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E2RK09

- UBP37_CANFA

UniProt

E2RK09 - UBP37_CANFA

Protein

Ubiquitin carboxyl-terminal hydrolase 37

Gene

USP37

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (30 Nov 2010)
      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-630 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 sitei352 – 3521NucleophilePROSITE-ProRule annotation
    Active sitei908 – 9081Proton 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

    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:USP37
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Chromosome 37

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 981981Ubiquitin carboxyl-terminal hydrolase 37PRO_0000412645Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei630 – 6301Phosphoserine; by CDK2By similarity
    Modified residuei652 – 6521PhosphoserineBy similarity
    Modified residuei654 – 6541PhosphoserineBy 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-630 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-630 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Interactioni

    Subunit structurei

    Interacts with FZR1/CDH1.By similarity

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini343 – 953611USPAdd
    BLAST
    Repeati706 – 72520UIM 1Add
    BLAST
    Repeati808 – 82720UIM 2Add
    BLAST
    Repeati830 – 84920UIM 3Add
    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
    Motifi223 – 2253KEN box 2By similarity
    Motifi784 – 7863KEN 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.Curated
    Contains 3 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    GeneTreeiENSGT00440000033542.
    KOiK11850.
    OMAiLQEFNNS.
    OrthoDBiEOG7HMS09.

    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. 4 hits.
    [Graphical view]
    PROSITEiPS50330. UIM. 3 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E2RK09-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI    50
    FQLSHNIKNV VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD 100
    AVHQNRLHAA MKPSQGSGSF GAILGSRTSQ KETNRQLSYS DNQASSKRGS 150
    LETKDDIPFR KVLGNPGRGS IKTATGSGIT VTRTIPSLTS ASTPLRSGLL 200
    ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK YLTSSREKQL 250
    SLKQSEENRT SGLLPLQSSS FYGSRTGSKD YSSGSTNLDR TNVSGQTPSA 300
    KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN 350
    TCYMNAILQS LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC 400
    NSETKKDLLK KVKNAISATA ERFSGYMQND AHEFLSQCLD QLKEDMEKLN 450
    KTWKTEPVPG EENSPDISAT RVYTCPVITN LEFEVQHSII CKACGEIIPK 500
    REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC EKCGGKCALV 550
    RHKFNRLPRI LILHLKRYSF NVTLSLNNKI GQQVIIPRYL TLSSHCTENT 600
    KPPFTLGWSA HMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKSSLALCL 650
    DSDSEDELKR SVALSQRLCE MSGCEQQQDD LEKDSKPCRI EPDKSELENS 700
    GFDGMSEEEL LAAVLEMSKR EASPTLSHED DDKPTSSPDT GFAEDDIQEM 750
    PENQDPVETE KPKTVTEPDP ASFTEITKDC DENKENKTPE GSQGEVDWLQ 800
    QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE LSLQEFNNSF 850
    LDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI 900
    GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY 950
    MHKEIFDELL ETEKNSQALS MEVGKTTRQA L 981
    Length:981
    Mass (Da):110,453
    Last modified:November 30, 2010 - v1
    Checksum:iEBF79BF01F784AE5
    GO

    Sequence databases

    RefSeqiXP_005640701.1. XM_005640644.1.
    XP_005640702.1. XM_005640645.1.
    XP_545643.2. XM_545643.4.

    Genome annotation databases

    EnsembliENSCAFT00000023494; ENSCAFP00000021817; ENSCAFG00000014781.
    GeneIDi488523.
    KEGGicfa:488523.

    Cross-referencesi

    Sequence databases

    RefSeqi XP_005640701.1. XM_005640644.1.
    XP_005640702.1. XM_005640645.1.
    XP_545643.2. XM_545643.4.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCAFT00000023494 ; ENSCAFP00000021817 ; ENSCAFG00000014781 .
    GeneIDi 488523.
    KEGGi cfa:488523.

    Organism-specific databases

    CTDi 57695.

    Phylogenomic databases

    GeneTreei ENSGT00440000033542.
    KOi K11850.
    OMAi LQEFNNS.
    OrthoDBi EOG7HMS09.

    Miscellaneous databases

    NextBioi 20861854.

    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. 4 hits.
    [Graphical view ]
    PROSITEi PS50330. UIM. 3 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
      Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
      , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
      Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Boxer.

    Entry informationi

    Entry nameiUBP37_CANFA
    AccessioniPrimary (citable) accession number: E2RK09
    Secondary accession number(s): F1PGV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 27 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3