SSF1_YEAST
ID SSF1_YEAST Reviewed; 453 AA.
AC P38789; D3DL15;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ribosome biogenesis protein SSF1;
GN Name=SSF1; OrderedLocusNames=YHR066W;
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=7748491; DOI=10.1089/dna.1995.14.411;
RA Yu Y., Hirsch J.P.;
RT "An essential gene pair in Saccharomyces cerevisiae with a potential role
RT in mating.";
RL DNA Cell Biol. 14:411-418(1995).
RN [2]
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 [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.
RX PubMed=11864607; DOI=10.1016/s1097-2765(02)00458-6;
RA Fatica A., Cronshaw A.D., Dlakic M., Tollervey D.;
RT "Ssf1p prevents premature processing of an early pre-60S ribosomal
RT particle.";
RL Mol. Cell 9:341-351(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12702244; DOI=10.1111/j.1567-1364.2003.tb00136.x;
RA Bogengruber E., Briza P., Doppler E., Wimmer H., Koller L., Fasiolo F.,
RA Senger B., Hegemann J.H., Breitenbach M.;
RT "Functional analysis in yeast of the Brix protein superfamily involved in
RT the biogenesis of ribosomes.";
RL FEMS Yeast Res. 3:35-43(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-301, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-301, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Required for biogenesis of the 60S ribosomal subunit.
CC {ECO:0000269|PubMed:11864607, ECO:0000269|PubMed:12702244}.
CC -!- SUBUNIT: Part of a complex that includes BRX1, RPF1, RPF2 and SSF1 or
CC SSF2.
CC -!- INTERACTION:
CC P38789; P36049: EBP2; NbExp=3; IntAct=EBI-18160, EBI-6289;
CC P38789; Q06511: RRP15; NbExp=4; IntAct=EBI-18160, EBI-34602;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12702244}.
CC -!- MISCELLANEOUS: Present with 8150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18113; AAA79980.1; -; Genomic_DNA.
DR EMBL; U00061; AAB68379.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06759.1; -; Genomic_DNA.
DR PIR; S46700; S46700.
DR RefSeq; NP_011933.1; NM_001179196.1.
DR PDB; 6C0F; EM; 3.70 A; v=1-453.
DR PDBsum; 6C0F; -.
DR AlphaFoldDB; P38789; -.
DR SMR; P38789; -.
DR BioGRID; 36498; 341.
DR DIP; DIP-6501N; -.
DR IntAct; P38789; 51.
DR MINT; P38789; -.
DR STRING; 4932.YHR066W; -.
DR iPTMnet; P38789; -.
DR MaxQB; P38789; -.
DR PaxDb; P38789; -.
DR PRIDE; P38789; -.
DR EnsemblFungi; YHR066W_mRNA; YHR066W; YHR066W.
DR GeneID; 856463; -.
DR KEGG; sce:YHR066W; -.
DR SGD; S000001108; SSF1.
DR VEuPathDB; FungiDB:YHR066W; -.
DR eggNOG; KOG2963; Eukaryota.
DR GeneTree; ENSGT00530000064158; -.
DR HOGENOM; CLU_026936_2_0_1; -.
DR InParanoid; P38789; -.
DR OMA; MWHEYIH; -.
DR BioCyc; YEAST:G3O-31117-MON; -.
DR PRO; PR:P38789; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38789; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR045112; PPAN-like.
DR PANTHER; PTHR12661; PTHR12661; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..453
FT /note="Ribosome biogenesis protein SSF1"
FT /id="PRO_0000120259"
FT DOMAIN 26..348
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 453 AA; 51764 MW; 6F0344993BEF2217 CRC64;
MAKRRQKKRT HAQLTPEQEQ GIPKSMVIRV GQTSLANHSL NQLVKDFRQI MQPHTAIKLK
ERKSNKLKDF VVMCGPLGVT HLFMFTQSEK TGNVSLKIAR TPQGPTVTFQ VLDYSLGRDI
KKFLKRPKSL NNDDVLNPPL LVLNGFSTSK RSGEDDQDVN VEKVIVSMFQ NIFPPLNPAR
TSLNSIKRVF MINKDRETGE ISMRHYFIDI REVEISRNLK RLYKAKNNLS KTVPNLHRKE
DISSLILDHD LGAYTSESEI EDDAIVRVVD NQDVKAKHSQ SLKSQRTPVE KKDNKEREKE
TEEEDVEMEE PKPSENLQPT PRKKAIKLTE LGPRLTLKLV KIEEGICSGK VLHHEFVQKS
SEEIKALEKR HAAKMRLKEQ RKKEQEENIA KKKAVKDAKK QRKLERRKAR AAEGGEGQGK
DDAMSDDESS SSDSEHYGSV PEDLDSDLFS EVE
