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Q8BW70

- UBP38_MOUSE

UniProt

Q8BW70 - UBP38_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 38

Gene

Usp38

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (10 Oct 2003)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme exhibiting a preference towards 'Lys-63'-linked Ubiquitin chains.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 sitei454 – 4541NucleophilePROSITE-ProRule annotation
    Active sitei857 – 8571Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. ubiquitinyl hydrolase activity 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

    Protein family/group databases

    MEROPSiC19.056.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 38 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 38
    Ubiquitin thioesterase 38
    Ubiquitin-specific-processing protease 38
    Gene namesi
    Name:Usp38
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1922091. Usp38.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10421042Ubiquitin carboxyl-terminal hydrolase 38PRO_0000080669Add
    BLAST

    Proteomic databases

    MaxQBiQ8BW70.
    PaxDbiQ8BW70.
    PRIDEiQ8BW70.

    PTM databases

    PhosphoSiteiQ8BW70.

    Expressioni

    Gene expression databases

    BgeeiQ8BW70.
    CleanExiMM_USP38.
    GenevestigatoriQ8BW70.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BW70.
    SMRiQ8BW70. Positions 443-657, 714-946.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini445 – 949505USPAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5560.
    GeneTreeiENSGT00650000093027.
    HOVERGENiHBG060424.
    InParanoidiQ8BW70.
    KOiK11854.
    OMAiHYYSYAR.
    OrthoDBiEOG7327ND.
    PhylomeDBiQ8BW70.
    TreeFamiTF324529.

    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.

    Q8BW70-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKILEGLVS SSHPLPLKRM IVRKVVEFAE HWLDEAQCEA MFDLTTRLIL     50
    EGQDPFQRQV GHQVLEAYAR YHRPEFESFF NKTFVLGLLQ QGYHSVDRKD 100
    VAILDYIHNG LKLIMSCPSV LDLFSLLQVE VLRMVCERPE PVLCARLSDL 150
    LTDFVQCVPK GKLSVTFCQQ LVRTIGHFQC VSTQEKELRE YVSQVTKVST 200
    LLQNIWKAEP STLLPSLQEV FASISSTDAS FEPSVALASL VQHIPLQMIT 250
    VLIRSLTTDP NVKDASMTQA LCRMIDWLSW PLAQHVDTWV IALLKGLAAV 300
    QKFTILIDVT LLKIELVFNR LWFPLVRPGA LAVLSHMLLS FQHSPEAFHV 350
    IVPHIVNLVH SFRSDGLPSS TAFLVQLTEL VHCMMYHYSG FPDLYEPILE 400
    AVKDFPKPSE EKIKLILNQS AWTSQSNALA SCLSRLSGKS ETGKTGLINL 450
    GNTCYMNSVL QALFMATEFR RQVLSLNLNG CNSLMKKLQH LFAFLAHTQR 500
    EAYAPRIFFE ASRPPWFTPR SQQDCSEYLR FLLDRLHEEE KILRVQSSHK 550
    PSEGLDCAET CLQEVTSKVA VPTESPGTGD SEKTLIEKMF GGKLRTHICC 600
    LNCGSTSHKV EAFTDLSLAF CPSPSVEDLS FQDTASLPSA QDDGLMQTSV 650
    ADPEEEPVVY NPATAAFVCD SVVNQRVLGS PPVEFHCAES SSVPEESAKI 700
    LISKDVPQNP GGESTTSVTD LLNYFLAPEV LTGENQYYCE SCASLQNAEK 750
    TMQITEEPEY LILTLLRFSY DQKYHVRRKI LDNVSLPLVL ELPVKRTASF 800
    SSLSQSWSVD VDFTDINENL PKKLKPSGTE EAFCPKLVPY LLSSVVVHSG 850
    VSSESGHYYS YARNITGTES SYQMCPQSES LALAPSQSCL LGVESPNTVI 900
    EQDLENKEMS QEWFLFNDSR VTFTSFQSVQ KITSRFPKDT AYVLLYKKQS 950
    RANGIDSDNP ASGVWANGDP PLQKELMDAI TKDNKLYLQE QELNARARAL 1000
    QAASASCSFR PNGFDDNDPP GSCGPTGGGG GGGFNTVGRL VF 1042
    Length:1,042
    Mass (Da):116,102
    Last modified:October 10, 2003 - v2
    Checksum:iB039BCA53E16B178
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901Q → H in BAC35661. (PubMed:16141072)Curated
    Sequence conflicti266 – 2661S → G in BAC33659. (PubMed:16141072)Curated
    Sequence conflicti442 – 4421T → A in BAC34890. (PubMed:16141072)Curated
    Sequence conflicti776 – 7761V → A in BAC33659. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK049287 mRNA. Translation: BAC33659.2.
    AK052219 mRNA. Translation: BAC34890.1.
    AK054116 mRNA. Translation: BAC35661.1.
    BC054404 mRNA. Translation: AAH54404.1.
    BC057122 mRNA. Translation: AAH57122.1.
    BC058784 mRNA. Translation: AAH58784.1.
    CCDSiCCDS22444.1.
    RefSeqiNP_081830.2. NM_027554.2.
    UniGeneiMm.246018.

    Genome annotation databases

    EnsembliENSMUST00000042724; ENSMUSP00000039943; ENSMUSG00000038250.
    GeneIDi74841.
    KEGGimmu:74841.
    UCSCiuc009mjd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK049287 mRNA. Translation: BAC33659.2 .
    AK052219 mRNA. Translation: BAC34890.1 .
    AK054116 mRNA. Translation: BAC35661.1 .
    BC054404 mRNA. Translation: AAH54404.1 .
    BC057122 mRNA. Translation: AAH57122.1 .
    BC058784 mRNA. Translation: AAH58784.1 .
    CCDSi CCDS22444.1.
    RefSeqi NP_081830.2. NM_027554.2.
    UniGenei Mm.246018.

    3D structure databases

    ProteinModelPortali Q8BW70.
    SMRi Q8BW70. Positions 443-657, 714-946.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C19.056.

    PTM databases

    PhosphoSitei Q8BW70.

    Proteomic databases

    MaxQBi Q8BW70.
    PaxDbi Q8BW70.
    PRIDEi Q8BW70.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000042724 ; ENSMUSP00000039943 ; ENSMUSG00000038250 .
    GeneIDi 74841.
    KEGGi mmu:74841.
    UCSCi uc009mjd.1. mouse.

    Organism-specific databases

    CTDi 84640.
    MGIi MGI:1922091. Usp38.

    Phylogenomic databases

    eggNOGi COG5560.
    GeneTreei ENSGT00650000093027.
    HOVERGENi HBG060424.
    InParanoidi Q8BW70.
    KOi K11854.
    OMAi HYYSYAR.
    OrthoDBi EOG7327ND.
    PhylomeDBi Q8BW70.
    TreeFami TF324529.

    Miscellaneous databases

    NextBioi 341642.
    PROi Q8BW70.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BW70.
    CleanExi MM_USP38.
    Genevestigatori Q8BW70.

    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. "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: Embryonic heart, Embryonic stem cell and Oviduct.
    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].
      Strain: C57BL/6.
      Tissue: Brain, Olfactory epithelium and Retina.

    Entry informationi

    Entry nameiUBP38_MOUSE
    AccessioniPrimary (citable) accession number: Q8BW70
    Secondary accession number(s): Q8BWL1, Q8BX03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: October 10, 2003
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 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