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COP9 signalosome complex subunit 5 (SGN5) (Signalosome subunit 5) (EC 3.4.-.-) (Jun activation domain-binding protein 1)

 CSN5_HUMAN              Reviewed;         334 AA.
Q92905; O15386; Q6AW95; Q86WQ4; Q9BQ17;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 165.
RecName: Full=COP9 signalosome complex subunit 5;
Short=SGN5;
Short=Signalosome subunit 5;
EC=3.4.-.-;
AltName: Full=Jun activation domain-binding protein 1;
Name=COPS5; Synonyms=CSN5, JAB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH JUN.
PubMed=8837781; DOI=10.1038/383453a0;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
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).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-47.
TISSUE=Liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
PROTEIN SEQUENCE OF 2-11; 57-64; 181-187; 237-244 AND 273-282,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Quadroni M.;
Submitted (OCT-2005) to UniProtKB.
[7]
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.
[8]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9535219;
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).
[9]
INTERACTION WITH BCL3.
PubMed=10362352; DOI=10.1038/sj.onc.1202717;
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).
[10]
INTERACTION WITH NCOA1 AND PGR.
PubMed=10722692; DOI=10.1074/jbc.275.12.8540;
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).
[11]
INTERACTION WITH MIF.
PubMed=11089976; DOI=10.1038/35041591;
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).
[12]
INTERACTION WITH ITGB2.
PubMed=10766246; DOI=10.1038/35007098;
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).
[13]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=11285227; DOI=10.1093/emboj/20.7.1630;
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).
[14]
FUNCTION, AND COMPOSITION OF THE CSN COMPLEX.
PubMed=11337588; DOI=10.1126/science.1059780;
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).
[15]
INTERACTION WITH SMAD4.
PubMed=11818334; DOI=10.1093/embo-reports/kvf024;
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).
[16]
INTERACTION WITH GFER.
PubMed=11709497; DOI=10.1096/fj.01-0506fje;
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).
[17]
INTERACTION WITH UCHL1.
PubMed=12082530; DOI=10.1038/sj.onc.1205390;
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).
[18]
FUNCTION.
PubMed=12732143; DOI=10.1016/S0092-8674(03)00316-7;
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).
[19]
FUNCTION.
PubMed=12628923; DOI=10.1093/emboj/cdg127;
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).
[20]
IDENTIFICATION IN A COMPLEX WITH RAN; RANBP9 AND DYRK1B.
PubMed=14500717; DOI=10.1074/jbc.M307556200;
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).
[21]
INTERACTION WITH TOP2A.
PubMed=15126503; DOI=10.1074/jbc.M401411200;
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).
[22]
INTERACTION WITH SMAD7.
PubMed=14993265; DOI=10.1128/MCB.24.6.2251-2262.2004;
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).
[23]
INTERACTION WITH ZDHHC16.
TISSUE=Placenta;
PubMed=17123647; DOI=10.1016/j.bbaexp.2006.10.002;
Zhang F., Di Y., Li J., Shi Y., Zhang L., Wang C., He X., Liu Y.,
Wan D., Huo K., Gu J.;
"Molecular cloning and characterization of human Aph2 gene, involved
in AP-1 regulation by interaction with JAB1.";
Biochim. Biophys. Acta 1759:514-525(2006).
[24]
SUBCELLULAR LOCATION, AND INTERACTION WITH IFIT3.
PubMed=17050680; DOI=10.1073/pnas.0607830103;
Xiao S., Li D., Zhu H.Q., Song M.G., Pan X.R., Jia P.M., Peng L.L.,
Dou A.X., Chen G.Q., Chen S.J., Chen Z., Tong J.H.;
"RIG-G as a key mediator of the antiproliferative activity of
interferon-related pathways through enhancing p21 and p27 proteins.";
Proc. Natl. Acad. Sci. U.S.A. 103:16448-16453(2006).
[25]
IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
AND ACETYLATION AT ALA-2.
PubMed=18850735; DOI=10.1021/pr800574c;
Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
"Characterization of the human COP9 signalosome complex using affinity
purification and mass spectrometry.";
J. Proteome Res. 7:4914-4925(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
FUNCTION, IDENTIFICATION IN THE SIGNALOSOME COMPLEX, INTERACTION WITH
THE BRISC COMPLEX, AND MUTAGENESIS OF HIS-138.
PubMed=19214193; DOI=10.1038/emboj.2009.27;
Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
Cohen R.E.;
"K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
associated Brcc36 and proteasomal Poh1.";
EMBO J. 28:621-631(2009).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
FUNCTION, INTERACTION WITH FANK1, AND SUBCELLULAR LOCATION.
