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Q9DBJ6 (JOS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Josephin-1

EC=3.4.19.12
Alternative name(s):
Josephin domain-containing protein 1
Gene names
Name:Josd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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).

Subunit structure

Interacts with beta-actin/ACTB By similarity.

Subcellular location

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

Tissue specificity

Widely expressed (at protein level). Ref.3

Post-translational modification

Monoubiquitinated. Ubiquitination activates deubiquitination activity in vitro.

Sequence similarities

Contains 1 Josephin domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
   Molecular functionHydrolase
Protease
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionomega peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Josephin-1
PRO_0000053840

Regions

Domain23 – 202180Josephin

Sites

Active site361Nucleophile By similarity
Active site1391Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DBJ6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8F04FB5C37529BF7

FASTA20223,152
        10         20         30         40         50         60 
MSCVPWKGDK AKAESSDLPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRETLQEIF 

        70         80         90        100        110        120 
QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALTNVMGFIM 

       130        140        150        160        170        180 
NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKYHLRGK 

       190        200 
NCELLLVVPE EVEAHQSWRA DV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 and NOD.
Tissue: Liver.
[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 and Mammary tumor.
[3]"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: TISSUE SPECIFICITY, UBIQUITINATION.
[4]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004913 mRNA. Translation: BAB23664.1.
AK154799 mRNA. Translation: BAE32837.1.
BC006928 mRNA. Translation: AAH06928.1.
BC086769 mRNA. Translation: AAH86769.1.
CCDSCCDS27647.1.
RefSeqNP_083068.1. NM_028792.3.
XP_001481034.3. XM_001480984.4.
XP_006544219.1. XM_006544156.1.
UniGeneMm.323393.
Mm.491099.

3D structure databases

ProteinModelPortalQ9DBJ6.
SMRQ9DBJ6. Positions 26-163.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC86.004.

PTM databases

PhosphoSiteQ9DBJ6.

Proteomic databases

PaxDbQ9DBJ6.
PRIDEQ9DBJ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023061; ENSMUSP00000023061; ENSMUSG00000022426.
GeneID100043771.
74158.
KEGGmmu:100043771.
mmu:74158.
UCSCuc007wue.2. mouse.

Organism-specific databases

CTD9929.
MGIMGI:1921408. Josd1.

Phylogenomic databases

eggNOGNOG321724.
GeneTreeENSGT00390000009228.
HOGENOMHOG000005731.
HOVERGENHBG039523.
InParanoidQ9DBJ6.
KOK15235.
OMAREVGGTY.
OrthoDBEOG75B871.
PhylomeDBQ9DBJ6.
TreeFamTF313660.

Gene expression databases

BgeeQ9DBJ6.
CleanExMM_JOSD1.
GenevestigatorQ9DBJ6.

Family and domain databases

InterProIPR006155. Josephin.
[Graphical view]
PfamPF02099. Josephin. 1 hit.
[Graphical view]
PROSITEPS50957. JOSEPHIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339942.
PROQ9DBJ6.
SOURCESearch...

Entry information

Entry nameJOS1_MOUSE
AccessionPrimary (citable) accession number: Q9DBJ6
Secondary accession number(s): Q3U3E9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot