ID   UTP11_YEAST             Reviewed;         250 AA.
AC   P34247; D6VXI8;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   02-SEP-2026, entry version 167.
DE   RecName: Full=U3 small nucleolar RNA-associated protein 11;
DE            Short=U3 snoRNA-associated protein 11;
DE   AltName: Full=U three protein 11;
GN   Name=UTP11; OrderedLocusNames=YKL099C; ORFNames=YKL449;
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=8256524; DOI=10.1002/yea.320091016;
RA   Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA   Bolotin-Fukuhara M.;
RT   "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT   physically localizes the MRB1 gene and reveals eight new open reading
RT   frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL   Yeast 9:1149-1155(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(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, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP   PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=12068309; DOI=10.1038/nature00769;
RA   Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA   Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA   Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT   "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT   biogenesis.";
RL   Nature 417:967-970(2002).
RN   [5]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [6]
RP   INTERACTION WITH EBP2; FAF1 AND RPS16A.
RX   PubMed=15078877; DOI=10.1074/jbc.m403338200;
RA   Shirai C., Takai T., Nariai M., Horigome C., Mizuta K.;
RT   "Ebp2p, the yeast homolog of Epstein-Barr virus nuclear antigen 1-binding
RT   protein 2, interacts with factors of both the 60 S and the 40 s ribosomal
RT   subunit assembly.";
RL   J. Biol. Chem. 279:25353-25358(2004).
RN   [7]
RP   INTERACTION WITH RRP14.
RX   PubMed=17804645; DOI=10.1261/rna.553807;
RA   Yamada H., Horigome C., Okada T., Shirai C., Mizuta K.;
RT   "Yeast Rrp14p is a nucleolar protein involved in both ribosome biogenesis
RT   and cell polarity.";
RL   RNA 13:1977-1987(2007).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       {ECO:0000269|PubMed:12068309}.
CC   -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome
CC       composed of at least 40 protein subunits and snoRNA U3. Interacts with
CC       snoRNA U3. Interacts with EBP2, FAF1, MPP10, RPS16A and RRP14.
CC       {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15078877,
CC       ECO:0000269|PubMed:17804645}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
CC   -!- SIMILARITY: Belongs to the UTP11 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA50458.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA81939.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X71133; CAA50458.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z28099; CAA81939.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006944; DAA09058.1; -; Genomic_DNA.
DR   PIR; S37926; S37926.
DR   RefSeq; NP_012823.2; NM_001179665.1.
DR   PDB; 5WLC; EM; 3.80 A; SY=1-250.
DR   PDB; 6KE6; EM; 3.40 A; 5D=1-250.
DR   PDB; 6LQP; EM; 3.20 A; 5D=1-250.
DR   PDB; 6LQQ; EM; 4.10 A; 5D=1-250.
DR   PDB; 6LQR; EM; 8.60 A; 5D=1-250.
DR   PDB; 6LQS; EM; 3.80 A; 5D=1-250.
DR   PDB; 6LQT; EM; 4.90 A; 5D=1-250.
DR   PDB; 6LQU; EM; 3.70 A; 5D=1-250.
DR   PDB; 6LQV; EM; 4.80 A; 5D=1-250.
DR   PDB; 6ZQA; EM; 4.40 A; UK=1-250.
DR   PDB; 6ZQB; EM; 3.90 A; UK=1-250.
DR   PDB; 6ZQC; EM; 3.80 A; UK=1-250.
DR   PDB; 6ZQD; EM; 3.80 A; UK=1-250.
DR   PDB; 6ZQE; EM; 7.10 A; UK=1-250.
DR   PDB; 7AJT; EM; 4.60 A; UK=1-250.
DR   PDB; 7AJU; EM; 3.80 A; UK=1-250.
DR   PDB; 7D4I; EM; 4.00 A; 5D=1-250.
DR   PDB; 7D5S; EM; 4.60 A; 5D=1-250.
DR   PDB; 7D5T; EM; 6.00 A; 5D=1-250.
DR   PDB; 7D63; EM; 12.30 A; 5D=1-250.
DR   PDB; 7SUK; EM; 3.99 A; SY=3-250.
DR   PDB; 9G33; EM; 3.05 A; UK=1-250.
DR   PDB; 9N6V; EM; 3.16 A; SY=1-250.
DR   PDB; 9N6W; EM; 3.05 A; SY=1-250.
DR   PDB; 9N6X; EM; 3.71 A; SY=1-250.
DR   PDB; 9N6Y; EM; 3.65 A; SY=1-250.
DR   PDB; 9N6Z; EM; 4.74 A; SY=1-250.
DR   PDB; 9N70; EM; 5.17 A; SY=1-250.
DR   PDB; 9N72; EM; 5.94 A; SY=1-250.
DR   PDB; 9N73; EM; 5.96 A; SY=1-250.
DR   PDB; 9N74; EM; 2.65 A; SY=1-250.
DR   PDB; 9N75; EM; 3.01 A; SY=1-250.
DR   PDB; 9N76; EM; 4.20 A; SY=1-250.
DR   PDB; 9N77; EM; 3.94 A; SY=1-250.
DR   PDB; 9N78; EM; 4.17 A; SY=1-250.
DR   AlphaFoldDB; P34247; -.
DR   EMDB; EMD-0949; -.
DR   EMDB; EMD-0950; -.
DR   EMDB; EMD-0951; -.
DR   EMDB; EMD-0952; -.
DR   EMDB; EMD-0953; -.
DR   EMDB; EMD-0954; -.
DR   EMDB; EMD-0955; -.
DR   EMDB; EMD-11357; -.
DR   EMDB; EMD-11358; -.
DR   EMDB; EMD-11359; -.
DR   EMDB; EMD-11360; -.
DR   EMDB; EMD-11361; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-30584; -.
DR   EMDB; EMD-30585; -.
DR   EMDB; EMD-30588; -.
DR   EMDB; EMD-49075; -.
DR   EMDB; EMD-49076; -.
DR   EMDB; EMD-49077; -.
DR   EMDB; EMD-49078; -.
DR   EMDB; EMD-49079; -.
DR   EMDB; EMD-49080; -.
DR   EMDB; EMD-49082; -.
DR   EMDB; EMD-49083; -.
DR   EMDB; EMD-49084; -.
DR   EMDB; EMD-49085; -.
DR   EMDB; EMD-49086; -.
DR   EMDB; EMD-49087; -.
DR   EMDB; EMD-49088; -.
DR   EMDB; EMD-50991; -.
DR   EMDB; EMD-9964; -.
DR   SMR; P34247; -.
DR   BioGRID; 34034; 107.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome.
DR   DIP; DIP-6569N; -.
DR   FunCoup; P34247; 874.
DR   IntAct; P34247; 77.
DR   MINT; P34247; -.
DR   STRING; 4932.YKL099C; -.
DR   iPTMnet; P34247; -.
DR   PaxDb; 4932-YKL099C; -.
DR   PeptideAtlas; P34247; -.
DR   EnsemblFungi; YKL099C_mRNA; YKL099C; YKL099C.
DR   GeneID; 853762; -.
DR   KEGG; sce:YKL099C; -.
DR   AGR; SGD:S000001582; -.
DR   SGD; S000001582; UTP11.
DR   VEuPathDB; FungiDB:YKL099C; -.
DR   eggNOG; KOG3237; Eukaryota.
DR   HOGENOM; CLU_061887_0_2_1; -.
DR   InParanoid; P34247; -.
DR   OMA; DLKYVVM; -.
DR   OrthoDB; 29058at2759; -.
DR   BioCyc; YEAST:G3O-31889-MONOMER; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 853762; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P34247; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P34247; protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; NAS:UniProtKB.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal.
DR   GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR   GO; GO:0006412; P:translation; IMP:UniProtKB.
DR   InterPro; IPR007144; SSU_processome_Utp11.
DR   PANTHER; PTHR12838; U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 11; 1.
DR   PANTHER; PTHR12838:SF0; U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 11-RELATED; 1.
DR   Pfam; PF03998; Utp11; 1.
DR   PIRSF; PIRSF015952; U3snoRNP11; 1.
DR   PDBsum; 5WLC; -.
DR   PDBsum; 6KE6; -.
DR   PDBsum; 6LQP; -.
DR   PDBsum; 6LQQ; -.
DR   PDBsum; 6LQR; -.
DR   PDBsum; 6LQS; -.
DR   PDBsum; 6LQT; -.
DR   PDBsum; 6LQU; -.
DR   PDBsum; 6LQV; -.
DR   PDBsum; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   PDBsum; 7D5S; -.
DR   PDBsum; 7D5T; -.
DR   PDBsum; 7D63; -.
DR   PDBsum; 7SUK; -.
DR   PDBsum; 9G33; -.
DR   PDBsum; 9N6V; -.
DR   PDBsum; 9N6W; -.
DR   PDBsum; 9N6X; -.
DR   PDBsum; 9N6Y; -.
DR   PDBsum; 9N6Z; -.
DR   PDBsum; 9N70; -.
DR   PDBsum; 9N72; -.
DR   PDBsum; 9N73; -.
DR   PDBsum; 9N74; -.
DR   PDBsum; 9N75; -.
DR   PDBsum; 9N76; -.
DR   PDBsum; 9N77; -.
DR   PDBsum; 9N78; -.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..250
FT                   /note="U3 small nucleolar RNA-associated protein 11"
FT                   /id="PRO_0000211052"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..10
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   TURN            7..10
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           11..16
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           20..25
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           31..57
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:6KE6"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:6LQP"
FT   HELIX           93..124
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:6KE6"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           140..144
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           148..152
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           156..159
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   HELIX           187..224
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:9G33"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:6LQP"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:9G33"
SQ   SEQUENCE   250 AA;  29735 MW;  AA013651708C4DB6 CRC64;
     MAKLVHDVQK KQHRERSQLT SRSRYGFLEK HKDYVKRAQD FHRKQSTLKV LREKAKERNP
     DEYYHAMHSR KTDAKGLLIS SRHGDEEDES LSMDQVKLLK TQDSNYVRTL RQIELKKLEK
     GAKQLMFKSS GNHTIFVDSR EKMNEFTPEK FFNTTSEMVN RSENRLTKDQ LAQDISNNRN
     ASSIMPKESL DKKKLKKFKQ VKQHLQRETQ LKQVQQRMDA QRELLKKGSK KKIVDSSGKI
     SFKWKKQRKR
//