CIC1_YEAST
ID CIC1_YEAST Reviewed; 376 AA.
AC P38779; D3DL01;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Proteasome-interacting protein CIC1;
DE AltName: Full=Core interacting component 1;
GN Name=CIC1; Synonyms=NSA3; OrderedLocusNames=YHR052W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, INTERACTION WITH PROTEASOME SUBUNITS, AND SUBCELLULAR LOCATION.
RX PubMed=11500370; DOI=10.1093/emboj/20.16.4423;
RA Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.;
RT "Cic1, an adaptor protein specifically linking the 26S proteasome to its
RT substrate, the SCF component Cdc4.";
RL EMBO J. 20:4423-4431(2001).
RN [5]
RP INTERACTION WITH NOP7.
RX PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA Woolford J.L. Jr.;
RT "Composition and functional characterization of yeast 66S ribosome assembly
RT intermediates.";
RL Mol. Cell 8:505-515(2001).
RN [6]
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 [7]
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).
RN [8]
RP FUNCTION.
RX PubMed=14623999; DOI=10.1261/rna.5130503;
RA Fatica A., Oeffinger M., Tollervey D., Bozzoni I.;
RT "Cic1p/Nsa3p is required for synthesis and nuclear export of 60S ribosomal
RT subunits.";
RL RNA 9:1431-1436(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: An adapter protein that specifically links the 26S proteasome
CC to its substrate CDC4 which is one of the substrate recognition
CC subunits of the SCF E3 ubiquitin ligase complex. Required for turnover
CC of cell cycle regulatory proteins CDC4 and GRR1. Required for synthesis
CC and nuclear export of 60S ribosomal subunits. Required for vegetative
CC growth. {ECO:0000269|PubMed:11500370, ECO:0000269|PubMed:14623999}.
CC -!- SUBUNIT: Interacts with CDC4, PRE4, PRE6, RPT1 and SCL1 as part of the
CC fully assembled 26S proteasome. Interacts with pre-ribosomal particles
CC constituent NOP7. {ECO:0000269|PubMed:11500370,
CC ECO:0000269|PubMed:11583614}.
CC -!- INTERACTION:
CC P38779; P07834: CDC4; NbExp=2; IntAct=EBI-24538, EBI-4434;
CC P38779; P38779: CIC1; NbExp=2; IntAct=EBI-24538, EBI-24538;
CC P38779; P53927: NOP15; NbExp=3; IntAct=EBI-24538, EBI-28853;
CC P38779; P37838: NOP4; NbExp=5; IntAct=EBI-24538, EBI-12122;
CC P38779; P53261: NOP7; NbExp=4; IntAct=EBI-24538, EBI-13145;
CC P38779; P40303: PRE6; NbExp=5; IntAct=EBI-24538, EBI-13980;
CC P38779; P40693: RLP7; NbExp=3; IntAct=EBI-24538, EBI-15415;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11500370,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 45900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U00062; AAB68898.1; -; Genomic_DNA.
DR EMBL; AY557834; AAS56160.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06745.1; -; Genomic_DNA.
DR PIR; S46729; S46729.
DR RefSeq; NP_011919.1; NM_001179182.1.
DR PDB; 3JCT; EM; 3.08 A; K=1-376.
DR PDB; 5Z3G; EM; 3.65 A; H=1-376.
DR PDB; 6C0F; EM; 3.70 A; K=1-376.
DR PDB; 6CB1; EM; 4.60 A; K=1-376.
DR PDB; 6ELZ; EM; 3.30 A; K=1-376.
DR PDB; 6EM1; EM; 3.60 A; K=1-376.
DR PDB; 6EM3; EM; 3.20 A; K=1-376.
DR PDB; 6EM4; EM; 4.10 A; K=1-376.
DR PDB; 6EM5; EM; 4.30 A; K=1-376.
DR PDB; 6M62; EM; 3.20 A; K=1-376.
DR PDB; 6YLX; EM; 3.90 A; K=1-376.
DR PDB; 6YLY; EM; 3.80 A; K=1-376.
DR PDB; 7BTB; EM; 3.22 A; K=1-376.
DR PDB; 7OHP; EM; 3.90 A; K=1-376.
DR PDB; 7OHQ; EM; 3.10 A; K=1-376.
DR PDB; 7OHR; EM; 4.72 A; K=1-376.
DR PDB; 7OHS; EM; 4.38 A; K=1-376.
DR PDB; 7OHV; EM; 3.90 A; K=1-376.
DR PDB; 7OHW; EM; 3.50 A; K=1-376.
DR PDB; 7OHX; EM; 3.30 A; K=1-376.
DR PDBsum; 3JCT; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P38779; -.
DR SMR; P38779; -.
DR BioGRID; 36484; 184.
DR DIP; DIP-6491N; -.
DR IntAct; P38779; 105.
DR MINT; P38779; -.
DR STRING; 4932.YHR052W; -.
DR iPTMnet; P38779; -.
DR MaxQB; P38779; -.
DR PaxDb; P38779; -.
DR PRIDE; P38779; -.
DR EnsemblFungi; YHR052W_mRNA; YHR052W; YHR052W.
DR GeneID; 856449; -.
DR KEGG; sce:YHR052W; -.
DR SGD; S000001094; CIC1.
DR VEuPathDB; FungiDB:YHR052W; -.
DR eggNOG; KOG1685; Eukaryota.
DR HOGENOM; CLU_049748_0_0_1; -.
DR InParanoid; P38779; -.
DR OMA; KPWKEAS; -.
DR BioCyc; YEAST:G3O-31106-MON; -.
DR PRO; PR:P38779; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38779; protein.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IDA:GO_Central.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IBA:GO_Central.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IDA:SGD.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR CDD; cd00403; Ribosomal_L1; 1.
DR InterPro; IPR028365; Cic1_fungi.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR PANTHER; PTHR23105:SF172; PTHR23105:SF172; 1.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Proteasome; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..376
FT /note="Proteasome-interacting protein CIC1"
FT /id="PRO_0000202895"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..376
FT /note="Required for interaction with CDC4"
FT REGION 356..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 240..254
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 376 AA; 42530 MW; 13A2AFA0B927CD98 CRC64;
MAKKSNSKKS TPVSTPSKEK KKVIEKKSST AIPRERVIKA VNELIKFTSK PQDENNEEGN
NGKKNLLEDD EEELKKDLQL IVVNNKSFTG TSKSFKLKLL NVKHSFYKPW KEASATAVKD
FKVLLILKDS DIKKVSEDDL FDQLDSEGIK VDEIICGKDL KTVYKAYEAR NAFISQFSLI
LADDSIVTSL PKLMGGKAYN KVETTPISIR THANKEFSLT TLTNNIKKVY MNQLPVKLPR
GTTLNVHLGN LEWLRPEEFV DNVELISEQL IKAYQIRSIF IKTNRSPVLP LYYNQDVLDE
LEAKKDKIEE THEDDMVTID GVQVHLSTFN KGLMEIANPS ELGSIFSKQI NNAKKRSSSE
LEKESSESEA VKKAKS
