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Q8C0R0

- UBP37_MOUSE

UniProt

Q8C0R0 - UBP37_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 37

Gene

Usp37

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2) By similarity.By similarity

    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 sitei350 – 3501NucleophilePROSITE-ProRule annotation
    Active sitei906 – 9061Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. protein K11-linked deubiquitination Source: UniProtKB
    4. protein K48-linked deubiquitination Source: UniProtKB
    5. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.053.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 37 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 37
    Ubiquitin thioesterase 37
    Ubiquitin-specific-processing protease 37
    Gene namesi
    Name:Usp37Imported
    Synonyms:Kiaa1594Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2442483. Usp37.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 979979Ubiquitin carboxyl-terminal hydrolase 37PRO_0000259610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei628 – 6281Phosphoserine; by CDK2By similarity
    Modified residuei650 – 6501PhosphoserineBy similarity
    Modified residuei652 – 6521PhosphoserineBy similarity

    Post-translational modificationi

    Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1) complex during late mitosis, leading to its degradation. Able to mediate auto-deubiquitination By similarity.By similarity
    Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ8C0R0.
    PRIDEiQ8C0R0.

    PTM databases

    PhosphoSiteiQ8C0R0.

    Expressioni

    Gene expression databases

    BgeeiQ8C0R0.
    CleanExiMM_USP37.
    GenevestigatoriQ8C0R0.

    Interactioni

    Subunit structurei

    Interacts with FZR1/CDH1.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C0R0.
    SMRiQ8C0R0. Positions 4-106, 331-601.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini341 – 951611USPAdd
    BLAST
    Repeati704 – 72320UIM 1Sequence AnalysisAdd
    BLAST
    Repeati806 – 82520UIM 2Sequence AnalysisAdd
    BLAST
    Repeati828 – 84720UIM 3Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 343KEN box 1By similarity
    Motifi71 – 799D-box 1By similarity
    Motifi96 – 10510D-box 2By similarity
    Motifi160 – 1689D-box 3By similarity
    Motifi222 – 2243KEN box 2By similarity
    Motifi782 – 7843KEN box 3By similarity

    Domaini

    The KEN box 3 is required for interaction with FZR1/CDH1 and is essential for APC(CDH1)-mediated ubiquitination.By similarity

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Sequence Analysis
    Contains 3 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG279142.
    GeneTreeiENSGT00440000033542.
    HOGENOMiHOG000060197.
    HOVERGENiHBG055893.
    InParanoidiB2RT12.
    KOiK11850.
    OrthoDBiEOG7HMS09.
    PhylomeDBiQ8C0R0.
    TreeFamiTF323032.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR003903. Ubiquitin-int_motif.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    PF02809. UIM. 3 hits.
    [Graphical view]
    SMARTiSM00726. UIM. 3 hits.
    [Graphical view]
    PROSITEiPS50330. UIM. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q8C0R0-1) [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

    MSPLKIYGPI RIRSMQTGIT KWKEGSFEIV EKDNRVSLLV HYNTGGIPRV    50
    FQLSHNIKNV VLRPSGIKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD 100
    AVHQNRLHAA MKASQGSGSF GTILGSRTSQ KETNRQLSYS DNQASSKRGS 150
    LETKDEIPFR KVLGSPGRGP IKTVTGGGMA VTRTIPSLTL TSTPLRSGLL 200
    ENRTEKRKRM LSGSELTEDY PKENDSSSNN KAMTDPSRKY LTSCREKQLS 250
    LKQAEENRTS GLLPLQSSSF YGSRAGSKDY SSGVTNLDRC NVSSQTPSAK 300
    RSLGFLPQPT PLSVKKLRCN QDYAGWNRPR VPLSSHQQQL QGFSNLGNTC 350
    YMNAILQSLF SLQSFANDLL KQSIPWKKIP FNALIRRFAN LLIKKDICNS 400
    ETKKELLKKV KNAISATAER FSGYVQNDAH EFLSQCLDQL KEDMEKLNKT 450
    WKTEPVLGEE NLPDTSATKV FTCPVITNLE FEVQHSIICK ACGETIPKRE 500
    QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK CGGKCALVRH 550
    KFNRLPRVLI LHLKRYSFNV ALSLNNKLGQ QVIIPRFLTL ASHCTESTKP 600
    PVTLGWSAPV AISRPLRACQ MMNSCITSPS APSKKFTFKS KSSVTSCLDS 650
    DSEDELKRSV VLSQRLCDLP GNEQYQEDVE KDLKLCRLEP GKAELENSGF 700
    DRMSEEEVLA AVLEISRREA SPVLSPEDDD KPTSSPDTGF AEDDIPEMPE 750
    NPDAMEIEKS KTITEPGPAS FTEITKDCDE NKENKTPEGS QGEVDWLQQY 800
    DVDREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS LQEFNNSFLD 850
    SLGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGALPHSYR LISVVSHIGS 900
    TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH 950
    KEIFDELLET EKTSQALSME VGRAARQAS 979
    Length:979
    Mass (Da):110,063
    Last modified:March 1, 2003 - v1
    Checksum:iFF11DB673C1CA902
    GO
    Isoform 22 Publications (identifier: Q8C0R0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         612-634: ISRPLRACQMMNSCITSPSAPSK → M

