MPP10_YEAST
ID MPP10_YEAST Reviewed; 593 AA.
AC P47083; D6VWH6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=U3 small nucleolar RNA-associated protein MPP10;
DE Short=U3 snoRNA-associated protein MPP10;
DE AltName: Full=M phase phosphoprotein 10;
GN Name=MPP10; OrderedLocusNames=YJR002W; ORFNames=J1411, YJR83.5;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9315638; DOI=10.1128/mcb.17.10.5803;
RA Dunbar D.A., Wormsley S., Agentis T.M., Baserga S.J.;
RT "Mpp10p, a U3 small nucleolar ribonucleoprotein component required for pre-
RT 18S rRNA processing in yeast.";
RL Mol. Cell. Biol. 17:5803-5812(1997).
RN [4]
RP INTERACTION WITH NOP1; RRP5; UTP1-UTP17 AND SNORNA U3, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
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 INTERACTION WITH EMG1; KRR1; NOC4; RPS4A; RPS4B; RPS6A; RPS6B; RPS7A;
RP RPS7B; RPS9A; RPS9B; RPS14A; RPS14B; UTP18; UTP20; UTP21 AND UTP22.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH IMP3 AND IMP4.
RX PubMed=15489263; DOI=10.1073/pnas.0406819101;
RA Gerczei T., Correll C.C.;
RT "Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-
RT rRNA) duplexes, possibly to recruit the small subunit processome to the
RT pre-rRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15301-15306(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-177, AND
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-177, AND
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-177 AND TYR-181, 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 [11]
RP INTERACTION WITH UTP25.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC Required for the early cleavages at sites A0, A1 and A2 during 18S
CC ribosomal pre-RNA processing. {ECO:0000269|PubMed:15489263,
CC ECO:0000269|PubMed:9315638}.
CC -!- SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4
CC and MPP10. Interacts with snoRNA U3. Component of the ribosomal small
CC subunit (SSU) processome composed of at least 40 protein subunits and
CC snoRNA U3. Interacts with the SSU processome subunits EMG1, IMP3, IMP4,
CC KRR1, NOC4/UTP19, NOP1, RPS4A, RPS4B, RPS6A, RPS6B, RPS7A, RPS7B,
CC RPS9A, RPS9B, RPS14A, RPS14B, UTP1-UTP18, UTP20-UTP22 and UTP25.
CC {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15489263,
CC ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:20884785}.
CC -!- INTERACTION:
CC P47083; Q06631: BFR2; NbExp=8; IntAct=EBI-11168, EBI-36432;
CC P47083; Q04217: ECM16; NbExp=2; IntAct=EBI-11168, EBI-1820;
CC P47083; Q03532: HAS1; NbExp=3; IntAct=EBI-11168, EBI-8170;
CC P47083; P32899: IMP3; NbExp=7; IntAct=EBI-11168, EBI-9237;
CC P47083; P53941: IMP4; NbExp=7; IntAct=EBI-11168, EBI-9243;
CC P47083; P47083: MPP10; NbExp=2; IntAct=EBI-11168, EBI-11168;
CC P47083; Q99207: NOP14; NbExp=6; IntAct=EBI-11168, EBI-35157;
CC P47083; Q12136: SAS10; NbExp=10; IntAct=EBI-11168, EBI-36084;
CC P47083; P42945: UTP10; NbExp=7; IntAct=EBI-11168, EBI-1884;
CC P47083; P53254: UTP22; NbExp=4; IntAct=EBI-11168, EBI-1878;
CC P47083; P40498: UTP25; NbExp=6; IntAct=EBI-11168, EBI-25113;
CC P47083; Q02354: UTP6; NbExp=9; IntAct=EBI-11168, EBI-22119;
CC P47083; P53276: UTP8; NbExp=5; IntAct=EBI-11168, EBI-23301;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:9315638}.
CC -!- SIMILARITY: Belongs to the MPP10 family. {ECO:0000305}.
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DR EMBL; X87611; CAA60923.1; -; Genomic_DNA.
DR EMBL; Z49502; CAA89524.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08792.1; -; Genomic_DNA.
DR PIR; S55189; S55189.
DR RefSeq; NP_012535.3; NM_001181659.3.
DR PDB; 5WLC; EM; 3.80 A; NA=1-593.
DR PDB; 5WXM; X-ray; 2.30 A; U/V=430-461.
DR PDB; 5WYJ; EM; 8.70 A; MC=429-593.
DR PDB; 5WYK; EM; 4.50 A; MC=429-593.
DR PDB; 6KE6; EM; 3.40 A; 5E=1-593.
DR PDB; 6LQP; EM; 3.20 A; 5E=1-593.
