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Q15040

- JOS1_HUMAN

UniProt

Q15040 - JOS1_HUMAN

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Protein

Josephin-1

Gene
JOSD1, JSPH1, KIAA0063
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 – 361Nucleophile By similarity
Active sitei139 – 1391Proton acceptor By similarity

GO - Molecular functioni

  1. omega peptidase activity Source: InterPro
Complete GO annotation...

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 202180JosephinAdd
BLAST

Sequence similaritiesi

Contains 1 Josephin domain.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 111 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

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