PubMed=20978819; DOI=10.1007/s00018-010-0559-4;
Wang H., Song W., Hu T., Zhang N., Miao S., Zong S., Wang L.;
"Fank1 interacts with Jab1 and regulates cell apoptosis via the AP-1
pathway.";
Cell. Mol. Life Sci. 68:2129-2139(2011).
[30]
SUBCELLULAR LOCATION.
PubMed=21102408; DOI=10.1038/emboj.2010.285;
Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
"CSN complex controls the stability of selected synaptic proteins via
a torsinA-dependent process.";
EMBO J. 30:181-193(2011).
[31]
INTERACTION WITH MINDY3.
PubMed=21499297; DOI=10.1038/onc.2011.116;
Shi Y., Chen J., Li Z., Zhang Z., Yu H., Sun K., Wang X., Song X.,
Wang Y., Zhen Y., Yang T., Lou K., Zhang Y., Zhang G., Hu Y., Ji J.,
Hui R.;
"C10ORF97 is a novel tumor-suppressor gene of non-small-cell lung
cancer and a functional variant of this gene increases the risk of
non-small-cell lung cancer.";
Oncogene 30:4107-4117(2011).
[32]
FUNCTION, INTERACTION WITH BRSK2, AND SUBCELLULAR LOCATION.
PubMed=22609399; DOI=10.1016/j.bbrc.2012.05.045;
Zhou J., Wan B., Li R., Gu X., Zhong Z., Wang Y., Yu L.;
"Jab1 interacts with brain-specific kinase 2 (BRSK2) and promotes its
degradation in the ubiquitin-proteasome pathway.";
Biochem. Biophys. Res. Commun. 422:647-652(2012).
[33]
INTERACTION WITH COSP9.
PubMed=23776465; DOI=10.1371/journal.pone.0065285;
Ebina M., Tsuruta F., Katoh M.C., Kigoshi Y., Someya A., Chiba T.;
"Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear
localization through Nedd8 modification.";
PLoS ONE 8:E65285-E65285(2013).
[34]
COMPOSITION OF THE CSN COMPLEX, AND INTERACTION WITH COPS9.
PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L.,
Gabashvili A., Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
"CSNAP is a stoichiometric subunit of the COP9 signalosome.";
Cell Rep. 13:585-598(2015).
-!- 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 IRF8, 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 directly with a large number of
proteins that are regulated by the CSN complex, confirming a key
role in the complex. Promotes the proteasomal degradation of
BRSK2. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588,
ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143,
ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20978819,
ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
-!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8
and COPS9 isoform 1 (PubMed:26456823). In the complex, it probably
interacts directly with COPS1, COPS2, COPS4, COPS6 and COPS7
(COPS7A or COPS7B) and COPS9 isoform 1 (PubMed:26456823).
Interacts with COPS9 isoform 2 (PubMed:23776465). The CSN complex
interacts with the BRISC complex. 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. Interacts
with IFIT3. Interacts with BRSK2. Interacts with ZDHHC16
(PubMed:17123647). Interacts with MINDY3 (PubMed:21499297).
Interacts with FANK1; regulates the phosphorylation of JUN and the
transcriptional activity of AP-1 (PubMed:20978819).
{ECO:0000269|PubMed:10362352, ECO:0000269|PubMed:10722692,
ECO:0000269|PubMed:10766246, ECO:0000269|PubMed:11089976,
ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11709497,
ECO:0000269|PubMed:11818334, ECO:0000269|PubMed:12082530,
ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:14993265,
ECO:0000269|PubMed:15126503, ECO:0000269|PubMed:17050680,
ECO:0000269|PubMed:17123647, ECO:0000269|PubMed:18850735,
ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20978819,
ECO:0000269|PubMed:21499297, ECO:0000269|PubMed:22609399,
ECO:0000269|PubMed:23776465, ECO:0000269|PubMed:26456823,
ECO:0000269|PubMed:8837781}.