DR PDB; 6LQQ; EM; 4.10 A; 5E=1-593.
DR PDB; 6LQR; EM; 8.60 A; 5E=1-593.
DR PDB; 6LQS; EM; 3.80 A; 5E=1-593.
DR PDB; 6LQT; EM; 4.90 A; 5E=1-593.
DR PDB; 6LQU; EM; 3.70 A; 5E=1-593.
DR PDB; 6LQV; EM; 4.80 A; 5E=1-593.
DR PDB; 6ND4; EM; 4.30 A; A=1-593.
DR PDB; 6ZQA; EM; 4.40 A; CK=1-593.
DR PDB; 6ZQB; EM; 3.90 A; CK=1-593.
DR PDB; 6ZQC; EM; 3.80 A; CK=1-593.
DR PDB; 6ZQD; EM; 3.80 A; CK=1-593.
DR PDB; 6ZQE; EM; 7.10 A; CK=1-593.
DR PDB; 6ZQF; EM; 4.90 A; CK=1-593.
DR PDB; 6ZQG; EM; 3.50 A; CK=1-593.
DR PDB; 7AJT; EM; 4.60 A; CK=1-593.
DR PDB; 7AJU; EM; 3.80 A; CK=1-593.
DR PDB; 7D4I; EM; 4.00 A; 5E=1-593.
DR PDB; 7D5S; EM; 4.60 A; 5E=1-593.
DR PDB; 7D5T; EM; 6.00 A; 5E=1-593.
DR PDB; 7D63; EM; 12.30 A; 5E=1-593.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WXM; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
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; 6ND4; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P47083; -.
DR SMR; P47083; -.
DR BioGRID; 33758; 127.
DR ComplexPortal; CPX-1893; MPP10 complex.
DR DIP; DIP-4363N; -.
DR IntAct; P47083; 52.
DR MINT; P47083; -.
DR STRING; 4932.YJR002W; -.
DR iPTMnet; P47083; -.
DR MaxQB; P47083; -.
DR PaxDb; P47083; -.
DR PRIDE; P47083; -.
DR EnsemblFungi; YJR002W_mRNA; YJR002W; YJR002W.
DR GeneID; 853458; -.
DR KEGG; sce:YJR002W; -.
DR SGD; S000003762; MPP10.
DR VEuPathDB; FungiDB:YJR002W; -.
DR eggNOG; KOG2600; Eukaryota.
DR GeneTree; ENSGT00990000209865; -.
DR HOGENOM; CLU_011271_1_0_1; -.
DR InParanoid; P47083; -.
DR OMA; HFAEDFG; -.
DR BioCyc; YEAST:G3O-31648-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P47083; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47083; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0034457; C:Mpp10 complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IC:ComplexPortal.
DR InterPro; IPR012173; Mpp10.
DR PANTHER; PTHR17039; PTHR17039; 1.
DR Pfam; PF04006; Mpp10; 1.
DR PIRSF; PIRSF017300; snoRNP_Mpp10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..593
FT /note="U3 small nucleolar RNA-associated protein MPP10"
FT /id="PRO_0000121534"
FT REGION 90..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 430..451
FT /evidence="ECO:0007829|PDB:5WXM"
SQ SEQUENCE 593 AA; 66953 MW; DEAF52FC003A0FFD CRC64;
MSELFGVLKS NAGRIILKDP SATSKDVKAY IDSVINTCKN GSITKKAELD EITVDGLDAN
QVWWQVKLVL DSIDGDLIQG IQELKDVVTP SHNLSDGSTL NSSSGEESEL EEAESVFKEK
QMLSADVSEI EEQSNDSLSE NDEEPSMDDE KTSAEAAREE FAEEKRISSG QDERHSSPDP
YGINDKFFDL EKFNRDTLAA EDSNEASEGS EDEDIDYFQD MPSDDEEEEA IYYEDFFDKP
TKEPVKKHSD VKDPKEDEEL DEEEHDSAMD KVKLDLFADE EDEPNAEGVG EASDKNLSSF
EKQQIEIRKQ IEQLENEAVA EKKWSLKGEV KAKDRPEDAL LTEELEFDRT AKPVPVITSE
VTESLEDMIR RRIQDSNFDD LQRRTLLDIT RKSQRPQFEL SDVKSSKSLA EIYEDDYTRA
EDESALSEEL QKAHSEISEL YANLVYKLDV LSSVHFVPKP ASTSLEIRVE TPTISMEDAQ
PLYMSNASSL APQEIYNVGK AEKDGEIRLK NGVAMSKEEL TREDKNRLRR ALKRKRSKAN
LPNVNKRSKR NDVVDTLSKA KNITVINQKG EKKDVSGKTK KSRSGPDSTN IKL
