[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH JUN.
DOI=10.1038/383453a0; PubMed=8837781 [NCBI, ExPASy, EBI, Israel, Japan]
Claret F.-X.,
Hibi M.,
Dhut S.,
Toda T.,
Karin M.;
"A new group of conserved coactivators that increase the specificity of AP-1 transcription factors.";
Nature 383:453-457(1996).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.272.43.27042; PubMed=9341143 [NCBI, ExPASy, EBI, Israel, Japan]
Asano K.,
Vornlocher H.-P.,
Richter-Cook N.J.,
Merrick W.C.,
Hinnebusch A.G.,
Hershey J.W.B.;
"Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly.";
J. Biol. Chem. 272:27042-27052(1997).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A.,
Ebert L.,
Mkoundinya M.,
Schick M.,
Eisenstein S.,
Neubert P.,
Kstrang K.,
Schatten R.,
Shen B.,
Henze S.,
Mar W.,
Korn B.,
Zuo D.,
Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-47.
TISSUE=Liver;
The German cDNA consortium;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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[6]
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PROTEIN SEQUENCE OF 2-11; 57-64; 181-187; 237-244 AND 273-282, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V.,
Quadroni M.;
Submitted (OCT-2005) to UniProtKB.
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[7]
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NUCLEOTIDE SEQUENCE [MRNA] OF 146-334.
Hu W.,
Tian J.;
"The fusion gene of human Jun activation domain binding protein and membrane cofactor protein which cloned from multiple myeloma cell line ARH-77.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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[8]
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PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9535219 [NCBI, ExPASy, EBI, Israel, Japan]
Seeger M.,
Kraft R.,
Ferrell K.,
Bech-Otschir D.,
Dumdey R.,
Schade R.,
Gordon C.,
Naumann M.,
Dubiel W.;
"A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits.";
FASEB J. 12:469-478(1998).
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[9]
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INTERACTION WITH BCL3.
DOI=10.1038/sj.onc.1202717; PubMed=10362352 [NCBI, ExPASy, EBI, Israel, Japan]
Dechend R.,
Hirano F.,
Lehmann K.,
Heissmeyer V.,
Ansieau S.,
Wulczyn F.G.,
Scheidereit C.,
Leutz A.;
"The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators.";
Oncogene 18:3316-3323(1999).
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[10]
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INTERACTION WITH NCOA1 AND PGR.
DOI=10.1074/jbc.275.12.8540; PubMed=10722692 [NCBI, ExPASy, EBI, Israel, Japan]
Chauchereau A.,
Georgiakaki M.,
Perrin-Wolff M.,
Milgrom E.,
Loosfelt H.;
"JAB1 interacts with both the progesterone receptor and SRC-1.";
J. Biol. Chem. 275:8540-8548(2000).
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[11]
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INTERACTION WITH MIF.
DOI=10.1038/35041591; PubMed=11089976 [NCBI, ExPASy, EBI, Israel, Japan]
Kleemann R.,
Hausser A.,
Geiger G.,
Mischke R.,
Burger-Kentischer A.,
Flieger O.,
Johannes F.-J.,
Roger T.,
Calandra T.,
Kapurniotu A.,
Grell M.,
Finkelmeier D.,
Brunner H.,
Bernhagen J.;
"Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1.";
Nature 408:211-216(2000).
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[12]
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INTERACTION WITH ITGB2.
DOI=10.1038/35007098; PubMed=10766246 [NCBI, ExPASy, EBI, Israel, Japan]
Bianchi E.,
Denti S.,
Granata A.,
Bossi G.,
Geginat J.,
Villa A.,
Rogge L.,
Pardi R.;
"Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity.";
Nature 404:617-621(2000).
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[13]
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FUNCTION, AND INTERACTION WITH TP53.
DOI=10.1093/emboj/20.7.1630; PubMed=11285227 [NCBI, ExPASy, EBI, Israel, Japan]
Bech-Otschir D.,
Kraft R.,
Huang X.,
Henklein P.,
Kapelari B.,
Pollmann C.,
Dubiel W.;
"COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system.";
EMBO J. 20:1630-1639(2001).
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[14]
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FUNCTION, AND COMPOSITION OF THE CSN COMPLEX.
DOI=10.1126/science.1059780; PubMed=11337588 [NCBI, ExPASy, EBI, Israel, Japan]
Lyapina S.,
Cope G.,
Shevchenko A.,
Serino G.,
Tsuge T.,
Zhou C.,
Wolf D.A.,
Wei N.,
Shevchenko A.,
Deshaies R.J.;
"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
Science 292:1382-1385(2001).
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[15]
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INTERACTION WITH SMAD4.
