CSN4_MOUSE
ID CSN4_MOUSE Reviewed; 406 AA.
AC O88544;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN THE CSN COMPLEX.
RX PubMed=9707402; DOI=10.1016/s0960-9822(07)00372-7;
RA Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M., Deng X.-W.;
RT "The COP9 complex is conserved between plants and mammals and is related to
RT the 26S proteasome regulatory complex.";
RL Curr. Biol. 8:919-922(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 96-107; 154-170 AND 228-242, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP STRUCTURE BY NMR OF 296-366.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PCI domain.";
RL Submitted (JUN-2004) to the PDB data bank.
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes (By
CC similarity). The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By
CC similarity). Also involved in the deneddylation of non-cullin subunits
CC such as STON2 (By similarity). The complex is also involved in
CC phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1,
CC IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD
CC kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively (By
CC similarity). {ECO:0000250|UniProtKB:Q9BT78}.
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 (PubMed:9707402). In the complex, it probably interacts directly with
CC COPS1, COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8
CC (By similarity). Interacts with TOR1A; the interaction is direct and
CC associates TOR1A and SNAPIN with the CSN complex (By similarity).
CC Interacts with STON2; controls STON2 neddylation levels (By
CC similarity). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BT78, ECO:0000269|PubMed:9707402}.
CC -!- INTERACTION:
CC O88544; Q9QXJ2: Stat2; NbExp=6; IntAct=EBI-646659, EBI-646643;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BT78}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BT78}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:Q9BT78}.
CC -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR EMBL; AF071314; AAC33901.1; -; mRNA.
DR EMBL; AK009955; BAB26607.1; -; mRNA.
DR CCDS; CCDS19463.1; -.
DR RefSeq; NP_036131.1; NM_012001.2.
DR PDB; 1UFM; NMR; -; A=296-366.
DR PDBsum; 1UFM; -.
DR AlphaFoldDB; O88544; -.
DR SMR; O88544; -.
DR BioGRID; 205043; 36.
DR CORUM; O88544; -.
DR IntAct; O88544; 3.
DR STRING; 10090.ENSMUSP00000048416; -.
DR iPTMnet; O88544; -.
DR PhosphoSitePlus; O88544; -.
DR SwissPalm; O88544; -.
DR REPRODUCTION-2DPAGE; O88544; -.
DR EPD; O88544; -.
DR jPOST; O88544; -.
DR PaxDb; O88544; -.
DR PeptideAtlas; O88544; -.
DR PRIDE; O88544; -.
DR ProteomicsDB; 285377; -.
DR Antibodypedia; 14119; 135 antibodies from 27 providers.
DR DNASU; 26891; -.
DR Ensembl; ENSMUST00000045993; ENSMUSP00000048416; ENSMUSG00000035297.
DR GeneID; 26891; -.
DR KEGG; mmu:26891; -.
DR UCSC; uc008yhs.2; mouse.
DR CTD; 51138; -.
DR MGI; MGI:1349414; Cops4.
DR VEuPathDB; HostDB:ENSMUSG00000035297; -.
DR eggNOG; KOG1497; Eukaryota.
DR GeneTree; ENSGT00940000153510; -.
DR HOGENOM; CLU_028132_1_0_1; -.
DR InParanoid; O88544; -.
DR OMA; KNIMHTV; -.
DR OrthoDB; 866823at2759; -.
DR PhylomeDB; O88544; -.
DR TreeFam; TF101147; -.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 26891; 28 hits in 73 CRISPR screens.
DR ChiTaRS; Cops4; mouse.
DR EvolutionaryTrace; O88544; -.
DR PRO; PR:O88544; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O88544; protein.
DR Bgee; ENSMUSG00000035297; Expressed in spermatid and 266 other tissues.
DR ExpressionAtlas; O88544; baseline and differential.
DR Genevisible; O88544; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0000338; P:protein deneddylation; ISS:UniProtKB.
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; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Nucleus; Reference proteome; Signalosome;
KW Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BT78"
FT CHAIN 2..406
FT /note="COP9 signalosome complex subunit 4"
FT /id="PRO_0000120988"
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:0000250|UniProtKB:Q9BT78"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BT78"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:1UFM"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1UFM"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:1UFM"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:1UFM"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1UFM"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:1UFM"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1UFM"
SQ SEQUENCE 406 AA; 46285 MW; 9584559823F99EB4 CRC64;
MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGTE QLEALKAFVE AMVNENVSLV
ISRQLLTDFC THLPNLPDST AKEVYHFTLE 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
