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O00566

- MPP10_HUMAN

UniProt

O00566 - MPP10_HUMAN

Protein

U3 small nucleolar ribonucleoprotein protein MPP10

Gene

MPHOSPH10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. negative regulation of phosphatase activity Source: UniProtKB
    2. RNA processing Source: UniProtKB
    3. RNA splicing Source: UniProtKB
    4. RNA splicing, via transesterification reactions Source: UniProtKB
    5. rRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U3 small nucleolar ribonucleoprotein protein MPP10
    Alternative name(s):
    M phase phosphoprotein 10
    Gene namesi
    Name:MPHOSPH10
    Synonyms:MPP10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7213. MPHOSPH10.

    Subcellular locationi

    Nucleusnucleolus. Chromosome
    Note: Fibrillar region of the nucleolus. After dissolution of the nucleolus in early M phase becomes associated with chromosomes through metaphase and anaphase. In telophase localized to small cellular prenucleolar bodies that not always contain fibrillarin. The reassociation with nucleolus is preceeded by the arrival of fibrillarin.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleolus Source: UniProtKB
    3. small nucleolar ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30919.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 681681U3 small nucleolar ribonucleoprotein protein MPP10PRO_0000121535Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611PhosphoserineSequence Analysis
    Modified residuei120 – 1201Phosphoserine2 Publications
    Modified residuei139 – 1391Phosphoserine2 Publications
    Modified residuei163 – 1631Phosphoserine4 Publications
    Modified residuei167 – 1671Phosphoserine5 Publications
    Modified residuei171 – 1711Phosphoserine5 Publications
    Modified residuei242 – 2421Phosphoserine5 Publications
    Modified residuei275 – 2751Phosphoserine2 Publications
    Modified residuei289 – 2891Phosphoserine2 Publications
    Modified residuei609 – 6091N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated in M (mitotic) phase.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00566.
    PaxDbiO00566.
    PeptideAtlasiO00566.
    PRIDEiO00566.

    2D gel databases

    SWISS-2DPAGEO00566.

    PTM databases

    PhosphoSiteiO00566.

    Miscellaneous databases

    PMAP-CutDBO00566.

    Expressioni

    Gene expression databases

    ArrayExpressiO00566.
    BgeeiO00566.
    CleanExiHS_MPHOSPH10.
    GenevestigatoriO00566.

    Organism-specific databases

    HPAiHPA035059.
    HPA035060.
    HPA049907.

    Interactioni

    Subunit structurei

    Component of a heterotrimeric complex containing IMP3, IMP4 and MPHOSPH10. Interacts with IMP3 and IMP4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP1CAP621362EBI-5235884,EBI-357253

    Protein-protein interaction databases

    BioGridi115494. 11 interactions.
    IntActiO00566. 2 interactions.
    MINTiMINT-1192399.
    STRINGi9606.ENSP00000244230.

    Structurei

    3D structure databases

    ProteinModelPortaliO00566.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili109 – 13830Sequence AnalysisAdd
    BLAST
    Coiled coili205 – 23935Sequence AnalysisAdd
    BLAST
    Coiled coili284 – 32441Sequence AnalysisAdd
    BLAST
    Coiled coili348 – 38235Sequence AnalysisAdd
    BLAST
    Coiled coili469 – 49022Sequence AnalysisAdd
    BLAST
    Coiled coili574 – 60431Sequence AnalysisAdd
    BLAST
    Coiled coili648 – 67023Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi134 – 1374Poly-Glu
    Compositional biasi229 – 2324Poly-Glu
    Compositional biasi666 – 6705Poly-Lys

    Sequence similaritiesi

    Belongs to the MPP10 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5384.
    HOGENOMiHOG000046317.
    HOVERGENiHBG052502.
    InParanoidiO00566.
    KOiK14559.
    OMAiRSRPQNS.
    OrthoDBiEOG7VDXPQ.
    PhylomeDBiO00566.
    TreeFamiTF105794.

    Family and domain databases

    InterProiIPR007151. Mpp10.
    IPR012173. snoRNP_Mpp10.
    [Graphical view]
    PANTHERiPTHR17039. PTHR17039. 1 hit.
    PfamiPF04006. Mpp10. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017300. snoRNP_Mpp10. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O00566-1 [UniParc]FASTAAdd to Basket

