MPP10_MOUSE
ID MPP10_MOUSE Reviewed; 681 AA.
AC Q810V0; E9QM78;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=U3 small nucleolar ribonucleoprotein protein MPP10;
DE AltName: Full=M phase phosphoprotein 10;
GN Name=Mphosph10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-168; SER-172;
RP SER-244 AND SER-346, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein
CC (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal
CC RNA processing (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4
CC and MPHOSPH10. Interacts with IMP3 and IMP4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O00566}. Chromosome
CC {ECO:0000250|UniProtKB:O00566}. Note=Fibrillar region of the nucleolus.
CC After dissolution of the nucleolus in early M phase becomes associated
CC with chromosomes through metaphase and anaphase. In telophase localized
CC to small cellular prenucleolar bodies that not always contain
CC fibrillarin. The reassociation with nucleolus is preceeded by the
CC arrival of fibrillarin. {ECO:0000250|UniProtKB:O00566}.
CC -!- PTM: Phosphorylated in M (mitotic) phase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MPP10 family. {ECO:0000305}.
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DR EMBL; AC129199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049270; AAH49270.1; -; mRNA.
DR CCDS; CCDS21333.1; -.
DR RefSeq; NP_080759.2; NM_026483.2.
DR AlphaFoldDB; Q810V0; -.
DR SMR; Q810V0; -.
DR BioGRID; 212574; 1.
DR STRING; 10090.ENSMUSP00000032735; -.
DR iPTMnet; Q810V0; -.
DR PhosphoSitePlus; Q810V0; -.
DR EPD; Q810V0; -.
DR jPOST; Q810V0; -.
DR MaxQB; Q810V0; -.
DR PaxDb; Q810V0; -.
DR PeptideAtlas; Q810V0; -.
DR PRIDE; Q810V0; -.
DR ProteomicsDB; 291436; -.
DR Antibodypedia; 31197; 140 antibodies from 24 providers.
DR DNASU; 67973; -.
DR Ensembl; ENSMUST00000032735; ENSMUSP00000032735; ENSMUSG00000030521.
DR GeneID; 67973; -.
DR KEGG; mmu:67973; -.
DR UCSC; uc009hgg.1; mouse.
DR CTD; 10199; -.
DR MGI; MGI:1915223; Mphosph10.
DR VEuPathDB; HostDB:ENSMUSG00000030521; -.
DR eggNOG; KOG2600; Eukaryota.
DR GeneTree; ENSGT00390000011359; -.
DR HOGENOM; CLU_011271_3_1_1; -.
DR InParanoid; Q810V0; -.
DR OMA; HFAEDFG; -.
DR OrthoDB; 435993at2759; -.
DR PhylomeDB; Q810V0; -.
DR TreeFam; TF105794; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 67973; 27 hits in 72 CRISPR screens.
DR ChiTaRS; Mphosph10; mouse.
DR PRO; PR:Q810V0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q810V0; protein.
DR Bgee; ENSMUSG00000030521; Expressed in undifferentiated genital tubercle and 258 other tissues.
DR Genevisible; Q810V0; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0034457; C:Mpp10 complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 Acetylation; Chromosome; Coiled coil; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW rRNA processing; Ubl conjugation.
FT CHAIN 1..681
FT /note="U3 small nucleolar ribonucleoprotein protein MPP10"
FT /id="PRO_0000121536"
FT REGION 111..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..139
FT /evidence="ECO:0000255"
FT COILED 349..383
FT /evidence="ECO:0000255"
FT COILED 471..491
FT /evidence="ECO:0000255"
FT COILED 575..604
FT /evidence="ECO:0000255"
FT COMPBIAS 111..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..246
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..593
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CROSSLNK 351
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CROSSLNK 383
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CROSSLNK 395
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CROSSLNK 556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00566"
FT CONFLICT 99
FT /note="V -> I (in Ref. 2; AAH49270)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="D -> E (in Ref. 2; AAH49270)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> G (in Ref. 2; AAH49270)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="E -> A (in Ref. 2; AAH49270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 78735 MW; 2C4038ACA05F8ED2 CRC64;
MAPRVFRRQT LERCLREIRK ATNRPECFLT IQNGLASNFT SLTKVLYDFN KVLENGRISG
SPLQKLEINS FDDEQIWQQL ELQNEPVLQY FQNAVSETVE DEDISLLPEC EDEECEEDAS
EVEADNQENL ETDLDEEQLS DEGGDVPKGR DRAKSSRKSD PRKSPVFSDE DSDLDFDIGK
LEQQTKMQIK PPGKPREKSV VDDKFFKLSE MESFLEKVEK EEEKRPDGEE EDEEDIDLFE
DIDSDESEGG LFGRQKIKSN KSSRNLKYKD FFDPVESDED ITGVDEELGP DEEKEEEEGF
AEEADESISD TDEDNDLEED ENSDQHKGSL KRVTFALPDD EAEDTSPLAV KQESDEVKSS
FEKRQEKMNE KIASLEKELL DKKPWQLQGE VTAQKRPENS LLEETLHFDH AVRMAPVITE
ETTLHLEDII KQRIRDQAWD DVERKEKPKE DAYEYKKRLT LDHEKSKLSL AEIYEQEYLK
LNQQKTEEED NPEHVEIQKM MDSLFLKLDA LSNFHFIPKP PVPEIKVVSN LPAITMEEVA
PVSVSDAALL APEEIKEKNK AGDLKTAAEK TATDKKRERR KKKYQKRLKI KEKEKRKKLL
EKNNPDQSKS SRAAASEKLK QLTKTGKVSL LKDERKDKPL KSSQAFFSKL QDQVKMQIND
AKQPEKIKKK KQDISVHKLK L
