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Q8K387

- UBP45_MOUSE

UniProt

Q8K387 - UBP45_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 45

Gene

Usp45

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    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 sitei200 – 2001NucleophilePROSITE-ProRule annotation
    Active sitei745 – 7451Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri60 – 13677UBP-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. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.064.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 45 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 45
    Ubiquitin thioesterase 45
    Ubiquitin-specific-processing protease 45
    Gene namesi
    Name:Usp45
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:101850. Usp45.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 813813Ubiquitin carboxyl-terminal hydrolase 45PRO_0000280562Add
    BLAST

    Proteomic databases

    PaxDbiQ8K387.
    PRIDEiQ8K387.

    PTM databases

    PhosphoSiteiQ8K387.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8K387.
    BgeeiQ8K387.
    CleanExiMM_USP45.
    GenevestigatoriQ8K387.

    Interactioni

    Protein-protein interaction databases

    BioGridi218782. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K387.
    SMRiQ8K387. Positions 38-389, 602-810.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini191 – 812622USPAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri60 – 13677UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5560.
    GeneTreeiENSGT00750000117419.
    HOGENOMiHOG000154755.
    HOVERGENiHBG062704.
    InParanoidiQ8K387.
    KOiK11844.
    OMAiECEHISA.
    OrthoDBiEOG7J9VNZ.
    PhylomeDBiQ8K387.
    TreeFamiTF326075.

    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: Q8K387-1) [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

    MRVKDPSKDL PEKGKRNKRP LLPHDEDSSD DIAVGLTCQH VSYAVSVNHV    50
    KKAVAESLWS VCSECLKERR FCDGQPVLPA DVWLCLKCGL QGCGKNSESQ 100
    HSLRHFKSSG TESHCVVISL STWVIWCYEC NEKLSTHCNK KVLAQIVDFL 150
    QKHAFKTQTG AFSRIIKLCE EKREAGEIKK GKKGCTVPSV KGITNLGNTC 200
    FFNAVIQNLA QTYILFELMN EIKEDGTKFK ISLSSAPQLE PLVVELSSPG 250
    PLTSALFLFL HSMKEAEKGP LSPKVLFNQL CQKAPRFKGF QQQDSQELLH 300
    HLLDAVRTEE TKRIQASILK AFNNPTTKTA DDETRKKVKA YGKEGVKMNF 350
    IDRIFIGELT STVMCEECAN ISTMKDPFID ISLPIIEERV SKPVLLGKMS 400
    KCRSLQETDQ DHNKGTVTVG NAHQPRASRK HSSPNDKNQL SHDRKHLRKW 450
    PSEEEKTVVT HPKNDNLEAS PPASTLSTEA SLNESLTDGS ERDASLESSV 500
    DADSEASEPE IASKQPVLLR SRGDSCGHAE QHPHLPLASE LPQAKETHGG 550
    EEEMAEAIAE LHLSGTVTGN RDFHREKQPL NVPNNLCFSE GKHTRLHSAQ 600
    NAFQTLSQSY VTTSKECSVQ SCLYQFTSME LLMGNNKLLC EDCTEKRRKC 650
    HKETSSAEKK AGGVYTNARK QLLISAVPAI LILHLKRFHQ AGLSLRKVNR 700
    HVDFPLTLDL APFCAATCKN ISVGEKVLYG LYGIVEHSGS MRGGHYTAYV 750
    KVRVPSRKLS ECITGRKTAA GLKEPDGELG GHWVHVSDTY VQVVPESRAL 800
    SAQAYLLFYE RIL 813

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Length:813
    Mass (Da):90,361
    Last modified:October 1, 2002 - v1
    Checksum:iED1DD9B9F007B178
    GO
    Isoform 2 (identifier: Q8K387-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         390-437: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:765
    Mass (Da):85,110
    Checksum:i08254CA4B7DEE012
    GO

