Full text data of JOSD1
JOSD1
(JSPH1, KIAA0063)
[Confidence: low (only semi-automatic identification from reviews)]
Josephin-1; 3.4.19.12 (Josephin domain-containing protein 1)
Josephin-1; 3.4.19.12 (Josephin domain-containing protein 1)
UniProt
Q15040
ID JOS1_HUMAN Reviewed; 202 AA.
AC Q15040; A8K712;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Josephin-1;
DE EC=3.4.19.12;
DE AltName: Full=Josephin domain-containing protein 1;
GN Name=JOSD1; Synonyms=JSPH1, KIAA0063;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=17696782; DOI=10.1515/BC.2007.107;
RA Tzvetkov N., Breuer P.;
RT "Josephin domain-containing proteins from a variety of species are
RT active de-ubiquitination enzymes.";
RL Biol. Chem. 388:973-978(2007).
RN [8]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21118805; DOI=10.1074/jbc.M110.177360;
RA Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J.;
RT "Crystal structure of a Josephin-ubiquitin complex: evolutionary
RT restraints on ataxin-3 deubiquitinating activity.";
RL J. Biol. Chem. 286:4555-4565(2011).
RN [9]
RP FUNCTION, INTERACTION WITH ACTB, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF CYS-36.
RX PubMed=23625928; DOI=10.1074/jbc.M113.463406;
RA Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.;
RT "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by
RT ubiquitination and regulates membrane dynamics, cell motility, and
RT endocytosis.";
RL J. Biol. Chem. 288:17145-17155(2013).
RN [10]
RP 3D-STRUCTURE MODELING.
RX PubMed=12486728; DOI=10.1002/prot.10280;
RA Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U.,
RA Lengauer T.;
RT "Structural modeling of ataxin-3 reveals distant homology to
RT adaptins.";
RL Proteins 50:355-370(2003).
CC -!- FUNCTION: Deubiquitinates monoubiquitinated probes (in vitro).
CC When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked
CC poly-ubiquitin chains (in vitro), hence may act as a
CC deubiquitinating enzyme. May increase macropinocytosis and
CC suppress clathrin- and caveolae-mediated endocytosis. May enhance
CC membrane dynamics and cell motility independently of its catalytic
CC activity.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with beta-actin/ACTB.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm.
CC Note=Ubiquitination increases localization the plasma membrane. In
CC the cytosol, the unubiquinated form may be associated with the
CC cytoskeleton via ACTB-binding.
CC -!- PTM: Monoubiquitinated (By similarity). Ubiquitination activates
CC deubiquitination activity in vitro.
CC -!- SIMILARITY: Contains 1 Josephin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06682.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; D31884; BAA06682.2; ALT_INIT; mRNA.
DR EMBL; CR456473; CAG30359.1; -; mRNA.
DR EMBL; AK291827; BAF84516.1; -; mRNA.
DR EMBL; AL021707; CAB42863.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60259.1; -; Genomic_DNA.
DR EMBL; BC015026; AAH15026.1; -; mRNA.
DR RefSeq; NP_055691.1; NM_014876.5.
DR RefSeq; XP_005261933.1; XM_005261876.1.
DR RefSeq; XP_005261934.1; XM_005261877.1.
DR RefSeq; XP_005261935.1; XM_005261878.1.
DR RefSeq; XP_005261936.1; XM_005261879.1.
DR UniGene; Hs.3094; -.
DR ProteinModelPortal; Q15040; -.
DR SMR; Q15040; 26-163.
DR IntAct; Q15040; 3.
DR STRING; 9606.ENSP00000216039; -.
DR MEROPS; C86.004; -.
DR PhosphoSite; Q15040; -.
DR DMDM; 3123051; -.
DR PaxDb; Q15040; -.
DR PRIDE; Q15040; -.
DR DNASU; 9929; -.
DR Ensembl; ENST00000216039; ENSP00000216039; ENSG00000100221.
DR GeneID; 9929; -.
DR KEGG; hsa:9929; -.
DR UCSC; uc003awf.3; human.
DR CTD; 9929; -.
DR GeneCards; GC22M039081; -.
DR HGNC; HGNC:28953; JOSD1.
DR HPA; HPA001168; -.
DR MIM; 615323; gene.
DR neXtProt; NX_Q15040; -.
DR PharmGKB; PA142671644; -.
DR eggNOG; NOG321724; -.
DR HOGENOM; HOG000005731; -.
DR HOVERGEN; HBG039523; -.
DR InParanoid; Q15040; -.
DR KO; K15235; -.
DR OMA; REVGGTY; -.
DR PhylomeDB; Q15040; -.
DR GenomeRNAi; 9929; -.
DR NextBio; 37462; -.
