CSN12_YEAST
ID CSN12_YEAST Reviewed; 423 AA.
AC P47130; D6VWQ3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cop9 signalosome complex subunit 12;
GN Name=CSN12; OrderedLocusNames=YJR084W; ORFNames=J1860;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH RRI1; CSN9; RRI2 AND CSI1, IDENTIFICATION IN THE COP9
RP SIGNALOSOME COMPLEX, AND FUNCTION OF THE COP9 SIGNALOSOME COMPLEX.
RX PubMed=12446563; DOI=10.1093/embo-reports/kvf235;
RA Maytal-Kivity V., Piran R., Pick E., Hofmann K., Glickman M.H.;
RT "COP9 signalosome components play a role in the mating pheromone response
RT of S. cerevisiae.";
RL EMBO Rep. 3:1215-1221(2002).
RN [5]
RP INTERACTION WITH RRI1/CSN5; CSN9; RRI2/CSN10 AND CSI1, AND IDENTIFICATION
RP IN THE COP9 SIGNALOSOME COMPLEX.
RX PubMed=12672462; DOI=10.1016/s1357-2725(02)00378-3;
RA Maytal-Kivity V., Pick E., Piran R., Hofmann K., Glickman M.H.;
RT "The COP9 signalosome-like complex in S. cerevisiae and links to other PCI
RT complexes.";
RL Int. J. Biochem. Cell Biol. 35:706-715(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH SEM1 AND THP3.
RX PubMed=19061648; DOI=10.1016/j.molcel.2008.11.012;
RA Wilmes G.M., Bergkessel M., Bandyopadhyay S., Shales M., Braberg H.,
RA Cagney G., Collins S.R., Whitworth G.B., Kress T.L., Weissman J.S.,
RA Ideker T., Guthrie C., Krogan N.J.;
RT "A genetic interaction map of RNA-processing factors reveals links between
RT Sem1/Dss1-containing complexes and mRNA export and splicing.";
RL Mol. Cell 32:735-746(2008).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH SEM1 AND THP3.
RX PubMed=19289793; DOI=10.1083/jcb.200810059;
RA Faza M.B., Kemmler S., Jimeno S., Gonzalez-Aguilera C., Aguilera A.,
RA Hurt E., Panse V.G.;
RT "Sem1 is a functional component of the nuclear pore complex-associated
RT messenger RNA export machinery.";
RL J. Cell Biol. 184:833-846(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH THP3.
RX PubMed=21149575; DOI=10.1128/mcb.01188-10;
RA Jimeno S., Tous C., Garcia-Rubio M.L., Ranes M., Gonzalez-Aguilera C.,
RA Marin A., Aguilera A.;
RT "New suppressors of THO mutations identify Thp3 (Ypr045c)-Csn12 as a
RT protein complex involved in transcription elongation.";
RL Mol. Cell. Biol. 31:674-685(2011).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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. The CSN complex is involved in the regulation
CC of the mating pheromone response. CSN12 forms a complex with THP3 that
CC is recruited to transcribed genes and required for transcription
CC elongation. {ECO:0000269|PubMed:12446563, ECO:0000269|PubMed:19061648,
CC ECO:0000269|PubMed:19289793, ECO:0000269|PubMed:21149575}.
CC -!- SUBUNIT: Component of a COP9 signalosome-like (CSN) complex, composed
CC of RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the
CC complex, it probably interacts directly with RRI1/CSN5, CSN9,
CC RRI2/CSN10 and CSI1. Interacts with SEM1 and THP3.
CC {ECO:0000269|PubMed:12446563, ECO:0000269|PubMed:12672462,
CC ECO:0000269|PubMed:19061648, ECO:0000269|PubMed:19289793,
CC ECO:0000269|PubMed:21149575}.
CC -!- INTERACTION:
CC P47130; Q12468: RRI1; NbExp=3; IntAct=EBI-763, EBI-37511;
CC P47130; Q12049: THP3; NbExp=2; IntAct=EBI-763, EBI-34263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CSN12 family. {ECO:0000305}.
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DR EMBL; Z49584; CAA89611.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39307.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08869.1; -; Genomic_DNA.
DR PIR; S57103; S57103.
DR RefSeq; NP_012617.1; NM_001181741.1.
DR AlphaFoldDB; P47130; -.
DR SMR; P47130; -.
DR BioGRID; 33839; 624.
DR ComplexPortal; CPX-1894; COP9 signalosome complex.
DR DIP; DIP-6710N; -.
DR IntAct; P47130; 10.
DR MINT; P47130; -.
DR STRING; 4932.YJR084W; -.
DR MaxQB; P47130; -.
DR PaxDb; P47130; -.
DR PRIDE; P47130; -.
DR EnsemblFungi; YJR084W_mRNA; YJR084W; YJR084W.
DR GeneID; 853546; -.
DR KEGG; sce:YJR084W; -.
DR SGD; S000003844; YJR084W.
DR VEuPathDB; FungiDB:YJR084W; -.
DR eggNOG; KOG2688; Eukaryota.
DR GeneTree; ENSGT00390000001101; -.
DR HOGENOM; CLU_031567_2_1_1; -.
DR InParanoid; P47130; -.
DR OMA; TYLIPCH; -.
DR BioCyc; YEAST:G3O-31712-MON; -.
DR PRO; PR:P47130; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47130; protein.
DR GO; GO:0008180; C:COP9 signalosome; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0070390; C:transcription export complex 2; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0000338; P:protein deneddylation; IC:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045114; Csn12-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12732; PTHR12732; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Signalosome; Transcription.
FT CHAIN 1..423
FT /note="Cop9 signalosome complex subunit 12"
FT /id="PRO_0000121047"
FT DOMAIN 232..418
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 423 AA; 49482 MW; 750CDA631916A621 CRC64;
MDVDIGCYFE EKRYDDKLLD FIRYDVKTPK KTKYILQRPT ATDEESVRLQ RFYQLGVDLK
LKYSKRRSLK KQGRIKNATE ELLRLANEQL KLFNRIVERE TNWIIYPLWV MAKQLIRLAN
ESSELNKDSI EECGRTIHRS FTICLNDRNP RLNENKKIGC YMFANLEFSI YHRLSNKDMI
KNLVKVLESR VNARDIPPLN KSLAMEHKSQ VVLYNYYLGQ YYGCLENDHE RGFFHLNEAL
LQCPMLYVES TGKFVLQGQM EKIMILLVPL ALLTKRLYPH WDHPVIAGVI TRSKRLSQVY
PTLVRSVISG NLSLYEATAA SHERFFLSQG LHVVITLLRE VVFTRLVQRC WQWGNDRKSI
MPLKILLATK QHDSSANEDE EEQLDALECR LASAIASGLL RAYLSHSNRC IVFSKKEPFP
HSK
