Full text data of JOSD2
JOSD2
[Confidence: low (only semi-automatic identification from reviews)]
Josephin-2; 3.4.19.12 (Josephin domain-containing protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Josephin-2; 3.4.19.12 (Josephin domain-containing protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TAC2
ID JOS2_HUMAN Reviewed; 188 AA.
AC Q8TAC2; M0QX25;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 84.
DE RecName: Full=Josephin-2;
DE EC=3.4.19.12;
DE AltName: Full=Josephin domain-containing protein 2;
GN Name=JOSD2; ORFNames=SBBI54;
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 [MRNA] (ISOFORM 1).
RA Li N., Wan T., Zhang W., Cao X.;
RT "Hypothetical transmembrane protein SBBI54.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Macrophage;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-24.
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 [9]
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: Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with
CC lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in
CC vitro). May act as a deubiquitinating enzyme.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TAC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAC2-2; Sequence=VSP_047537;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 Josephin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF247787; AAL95692.1; -; mRNA.
DR EMBL; AK131052; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC008743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW71877.1; -; Genomic_DNA.
DR EMBL; BC062416; AAH62416.1; -; mRNA.
DR RefSeq; NP_001257568.1; NM_001270639.1.
DR RefSeq; NP_001257569.1; NM_001270640.1.
DR RefSeq; NP_001257570.1; NM_001270641.1.
DR RefSeq; NP_001257615.1; NM_001270686.1.
DR RefSeq; NP_612207.1; NM_138334.3.
DR UniGene; Hs.467151; -.
DR UniGene; Hs.737597; -.
DR ProteinModelPortal; Q8TAC2; -.
DR SMR; Q8TAC2; 14-151.
DR STRING; 9606.ENSP00000293431; -.
DR MEROPS; C86.005; -.
DR PhosphoSite; Q8TAC2; -.
DR DMDM; 29840785; -.
DR PaxDb; Q8TAC2; -.
DR PRIDE; Q8TAC2; -.
DR Ensembl; ENST00000391815; ENSP00000375691; ENSG00000161677.
DR Ensembl; ENST00000595669; ENSP00000468860; ENSG00000161677.
DR Ensembl; ENST00000598418; ENSP00000468956; ENSG00000161677.
DR Ensembl; ENST00000601423; ENSP00000472116; ENSG00000161677.
DR GeneID; 126119; -.
DR KEGG; hsa:126119; -.
DR UCSC; uc002psn.2; human.
DR CTD; 126119; -.
DR GeneCards; GC19M051009; -.
DR HGNC; HGNC:28853; JOSD2.
DR MIM; 615324; gene.
DR neXtProt; NX_Q8TAC2; -.
DR PharmGKB; PA142671645; -.
DR eggNOG; NOG321724; -.
DR HOVERGEN; HBG039523; -.
DR InParanoid; Q8TAC2; -.
DR KO; K15235; -.
DR OMA; VWWDRRR; -.
DR OrthoDB; EOG75B871; -.
DR PhylomeDB; Q8TAC2; -.
DR ChiTaRS; JOSD2; human.
DR GenomeRNAi; 126119; -.
DR NextBio; 81688; -.
DR PRO; PR:Q8TAC2; -.
DR ArrayExpress; Q8TAC2; -.
DR Bgee; Q8TAC2; -.
DR CleanEx; HS_JOSD2; -.
DR Genevestigator; Q8TAC2; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006155; Josephin.
DR Pfam; PF02099; Josephin; 1.
DR PRINTS; PR01233; JOSEPHIN.
DR PROSITE; PS50957; JOSEPHIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
KW Protease; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 188 Josephin-2.
FT /FTId=PRO_0000053843.
FT DOMAIN 11 188 Josephin.
FT ACT_SITE 24 24 Nucleophile (By similarity).
FT ACT_SITE 125 125 Proton acceptor (By similarity).
FT VAR_SEQ 49 90 Missing (in isoform 2).
FT /FTId=VSP_047537.
FT MUTAGEN 24 24 C->A: Loss of deubiquitination activity,
FT no change in subcellular location.