-!- INTERACTION:
O95273:CCNDBP1; NbExp=5; IntAct=EBI-594661, EBI-748961;
P46527:CDKN1B; NbExp=3; IntAct=EBI-594661, EBI-519280;
P61201:COPS2; NbExp=3; IntAct=EBI-594661, EBI-1050386;
Q9UNS2:COPS3; NbExp=9; IntAct=EBI-594661, EBI-350590;
Q9BT78:COPS4; NbExp=3; IntAct=EBI-594661, EBI-742413;
Q7L5N1:COPS6; NbExp=6; IntAct=EBI-594661, EBI-486838;
Q9H9Q2:COPS7B; NbExp=3; IntAct=EBI-594661, EBI-2510162;
Q99627:COPS8; NbExp=4; IntAct=EBI-594661, EBI-2510102;
P55085:F2RL1; NbExp=8; IntAct=EBI-594661, EBI-4303189;
P55789:GFER; NbExp=4; IntAct=EBI-594661, EBI-718281;
Q13098:GPS1; NbExp=4; IntAct=EBI-594661, EBI-725197;
P14174:MIF; NbExp=3; IntAct=EBI-594661, EBI-372712;
Q9H8M7:MINDY3; NbExp=3; IntAct=EBI-594661, EBI-724928;
P35372:OPRM1; NbExp=5; IntAct=EBI-594661, EBI-2624570;
Q5VTR2:RNF20; NbExp=2; IntAct=EBI-594661, EBI-2372238;
O15105:SMAD7; NbExp=10; IntAct=EBI-594661, EBI-3861591;
P10599:TXN; NbExp=8; IntAct=EBI-594661, EBI-594644;
P09936:UCHL1; NbExp=3; IntAct=EBI-594661, EBI-714860;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819,
ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}. Nucleus
{ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819,
ECO:0000269|PubMed:22609399}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:9535219}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle {ECO:0000269|PubMed:21102408}.
Note=Nuclear localization is diminished in the presence of IFIT3.
{ECO:0000269|PubMed:17050680}.
-!- DOMAIN: The JAMM motif is essential for the protease activity of
the CSN complex resulting in deneddylation of cullins. It
constitutes the catalytic center of the complex (By similarity).
{ECO:0000250}.
-!- MISCELLANEOUS: The CSN complex is associated with some 'Lys-63'-
specific deubiquitination. Such activity is however not mediated
by the core CSN complex but by the BRCC3/BRCC36 component of the
BRISC complex.
-!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL82571.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U65928; AAB16847.1; -; mRNA.
EMBL; U70734; AAD03468.1; -; mRNA.
EMBL; CR541678; CAG46479.1; -; mRNA.
EMBL; BC001187; AAH01187.1; -; mRNA.
EMBL; BC001859; AAH01859.1; -; mRNA.
EMBL; BC007272; AAH07272.1; -; mRNA.
EMBL; BX648542; CAH10375.1; -; mRNA.
EMBL; AY078082; AAL82571.1; ALT_INIT; mRNA.
CCDS; CCDS6198.1; -.
PIR; S71820; S71820.
RefSeq; NP_006828.2; NM_006837.2.
UniGene; Hs.491912; -.
PDB; 4D10; X-ray; 3.80 A; E/M=1-334.
PDB; 4D18; X-ray; 4.08 A; E/M=12-334.
PDB; 4F7O; X-ray; 2.60 A; A/B=1-257.
PDB; 4WSN; X-ray; 5.50 A; E/M/U/c/k/s=14-334.
PDB; 5JOG; X-ray; 2.46 A; A=2-257.
PDB; 5JOH; X-ray; 1.99 A; A=2-257.
PDB; 5M5Q; X-ray; 2.20 A; A=2-257.
PDBsum; 4D10; -.
PDBsum; 4D18; -.
PDBsum; 4F7O; -.
PDBsum; 4WSN; -.
PDBsum; 5JOG; -.
PDBsum; 5JOH; -.
PDBsum; 5M5Q; -.
ProteinModelPortal; Q92905; -.
SMR; Q92905; -.
BioGrid; 116183; 812.
CORUM; Q92905; -.
DIP; DIP-34546N; -.
IntAct; Q92905; 136.
MINT; MINT-1188008; -.
STRING; 9606.ENSP00000350512; -.
BindingDB; Q92905; -.
MEROPS; M67.002; -.
iPTMnet; Q92905; -.
PhosphoSitePlus; Q92905; -.
SwissPalm; Q92905; -.
BioMuta; COPS5; -.
DMDM; 55976562; -.
REPRODUCTION-2DPAGE; IPI00009958; -.
EPD; Q92905; -.
MaxQB; Q92905; -.
PaxDb; Q92905; -.
PeptideAtlas; Q92905; -.
PRIDE; Q92905; -.
DNASU; 10987; -.
Ensembl; ENST00000357849; ENSP00000350512; ENSG00000121022.
GeneID; 10987; -.
KEGG; hsa:10987; -.
UCSC; uc003xxe.4; human.
CTD; 10987; -.
DisGeNET; 10987; -.
EuPathDB; HostDB:ENSG00000121022.13; -.
GeneCards; COPS5; -.
HGNC; HGNC:2240; COPS5.
