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Protein

Josephin-1

Gene

JOSD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 – 361NucleophilePROSITE-ProRule annotation
Active sitei139 – 1391Proton acceptorPROSITE-ProRule annotation

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 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:28953. JOSD1.

Subcellular locationi

  1. Cell membrane 1 Publication
  2. Cytoplasm 1 Publication

  3. 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
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.

Polymorphism and mutation databases

BioMutaiJOSD1.
DMDMi3123051.

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

BgeeiQ15040.
CleanExiHS_JOSD1.
ExpressionAtlasiQ15040. baseline and differential.
GenevestigatoriQ15040.

Organism-specific databases

HPAiHPA001168.

Interactioni

Subunit structurei

Interacts with beta-actin/ACTB.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT31Q153233EBI-2510602,EBI-948001
KRT40Q6A1623EBI-2510602,EBI-10171697
KRTAP10-4P603723EBI-2510602,EBI-10178153
KRTAP10-8P604103EBI-2510602,EBI-10171774
KRTAP5-9P263713EBI-2510602,EBI-3958099
KRTAP9-2Q9BYQ43EBI-2510602,EBI-1044640
MID2Q9UJV3-23EBI-2510602,EBI-10172526
NOTCH2NLQ7Z3S93EBI-2510602,EBI-945833
TRAF1Q130773EBI-2510602,EBI-359224
TRIM23P364063EBI-2510602,EBI-740098
TRIM27P143734EBI-2510602,EBI-719493

Protein-protein interaction databases

BioGridi115257. 25 interactions.
IntActiQ15040. 13 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.
GeneTreeiENSGT00390000009228.
HOGENOMiHOG000005731.
HOVERGENiHBG039523.
InParanoidiQ15040.
KOiK15235.
OMAiREVGGTY.
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

        10         20         30         40         50
MSCVPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA
60 70 80 90 100
FTRDTLQEIF QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW
110 120 130 140 150
WDKRRDVGVI ALTNVMGFIM NLPSSLCWGP LKLPLKRQHW ICVREVGGAY
160 170 180 190 200
YNLDSKLKMP EWIGGESELR KFLKHHLRGK NCELLLVVPE EVEAHQSWRT

DV
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.Curated

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:
EMBLi
GenBanki
DDBJi
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_005261876.2.
XP_005261934.1. XM_005261877.2.
XP_005261935.1. XM_005261878.2.
XP_005261936.1. XM_005261879.2.
UniGeneiHs.3094.

Genome annotation databases

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

Polymorphism and mutation databases

BioMutaiJOSD1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005261876.2.
XP_005261934.1. XM_005261877.2.
XP_005261935.1. XM_005261878.2.
XP_005261936.1. XM_005261879.2.
UniGeneiHs.3094.

3D structure databases

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

Protein-protein interaction databases

BioGridi115257. 25 interactions.
IntActiQ15040. 13 interactions.
STRINGi9606.ENSP00000216039.

Protein family/group databases

MEROPSiC86.004.

PTM databases

PhosphoSiteiQ15040.

Polymorphism and mutation databases

BioMutaiJOSD1.
DMDMi3123051.

Proteomic databases

MaxQBiQ15040.
PaxDbiQ15040.
PRIDEiQ15040.

Protocols and materials databases

DNASUi9929.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9929.
GeneCardsiGC22M039081.
HGNCiHGNC:28953. JOSD1.
HPAiHPA001168.
MIMi615323. gene.
neXtProtiNX_Q15040.
PharmGKBiPA142671644.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321724.
GeneTreeiENSGT00390000009228.
HOGENOMiHOG000005731.
HOVERGENiHBG039523.
InParanoidiQ15040.
KOiK15235.
OMAiREVGGTY.
PhylomeDBiQ15040.
TreeFamiTF313660.

Miscellaneous databases

ChiTaRSiJOSD1. human.
GenomeRNAii9929.
NextBioi37462.
PROiQ15040.
SOURCEiSearch...

Gene expression databases

BgeeiQ15040.
CleanExiHS_JOSD1.
ExpressionAtlasiQ15040. baseline and differential.
GenevestigatoriQ15040.

Family and domain databases

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

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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: April 29, 2015
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.