JOS2_MOUSE
ID JOS2_MOUSE Reviewed; 188 AA.
AC Q9CR30;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Josephin-2;
DE EC=3.4.19.12;
DE AltName: Full=Josephin domain-containing protein 2;
GN Name=Josd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP 3D-STRUCTURE MODELING.
RX PubMed=12486728; DOI=10.1002/prot.10280;
RA Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.;
RT "Structural modeling of ataxin-3 reveals distant homology to adaptins.";
RL Proteins 50:355-370(2003).
CC -!- FUNCTION: Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with
CC lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May
CC act as a deubiquitinating enzyme (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
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DR EMBL; AK003525; BAB22837.1; -; mRNA.
DR EMBL; AK002872; BAB22420.1; -; mRNA.
DR CCDS; CCDS21208.1; -.
DR RefSeq; NP_001191999.1; NM_001205070.1.
DR RefSeq; NP_001192000.1; NM_001205071.1.
DR RefSeq; NP_001192001.1; NM_001205072.1.
DR RefSeq; NP_001192002.1; NM_001205073.1.
DR RefSeq; NP_079644.1; NM_025368.4.
DR RefSeq; XP_006541137.1; XM_006541074.2.
DR AlphaFoldDB; Q9CR30; -.
DR SMR; Q9CR30; -.
DR BioGRID; 211232; 1.
DR STRING; 10090.ENSMUSP00000048415; -.
DR MEROPS; C86.005; -.
DR MaxQB; Q9CR30; -.
DR PaxDb; Q9CR30; -.
DR PRIDE; Q9CR30; -.
DR ProteomicsDB; 269124; -.
DR Antibodypedia; 53685; 84 antibodies from 18 providers.
DR DNASU; 66124; -.
DR Ensembl; ENSMUST00000035844; ENSMUSP00000048415; ENSMUSG00000038695.
DR Ensembl; ENSMUST00000117324; ENSMUSP00000113313; ENSMUSG00000038695.
DR Ensembl; ENSMUST00000118493; ENSMUSP00000113226; ENSMUSG00000038695.
DR Ensembl; ENSMUST00000118628; ENSMUSP00000113172; ENSMUSG00000038695.
DR Ensembl; ENSMUST00000120852; ENSMUSP00000114105; ENSMUSG00000038695.
DR GeneID; 66124; -.
DR KEGG; mmu:66124; -.
DR UCSC; uc009gpl.2; mouse.
DR CTD; 126119; -.
DR MGI; MGI:1913374; Josd2.
DR VEuPathDB; HostDB:ENSMUSG00000038695; -.
DR eggNOG; KOG2934; Eukaryota.
DR GeneTree; ENSGT00390000009228; -.
DR HOGENOM; CLU_103892_0_0_1; -.
DR InParanoid; Q9CR30; -.
DR OMA; QRWLLPQ; -.
DR OrthoDB; 1482722at2759; -.
DR PhylomeDB; Q9CR30; -.
DR TreeFam; TF313660; -.
DR Reactome; R-MMU-5689877; Josephin domain DUBs.
DR BioGRID-ORCS; 66124; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Josd2; mouse.
DR PRO; PR:Q9CR30; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CR30; protein.
DR Bgee; ENSMUSG00000038695; Expressed in bone marrow and 61 other tissues.
DR ExpressionAtlas; Q9CR30; baseline and differential.
DR Genevisible; Q9CR30; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR InterPro; IPR040053; JOSD1/2.
DR InterPro; IPR006155; Josephin.
DR PANTHER; PTHR13291; PTHR13291; 1.
DR Pfam; PF02099; Josephin; 1.
DR SMART; SM01246; Josephin; 1.
DR PROSITE; PS50957; JOSEPHIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..188
FT /note="Josephin-2"
FT /id="PRO_0000053844"
FT DOMAIN 11..188
FT /note="Josephin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 188 AA; 20776 MW; 2B2DE4BB1E9243F9 CRC64;
MSQAPEARPS PPSVYHERQR LELCAVHALN NVLQEQLFSQ EAADEICKRL APDSRLNPHR
SLLGTGNYDV NVIMAALQGL GLAAVWWDRR RPLSQLALPQ VLGLILNLPS PVSLGLLSLP
LRRRHWVALR QVDGIYYNLD SKLRAPEALG DEDGVRTFLA AALAQGLCEV LLVVTKEVEE
AGCWLNTS