DOI=10.1093/embo-reports/kvf024; PubMed=11818334 [NCBI, ExPASy, EBI, Israel, Japan]
Wan M.,
Cao X.,
Wu Y.,
Bai S.,
Wu L.,
Shi X.,
Wang N.,
Cao X.;
"Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation.";
EMBO Rep. 3:171-176(2002).
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[16]
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INTERACTION WITH GFER.
DOI=10.1096/fj.01-0506fje; PubMed=11709497 [NCBI, ExPASy, EBI, Israel, Japan]
Lu C.,
Li Y.,
Zhao Y.,
Xing G.,
Tang F.,
Wang Q.,
Sun Y.,
Wei H.,
Yang X.,
Wu C.,
Chen J.,
Guan K.-L.,
Zhang C.,
Chen H.,
He F.;
"Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathway.";
FASEB J. 16:90-92(2002).
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[17]
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INTERACTION WITH UCHL1.
DOI=10.1038/sj.onc.1205390; PubMed=12082530 [NCBI, ExPASy, EBI, Israel, Japan]
Caballero O.L.,
Resto V.,
Patturajan M.,
Meerzaman D.,
Guo M.Z.,
Engles J.,
Yochem R.,
Ratovitski E.,
Sidransky D.,
Jen J.;
"Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1).";
Oncogene 21:3003-3010(2002).
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[18]
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FUNCTION.
DOI=10.1016/S0092-8674(03)00316-7; PubMed=12732143 [NCBI, ExPASy, EBI, Israel, Japan]
Groisman R.,
Polanowska J.,
Kuraoka I.,
Sawada J.,
Saijo M.,
Drapkin R.,
Kisselev A.F.,
Tanaka K.,
Nakatani Y.;
"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage.";
Cell 113:357-367(2003).
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[19]
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FUNCTION.
DOI=10.1093/emboj/cdg127; PubMed=12628923 [NCBI, ExPASy, EBI, Israel, Japan]
Uhle S.,
Medalia O.,
Waldron R.,
Dumdey R.,
Henklein P.,
Bech-Otschir D.,
Huang X.,
Berse M.,
Sperling J.,
Schade R.,
Dubiel W.;
"Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome.";
EMBO J. 22:1302-1312(2003).
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[20]
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IDENTIFICATION IN A COMPLEX WITH RAN; RANBP9 AND DYRK1B.
DOI=10.1074/jbc.M307556200; PubMed=14500717 [NCBI, ExPASy, EBI, Israel, Japan]
Zou Y.,
Lim S.,
Lee K.,
Deng X.,
Friedman E.;
"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M.";
J. Biol. Chem. 278:49573-49581(2003).
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[21]
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INTERACTION WITH TOP2A.
DOI=10.1074/jbc.M401411200; PubMed=15126503 [NCBI, ExPASy, EBI, Israel, Japan]
Yun J.,
Tomida A.,
Andoh T.,
Tsuruo T.;
"Interaction between glucose-regulated destruction domain of DNA topoisomerase IIalpha and MPN domain of Jab1/CSN5.";
J. Biol. Chem. 279:31296-31303(2004).
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[22]
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INTERACTION WITH SMAD7.
DOI=10.1128/MCB.24.6.2251-2262.2004; PubMed=14993265 [NCBI, ExPASy, EBI, Israel, Japan]
Kim B.-C.,
Lee H.-J.,
Park S.H.,
Lee S.R.,
Karpova T.S.,
McNally J.G.,
Felici A.,
Lee D.K.,
Kim S.-J.;
"Jab1/CSN5, a component of the COP9 signalosome, regulates transforming growth factor beta signaling by binding to Smad7 and promoting its degradation.";
Mol. Cell. Biol. 24:2251-2262(2004).
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- FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts direclty with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex.
- COFACTOR: Divalent metal ions (By similarity).
- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS6 and COPS7 (COPS7A or COPS7B). Also exists as monomeric form. Interacts with TP53, MIF, JUN, UCHL1, NCOA1, HIF1A, CDKN1B, BCL3, GFER, PGR, LHCGR, SMAD4, SMAD7, ID1, ID3, ITGB2 and TOP2A. Part of a complex consisting of RANBP9, Ran, DYRK1B and COPS5.
- INTERACTION:
O95273:CCNDBP1; NbExp=1; IntAct=EBI-594661, EBI-748961;
P46527:CDKN1B; NbExp=1; IntAct=EBI-594661, EBI-519280;
P10599:TXN; NbExp=5; IntAct=EBI-594661, EBI-594644;
P09936:UCHL1; NbExp=1; IntAct=EBI-594661, EBI-714860;
P40337:VHL; NbExp=1; IntAct=EBI-594661, EBI-301246;
- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
- DOMAIN: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It may constitute the catalytic center of the complex (By similarity).
- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily [view classification].
- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
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