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Q15040

- JOS1_HUMAN

UniProt

Q15040 - JOS1_HUMAN

Protein

Josephin-1

Gene

JOSD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance membrane dynamics and cell motility independently of its catalytic activity.2 Publications

    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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361NucleophilePROSITE-ProRule annotation
    Active sitei139 – 1391Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. omega peptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC86.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Josephin-1 (EC:3.4.19.12)
    Alternative name(s):
    Josephin domain-containing protein 1
    Gene namesi
    Name:JOSD1
    Synonyms:JSPH1, KIAA0063
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:28953. JOSD1.

    Subcellular locationi

    Cell membrane 1 Publication. Cytoplasm 1 Publication
    Note: Ubiquitination increases localization the plasma membrane. In the cytosol, the unubiquitinated form may be associated with the cytoskeleton via ACTB-binding.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361C → A: Loss of deubiquitination activity, no change in subcellular location. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671644.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 202202Josephin-1PRO_0000053839Add
    BLAST

    Post-translational modificationi

    Monoubiquitinated By similarity. Ubiquitination activates deubiquitination activity in vitro.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ15040.
    PaxDbiQ15040.
    PRIDEiQ15040.

    PTM databases

    PhosphoSiteiQ15040.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15040.
    BgeeiQ15040.
    CleanExiHS_JOSD1.
    GenevestigatoriQ15040.

    Organism-specific databases

    HPAiHPA001168.

    Interactioni

    Subunit structurei

    Interacts with beta-actin/ACTB.1 Publication

    Protein-protein interaction databases

    BioGridi115257. 12 interactions.
    IntActiQ15040. 3 interactions.
    STRINGi9606.ENSP00000216039.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15040.
    SMRiQ15040. Positions 26-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 202180JosephinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Josephin domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG321724.
    HOGENOMiHOG000005731.
    HOVERGENiHBG039523.
    InParanoidiQ15040.
    KOiK15235.
    OMAiSANTQIM.
    PhylomeDBiQ15040.
    TreeFamiTF313660.

    Family and domain databases

    InterProiIPR006155. Josephin.
    [Graphical view]
    PfamiPF02099. Josephin. 1 hit.
    [Graphical view]
    PROSITEiPS50957. JOSEPHIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15040-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSCVPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA    50
    FTRDTLQEIF QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW 100
    WDKRRDVGVI ALTNVMGFIM NLPSSLCWGP LKLPLKRQHW ICVREVGGAY 150
    YNLDSKLKMP EWIGGESELR KFLKHHLRGK NCELLLVVPE EVEAHQSWRT 200
    DV 202
    Length:202
    Mass (Da):23,198
    Last modified:November 1, 1996 - v1
    Checksum:i837268C393C0A5A9
    GO

    Sequence cautioni

    The sequence BAA06682.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481S → R.
    Corresponds to variant rs6001200 [ dbSNP | Ensembl ].
    VAR_050031

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31884 mRNA. Translation: BAA06682.2. Different initiation.
    CR456473 mRNA. Translation: CAG30359.1.
    AK291827 mRNA. Translation: BAF84516.1.
    AL021707 Genomic DNA. Translation: CAB42863.1.
    CH471095 Genomic DNA. Translation: EAW60259.1.
    BC015026 mRNA. Translation: AAH15026.1.
    CCDSiCCDS13976.1.
    RefSeqiNP_055691.1. NM_014876.5.
    XP_005261933.1. XM_005261876.1.
    XP_005261934.1. XM_005261877.1.
    XP_005261935.1. XM_005261878.1.
    XP_005261936.1. XM_005261879.1.
    UniGeneiHs.3094.

    Genome annotation databases

    EnsembliENST00000216039; ENSP00000216039; ENSG00000100221.
    GeneIDi9929.
    KEGGihsa:9929.
    UCSCiuc003awf.3. human.

    Polymorphism databases

    DMDMi3123051.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31884 mRNA. Translation: BAA06682.2 . Different initiation.
    CR456473 mRNA. Translation: CAG30359.1 .
    AK291827 mRNA. Translation: BAF84516.1 .
    AL021707 Genomic DNA. Translation: CAB42863.1 .
    CH471095 Genomic DNA. Translation: EAW60259.1 .
    BC015026 mRNA. Translation: AAH15026.1 .
    CCDSi CCDS13976.1.
    RefSeqi NP_055691.1. NM_014876.5.
    XP_005261933.1. XM_005261876.1.
    XP_005261934.1. XM_005261877.1.
    XP_005261935.1. XM_005261878.1.
    XP_005261936.1. XM_005261879.1.
    UniGenei Hs.3094.

    3D structure databases

    ProteinModelPortali Q15040.
    SMRi Q15040. Positions 26-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115257. 12 interactions.
    IntActi Q15040. 3 interactions.
    STRINGi 9606.ENSP00000216039.

    Protein family/group databases

    MEROPSi C86.004.

    PTM databases

    PhosphoSitei Q15040.

    Polymorphism databases

    DMDMi 3123051.

    Proteomic databases

    MaxQBi Q15040.
    PaxDbi Q15040.
    PRIDEi Q15040.

    Protocols and materials databases

    DNASUi 9929.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216039 ; ENSP00000216039 ; ENSG00000100221 .
    GeneIDi 9929.
    KEGGi hsa:9929.
    UCSCi uc003awf.3. human.

    Organism-specific databases

    CTDi 9929.
    GeneCardsi GC22M039081.
    HGNCi HGNC:28953. JOSD1.
    HPAi HPA001168.
    MIMi 615323. gene.
    neXtProti NX_Q15040.
    PharmGKBi PA142671644.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG321724.
    HOGENOMi HOG000005731.
    HOVERGENi HBG039523.
    InParanoidi Q15040.
    KOi K15235.
    OMAi SANTQIM.
    PhylomeDBi Q15040.
    TreeFami TF313660.

    Miscellaneous databases

    GenomeRNAii 9929.
    NextBioi 37462.
    PROi Q15040.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15040.
    Bgeei Q15040.
    CleanExi HS_JOSD1.
    Genevestigatori Q15040.

    Family and domain databases

    InterProi IPR006155. Josephin.
    [Graphical view ]
    Pfami PF02099. Josephin. 1 hit.
    [Graphical view ]
    PROSITEi PS50957. JOSEPHIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Skin.
    7. "Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes."
      Tzvetkov N., Breuer P.
      Biol. Chem. 388:973-978(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    8. "Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity."
      Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J.
      J. Biol. Chem. 286:4555-4565(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION.
    9. "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis."
      Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.
      J. Biol. Chem. 288:17145-17155(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACTB, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-36.
    10. "Structural modeling of ataxin-3 reveals distant homology to adaptins."
      Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.
      Proteins 50:355-370(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiJOS1_HUMAN
    AccessioniPrimary (citable) accession number: Q15040
    Secondary accession number(s): A8K712
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3