CSN4_HUMAN
ID CSN4_HUMAN Reviewed; 406 AA.
AC Q9BT78; B3KN88; B3KST5; Q561W7; Q9NW31; Q9Y677;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=COP9 signalosome complex subunit 4;
DE Short=SGN4;
DE Short=Signalosome subunit 4;
DE AltName: Full=JAB1-containing signalosome subunit 4;
GN Name=COPS4; Synonyms=CSN4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human COP9 complex subunit 4 gene.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Teratocarcinoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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=Muscle, Pancreas, and Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9535219; DOI=10.1096/fasebj.12.6.469;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R.,
RA Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [7]
RP FUNCTION.
RX PubMed=11285227; DOI=10.1093/emboj/20.7.1630;
RA Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C.,
RA Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation by
RT the ubiquitin system.";
RL EMBO J. 20:1630-1639(2001).
RN [8]
RP FUNCTION, AND COMPOSITION OF THE CSN COMPLEX.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11824616;
RX DOI=10.1002/1522-2683(200201)23:1<152::aid-elps152>3.0.co;2-t;
RA Peyrl A., Weitzdoerfer R., Gulesserian T., Fountoulakis M., Lubec G.;
RT "Aberrant expression of signaling-related proteins 14-3-3 gamma and RACK1
RT in fetal Down syndrome brain (trisomy 21), AND MASS SPECTROMETRY.";
RL Electrophoresis 23:152-157(2002).
RN [10]
RP FUNCTION.
RX PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [11]
RP FUNCTION.
RX PubMed=12628923; DOI=10.1093/emboj/cdg127;
RA Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D.,
RA Huang X., Berse M., Sperling J., Schade R., Dubiel W.;
RT "Protein kinase CK2 and protein kinase D are associated with the COP9
RT signalosome.";
RL EMBO J. 22:1302-1312(2003).
RN [12]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RX PubMed=18850735; DOI=10.1021/pr800574c;
RA Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
RT "Characterization of the human COP9 signalosome complex using affinity
RT purification and mass spectrometry.";
RL J. Proteome Res. 7:4914-4925(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION IN DENEDDYLATION AND PHOSPHORYLATION, INTERACTION WITH TOR1A AND
RP STON2, AND SUBCELLULAR LOCATION.
RX PubMed=21102408; DOI=10.1038/emboj.2010.285;
RA Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
RT "CSN complex controls the stability of selected synaptic proteins via a
RT torsinA-dependent process.";
RL EMBO J. 30:181-193(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP COMPOSITION OF THE CSN COMPLEX.
RX PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
RA Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L., Gabashvili A.,
RA Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
RT "CSNAP is a stoichiometric subunit of the COP9 signalosome.";
RL Cell Rep. 13:585-598(2015).
RN [19]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes. The CSN
CC complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC pathway by mediating the deneddylation of the cullin subunits of SCF-
CC type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the
CC deneddylation of non-cullin subunits such as STON2. The complex is also
CC involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its
CC association with CK2 and PKD kinases. CSN-dependent phosphorylation of
CC TP53 and JUN promotes and protects degradation by the Ubl system,
CC respectively. {ECO:0000269|PubMed:11285227,
CC ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923,
CC ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21102408,
CC ECO:0000269|PubMed:9535219}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC isoform 1 (PubMed:18850735, PubMed:26456823). In the complex, it
CC probably interacts directly with COPS1, COPS2, COPS3, COPS5, COPS6,
CC COPS7 (COPS7A or COPS7B) and COPS8 (PubMed:18850735). Interacts with
CC TOR1A; the interaction is direct and associates TOR1A and SNAPIN with
CC the CSN complex (PubMed:21102408). Interacts with STON2; controls STON2
CC neddylation levels (PubMed:21102408). Interacts with ERCC6
CC (PubMed:26030138). {ECO:0000269|PubMed:18850735,
CC ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:26456823}.