DR PRO; PR:Q15040; -.
DR ArrayExpress; Q15040; -.
DR Bgee; Q15040; -.
DR CleanEx; HS_JOSD1; -.
DR Genevestigator; Q15040; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006155; Josephin.
DR Pfam; PF02099; Josephin; 1.
DR PROSITE; PS50957; JOSEPHIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasm; Hydrolase; Membrane;
KW Polymorphism; Protease; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1 202 Josephin-1.
FT /FTId=PRO_0000053839.
FT DOMAIN 23 202 Josephin.
FT ACT_SITE 36 36 Nucleophile (By similarity).
FT ACT_SITE 139 139 Proton acceptor (By similarity).
FT VARIANT 48 48 S -> R (in dbSNP:rs6001200).
FT /FTId=VAR_050031.
FT MUTAGEN 36 36 C->A: Loss of deubiquitination activity,
FT no change in subcellular location.
SQ SEQUENCE 202 AA; 23198 MW; 837268C393C0A5A9 CRC64;
MSCVPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRDTLQEIF
QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALTNVMGFIM
NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKHHLRGK
NCELLLVVPE EVEAHQSWRT DV
//
ID JOS1_HUMAN Reviewed; 202 AA.
AC Q15040; A8K712;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Josephin-1;
DE EC=3.4.19.12;
DE AltName: Full=Josephin domain-containing protein 1;
GN Name=JOSD1; Synonyms=JSPH1, KIAA0063;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=17696782; DOI=10.1515/BC.2007.107;
RA Tzvetkov N., Breuer P.;
RT "Josephin domain-containing proteins from a variety of species are
RT active de-ubiquitination enzymes.";
RL Biol. Chem. 388:973-978(2007).
RN [8]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21118805; DOI=10.1074/jbc.M110.177360;
RA Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J.;
RT "Crystal structure of a Josephin-ubiquitin complex: evolutionary
RT restraints on ataxin-3 deubiquitinating activity.";
RL J. Biol. Chem. 286:4555-4565(2011).
RN [9]
RP FUNCTION, INTERACTION WITH ACTB, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF CYS-36.
RX PubMed=23625928; DOI=10.1074/jbc.M113.463406;
RA Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.;
RT "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by
RT ubiquitination and regulates membrane dynamics, cell motility, and
RT endocytosis.";
RL J. Biol. Chem. 288:17145-17155(2013).
RN [10]
RP 3D-STRUCTURE MODELING.
RX PubMed=12486728; DOI=10.1002/prot.10280;
RA Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U.,
RA Lengauer T.;
RT "Structural modeling of ataxin-3 reveals distant homology to
RT adaptins.";
RL Proteins 50:355-370(2003).
CC -!- FUNCTION: Deubiquitinates monoubiquitinated probes (in vitro).
CC When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked
CC poly-ubiquitin chains (in vitro), hence may act as a
CC deubiquitinating enzyme. May increase macropinocytosis and
CC suppress clathrin- and caveolae-mediated endocytosis. May enhance
CC membrane dynamics and cell motility independently of its catalytic
CC activity.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with beta-actin/ACTB.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm.
CC Note=Ubiquitination increases localization the plasma membrane. In
CC the cytosol, the unubiquinated form may be associated with the
CC cytoskeleton via ACTB-binding.
CC -!- PTM: Monoubiquitinated (By similarity). Ubiquitination activates
CC deubiquitination activity in vitro.
CC -!- SIMILARITY: Contains 1 Josephin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06682.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; D31884; BAA06682.2; ALT_INIT; mRNA.
DR EMBL; CR456473; CAG30359.1; -; mRNA.
DR EMBL; AK291827; BAF84516.1; -; mRNA.
DR EMBL; AL021707; CAB42863.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60259.1; -; Genomic_DNA.
DR EMBL; BC015026; AAH15026.1; -; mRNA.
DR RefSeq; NP_055691.1; NM_014876.5.
DR RefSeq; XP_005261933.1; XM_005261876.1.
DR RefSeq; XP_005261934.1; XM_005261877.1.
DR RefSeq; XP_005261935.1; XM_005261878.1.
DR RefSeq; XP_005261936.1; XM_005261879.1.
DR UniGene; Hs.3094; -.
DR ProteinModelPortal; Q15040; -.
DR SMR; Q15040; 26-163.
DR IntAct; Q15040; 3.
DR STRING; 9606.ENSP00000216039; -.
DR MEROPS; C86.004; -.
DR PhosphoSite; Q15040; -.
DR DMDM; 3123051; -.
DR PaxDb; Q15040; -.
DR PRIDE; Q15040; -.
DR DNASU; 9929; -.
DR Ensembl; ENST00000216039; ENSP00000216039; ENSG00000100221.