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    MAPQVWRRRT LERCLTEVGK ATGRPECFLT IQEGLASKFT SLTKVLYDFN    50
    KILENGRIHG SPLQKLVIEN FDDEQIWQQL ELQNEPILQY FQNAVSETIN 100
    DEDISLLPES EEQEREEDGS EIEADDKEDL EDLEEEEVSD MGNDDPEMGE 150
    RAENSSKSDL RKSPVFSDED SDLDFDISKL EQQSKVQNKG QGKPREKSIV 200
    DDKFFKLSEM EAYLENIEKE EERKDDNDEE EEDIDFFEDI DSDEDEGGLF 250
    GSKKLKSGKS SRNLKYKDFF DPVESDEDIT NVHDDELDSN KEDDEIAEEE 300
    AEELSISETD EDDDLQENED NKQHKESLKR VTFALPDDAE TEDTGVLNVK 350
    KNSDEVKSSF EKRQEKMNEK IASLEKELLE KKPWQLQGEV TAQKRPENSL 400
    LEETLHFDHA VRMAPVITEE TTLQLEDIIK QRIRDQAWDD VVRKEKPKED 450
    AYEYKKRLTL DHEKSKLSLA EIYEQEYIKL NQQKTAEEEN PEHVEIQKMM 500
    DSLFLKLDAL SNFHFIPKPP VPEIKVVSNL PAITMEEVAP VSVSDAALLA 550
    PEEIKEKNKA GDIKTAAEKT ATDKKRERRK KKYQKRMKIK EKEKRRKLLE 600
    KSSVDQAGKY SKTVASEKLK QLTKTGKASF IKDEGKDKAL KSSQAFFSKL 650
    QDQVKMQIND AKKTEKKKKK RQDISVHKLK L 681
    Length:681
    Mass (Da):78,864
    Last modified:May 30, 2000 - v2
    Checksum:iEDF27859D735D4E2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti69 – 691E → A.
    Corresponds to variant rs10199088 [ dbSNP | Ensembl ].
    VAR_053511
    Natural varianti115 – 1151R → H.
    Corresponds to variant rs13010513 [ dbSNP | Ensembl ].
    VAR_053512
    Natural varianti140 – 1401D → N.
    Corresponds to variant rs10175940 [ dbSNP | Ensembl ].
    VAR_053513
    Natural varianti229 – 2291E → D.
    Corresponds to variant rs1813160 [ dbSNP | Ensembl ].
    VAR_024539
    Natural varianti425 – 4251L → M.
    Corresponds to variant rs3732240 [ dbSNP | Ensembl ].
    VAR_022000
    Natural varianti634 – 6341E → K.
    Corresponds to variant rs6574 [ dbSNP | Ensembl ].
    VAR_014470
    Natural varianti639 – 6391A → T.
    Corresponds to variant rs4852764 [ dbSNP | Ensembl ].
    VAR_053514

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98494 mRNA. Translation: CAA67120.1.
    BC126389 mRNA. Translation: AAI26390.1.
    CCDSiCCDS1916.1.
    RefSeqiNP_005782.1. NM_005791.2.
    UniGeneiHs.656208.

    Genome annotation databases

    EnsembliENST00000244230; ENSP00000244230; ENSG00000124383.
    GeneIDi10199.
    KEGGihsa:10199.
    UCSCiuc002sht.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98494 mRNA. Translation: CAA67120.1 .
    BC126389 mRNA. Translation: AAI26390.1 .
    CCDSi CCDS1916.1.
    RefSeqi NP_005782.1. NM_005791.2.
    UniGenei Hs.656208.

    3D structure databases

    ProteinModelPortali O00566.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115494. 11 interactions.
    IntActi O00566. 2 interactions.
    MINTi MINT-1192399.
    STRINGi 9606.ENSP00000244230.

    PTM databases

    PhosphoSitei O00566.

    2D gel databases

    SWISS-2DPAGE O00566.

    Proteomic databases

    MaxQBi O00566.
    PaxDbi O00566.
    PeptideAtlasi O00566.
    PRIDEi O00566.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244230 ; ENSP00000244230 ; ENSG00000124383 .
    GeneIDi 10199.
    KEGGi hsa:10199.
    UCSCi uc002sht.2. human.

    Organism-specific databases

    CTDi 10199.
    GeneCardsi GC02P071358.
    HGNCi HGNC:7213. MPHOSPH10.
    HPAi HPA035059.
    HPA035060.
    HPA049907.
    MIMi 605503. gene.
    neXtProti NX_O00566.
    PharmGKBi PA30919.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5384.
    HOGENOMi HOG000046317.
    HOVERGENi HBG052502.
    InParanoidi O00566.
    KOi K14559.
    OMAi RSRPQNS.
    OrthoDBi EOG7VDXPQ.
    PhylomeDBi O00566.
    TreeFami TF105794.

    Miscellaneous databases

    ChiTaRSi MPHOSPH10. human.
    GeneWikii MPHOSPH10.
    GenomeRNAii 10199.
    NextBioi 38602.
    PMAP-CutDB O00566.
    PROi O00566.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00566.
    Bgeei O00566.
    CleanExi HS_MPHOSPH10.
    Genevestigatori O00566.

    Family and domain databases

    InterProi IPR007151. Mpp10.
    IPR012173. snoRNP_Mpp10.
    [Graphical view ]
    PANTHERi PTHR17039. PTHR17039. 1 hit.
    Pfami PF04006. Mpp10. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017300. snoRNP_Mpp10. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel M phase phosphoproteins by expression cloning."
      Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
      Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-681.
      Tissue: Blood.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary cancer and Placenta.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes."
      Granneman S., Gallagher J.E.G., Vogelzangs J., Horstman W., van Venrooij W.J., Baserga S.J., Pruijn G.J.M.
      Nucleic Acids Res. 31:1877-1887(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IMP3 AND IMP4.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-171; SER-242; SER-275 AND SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-171 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-171 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-139; SER-163; SER-167; SER-171 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-139; SER-163; SER-167; SER-171; SER-242; SER-275 AND SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMPP10_HUMAN
    AccessioniPrimary (citable) accession number: O00566
    Secondary accession number(s): A0AVJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3