Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9QZL6

- UBP21_MOUSE

UniProt

Q9QZL6 - UBP21_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 21

Gene

Usp21

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates.1 Publication

    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 sitei221 – 2211Nucleophile
    Metal bindingi385 – 3851ZincBy similarity
    Metal bindingi388 – 3881ZincBy similarity
    Metal bindingi438 – 4381ZincBy similarity
    Metal bindingi441 – 4411ZincBy similarity
    Active sitei519 – 5191Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. NEDD8-specific protease activity Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. histone deubiquitination Source: UniProtKB
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. transcription, DNA-templated Source: UniProtKB-KW
    4. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.034.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 21 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 21
    Ubiquitin thioesterase 21
    Ubiquitin-specific-processing protease 21
    Gene namesi
    Name:Usp21
    Synonyms:Usp23
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1353665. Usp21.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi221 – 2211C → A: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. 1 Publication
    Mutagenesisi519 – 5191H → A: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. 1 Publication
    Mutagenesisi535 – 5351D → N: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 566566Ubiquitin carboxyl-terminal hydrolase 21PRO_0000080649Add
    BLAST

    Proteomic databases

    PaxDbiQ9QZL6.
    PRIDEiQ9QZL6.

    PTM databases

    PhosphoSiteiQ9QZL6.

    Expressioni

    Gene expression databases

    BgeeiQ9QZL6.
    CleanExiMM_USP21.
    GenevestigatoriQ9QZL6.

    Interactioni

    Protein-protein interaction databases

    BioGridi206018. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QZL6.
    SMRiQ9QZL6. Positions 202-560.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini212 – 559348USPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi134 – 15219Nuclear export signalBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP21 subfamily.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5533.
    GeneTreeiENSGT00750000117710.
    HOGENOMiHOG000231498.
    HOVERGENiHBG011164.
    KOiK11833.
    OrthoDBiEOG7FR7GN.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QZL6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQASEHRLG RTREPPVNVQ PRVGAKIPFP PRARSKERRN PVPGPNSMLR    50
    PLPPRPGPPD ERLKKLELGR GRTSGSRPRG PLRADHGVPL PGSPPPAVAL 100
    PLPSRTNLAR SKSVSSGDLR PMGIALGGHR GAGELGAALS RLALRPEPPT 150
    LRRSTSLRRL GGFPGPPTLL SIRTEPPTSH GSFHMISARP SEPFYSDDKM 200
    AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC LRRDFRQEVP 250
    GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ 300
    DAQEFLKLLM ERLHLEINRR GRRAPPILAS GPVPSPPRRG GGALHEEPEL 350
    SDDDRANLMW KRYLEREDSK IVDLFVGQLK SCLKCQACGY RSTTFEVFCD 400
    LSLPIPKKGF AGGKVSLRDC FSLFTKEEEL ESENAPVCDR CRQKTRSTKK 450
    LTVQRFPRIL VLHLNRFSTS RGSIKKSSVG VDFPLQRLSL GDFASDKAGS 500
    PVYQLYALCN HSGSVHYGHY TALCRCQTGW HVYNDSRVSP VSENQVASSE 550
    GYVLFYQLMQ EPLRCL 566
    Length:566
    Mass (Da):62,673
    Last modified:May 1, 2000 - v1
    Checksum:iF2E1828E9BDB1AFD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti220 – 2201T → TLPQ in BAB27431. (PubMed:16141072)Curated
    Sequence conflicti338 – 3381R → C in BAB27431. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177759 mRNA. Translation: AAD54322.1.
    AK011148 mRNA. Translation: BAB27431.1.
    BC021903 mRNA. Translation: AAH21903.1.
    CCDSiCCDS35774.1.
    RefSeqiNP_038947.2. NM_013919.4.
    UniGeneiMm.27510.

    Genome annotation databases

    EnsembliENSMUST00000111306; ENSMUSP00000106938; ENSMUSG00000053483.
    GeneIDi30941.
    KEGGimmu:30941.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177759 mRNA. Translation: AAD54322.1 .
    AK011148 mRNA. Translation: BAB27431.1 .
    BC021903 mRNA. Translation: AAH21903.1 .
    CCDSi CCDS35774.1.
    RefSeqi NP_038947.2. NM_013919.4.
    UniGenei Mm.27510.

    3D structure databases

    ProteinModelPortali Q9QZL6.
    SMRi Q9QZL6. Positions 202-560.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206018. 3 interactions.

    Protein family/group databases

    MEROPSi C19.034.

    PTM databases

    PhosphoSitei Q9QZL6.

    Proteomic databases

    PaxDbi Q9QZL6.
    PRIDEi Q9QZL6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000111306 ; ENSMUSP00000106938 ; ENSMUSG00000053483 .
    GeneIDi 30941.
    KEGGi mmu:30941.

    Organism-specific databases

    CTDi 27005.
    MGIi MGI:1353665. Usp21.

    Phylogenomic databases

    eggNOGi COG5533.
    GeneTreei ENSGT00750000117710.
    HOGENOMi HOG000231498.
    HOVERGENi HBG011164.
    KOi K11833.
    OrthoDBi EOG7FR7GN.

    Miscellaneous databases

    NextBioi 307382.
    PROi Q9QZL6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QZL6.
    CleanExi MM_USP21.
    Genevestigatori Q9QZL6.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing, tissue distribution and chromosomal assignment of a novel ubiquitin-specific protease USP23."
      Smith T.S., Southan C.
      Biochim. Biophys. Acta 1490:184-188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
      Tissue: Embryo.
    3. "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: Mammary gland.
    4. "Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation."
      Nakagawa T., Kajitani T., Togo S., Masuko N., Ohdan H., Hishikawa Y., Koji T., Matsuyama T., Ikura T., Muramatsu M., Ito T.
      Genes Dev. 22:37-49(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-221; HIS-519 AND ASP-535.

    Entry informationi

    Entry nameiUBP21_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZL6
    Secondary accession number(s): Q9D0R1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3