DR GeneID; 9929; -.
DR KEGG; hsa:9929; -.
DR UCSC; uc003awf.3; human.
DR CTD; 9929; -.
DR GeneCards; GC22M039081; -.
DR HGNC; HGNC:28953; JOSD1.
DR HPA; HPA001168; -.
DR MIM; 615323; gene.
DR neXtProt; NX_Q15040; -.
DR PharmGKB; PA142671644; -.
DR eggNOG; NOG321724; -.
DR HOGENOM; HOG000005731; -.
DR HOVERGEN; HBG039523; -.
DR InParanoid; Q15040; -.
DR KO; K15235; -.
DR OMA; REVGGTY; -.
DR PhylomeDB; Q15040; -.
DR GenomeRNAi; 9929; -.
DR NextBio; 37462; -.
DR PRO; PR:Q15040; -.
DR ArrayExpress; Q15040; -.
DR Bgee; Q15040; -.
DR CleanEx; HS_JOSD1; -.
DR Genevestigator; Q15040; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006155; Josephin.
DR Pfam; PF02099; Josephin; 1.
DR PROSITE; PS50957; JOSEPHIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasm; Hydrolase; Membrane;
KW Polymorphism; Protease; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1 202 Josephin-1.
FT /FTId=PRO_0000053839.
FT DOMAIN 23 202 Josephin.
FT ACT_SITE 36 36 Nucleophile (By similarity).
FT ACT_SITE 139 139 Proton acceptor (By similarity).
FT VARIANT 48 48 S -> R (in dbSNP:rs6001200).
FT /FTId=VAR_050031.
FT MUTAGEN 36 36 C->A: Loss of deubiquitination activity,
FT no change in subcellular location.
SQ SEQUENCE 202 AA; 23198 MW; 837268C393C0A5A9 CRC64;
MSCVPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRDTLQEIF
QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALTNVMGFIM
NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKHHLRGK
NCELLLVVPE EVEAHQSWRT DV
//
MIM
615323
*RECORD*
*FIELD* NO
615323
*FIELD* TI
*615323 JOSEPHIN DOMAIN-CONTAINING PROTEIN 1; JOSD1
;;KIAA0063
*FIELD* TX
DESCRIPTION
read more
JOSD1 belongs to a family of Josephin domain-containing deubiquitinating
enzymes related to ATXN3 (607047). JOSD1 is activated by
monoubiquitination and functions in cytoskeletal dynamics, cell
motility, and endocytosis (Seki et al., 2013).
CLONING
By sequencing clones obtained from a size-fractionated KG-1 human
immature myeloid cell line cDNA library, (Nomura et al., 1994) obtained
a partial JOSD1 clone, which they designated KIAA0063. The 3-prime
untranslated region contains an Alu element and its 202-amino acid
sequence was predicted to include a transmembrane domain. Northern blot
analysis detected JOSD1 in all human tissues and cell lines examined.
Seki et al. (2013) stated that the deduced 202-amino acid JOSD1 protein
is made up almost entirely of an approximately 180-amino acid Josephin
catalytic domain, including a catalytic cys36. Western blot analysis
detected robust Josd1 expression in all mouse tissues examined: anterior
and posterior brain, heart, kidney, liver, skeletal muscle, and spleen.
In transfected HEK293 cells, epitope- or fluorescence-tagged JOSD1
localized predominantly at the plasma membrane and cytoplasmic puncta.
In fractionated cells, JOSD1 localized to the cytoskeletal, cytosolic,
and membrane fractions, but not to the nuclear fraction. Database
analysis revealed 2 JOSD genes in vertebrates, JOSD1 and JOSD2 (615324),
but only a single Josd gene in C. elegans and Drosophila.
GENE FUNCTION
Seki et al. (2013) found that recombinant human JOSD1 deubiquitinated a
monoubiquitinated probe. However, monoubiquitinated JOSD1 showed
activity against both lys48- and lys63-linked polyubiquitin chains,
which are associated with protein degradative and regulatory pathways,
respectively. A substantial proportion of JOSD1 appeared to be
monoubiquitinated in cultured cells. In contrast, JOSD2 did not require
monoubiquitination for activity against either lys48- or lys63-linked
ubiquitin chains. Monoubiquitination of JOSD1 caused its relocalization
from the cytoskeletal fraction to the membrane fraction in transfected
cells. Time-lapse microscopy revealed that catalytically inactive JOSD1
altered membrane dynamics and cell motility; monoubiquitinated and
catalytic active JOSD1 also enhanced macropinocytosis and suppressed
clathrin- and caveolae-mediated endocytosis. Seki et al. (2013)
concluded that the activity of JOSD1 is regulated by monoubiquitination
and that it has a role in membrane dynamics and endocytosis.
