CSN10_YEAST
ID CSN10_YEAST Reviewed; 645 AA.
AC Q12348; D6W1V0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=COP9 signalosome complex subunit 10;
GN Name=RRI2; Synonyms=CSN10; OrderedLocusNames=YOL117W;
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].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 FUNCTION OF THE COP9 SIGNALOSOME COMPLEX.
RX PubMed=12186635; DOI=10.1186/1471-2156-3-15;
RA Wee S., Hetfeld B., Dubiel W., Wolf D.A.;
RT "Conservation of the COP9/signalosome in budding yeast.";
RL BMC Genet. 3:15-15(2002).
RN [5]
RP INTERACTION WITH CSN12, IDENTIFICATION IN THE COP9 SIGNALOSOME COMPLEX, AND
RP 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 [6]
RP INTERACTION WITH RRI1/CSN5, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C.,
RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA Neubauer G., Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis of
RT protein complexes.";
RL Nature 415:141-147(2002).
RN [7]
RP INTERACTION WITH CSN12, AND IDENTIFICATION 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 [8]
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 [9]
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. {ECO:0000269|PubMed:12186635,
CC ECO:0000269|PubMed:12446563}.
CC -!- SUBUNIT: Component of a COP9 signalosome-like (CSN) complex, composed
CC of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In
CC the complex, it probably interacts directly with CSN12.
CC {ECO:0000269|PubMed:11805826, ECO:0000269|PubMed:12446563,
CC ECO:0000269|PubMed:12672462}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14562095}. Nucleus
CC {ECO:0000305|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1320 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48149; CAA88143.1; -; Genomic_DNA.
DR EMBL; Z74859; CAA99136.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10666.1; -; Genomic_DNA.
DR PIR; S51880; S51880.
DR RefSeq; NP_014524.1; NM_001183371.1.
DR AlphaFoldDB; Q12348; -.
DR BioGRID; 34283; 63.
DR ComplexPortal; CPX-1894; COP9 signalosome complex.
DR DIP; DIP-4212N; -.
DR IntAct; Q12348; 6.
DR MINT; Q12348; -.
DR STRING; 4932.YOL117W; -.
DR iPTMnet; Q12348; -.
DR PaxDb; Q12348; -.
DR PRIDE; Q12348; -.
DR TopDownProteomics; Q12348; -.
DR EnsemblFungi; YOL117W_mRNA; YOL117W; YOL117W.
DR GeneID; 854032; -.
DR KEGG; sce:YOL117W; -.
DR SGD; S000005477; RRI2.
DR VEuPathDB; FungiDB:YOL117W; -.
DR eggNOG; ENOG502RXR9; Eukaryota.
DR HOGENOM; CLU_031729_0_0_1; -.
DR InParanoid; Q12348; -.
DR OMA; DFMMSDD; -.
DR BioCyc; YEAST:G3O-33514-MON; -.
DR PRO; PR:Q12348; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12348; protein.
DR GO; GO:0008180; C:COP9 signalosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IGI:SGD.
DR GO; GO:0000338; P:protein deneddylation; IMP:SGD.
DR InterPro; IPR000717; PCI_dom.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT CHAIN 1..645
FT /note="COP9 signalosome complex subunit 10"
FT /id="PRO_0000121024"
FT DOMAIN 348..543
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 76388 MW; ADCEEF9BCE27D83B CRC64;
MSDEDNNYDD FMLSDDEGME SIEMEEETDD EDKQNIEINE DNSQDDQDRG AARHKQHEQG
TFEKHDRVED ICERIFEQGQ ALKEDERYKE ARDLFLKIYY KEEFSSDESI ERLMTWKFKS
LIEILRLRAL QLYFQKNGAQ DLVLQILEDT ATMSVFLQRI DFQIDGNIFE LLSDTFEVLA
PKWERVFLFD IEKVDRENMI CKIDFQKNFM DQFQWILRKP GKDCKLQNLQ RIIRKKIFIA
VVWYQRLTMG NVFTPEISSQ IEILVKDNEC SSFEENNDLE SVSMLLQYYI LEYMNTARIN
NRRLFKKCID FFEMLISKSL TFSQESGLMV ILYTSKIVFI LDSDSENDLS FALMRYYDRK
EELKNMFLYI LKHLEEMGKL RERDITSLFH KFILSGFIFT SMILEAISTD KINPFGFEQV
KIALGSPIVN VLEDVYRCFA QLELRQLNAS ISLIPELSVV LSGIIQDIYY LAQTLKLWRK
IARLYSCISI SDIISMLQIS DDNEMTRDDL LTILMRSIMK NRSVVYFKLD LTSDLVYFGD
ENKVMLPRCS KEEFRLMISP KDEETTEKAR LIDFEYVNDV AIYNNPTRIR TKSSKEFFNT
LRKSRETVKL PRVSNQSNED TFLPSYMKFS NKYLELCKLA SNNLE
