Full text data of COPS4
COPS4
(CSN4)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
COP9 signalosome complex subunit 4; SGN4; Signalosome subunit 4 (JAB1-containing signalosome subunit 4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
COP9 signalosome complex subunit 4; SGN4; Signalosome subunit 4 (JAB1-containing signalosome subunit 4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00171844
IPI00171844 COP9 subunit 4 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 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic and nuclear n/a expected molecular weight found in band at molecular weight
IPI00171844 COP9 subunit 4 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 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic and nuclear n/a expected molecular weight found in band at molecular weight
UniProt
Q9BT78
ID CSN4_HUMAN Reviewed; 406 AA.
AC Q9BT78; B3KN88; B3KST5; Q561W7; Q9NW31; Q9Y677;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 108.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
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=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
RT project: 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;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R.,
RA Schade R., 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.,
RA Pollmann C., Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation
RT by 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
RT RACK1 in fetal Down syndrome brain (trisomy 21), AND MASS
RT 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.,
RA Drapkin R., 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.,
RA Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R.,
RA 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,
RP AND 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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes.
CC The CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the
CC Ubl ligase activity of SCF-type complexes such as SCF, CSA or
CC DDB2. The complex is also involved in phosphorylation of p53/TP53,
CC c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via
CC its association with CK2 and PKD kinases. CSN-dependent
CC phosphorylation of TP53 and JUN promotes and protects degradation
CC by the Ubl system, respectively.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
CC COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
CC COPS8. In the complex, it probably interacts directly with COPS1,
CC COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8.
CC -!- INTERACTION:
CC Q0VDD7:C19orf57; NbExp=2; IntAct=EBI-742413, EBI-741210;
CC P01100:FOS; NbExp=2; IntAct=EBI-742413, EBI-852851;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the CSN4 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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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 RefSeq; NP_001244935.1; NM_001258006.1.
DR RefSeq; NP_057213.2; NM_016129.2.
DR UniGene; Hs.190384; -.
DR ProteinModelPortal; Q9BT78; -.
DR SMR; Q9BT78; 299-366.
DR DIP; DIP-34516N; -.
DR IntAct; Q9BT78; 20.
DR MINT; MINT-1464138; -.
DR STRING; 9606.ENSP00000264389; -.
DR PhosphoSite; Q9BT78; -.
DR DMDM; 55976582; -.
DR OGP; Q9BT78; -.
DR REPRODUCTION-2DPAGE; IPI00171844; -.
DR PaxDb; Q9BT78; -.
DR PeptideAtlas; Q9BT78; -.
DR PRIDE; Q9BT78; -.
DR Ensembl; ENST00000264389; ENSP00000264389; ENSG00000138663.
DR Ensembl; ENST00000509093; ENSP00000425976; ENSG00000138663.
DR GeneID; 51138; -.
DR KEGG; hsa:51138; -.
DR UCSC; uc010ijx.3; human.
DR CTD; 51138; -.
DR GeneCards; GC04P083955; -.
DR HGNC; HGNC:16702; COPS4.
DR HPA; HPA036894; -.
DR neXtProt; NX_Q9BT78; -.
DR PharmGKB; PA26756; -.
DR eggNOG; NOG298640; -.
DR HOGENOM; HOG000158382; -.
DR HOVERGEN; HBG051136; -.
DR InParanoid; Q9BT78; -.
DR KO; K12178; -.
DR OrthoDB; EOG7P02HX; -.
DR PhylomeDB; Q9BT78; -.
DR ChiTaRS; COPS4; human.
DR GeneWiki; COPS4; -.
DR GenomeRNAi; 51138; -.
DR NextBio; 53990; -.
DR PRO; PR:Q9BT78; -.
DR ArrayExpress; Q9BT78; -.
DR Bgee; Q9BT78; -.
DR CleanEx; HS_COPS4; -.
DR Genevestigator; Q9BT78; -.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 406 COP9 signalosome complex subunit 4.
FT /FTId=PRO_0000120987.
FT DOMAIN 201 363 PCI.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 25 25 N6-acetyllysine.
FT VAR_SEQ 335 406 AEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQ
FT SLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ -> HEKPCQ
FT RGISRSNHFVSK (in isoform 2).
