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MPP10_ARATH
ID   MPP10_ARATH             Reviewed;         524 AA.
AC   Q9FJY5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=M phase phosphoprotein 10 {ECO:0000303|PubMed:27792779};
DE            Short=AtMPP10 {ECO:0000303|PubMed:27792779};
DE   AltName: Full=U3 small nucleolar ribonucleoprotein protein MPP10 {ECO:0000255|PIRNR:PIRNR017300};
GN   Name=MPP10 {ECO:0000303|PubMed:27792779};
GN   OrderedLocusNames=At5g66540 {ECO:0000312|Araport:AT5G66540};
GN   ORFNames=K1F13.21 {ECO:0000312|EMBL:BAB10930.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH THAL.
RC   STRAIN=cv. Columbia;
RX   PubMed=27792779; DOI=10.1371/journal.pgen.1006408;
RA   Chen Y.-J.C., Wang H.-J., Jauh G.-Y.;
RT   "Dual role of a SAS10/C1D family protein in ribosomal RNA gene expression
RT   and processing is essential for reproduction in Arabidopsis thaliana.";
RL   PLoS Genet. 12:e1006408-e1006408(2016).
RN   [8]
RP   INDUCTION BY SALT STRESS.
RC   STRAIN=cv. Columbia;
RX   PubMed=29490615; DOI=10.1186/s12870-018-1255-z;
RA   Huang K.-C., Lin W.-C., Cheng W.-H.;
RT   "Salt hypersensitive mutant 9, a nucleolar APUM23 protein, is essential for
RT   salt sensitivity in association with the ABA signaling pathway in
RT   Arabidopsis.";
RL   BMC Plant Biol. 18:40-40(2018).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       {ECO:0000250|UniProtKB:P47083}.
CC   -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome (By
CC       similarity). Interacts with THAL in the nucleus (PubMed:27792779).
CC       {ECO:0000250|UniProtKB:P47083, ECO:0000269|PubMed:27792779}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:27792779}.
CC   -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:29490615}.
CC   -!- SIMILARITY: Belongs to the MPP10 family. {ECO:0000305}.
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DR   EMBL; AB013389; BAB10930.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED98227.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM71175.1; -; Genomic_DNA.
DR   EMBL; AF389279; AAK63852.1; -; mRNA.
DR   EMBL; AY149928; AAN31082.1; -; mRNA.
DR   RefSeq; NP_001332723.1; NM_001345767.1.
DR   RefSeq; NP_569037.1; NM_126052.3.
DR   AlphaFoldDB; Q9FJY5; -.
DR   SMR; Q9FJY5; -.
DR   STRING; 3702.AT5G66540.1; -.
DR   PaxDb; Q9FJY5; -.
DR   PRIDE; Q9FJY5; -.
DR   ProteomicsDB; 183581; -.
DR   EnsemblPlants; AT5G66540.1; AT5G66540.1; AT5G66540.
DR   EnsemblPlants; AT5G66540.2; AT5G66540.2; AT5G66540.
DR   GeneID; 836786; -.
DR   Gramene; AT5G66540.1; AT5G66540.1; AT5G66540.
DR   Gramene; AT5G66540.2; AT5G66540.2; AT5G66540.
DR   KEGG; ath:AT5G66540; -.
DR   Araport; AT5G66540; -.
DR   TAIR; locus:2154885; AT5G66540.
DR   eggNOG; KOG2600; Eukaryota.
DR   HOGENOM; CLU_011271_5_1_1; -.
DR   InParanoid; Q9FJY5; -.
DR   OMA; HFAEDFG; -.
DR   OrthoDB; 435993at2759; -.
DR   PhylomeDB; Q9FJY5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJY5; baseline and differential.
DR   GO; GO:0034457; C:Mpp10 complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
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   Coiled coil; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..524
FT                   /note="M phase phosphoprotein 10"
FT                   /id="PRO_0000454730"
FT   REGION          100..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          131..165
FT                   /evidence="ECO:0000255"
FT   COILED          257..302
FT                   /evidence="ECO:0000255"
FT   MOTIF           85..92
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           373..380
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        112..166
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  59745 MW;  819B3FC05F9EB1F7 CRC64;
     MATVKDSGFE ALEKLKATEP PVFLAPSSIS EDARSASQYL FMKLKPHNPK CPFDQLSSDG
     FDAEQIWQQI DMQSQPLLTS LRQEVKRFAK NPEEIRKLGK LALKVSHEDD IDEMDMDGFD
     SDDVDDEDKE IESNDSEGED EEEEEEDEEE EEEEEEEEEE EKDGDNEGIE DKFFKIKELE
     EFLEEGEAEE YGIDHKNKKG VAQRKKQNLS DDEDEEDDDD EEEDVEFDAF AGGDDEETDK
     LGKARYDDFF GGKKETKMKL KDLSEDEEAE IENKGNEKLS THERARLKLQ SKIEQMEKAN
     LDPKHWTMQG EITAAKRPMN SALEVDLDFE HNARPAPVIT EEVTASLEDL IKSRIIEARF
     DDVQRAPRLP TKGKREAKEL DESKSKKGLA EVYEAEYFQK ANPAFAPTTH SDELKKEASM
     LFKKLCLKLD ALSHFHFTPK PVIEEMSIPN VSAIAMEEVA PVAVSDAAML APEEIFSGKG
     DIKDESELTQ EDRKRRRANK KRKFKAESAN EPPKKALDTS TKNP
 
 
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