SQ SEQUENCE 188 AA; 20756 MW; A2832B4D9BD675E9 CRC64;
MSQAPGAQPS PPTVYHERQR LELCAVHALN NVLQQQLFSQ EAADEICKRL APDSRLNPHR
SLLGTGNYDV NVIMAALQGL GLAAVWWDRR RPLSQLALPQ VLGLILNLPS PVSLGLLSLP
LRRRHWVALR QVDGVYYNLD SKLRAPEALG DEDGVRAFLA AALAQGLCEV LLVVTKEVEE
KGSWLRTD
//
ID JOS2_HUMAN Reviewed; 188 AA.
AC Q8TAC2; M0QX25;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 84.
DE RecName: Full=Josephin-2;
DE EC=3.4.19.12;
DE AltName: Full=Josephin domain-containing protein 2;
GN Name=JOSD2; ORFNames=SBBI54;
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 [MRNA] (ISOFORM 1).
RA Li N., Wan T., Zhang W., Cao X.;
RT "Hypothetical transmembrane protein SBBI54.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Macrophage;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-24.
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 [9]
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: Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with
CC lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in
CC vitro). May act as a deubiquitinating enzyme.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TAC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAC2-2; Sequence=VSP_047537;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 Josephin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF247787; AAL95692.1; -; mRNA.
DR EMBL; AK131052; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC008743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW71877.1; -; Genomic_DNA.
DR EMBL; BC062416; AAH62416.1; -; mRNA.
DR RefSeq; NP_001257568.1; NM_001270639.1.
DR RefSeq; NP_001257569.1; NM_001270640.1.
DR RefSeq; NP_001257570.1; NM_001270641.1.
DR RefSeq; NP_001257615.1; NM_001270686.1.
DR RefSeq; NP_612207.1; NM_138334.3.
DR UniGene; Hs.467151; -.
DR UniGene; Hs.737597; -.
DR ProteinModelPortal; Q8TAC2; -.
DR SMR; Q8TAC2; 14-151.
DR STRING; 9606.ENSP00000293431; -.
DR MEROPS; C86.005; -.
DR PhosphoSite; Q8TAC2; -.
DR DMDM; 29840785; -.
DR PaxDb; Q8TAC2; -.
DR PRIDE; Q8TAC2; -.
DR Ensembl; ENST00000391815; ENSP00000375691; ENSG00000161677.
DR Ensembl; ENST00000595669; ENSP00000468860; ENSG00000161677.
DR Ensembl; ENST00000598418; ENSP00000468956; ENSG00000161677.
DR Ensembl; ENST00000601423; ENSP00000472116; ENSG00000161677.
DR GeneID; 126119; -.
DR KEGG; hsa:126119; -.
DR UCSC; uc002psn.2; human.
DR CTD; 126119; -.
DR GeneCards; GC19M051009; -.
DR HGNC; HGNC:28853; JOSD2.
DR MIM; 615324; gene.
DR neXtProt; NX_Q8TAC2; -.
DR PharmGKB; PA142671645; -.
DR eggNOG; NOG321724; -.
DR HOVERGEN; HBG039523; -.
DR InParanoid; Q8TAC2; -.
DR KO; K15235; -.
DR OMA; VWWDRRR; -.
DR OrthoDB; EOG75B871; -.
DR PhylomeDB; Q8TAC2; -.
DR ChiTaRS; JOSD2; human.
DR GenomeRNAi; 126119; -.
DR NextBio; 81688; -.
DR PRO; PR:Q8TAC2; -.
DR ArrayExpress; Q8TAC2; -.
DR Bgee; Q8TAC2; -.
DR CleanEx; HS_JOSD2; -.
DR Genevestigator; Q8TAC2; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006155; Josephin.
DR Pfam; PF02099; Josephin; 1.
DR PRINTS; PR01233; JOSEPHIN.
DR PROSITE; PS50957; JOSEPHIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
KW Protease; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 188 Josephin-2.
FT /FTId=PRO_0000053843.