    Sequence cautioni

    The sequence BAC29631.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti595 – 5951R → G in BAC40129. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei390 – 43748Missing in isoform 2. 1 PublicationVSP_023794Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK036903 mRNA. Translation: BAC29631.1. Different initiation.
    AK088073 mRNA. Translation: BAC40129.1.
    AL772187 Genomic DNA. Translation: CAM22881.1.
    BC027768 mRNA. Translation: AAH27768.1.
    CCDSiCCDS38700.1. [Q8K387-1]
    CCDS71351.1. [Q8K387-2]
    RefSeqiNP_001277354.1. NM_001290425.1. [Q8K387-2]
    NP_690038.1. NM_152825.2. [Q8K387-1]
    XP_006538424.1. XM_006538361.1. [Q8K387-1]
    UniGeneiMm.154306.

    Genome annotation databases

    EnsembliENSMUST00000040429; ENSMUSP00000048324; ENSMUSG00000040455. [Q8K387-2]
    ENSMUST00000065111; ENSMUSP00000067109; ENSMUSG00000040455. [Q8K387-1]
    ENSMUST00000108232; ENSMUSP00000103867; ENSMUSG00000040455. [Q8K387-1]
    GeneIDi77593.
    KEGGimmu:77593.
    UCSCiuc008sda.1. mouse. [Q8K387-1]
    uc008sdc.1. mouse. [Q8K387-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK036903 mRNA. Translation: BAC29631.1 . Different initiation.
    AK088073 mRNA. Translation: BAC40129.1 .
    AL772187 Genomic DNA. Translation: CAM22881.1 .
    BC027768 mRNA. Translation: AAH27768.1 .
    CCDSi CCDS38700.1. [Q8K387-1 ]
    CCDS71351.1. [Q8K387-2 ]
    RefSeqi NP_001277354.1. NM_001290425.1. [Q8K387-2 ]
    NP_690038.1. NM_152825.2. [Q8K387-1 ]
    XP_006538424.1. XM_006538361.1. [Q8K387-1 ]
    UniGenei Mm.154306.

    3D structure databases

    ProteinModelPortali Q8K387.
    SMRi Q8K387. Positions 38-389, 602-810.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 218782. 3 interactions.

    Protein family/group databases

    MEROPSi C19.064.

    PTM databases

    PhosphoSitei Q8K387.

    Proteomic databases

    PaxDbi Q8K387.
    PRIDEi Q8K387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040429 ; ENSMUSP00000048324 ; ENSMUSG00000040455 . [Q8K387-2 ]
    ENSMUST00000065111 ; ENSMUSP00000067109 ; ENSMUSG00000040455 . [Q8K387-1 ]
    ENSMUST00000108232 ; ENSMUSP00000103867 ; ENSMUSG00000040455 . [Q8K387-1 ]
    GeneIDi 77593.
    KEGGi mmu:77593.
    UCSCi uc008sda.1. mouse. [Q8K387-1 ]
    uc008sdc.1. mouse. [Q8K387-2 ]

    Organism-specific databases

    CTDi 85015.
    MGIi MGI:101850. Usp45.

    Phylogenomic databases

    eggNOGi COG5560.
    GeneTreei ENSGT00750000117419.
    HOGENOMi HOG000154755.
    HOVERGENi HBG062704.
    InParanoidi Q8K387.
    KOi K11844.
    OMAi ECEHISA.
    OrthoDBi EOG7J9VNZ.
    PhylomeDBi Q8K387.
    TreeFami TF326075.

    Miscellaneous databases

    NextBioi 347172.
    PROi Q8K387.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8K387.
    Bgeei Q8K387.
    CleanExi MM_USP45.
    Genevestigatori Q8K387.

    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. "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] (ISOFORM 2).
      Strain: C57BL/6J and NOD.
      Tissue: Thymus and Vagina.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiUBP45_MOUSE
    AccessioniPrimary (citable) accession number: Q8K387
    Secondary accession number(s): A2AJT1, Q8BU19, Q8BZ19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 98 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