000124422 . [Q9UPT9-1 ]
    ENST00000537526 ; ENSP00000440950 ; ENSG00000124422 . [Q9UPT9-2 ]
    GeneIDi 23326.
    KEGGi hsa:23326.
    UCSCi uc002gyl.4. human. [Q9UPT9-1 ]
    uc002gyn.4. human. [Q9UPT9-2 ]

    Organism-specific databases

    CTDi 23326.
    GeneCardsi GC17M020902.
    HGNCi HGNC:12621. USP22.
    HPAi HPA044980.
    MIMi 612116. gene.
    neXtProti NX_Q9UPT9.
    PharmGKBi PA37247.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5533.
    HOGENOMi HOG000007260.
    HOVERGENi HBG058014.
    InParanoidi Q9UPT9.
    KOi K11366.
    OMAi YCQMCDD.
    OrthoDBi EOG7FR7G7.
    PhylomeDBi Q9UPT9.
    TreeFami TF323554.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi USP22. human.
    GenomeRNAii 23326.
    NextBioi 45232.
    PROi Q9UPT9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UPT9.
    Bgeei Q9UPT9.
    CleanExi HS_USP22.
    Genevestigatori Q9UPT9.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "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] (ISOFORM 2).
      Tissue: Uterus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-525.
      Tissue: Colon endothelium.
    4. "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.
    5. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
      Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
      Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE DEUBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SAGA COMPLEX, MUTAGENESIS OF HIS-471 AND HIS-479.
    6. "The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression."
      Zhang X.-Y., Varthi M., Sykes S.M., Phillips C., Warzecha C., Zhu W., Wyce A., Thorne A.W., Berger S.L., McMahon S.B.
      Mol. Cell 29:102-111(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H2A DEUBIQUITINATION, CATALYTIC ACTIVITY.
    7. "USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A."
      Zhang X.-Y., Pfeiffer H.K., Thorne A.W., McMahon S.B.
      Cell Cycle 7:1522-1524(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H2B DEUBIQUITINATION.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP22_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPT9
    Secondary accession number(s): A0JNS3
    , Q2NLE2, Q6MZY4, Q8TBS8, Q96IW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3