FT DOMAIN 11 188 Josephin.
FT ACT_SITE 24 24 Nucleophile (By similarity).
FT ACT_SITE 125 125 Proton acceptor (By similarity).
FT VAR_SEQ 49 90 Missing (in isoform 2).
FT /FTId=VSP_047537.
FT MUTAGEN 24 24 C->A: Loss of deubiquitination activity,
FT no change in subcellular location.
SQ SEQUENCE 188 AA; 20756 MW; A2832B4D9BD675E9 CRC64;
MSQAPGAQPS PPTVYHERQR LELCAVHALN NVLQQQLFSQ EAADEICKRL APDSRLNPHR
SLLGTGNYDV NVIMAALQGL GLAAVWWDRR RPLSQLALPQ VLGLILNLPS PVSLGLLSLP
LRRRHWVALR QVDGVYYNLD SKLRAPEALG DEDGVRAFLA AALAQGLCEV LLVVTKEVEE
KGSWLRTD
//
MIM
615324
*RECORD*
*FIELD* NO
615324
*FIELD* TI
*615324 JOSEPHIN DOMAIN-CONTAINING PROTEIN 2; JOSD2
*FIELD* TX
DESCRIPTION
JOSD2 belongs to a family of Josephin domain-containing deubiquitinating
read moreenzymes related to ATXN3 (607047) (Seki et al., 2013).
CLONING
Seki et al. (2013) stated that the deduced 188-amino acid JOSD2 protein
is made up almost entirely of an approximately 180-amino acid Josephin
catalytic domain with a catalytic cys24. Epitope-tagged JOSD2 had a
diffuse cytoplasmic distribution in transfected HEK293 cells. Database
analysis revealed 2 JOSD genes in vertebrates, JOSD1 (615323) and JOSD2,
but only a single Josd gene in C. elegans and Drosophila.
GENE FUNCTION
Seki et al. (2013) found that recombinant human JOSD2 deubiquitinates
both lys48- and lys63-linked polyubiquitin chains, which are associated
with protein degradative and nondegradative pathways, respectively.
JOSD2 showed a preference for lys63-linked ubiquitin chains. In
contrast, JOSD1 required modification by monoubiquitination for
activation against polyubiquitin chains.
MAPPING
Hartz (2013) mapped the JOSD2 gene to chromosome 19q13.33 based on an
alignment of the JOSD2 sequence (GenBank GENBANK AF247787) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/21/2013.
2. 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
alopez: 07/23/2013
tpirozzi: 7/23/2013
*RECORD*
*FIELD* NO
615324
*FIELD* TI
*615324 JOSEPHIN DOMAIN-CONTAINING PROTEIN 2; JOSD2
*FIELD* TX
DESCRIPTION
JOSD2 belongs to a family of Josephin domain-containing deubiquitinating
read moreenzymes related to ATXN3 (607047) (Seki et al., 2013).
CLONING
Seki et al. (2013) stated that the deduced 188-amino acid JOSD2 protein
is made up almost entirely of an approximately 180-amino acid Josephin
catalytic domain with a catalytic cys24. Epitope-tagged JOSD2 had a
diffuse cytoplasmic distribution in transfected HEK293 cells. Database
analysis revealed 2 JOSD genes in vertebrates, JOSD1 (615323) and JOSD2,
but only a single Josd gene in C. elegans and Drosophila.
GENE FUNCTION
Seki et al. (2013) found that recombinant human JOSD2 deubiquitinates
both lys48- and lys63-linked polyubiquitin chains, which are associated
with protein degradative and nondegradative pathways, respectively.
JOSD2 showed a preference for lys63-linked ubiquitin chains. In
contrast, JOSD1 required modification by monoubiquitination for
activation against polyubiquitin chains.
MAPPING
Hartz (2013) mapped the JOSD2 gene to chromosome 19q13.33 based on an
alignment of the JOSD2 sequence (GenBank GENBANK AF247787) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/21/2013.
2. 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
alopez: 07/23/2013
tpirozzi: 7/23/2013