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Q8C2S0

- UBP44_MOUSE

UniProt

Q8C2S0 - UBP44_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 44

Gene

Usp44

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 3 (28 Nov 2012)
      Previous versions | rss
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    Functioni

    Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination.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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei281 – 2811NucleophilePROSITE-ProRule annotation
    Active sitei635 – 6351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri24 – 8562UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. ubiquitinyl hydrolase activity Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 44 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 44
    Ubiquitin thioesterase 44
    Ubiquitin-specific-processing protease 44
    Gene namesi
    Name:Usp44
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:3045318. Usp44.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Peaks in interphase, with relatively low levels maintained throughout mitosis.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 711711Ubiquitin carboxyl-terminal hydrolase 44PRO_0000395811Add
    BLAST

    Post-translational modificationi

    Dephosphorylated by CTDP1.By similarity
    Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome.

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PRIDEiQ8C2S0.

    PTM databases

    PhosphoSiteiQ8C2S0.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in lung, pancreas, skin, liver, stomach and intestine.1 Publication

    Gene expression databases

    BgeeiQ8C2S0.
    GenevestigatoriQ8C2S0.

    Interactioni

    Protein-protein interaction databases

    BioGridi236490. 1 interaction.
    STRINGi10090.ENSMUSP00000092975.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C2S0.
    SMRiQ8C2S0. Positions 26-83, 371-677.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini272 – 677406USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP44 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 fingeri24 – 8562UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiKOG1867.
    HOGENOMiHOG000015084.
    HOVERGENiHBG018027.
    InParanoidiQ8C2S0.
    KOiK11834.
    OrthoDBiEOG7JX33S.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q8C2S0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRCKHVEQL QLAQGHSILD PQKWYCMVCN TTESIWACLS CSHVACGKYI    50
    QEHALKHFQE SSHPVAFEVN DMYAFCYLCN DYVLNDNAAG DLKSLRSTLS 100
    TIKSKKYPCV VPSDSVLHPV DAQDRVYSLL DGTQSLPGNE DPTCAALWHR 150
    RRVLMGKAFR TWFEQSAIGR KGQEPTQERM VAKREAKRRQ QQELEQQMKA 200
    ELESTPPRKS LRLQGSSEEA ATIEIVPVRA PPPPPASPAK DKAALPTSED 250
    RTFKKVSDSL IKRRPMVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF 300
    LKLDLNQWLA VAASDKARSY KHSAVTEAAA QQMNEGQEKE KGFVCSRHSG 350
    LSSGLSGGAS KGRNMELIQP REPSSPYSSL CHELHILFQV MWSGEWALVS 400
    PFAMLHSVWR LIPAFRGYAQ QDAQEFLCEL LDKIQRELET TGTKLPALIP 450
    TSQRRLIEQV LNVVNNIFHG QFLSQVTCLA CDNKSDTIES FWDLSLEFPE 500
    RYQCSGKDAA SQPCLVTDML DKFTETEALE GKIYMCDHCN SKRRKFSSKS 550
    VVFTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VVFEETLNME 600
    PYCCRETLNA LRPECFLYNL SAVVIHHGKG FGSGHYTAYC YNSEGGFWVH 650
    CNDSKLSMCT MEEVRKAQAY ILFYTQRVTE NGHSKLLPPE LLSNSQHPSK 700
    ETDASSNEVL S 711
    Length:711
    Mass (Da):80,479
    Last modified:November 28, 2012 - v3
    Checksum:iF176DB2BA3C658BE
    GO

    Sequence cautioni

    The sequence AAI11887.1 differs from that shown. Reason: Intron retention.
    The sequence BAC40148.1 differs from that shown. Reason: Intron retention.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK088109 mRNA. Translation: BAC40148.1. Sequence problems.
    CJ236846 mRNA. No translation available.
    AC124686 Genomic DNA. No translation available.
    BC111886 mRNA. Translation: AAI11887.1. Sequence problems.
    RefSeqiNP_001193780.1. NM_001206851.1.
    UniGeneiMm.491598.

    Genome annotation databases

    GeneIDi327799.
    KEGGimmu:327799.
    UCSCiuc011xlw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK088109 mRNA. Translation: BAC40148.1 . Sequence problems.
    CJ236846 mRNA. No translation available.
    AC124686 Genomic DNA. No translation available.
    BC111886 mRNA. Translation: AAI11887.1 . Sequence problems.
    RefSeqi NP_001193780.1. NM_001206851.1.
    UniGenei Mm.491598.

    3D structure databases

    ProteinModelPortali Q8C2S0.
    SMRi Q8C2S0. Positions 26-83, 371-677.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 236490. 1 interaction.
    STRINGi 10090.ENSMUSP00000092975.

    PTM databases

    PhosphoSitei Q8C2S0.

    Proteomic databases

    PRIDEi Q8C2S0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 327799.
    KEGGi mmu:327799.
    UCSCi uc011xlw.1. mouse.

    Organism-specific databases

    CTDi 84101.
    MGIi MGI:3045318. Usp44.

    Phylogenomic databases

    eggNOGi KOG1867.
    HOGENOMi HOG000015084.
    HOVERGENi HBG018027.
    InParanoidi Q8C2S0.
    KOi K11834.
    OrthoDBi EOG7JX33S.

    Miscellaneous databases

    NextBioi 397964.
    PROi Q8C2S0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C2S0.
    Genevestigatori Q8C2S0.

    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. "Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia."
      Zhang Y., van Deursen J., Galardy P.J.
      PLoS ONE 6:E23389-E23389(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, PROTEASOMAL DEGRADATION.
      Tissue: Kidney.
    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: NOD.
      Tissue: Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
    5. "K48- and K63-linked polyubiquitination of deubiquitinating enzyme USP44."
      Suresh B., Ramakrishna S., Lee H.J., Choi J.H., Kim J.Y., Ahn W.S., Baek K.H.
      Cell Biol. Int. 34:799-808(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiUBP44_MOUSE
    AccessioniPrimary (citable) accession number: Q8C2S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 95 of the entry and version 3 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