ID   CSN2_SCHPO              Reviewed;         437 AA.
AC   Q9HFR0;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=COP9 signalosome complex subunit 2;
DE            Short=CSN complex subunit 2;
DE            Short=SGN2;
GN   Name=csn2; ORFNames=SPAPB17E12.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11854407; DOI=10.1091/mbc.01-10-0521;
RA   Mundt K.E., Liu C., Carr A.M.;
RT   "Deletion mutants in COP9/signalosome subunits in fission yeast
RT   Schizosaccharomyces pombe display distinct phenotypes.";
RL   Mol. Biol. Cell 13:493-502(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=12695334; DOI=10.1101/gad.1090803;
RA   Liu C., Powell K.A., Mundt K., Wu L., Carr A.M., Caspari T.;
RT   "Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by
RT   both checkpoint-dependent and -independent mechanisms.";
RL   Genes Dev. 17:1130-1140(2003).
CC   -!- FUNCTION: Component of the COP9 signalosome (CSN) complex that acts as
CC       an regulator of the ubiquitin (Ubl) conjugation pathway by mediating
CC       the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-
CC       protein ligase complexes (By similarity). Required, indirectly, for
CC       activation of ribonucleotide reductase through the degradation of the
CC       protein spd1, thereby supplying deoxyribonucleotides for DNA
CC       replication and repair. {ECO:0000250, ECO:0000269|PubMed:12695334}.
CC   -!- SUBUNIT: Component of the COP9 signalosome (CSN) complex composed of at
CC       least csn1, csn2, csn4 and csn5 subunits.
CC       {ECO:0000269|PubMed:11854407}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11854407}. Nucleus
CC       {ECO:0000269|PubMed:11854407}.
CC   -!- SIMILARITY: Belongs to the CSN2 family. {ECO:0000305}.
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DR   EMBL; AF314168; AAG29547.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAD27497.1; -; Genomic_DNA.
DR   RefSeq; NP_001018220.1; NM_001018700.2.
DR   AlphaFoldDB; Q9HFR0; -.
DR   SMR; Q9HFR0; -.
DR   BioGRID; 280496; 54.
DR   IntAct; Q9HFR0; 1.
DR   STRING; 4896.SPAPB17E12.04c.1; -.
DR   MaxQB; Q9HFR0; -.
DR   PaxDb; Q9HFR0; -.
DR   PRIDE; Q9HFR0; -.
DR   EnsemblFungi; SPAPB17E12.04c.1; SPAPB17E12.04c.1:pep; SPAPB17E12.04c.
DR   GeneID; 3361420; -.
DR   KEGG; spo:SPAPB17E12.04c; -.
DR   PomBase; SPAPB17E12.04c; csn2.
DR   VEuPathDB; FungiDB:SPAPB17E12.04c; -.
DR   eggNOG; KOG1464; Eukaryota.
DR   HOGENOM; CLU_028981_0_1_1; -.
DR   InParanoid; Q9HFR0; -.
DR   OMA; EEQYDFE; -.
DR   PhylomeDB; Q9HFR0; -.
DR   Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   PRO; PR:Q9HFR0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0008180; C:COP9 signalosome; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; EXP:PomBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR   GO; GO:0000338; P:protein deneddylation; IMP:PomBase.
DR   InterPro; IPR037750; COPS2.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10678:SF3; PTHR10678:SF3; 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   Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT   CHAIN           1..437
FT                   /note="COP9 signalosome complex subunit 2"
FT                   /id="PRO_0000120977"
FT   DOMAIN          249..418
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ   SEQUENCE   437 AA;  51375 MW;  D36C501FB43B52FA CRC64;
     MSNDFMLEDD ENYDFEFEDD DDDMIEPYVD VENCYYNSKS LKEENPESAL TSFYSIVEKC
     EGEQNEWAFK ALKQITKINF QLKKYDDMLQ SYQRLLGYTN WLSITKNYSE KSIYNIVEYA
     SSCENTEFLE KFYDVTTKAL QNLNNERLML KVLMHVARFL LTQKNYHKFK YLLRQMHELL
     SDENNSVADQ NRGTHLLELY SLEIQMYSDI EDNKRLKELY QSSLRVKTAI PHPRIMGIIR
     ECGGKMHMQE NQWSEAQTNF FESFKSYDEA GSSDRIRVLK YLVLANMLSE SEINPFDSPE
     TQPYKDNPHI IAMTKLVEAY QIRDITAVER ILQTYQHDIL DDDFIRQYVD KILYSIRSQV
     LIELVKPYTS VKLSLLAKKL GVSISIIEQA LVGLIIDERV NGKIDMVNEV FTISQPKNTI
     HNQLVEDVQK LWNTATK