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COP9 signalosome complex subunit 8 (SGN8) (Signalosome subunit 8) (COP9 homolog) (hCOP9) (JAB1-containing signalosome subunit 8)

 CSN8_HUMAN              Reviewed;         209 AA.
Q99627; A8K1H6; Q53QS9;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
28-MAR-2018, entry version 153.
RecName: Full=COP9 signalosome complex subunit 8;
Short=SGN8;
Short=Signalosome subunit 8;
AltName: Full=COP9 homolog;
Short=hCOP9;
AltName: Full=JAB1-containing signalosome subunit 8;
Name=COPS8; Synonyms=CSN8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7634324; DOI=10.1016/0092-8674(95)90423-9;
Chamovitz D.A., Deng X.-W.;
"The novel components of the Arabidopsis light signaling pathway may
define a group of general developmental regulators shared by both
animal and plant kingdoms.";
Cell 82:353-354(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Corpus callosum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"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 GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Skin;
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).
[7]
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).
[8]
FUNCTION.
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).
[9]
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).
[10]
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).
[11]
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).
[12]
IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,
AND PHOSPHORYLATION AT SER-175.
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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
COMPOSITION OF THE CSN COMPLEX.
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: Component 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 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/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. {ECO:0000269|PubMed:11285227,
ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923,
ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.
-!- 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:11337588, PubMed:18850735,
PubMed:26456823). In the complex, it probably interacts directly
with COPS3, COPS4 and COPS7 (COPS7A or COPS7B) (PubMed:18850735).
{ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:18850735,
ECO:0000269|PubMed:26456823}.
-!- INTERACTION:
P61201:COPS2; NbExp=8; IntAct=EBI-2510102, EBI-1050386;
Q9UNS2:COPS3; NbExp=10; IntAct=EBI-2510102, EBI-350590;
Q9BT78:COPS4; NbExp=4; IntAct=EBI-2510102, EBI-742413;
Q92905:COPS5; NbExp=7; IntAct=EBI-2510102, EBI-594661;
Q7L5N1:COPS6; NbExp=11; IntAct=EBI-2510102, EBI-486838;
Q13620:CUL4B; NbExp=3; IntAct=EBI-2510102, EBI-456067;
P55789:GFER; NbExp=5; IntAct=EBI-2510102, EBI-718281;
Q13098:GPS1; NbExp=10; IntAct=EBI-2510102, EBI-725197;
Q13098-7:GPS1; NbExp=4; IntAct=EBI-2510102, EBI-10983983;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-2510102, EBI-739895;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}.
Nucleus {ECO:0000269|PubMed:9535219}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99627-1; Sequence=Displayed;
Name=2;
IsoId=Q99627-2; Sequence=VSP_042715;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the CSN8 family. {ECO:0000305}.
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EMBL; U51205; AAB38529.1; -; mRNA.
EMBL; AK289891; BAF82580.1; -; mRNA.
EMBL; CR456994; CAG33275.1; -; mRNA.
EMBL; AC105760; AAY14978.1; -; Genomic_DNA.
EMBL; CH471063; EAW71097.1; -; Genomic_DNA.
EMBL; CH471063; EAW71098.1; -; Genomic_DNA.
EMBL; BC003090; AAH03090.1; -; mRNA.
EMBL; BC036499; AAH36499.1; -; mRNA.
EMBL; BC080617; AAH80617.1; -; mRNA.
CCDS; CCDS2517.1; -. [Q99627-1]
CCDS; CCDS42835.1; -. [Q99627-2]
RefSeq; NP_006701.1; NM_006710.4. [Q99627-1]
RefSeq; NP_937832.1; NM_198189.2. [Q99627-2]
UniGene; Hs.531713; -.
PDB; 4D10; X-ray; 3.80 A; H/P=2-209.
PDB; 4D18; X-ray; 4.08 A; H/P=1-209.
PDB; 4WSN; X-ray; 5.50 A; H/P/X/f/n/v=1-209.
PDBsum; 4D10; -.
PDBsum; 4D18; -.
PDBsum; 4WSN; -.
ProteinModelPortal; Q99627; -.
SMR; Q99627; -.
BioGrid; 116124; 71.
CORUM; Q99627; -.
DIP; DIP-42075N; -.
IntAct; Q99627; 22.
MINT; Q99627; -.
STRING; 9606.ENSP00000346340; -.
iPTMnet; Q99627; -.
PhosphoSitePlus; Q99627; -.
BioMuta; COPS8; -.
EPD; Q99627; -.
MaxQB; Q99627; -.
PaxDb; Q99627; -.
PeptideAtlas; Q99627; -.
PRIDE; Q99627; -.
TopDownProteomics; Q99627-1; -. [Q99627-1]
DNASU; 10920; -.
Ensembl; ENST00000354371; ENSP00000346340; ENSG00000198612. [Q99627-1]
Ensembl; ENST00000392008; ENSP00000375865; ENSG00000198612. [Q99627-2]
GeneID; 10920; -.
KEGG; hsa:10920; -.
UCSC; uc002vwg.4; human. [Q99627-1]
CTD; 10920; -.
DisGeNET; 10920; -.
EuPathDB; HostDB:ENSG00000198612.10; -.
GeneCards; COPS8; -.
HGNC; HGNC:24335; COPS8.
HPA; HPA036485; -.
MIM; 616011; gene.
neXtProt; NX_Q99627; -.
OpenTargets; ENSG00000198612; -.
PharmGKB; PA134968686; -.
eggNOG; KOG4414; Eukaryota.
eggNOG; ENOG410XW9N; LUCA.
GeneTree; ENSGT00390000000977; -.
HOGENOM; HOG000253954; -.
HOVERGEN; HBG051139; -.
InParanoid; Q99627; -.
KO; K12181; -.
OMA; CETQELE; -.
OrthoDB; EOG091G0O7O; -.
PhylomeDB; Q99627; -.
TreeFam; TF101150; -.
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.
ChiTaRS; COPS8; human.
GeneWiki; COPS8; -.
GenomeRNAi; 10920; -.
PRO; PR:Q99627; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000198612; -.
CleanEx; HS_COPS8; -.
ExpressionAtlas; Q99627; baseline and differential.
Genevisible; Q99627; HS.
GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:UniProtKB.
GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
InterPro; IPR033205; COP9_CSN8.
InterPro; IPR033464; CSN8_PSD8_EIF3K.
PANTHER; PTHR13339; PTHR13339; 1.
Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome; Signalosome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:18850735}.
CHAIN 2 209 COP9 signalosome complex subunit 8.
/FTId=PRO_0000121007.
DOMAIN 8 179 PCI. {ECO:0000255|PROSITE-
ProRule:PRU01185}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:18850735}.
VAR_SEQ 1 49 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042715.
SEQUENCE 209 AA; 23226 MW; 203E236D8E304A8A CRC64;
MPVAVMAESA FSFKKLLDQC ENQELEAPGG IATPPVYGQL LALYLLHNDM NNARYLWKRI
PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL
VSQAYTSIIA DDFAAFVGLP VEEAVKGILE QGWQADSTTR MVLPRKPVAG ALDVSFNKFI
PLSEPAPVPP IPNEQQLARL TDYVAFLEN


