UTP25_YEAST
ID UTP25_YEAST Reviewed; 721 AA.
AC P40498; D6VVJ6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=U3 small nucleolar RNA-associated protein 25;
DE Short=U3 snoRNA-associated protein 25;
DE AltName: Full=U three protein 25;
GN Name=UTP25; OrderedLocusNames=YIL091C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-63, AND
RP IDENTIFICATION BY 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).
RN [7]
RP IDENTIFICATION IN THE SSU PROCESSOME, FUNCTION, AND INTERACTION WITH U3
RP SNORNA; MMP10; RRP9; UTP8 AND UTP18.
RX PubMed=20884785; DOI=10.1261/rna.2359810;
RA Charette J.M., Baserga S.J.;
RT "The DEAD-box RNA helicase-like Utp25 is an SSU processome component.";
RL RNA 16:2156-2169(2010).
RN [8]
RP INTERACTION WITH NOP19, AND FUNCTION.
RX PubMed=21941128; DOI=10.4161/rna.8.6.17699;
RA Choque E., Marcellin M., Burlet-Schiltz O., Gadal O., Dez C.;
RT "The nucleolar protein Nop19p interacts preferentially with Utp25p and
RT Dhr2p and is essential for the production of the 40S ribosomal subunit in
RT Saccharomyces cerevisiae.";
RL RNA Biol. 8:1158-1172(2011).
CC -!- FUNCTION: DEAD-box RNA helicase-like protein required for pre-18S rRNA
CC processing, specifically at sites A0, A1, and A2.
CC {ECO:0000269|PubMed:20884785, ECO:0000269|PubMed:21941128}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10, NOP19, RRP9,
CC UTP8 and UTP18. Component of the ribosomal small subunit (SSU)
CC processome composed of at least 40 protein subunits and snoRNA U3.
CC {ECO:0000269|PubMed:20884785, ECO:0000269|PubMed:21941128}.
CC -!- INTERACTION:
CC P40498; P36009: DHR2; NbExp=2; IntAct=EBI-25113, EBI-5844;
CC P40498; P47083: MPP10; NbExp=6; IntAct=EBI-25113, EBI-11168;
CC P40498; Q12481: RRP36; NbExp=2; IntAct=EBI-25113, EBI-31770;
CC P40498; Q12136: SAS10; NbExp=7; IntAct=EBI-25113, EBI-36084;
CC P40498; P53254: UTP22; NbExp=2; IntAct=EBI-25113, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UTP25 family. {ECO:0000305}.
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DR EMBL; Z46728; CAA86703.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08462.1; -; Genomic_DNA.
DR PIR; S49789; S49789.
DR RefSeq; NP_012175.1; NM_001179439.1.
DR AlphaFoldDB; P40498; -.
DR BioGRID; 34901; 144.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-5629N; -.
DR IntAct; P40498; 18.
DR MINT; P40498; -.
DR STRING; 4932.YIL091C; -.
DR iPTMnet; P40498; -.
DR MaxQB; P40498; -.
DR PaxDb; P40498; -.
DR PRIDE; P40498; -.
DR EnsemblFungi; YIL091C_mRNA; YIL091C; YIL091C.
DR GeneID; 854717; -.
DR KEGG; sce:YIL091C; -.
DR SGD; S000001353; UTP25.
DR VEuPathDB; FungiDB:YIL091C; -.
DR eggNOG; KOG2340; Eukaryota.
DR GeneTree; ENSGT00390000000709; -.
DR HOGENOM; CLU_018705_0_1_1; -.
DR InParanoid; P40498; -.
DR OMA; KYFRQTI; -.
DR BioCyc; YEAST:G3O-31351-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40498; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40498; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010678; UTP25.
DR PANTHER; PTHR12933; PTHR12933; 1.
DR Pfam; PF06862; UTP25; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..721
FT /note="U3 small nucleolar RNA-associated protein 25"
FT /id="PRO_0000202974"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 721 AA; 83991 MW; 301BC87BCA027104 CRC64;
MSDSSVREKN DNFRGYRKRG RQELRKIKRS SARTEGGSTE TLEDVAEDID HRSDEDEVSD
VDSGDDFDIE DEEGKKEKVY DALLTILKSE HPEPKRRRRE ADESNKAPAE VGEDEHENTE
HGPVDDQLEI ENGLLGNHED DNDDDSSGDE KDIDSEDEQD PFESHFNQVP EKFVDKLSNA
FKTKSVKYKS VKGSLSDSES YIYAKPVVIG EEALVESPYR SSSIYSYFLK QRLKVQNGLL
DKKTDPLTAL QKKLVDPMFQ YKDILYEYDS YEKDEDEYRD LYALHVLNHI YKTRDRILKN
NQRLQDNPDT EHLDQGFTRP KVLIVVPTRE VAYRVVDKII SKSGIDQVDK KGKFYDQFRD
DSLPPKSKPK SFQHIFRGNT NDFFVVGLKF TRKAIKLYSN FYQSDIIVCS PLGIQMILEN
TDKKKRQDDF LSSIELMVID QLHSIEYQNI SHIFTIFDHL NKIPDQQHEA DFSRIRMWYI
NEQAKLFRQT MVFTKYISPA ANSLINGRCR NMAGRWKNHK VIGSENSSIG QSGLKIRQIF
QRFDIIGNSI IEEPDYRFKF FTSVIIPGIV KSTGYEDGIL IYIPDYTDFI RIRNYMKEKT
TILFGDINEY SSQRQLNANR SLFQQGRLKV MLYTERLHHY RRYEIKGVKS VVFYKPPNNP
EFYNEVVRFI GKNAFLGNTD LNISTVRCIY SKLDGLSLER IVGTKRAAVL SHAQKEIYEF
K