CC -!- INTERACTION:
CC Q9BT78; Q0VDD7: BRME1; NbExp=2; IntAct=EBI-742413, EBI-741210;
CC Q9BT78; Q7L5N1: COPS6; NbExp=18; IntAct=EBI-742413, EBI-486838;
CC Q9BT78; P01100: FOS; NbExp=2; IntAct=EBI-742413, EBI-852851;
CC Q9BT78; P08727: KRT19; NbExp=3; IntAct=EBI-742413, EBI-742756;
CC Q9BT78; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-742413, EBI-2811583;
CC Q9BT78; Q9Y5F1: PCDHB12; NbExp=3; IntAct=EBI-742413, EBI-12012016;
CC Q9BT78; O75381: PEX14; NbExp=3; IntAct=EBI-742413, EBI-594898;
CC Q9BT78; Q15831: STK11; NbExp=3; IntAct=EBI-742413, EBI-306838;
CC Q9BT78; Q8N6Y0: USHBP1; NbExp=7; IntAct=EBI-742413, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus
CC {ECO:0000269|PubMed:9535219}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000269|PubMed:21102408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT78-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT78-2; Sequence=VSP_046336;
CC -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR EMBL; AF100757; AAD43021.1; -; mRNA.
DR EMBL; AK001210; BAA91555.1; -; mRNA.
DR EMBL; AK024005; BAG51250.1; -; mRNA.
DR EMBL; AK094238; BAG52847.1; -; mRNA.
DR EMBL; AC021105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05921.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05922.1; -; Genomic_DNA.
DR EMBL; BC004302; AAH04302.1; -; mRNA.
DR EMBL; BC009292; AAH09292.1; -; mRNA.
DR EMBL; BC093007; AAH93007.1; -; mRNA.
DR CCDS; CCDS3600.1; -. [Q9BT78-1]
DR CCDS; CCDS58909.1; -. [Q9BT78-2]
DR RefSeq; NP_001244935.1; NM_001258006.1. [Q9BT78-2]
DR RefSeq; NP_001317656.1; NM_001330727.1.
DR RefSeq; NP_057213.2; NM_016129.2. [Q9BT78-1]
DR PDB; 4D0P; X-ray; 1.60 A; A=1-363.
DR PDB; 4D10; X-ray; 3.80 A; D/L=1-406.
DR PDB; 4D18; X-ray; 4.08 A; D/L=1-406.
DR PDB; 4WSN; X-ray; 5.50 A; D/L/T/b/j/r=1-406.
DR PDB; 6R6H; EM; 8.40 A; D=1-406.
DR PDB; 6R7F; EM; 8.20 A; D=1-406.
DR PDB; 6R7H; EM; 8.80 A; D=1-406.
DR PDB; 6R7I; EM; 5.90 A; D=1-406.
DR PDB; 6R7N; EM; 6.50 A; D=1-406.
DR PDBsum; 4D0P; -.
DR PDBsum; 4D10; -.
DR PDBsum; 4D18; -.
DR PDBsum; 4WSN; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6R7N; -.
DR AlphaFoldDB; Q9BT78; -.
DR SMR; Q9BT78; -.
DR BioGRID; 119324; 163.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR CORUM; Q9BT78; -.
DR DIP; DIP-34516N; -.
DR IntAct; Q9BT78; 65.
DR MINT; Q9BT78; -.
DR STRING; 9606.ENSP00000264389; -.
DR GlyGen; Q9BT78; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BT78; -.
DR PhosphoSitePlus; Q9BT78; -.
DR SwissPalm; Q9BT78; -.
DR BioMuta; COPS4; -.
DR DMDM; 55976582; -.
DR OGP; Q9BT78; -.
DR REPRODUCTION-2DPAGE; IPI00171844; -.
DR EPD; Q9BT78; -.
DR jPOST; Q9BT78; -.
DR MassIVE; Q9BT78; -.
DR MaxQB; Q9BT78; -.
DR PaxDb; Q9BT78; -.
DR PeptideAtlas; Q9BT78; -.
DR PRIDE; Q9BT78; -.
DR ProteomicsDB; 3653; -.
DR ProteomicsDB; 78958; -. [Q9BT78-1]
DR Antibodypedia; 14119; 135 antibodies from 27 providers.