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EIAAB09603 COP9 signalosome complex subunit 3,COPS3,CSN3,Homo sapiens,Human,JAB1-containing signalosome subunit 3,SGN3,Signalosome subunit 3
EIAAB09601 Alien homolog,COP9 signalosome complex subunit 2,COPS2,CSN2,Homo sapiens,Human,JAB1-containing signalosome subunit 2,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
EIAAB09619 COP9 signalosome complex subunit 7a,COPS7A,CSN7A,Dermal papilla-derived protein 10,DERP10,Homo sapiens,Human,JAB1-containing signalosome subunit 7a,SGN7a,Signalosome subunit 7a
EIAAB09622 COP9 signalosome complex subunit 7b,Cops7b,Csn7b,JAB1-containing signalosome subunit 7b,Mouse,Mus musculus,SGN7b,Signalosome subunit 7b
EIAAB09608 COP9 signalosome complex subunit 4,Cops4,Csn4,JAB1-containing signalosome subunit 4,Rat,Rattus norvegicus,SGN4,Signalosome subunit 4
EIAAB09606 COP9 signalosome complex subunit 3,Cops3,Csn3,JAB1-containing signalosome subunit 3,Mouse,Mus musculus,SGN3,Signalosome subunit 3
EIAAB09617 COP9 signalosome complex subunit 6,Cops6,Csn6,JAB1-containing signalosome subunit 6,Mouse,Mus musculus,SGN6,Signalosome subunit 6
EIAAB09612 COP9 signalosome complex subunit 4,Cops4,Csn4,JAB1-containing signalosome subunit 4,Mouse,Mus musculus,SGN4,Signalosome subunit 4
EIAAB09620 COP9 signalosome complex subunit 7a,Cops7a,Csn7a,JAB1-containing signalosome subunit 7a,Mouse,Mus musculus,SGN7a,Signalosome subunit 7a
EIAAB09597 COP9 signalosome complex subunit 1,COPS1,CSN1,G protein pathway suppressor 1,GPS1,GPS-1,Homo sapiens,Human,JAB1-containing signalosome subunit 1,Protein MFH,SGN1,Signalosome subunit 1
EIAAB09599 COP9 signalosome complex subunit 1,Cops1,Csn1,G protein pathway suppressor 1,Gps1,GPS-1,JAB1-containing signalosome subunit 1,MFH protein,Rat,Rattus norvegicus,SGN1,Signalosome subunit 1
EIAAB09614 COP9 signalosome complex subunit 5,COPS5,CSN5,Homo sapiens,Human,JAB1,Jun activation domain-binding protein 1,SGN5,Signalosome subunit 5
EIAAB09613 COP9 signalosome complex subunit 5,Cops5,Csn5,Jab1,Jun activation domain-binding protein 1,Kic2,Kip1 C-terminus-interacting protein 2,Mouse,Mus musculus,SGN5,Signalosome subunit 5


 

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