MAPPING
By PCR of a human-rodent hybrid panel, Nomura et al. (1994) mapped the
JOSD1 gene to chromosome 22. Hartz (2013) mapped the JOSD1 gene to
chromosome 22q13.1 based on an alignment of the JOSD1 sequence (GenBank
GENBANK D31884) with the genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/21/2013.
2. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: 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. DNA Res. 1: 223-229, 1994.
3. Seki, T.; Gong, L.; Williams, A. J.; Sakai, N.; Todi, S. V.; Paulson,
H. L.: JosD1, a membrane-targeted deubiquitinating enzyme, is activated
by ubiquitination and regulates membrane dynamics, cell motility,
and endocytosis. J. Biol. Chem. 288: 17145-17155, 2013.
*FIELD* CD
Patricia A. Hartz: 7/22/2013
*FIELD* ED
joanna: 07/25/2013
alopez: 7/23/2013
tpirozzi: 7/23/2013
*RECORD*
*FIELD* NO
615323
*FIELD* TI
*615323 JOSEPHIN DOMAIN-CONTAINING PROTEIN 1; JOSD1
;;KIAA0063
*FIELD* TX
DESCRIPTION
read more
JOSD1 belongs to a family of Josephin domain-containing deubiquitinating
enzymes related to ATXN3 (607047). JOSD1 is activated by
monoubiquitination and functions in cytoskeletal dynamics, cell
motility, and endocytosis (Seki et al., 2013).
CLONING
By sequencing clones obtained from a size-fractionated KG-1 human
immature myeloid cell line cDNA library, (Nomura et al., 1994) obtained
a partial JOSD1 clone, which they designated KIAA0063. The 3-prime
untranslated region contains an Alu element and its 202-amino acid
sequence was predicted to include a transmembrane domain. Northern blot
analysis detected JOSD1 in all human tissues and cell lines examined.
Seki et al. (2013) stated that the deduced 202-amino acid JOSD1 protein
is made up almost entirely of an approximately 180-amino acid Josephin
catalytic domain, including a catalytic cys36. Western blot analysis
detected robust Josd1 expression in all mouse tissues examined: anterior
and posterior brain, heart, kidney, liver, skeletal muscle, and spleen.
In transfected HEK293 cells, epitope- or fluorescence-tagged JOSD1
localized predominantly at the plasma membrane and cytoplasmic puncta.
In fractionated cells, JOSD1 localized to the cytoskeletal, cytosolic,
and membrane fractions, but not to the nuclear fraction. Database
analysis revealed 2 JOSD genes in vertebrates, JOSD1 and JOSD2 (615324),
but only a single Josd gene in C. elegans and Drosophila.
GENE FUNCTION
Seki et al. (2013) found that recombinant human JOSD1 deubiquitinated a
monoubiquitinated probe. However, monoubiquitinated JOSD1 showed
activity against both lys48- and lys63-linked polyubiquitin chains,
which are associated with protein degradative and regulatory pathways,
respectively. A substantial proportion of JOSD1 appeared to be
monoubiquitinated in cultured cells. In contrast, JOSD2 did not require
monoubiquitination for activity against either lys48- or lys63-linked
ubiquitin chains. Monoubiquitination of JOSD1 caused its relocalization
from the cytoskeletal fraction to the membrane fraction in transfected
cells. Time-lapse microscopy revealed that catalytically inactive JOSD1
altered membrane dynamics and cell motility; monoubiquitinated and
catalytic active JOSD1 also enhanced macropinocytosis and suppressed
clathrin- and caveolae-mediated endocytosis. Seki et al. (2013)
concluded that the activity of JOSD1 is regulated by monoubiquitination
and that it has a role in membrane dynamics and endocytosis.
MAPPING
By PCR of a human-rodent hybrid panel, Nomura et al. (1994) mapped the
JOSD1 gene to chromosome 22. Hartz (2013) mapped the JOSD1 gene to
chromosome 22q13.1 based on an alignment of the JOSD1 sequence (GenBank
GENBANK D31884) with the genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/21/2013.
2. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: 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. DNA Res. 1: 223-229, 1994.
3. Seki, T.; Gong, L.; Williams, A. J.; Sakai, N.; Todi, S. V.; Paulson,
H. L.: JosD1, a membrane-targeted deubiquitinating enzyme, is activated
by ubiquitination and regulates membrane dynamics, cell motility,
and endocytosis. J. Biol. Chem. 288: 17145-17155, 2013.
*FIELD* CD
Patricia A. Hartz: 7/22/2013
*FIELD* ED
joanna: 07/25/2013
alopez: 7/23/2013
tpirozzi: 7/23/2013