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Q9CR30 (JOS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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-2

EC=3.4.19.12
Alternative name(s):
Josephin domain-containing protein 2
Gene names
Name:Josd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme 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).

Subcellular location

Cytoplasmcytosol By similarity.

Sequence similarities

Contains 1 Josephin domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein deubiquitination

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionomega peptidase activity

Inferred from electronic annotation. Source: InterPro

ubiquitin-specific protease activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Josephin-2
PRO_0000053844

Regions

Domain11 – 188178Josephin

Sites

Active site241Nucleophile By similarity
Active site1251Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CR30 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2B2DE4BB1E9243F9

FASTA18820,776
        10         20         30         40         50         60 
MSQAPEARPS PPSVYHERQR LELCAVHALN NVLQEQLFSQ EAADEICKRL APDSRLNPHR 

        70         80         90        100        110        120 
SLLGTGNYDV NVIMAALQGL GLAAVWWDRR RPLSQLALPQ VLGLILNLPS PVSLGLLSLP 

       130        140        150        160        170        180 
LRRRHWVALR QVDGIYYNLD SKLRAPEALG DEDGVRTFLA AALAQGLCEV LLVVTKEVEE 


AGCWLNTS 

« 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.
Tissue: Embryo and Kidney.
[2]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003525 mRNA. Translation: BAB22837.1.
AK002872 mRNA. Translation: BAB22420.1.
RefSeqNP_001191999.1. NM_001205070.1.
NP_001192000.1. NM_001205071.1.
NP_001192001.1. NM_001205072.1.
NP_001192002.1. NM_001205073.1.
NP_079644.1. NM_025368.4.
XP_006541136.1. XM_006541073.1.
XP_006541137.1. XM_006541074.1.
UniGeneMm.358691.

3D structure databases

ProteinModelPortalQ9CR30.
SMRQ9CR30. Positions 13-165.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC86.005.

Proteomic databases

PaxDbQ9CR30.
PRIDEQ9CR30.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035844; ENSMUSP00000048415; ENSMUSG00000038695.
ENSMUST00000117324; ENSMUSP00000113313; ENSMUSG00000038695.
ENSMUST00000118493; ENSMUSP00000113226; ENSMUSG00000038695.
ENSMUST00000118628; ENSMUSP00000113172; ENSMUSG00000038695.
ENSMUST00000120852; ENSMUSP00000114105; ENSMUSG00000038695.
GeneID66124.
KEGGmmu:66124.
UCSCuc009gpl.2. mouse.

Organism-specific databases

CTD126119.
MGIMGI:1913374. Josd2.

Phylogenomic databases

eggNOGNOG321724.
GeneTreeENSGT00390000009228.
HOGENOMHOG000005731.
HOVERGENHBG039523.
InParanoidQ9CR30.
KOK15235.
OMAVWWDRRR.
OrthoDBEOG75B871.
PhylomeDBQ9CR30.
TreeFamTF313660.

Gene expression databases

ArrayExpressQ9CR30.
BgeeQ9CR30.
CleanExMM_JOSD2.
GenevestigatorQ9CR30.

Family and domain databases

InterProIPR006155. Josephin.
[Graphical view]
PfamPF02099. Josephin. 1 hit.
[Graphical view]
PRINTSPR01233. JOSEPHIN.
PROSITEPS50957. JOSEPHIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320702.
PROQ9CR30.
SOURCESearch...

Entry information

Entry nameJOS2_MOUSE
AccessionPrimary (citable) accession number: Q9CR30
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 82 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