    Show »
    Length:957
    Mass (Da):107,733
    Checksum:i1ACD5A844FBCB4D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti622 – 6221M → V in AAI39092. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei612 – 63423ISRPL…SAPSK → M in isoform 2. 2 PublicationsVSP_052196Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030013 mRNA. Translation: BAC26734.1.
    AK035640 mRNA. Translation: BAC29135.1.
    AK173210 mRNA. Translation: BAD32488.1.
    BC139091 mRNA. Translation: AAI39092.1.
    CCDSiCCDS15050.1. [Q8C0R0-1]
    RefSeqiNP_795946.2. NM_176972.4.
    XP_006496117.1. XM_006496054.1.
    XP_006496118.1. XM_006496055.1.
    XP_006496119.1. XM_006496056.1.
    XP_006496121.1. XM_006496058.1. [Q8C0R0-2]
    UniGeneiMm.471601.
    Mm.66568.

    Genome annotation databases

    EnsembliENSMUST00000044260; ENSMUSP00000035445; ENSMUSG00000033364.
    GeneIDi319651.
    KEGGimmu:319651.
    UCSCiuc007bmc.2. mouse. [Q8C0R0-2]
    uc007bmd.2. mouse. [Q8C0R0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030013 mRNA. Translation: BAC26734.1 .
    AK035640 mRNA. Translation: BAC29135.1 .
    AK173210 mRNA. Translation: BAD32488.1 .
    BC139091 mRNA. Translation: AAI39092.1 .
    CCDSi CCDS15050.1. [Q8C0R0-1 ]
    RefSeqi NP_795946.2. NM_176972.4.
    XP_006496117.1. XM_006496054.1.
    XP_006496118.1. XM_006496055.1.
    XP_006496119.1. XM_006496056.1.
    XP_006496121.1. XM_006496058.1. [Q8C0R0-2 ]
    UniGenei Mm.471601.
    Mm.66568.

    3D structure databases

    ProteinModelPortali Q8C0R0.
    SMRi Q8C0R0. Positions 4-106, 331-601.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C19.053.

    PTM databases

    PhosphoSitei Q8C0R0.

    Proteomic databases

    PaxDbi Q8C0R0.
    PRIDEi Q8C0R0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044260 ; ENSMUSP00000035445 ; ENSMUSG00000033364 .
    GeneIDi 319651.
    KEGGi mmu:319651.
    UCSCi uc007bmc.2. mouse. [Q8C0R0-2 ]
    uc007bmd.2. mouse. [Q8C0R0-1 ]

    Organism-specific databases

    CTDi 57695.
    MGIi MGI:2442483. Usp37.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG279142.
    GeneTreei ENSGT00440000033542.
    HOGENOMi HOG000060197.
    HOVERGENi HBG055893.
    InParanoidi B2RT12.
    KOi K11850.
    OrthoDBi EOG7HMS09.
    PhylomeDBi Q8C0R0.
    TreeFami TF323032.

    Miscellaneous databases

    ChiTaRSi USP37. mouse.
    NextBioi 395152.
    PROi Q8C0R0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C0R0.
    CleanExi MM_USP37.
    Genevestigatori Q8C0R0.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR003903. Ubiquitin-int_motif.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    PF02809. UIM. 3 hits.
    [Graphical view ]
    SMARTi SM00726. UIM. 3 hits.
    [Graphical view ]
    PROSITEi PS50330. UIM. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-779 (ISOFORM 2).
      Strain: C57BL/6JImported.
      Tissue: TestisImported and Urinary bladderImported.
    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].
      Tissue: Testis.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-979 (ISOFORM 2).
      Tissue: Pancreatic isletImported.

    Entry informationi

    Entry nameiUBP37_MOUSE
    AccessioniPrimary (citable) accession number: Q8C0R0
    Secondary accession number(s): B2RT12, Q69ZF6, Q8BZE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 91 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