HPA; CAB004242; -.
HPA; HPA004845; -.
HPA; HPA051531; -.
MIM; 604850; gene.
neXtProt; NX_Q92905; -.
OpenTargets; ENSG00000121022; -.
PharmGKB; PA26757; -.
eggNOG; KOG1554; Eukaryota.
eggNOG; COG1310; LUCA.
GeneTree; ENSGT00550000074850; -.
HOGENOM; HOG000116528; -.
HOVERGEN; HBG051137; -.
InParanoid; Q92905; -.
KO; K09613; -.
OMA; KYWVQTL; -.
OrthoDB; EOG091G0AAO; -.
PhylomeDB; Q92905; -.
TreeFam; TF105601; -.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8951664; Neddylation.
SIGNOR; Q92905; -.
ChiTaRS; COPS5; human.
GenomeRNAi; 10987; -.
PRO; PR:Q92905; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000121022; -.
CleanEx; HS_COPS5; -.
ExpressionAtlas; Q92905; baseline and differential.
Genevisible; Q92905; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
GO; GO:0019784; F:NEDD8-specific protease activity; TAS:Reactome.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:FlyBase.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
GO; GO:1990182; P:exosomal secretion; IDA:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; IMP:ParkinsonsUK-UCL.
GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0006412; P:translation; TAS:ProtInc.
InterPro; IPR000555; JAMM/MPN+_dom.
Pfam; PF01398; JAB; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell junction; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Hydrolase;
Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome;
Signalosome; Synapse.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:18850735,
ECO:0000269|Ref.6}.
CHAIN 2 334 COP9 signalosome complex subunit 5.
/FTId=PRO_0000194835.
DOMAIN 55 192 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOTIF 138 151 JAMM motif. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 138 138 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 140 140 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 151 151 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:18850735,
ECO:0000269|Ref.6}.
MUTAGEN 138 138 H->Q: Abolishes ability to deneddylate
cullins, without affecting the 'Lys-63'-
specific deubiquitination associated with
the COP9 signalosome complex.
{ECO:0000269|PubMed:19214193}.
CONFLICT 43 45 KPW -> NLG (in Ref. 2; AAD03468).
{ECO:0000305}.
CONFLICT 129 129 R -> H (in Ref. 1; AAB16847).
{ECO:0000305}.
HELIX 6 42 {ECO:0000244|PDB:5JOH}.
HELIX 44 46 {ECO:0000244|PDB:5JOH}.
STRAND 54 58 {ECO:0000244|PDB:5JOH}.
HELIX 59 71 {ECO:0000244|PDB:5JOH}.
TURN 72 74 {ECO:0000244|PDB:5JOH}.
STRAND 78 86 {ECO:0000244|PDB:5JOH}.
STRAND 89 97 {ECO:0000244|PDB:5JOH}.
HELIX 104 107 {ECO:0000244|PDB:4F7O}.
HELIX 111 126 {ECO:0000244|PDB:5JOH}.
STRAND 132 139 {ECO:0000244|PDB:5JOH}.
TURN 141 143 {ECO:0000244|PDB:5JOH}.
HELIX 149 161 {ECO:0000244|PDB:5JOH}.
STRAND 166 170 {ECO:0000244|PDB:5JOH}.
STRAND 183 188 {ECO:0000244|PDB:5JOH}.
TURN 208 210 {ECO:0000244|PDB:5JOH}.
HELIX 211 217 {ECO:0000244|PDB:5JOH}.
STRAND 220 223 {ECO:0000244|PDB:5JOH}.
STRAND 225 229 {ECO:0000244|PDB:5JOH}.
HELIX 233 235 {ECO:0000244|PDB:5JOH}.
SEQUENCE 334 AA; 37579 MW; B5742F4AAD03A1CF CRC64;
MAASGSGMAQ KTWELANNMQ EAQSIDEIYK YDKKQQQEIL AAKPWTKDHH YFKYCKISAL
ALLKMVMHAR SGGNLEVMGL MLGKVDGETM IIMDSFALPV EGTETRVNAQ AAAYEYMAAY
IENAKQVGRL ENAIGWYHSH PGYGCWLSGI DVSTQMLNQQ FQEPFVAVVI DPTRTISAGK
VNLGAFRTYP KGYKPPDEGP SEYQTIPLNK IEDFGVHCKQ YYALEVSYFK SSLDRKLLEL
LWNKYWVNTL SSSSLLTNAD YTTGQVFDLS EKLEQSEAQL GRGSFMLGLE THDRKSEDKL
AKATRDSCKT TIEAIHGLMS QVIKDKLFNQ INIS


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