FT /FTId=VSP_046336.
FT CONFLICT 2 2 Missing (in Ref. 1).
FT CONFLICT 97 97 I -> V (in Ref. 2; BAA91555).
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
//
ID CSN4_HUMAN Reviewed; 406 AA.
AC Q9BT78; B3KN88; B3KST5; Q561W7; Q9NW31; Q9Y677;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 108.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
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=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
RT project: 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;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R.,
RA Schade R., 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.,
RA Pollmann C., Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation
RT by 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
RT RACK1 in fetal Down syndrome brain (trisomy 21), AND MASS
RT 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.,
RA Drapkin R., 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.,
RA Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R.,
RA 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,
RP AND 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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes.
CC The CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the
CC Ubl ligase activity of SCF-type complexes such as SCF, CSA or
CC DDB2. The complex is also involved in phosphorylation of p53/TP53,
CC c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via
CC its association with CK2 and PKD kinases. CSN-dependent
CC phosphorylation of TP53 and JUN promotes and protects degradation
CC by the Ubl system, respectively.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
CC COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
CC COPS8. In the complex, it probably interacts directly with COPS1,
CC COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8.
CC -!- INTERACTION:
CC Q0VDD7:C19orf57; NbExp=2; IntAct=EBI-742413, EBI-741210;
CC P01100:FOS; NbExp=2; IntAct=EBI-742413, EBI-852851;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the CSN4 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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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 RefSeq; NP_001244935.1; NM_001258006.1.
DR RefSeq; NP_057213.2; NM_016129.2.
DR UniGene; Hs.190384; -.
DR ProteinModelPortal; Q9BT78; -.
DR SMR; Q9BT78; 299-366.
DR DIP; DIP-34516N; -.
DR IntAct; Q9BT78; 20.
DR MINT; MINT-1464138; -.
DR STRING; 9606.ENSP00000264389; -.
DR PhosphoSite; Q9BT78; -.
DR DMDM; 55976582; -.
DR OGP; Q9BT78; -.
DR REPRODUCTION-2DPAGE; IPI00171844; -.
DR PaxDb; Q9BT78; -.
DR PeptideAtlas; Q9BT78; -.
DR PRIDE; Q9BT78; -.
DR Ensembl; ENST00000264389; ENSP00000264389; ENSG00000138663.
DR Ensembl; ENST00000509093; ENSP00000425976; ENSG00000138663.
DR GeneID; 51138; -.
DR KEGG; hsa:51138; -.
DR UCSC; uc010ijx.3; human.
DR CTD; 51138; -.
DR GeneCards; GC04P083955; -.
DR HGNC; HGNC:16702; COPS4.
DR HPA; HPA036894; -.
DR neXtProt; NX_Q9BT78; -.
DR PharmGKB; PA26756; -.
DR eggNOG; NOG298640; -.
DR HOGENOM; HOG000158382; -.
DR HOVERGEN; HBG051136; -.
DR InParanoid; Q9BT78; -.
DR KO; K12178; -.
DR OrthoDB; EOG7P02HX; -.
DR PhylomeDB; Q9BT78; -.
DR ChiTaRS; COPS4; human.
DR GeneWiki; COPS4; -.
DR GenomeRNAi; 51138; -.
DR NextBio; 53990; -.
DR PRO; PR:Q9BT78; -.
DR ArrayExpress; Q9BT78; -.
DR Bgee; Q9BT78; -.
DR CleanEx; HS_COPS4; -.
DR Genevestigator; Q9BT78; -.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010388; P:cullin deneddylation; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Reference proteome; Signalosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 406 COP9 signalosome complex subunit 4.
FT /FTId=PRO_0000120987.
FT DOMAIN 201 363 PCI.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 25 25 N6-acetyllysine.
FT VAR_SEQ 335 406 AEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQ
FT SLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ -> HEKPCQ
FT RGISRSNHFVSK (in isoform 2).
FT /FTId=VSP_046336.
FT CONFLICT 2 2 Missing (in Ref. 1).
FT CONFLICT 97 97 I -> V (in Ref. 2; BAA91555).
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
//