DR DNASU; 51138; -.
DR Ensembl; ENST00000264389.7; ENSP00000264389.2; ENSG00000138663.9. [Q9BT78-1]
DR Ensembl; ENST00000509093.5; ENSP00000425976.1; ENSG00000138663.9. [Q9BT78-2]
DR GeneID; 51138; -.
DR KEGG; hsa:51138; -.
DR MANE-Select; ENST00000264389.7; ENSP00000264389.2; NM_016129.3; NP_057213.2.
DR UCSC; uc003hoa.4; human. [Q9BT78-1]
DR CTD; 51138; -.
DR DisGeNET; 51138; -.
DR GeneCards; COPS4; -.
DR HGNC; HGNC:16702; COPS4.
DR HPA; ENSG00000138663; Low tissue specificity.
DR MIM; 616008; gene.
DR neXtProt; NX_Q9BT78; -.
DR OpenTargets; ENSG00000138663; -.
DR PharmGKB; PA26756; -.
DR VEuPathDB; HostDB:ENSG00000138663; -.
DR eggNOG; KOG1497; Eukaryota.
DR GeneTree; ENSGT00940000153510; -.
DR InParanoid; Q9BT78; -.
DR OMA; KNIMHTV; -.
DR OrthoDB; 866823at2759; -.
DR PhylomeDB; Q9BT78; -.
DR TreeFam; TF101147; -.
DR PathwayCommons; Q9BT78; -.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q9BT78; -.
DR BioGRID-ORCS; 51138; 699 hits in 1103 CRISPR screens.
DR ChiTaRS; COPS4; human.
DR GeneWiki; COPS4; -.
DR GenomeRNAi; 51138; -.
DR Pharos; Q9BT78; Tbio.
DR PRO; PR:Q9BT78; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BT78; protein.
DR Bgee; ENSG00000138663; Expressed in biceps brachii and 211 other tissues.
DR ExpressionAtlas; Q9BT78; baseline and differential.
DR Genevisible; Q9BT78; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0019784; F:deNEDDylase activity; TAS:Reactome.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037754; CSN4.
DR InterPro; IPR041406; CSN4_HTH.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855; PTHR10855; 1.
DR PANTHER; PTHR10855:SF2; PTHR10855:SF2; 1.
DR Pfam; PF18420; CSN4_RPN5_eIF3a; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Nucleus;
KW Reference proteome; Signalosome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..406
FT /note="COP9 signalosome complex subunit 4"
FT /id="PRO_0000120987"
FT DOMAIN 197..366
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 335..406
FT /note="AEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLE
FT KISQTAPEWTAQAMEAQMAQ -> HEKPCQRGISRSNHFVSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046336"
FT CONFLICT 2
FT /note="Missing (in Ref. 1; AAD43021)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> V (in Ref. 2; BAA91555)"
FT /evidence="ECO:0000305"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:4D0P"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4D0P"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 181..197
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 219..235
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 299..315
FT /evidence="ECO:0007829|PDB:4D0P"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:4D0P"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:4D0P"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4D0P"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:4D0P"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4D0P"
SQ SEQUENCE 406 AA; 46269 MW; 4EFF9079058EB609 CRC64;
MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGAE QLEALKAFVE AMVNENVSLV
ISRQLLTDFC THLPNLPDST AKEIYHFTLE KIQPRVISFE EQVASIRQHL ASIYEKEEDW
RNAAQVLVGI PLETGQKQYN VDYKLETYLK IARLYLEDDD PVQAEAYINR ASLLQNESTN
EQLQIHYKVC YARVLDYRRK FIEAAQRYNE LSYKTIVHES ERLEALKHAL HCTILASAGQ
QRSRMLATLF KDERCQQLAA YGILEKMYLD RIIRGNQLQE FAAMLMPHQK ATTADGSSIL
DRAVIEHNLL SASKLYNNIT FEELGALLEI PAAKAEKIAS QMITEGRMNG FIDQIDGIVH
FETREALPTW DKQIQSLCFQ VNNLLEKISQ TAPEWTAQAM EAQMAQ
