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Q99547

- MPH6_HUMAN

UniProt

Q99547 - MPH6_HUMAN

Protein

M-phase phosphoprotein 6

Gene

MPHOSPH6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and may play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. maturation of 5.8S rRNA Source: UniProtKB
    2. mitotic M phase Source: ProtInc

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase phosphoprotein 6
    Gene namesi
    Name:MPHOSPH6
    Synonyms:MPP6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:7214. MPHOSPH6.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm
    Note: Cytoplasmic in M phase.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. exosome (RNase complex) Source: UniProtKB
    3. nucleolus Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30920.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 160160M-phase phosphoprotein 6PRO_0000122437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101Phosphoserine1 Publication
    Modified residuei147 – 1471Phosphothreonine5 Publications

    Post-translational modificationi

    Phosphorylated in M (mitotic) phase.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99547.
    PaxDbiQ99547.
    PRIDEiQ99547.

    PTM databases

    PhosphoSiteiQ99547.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99547.
    BgeeiQ99547.
    CleanExiHS_MPHOSPH6.
    HS_MPP6.
    GenevestigatoriQ99547.

    Organism-specific databases

    HPAiCAB003674.
    HPA026948.

    Interactioni

    Subunit structurei

    Associates with the RNA exosome complex, probably mediated by EXOSC10. Interacts with ARHGAP18, EXOSC10 and SKIV2L2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXOSC10Q017804EBI-373187,EBI-358236
    EXOSC2Q138683EBI-373187,EBI-301735
    SKIV2L2P422852EBI-373187,EBI-347612

    Protein-protein interaction databases

    BioGridi115495. 14 interactions.
    IntActiQ99547. 27 interactions.
    MINTiMINT-1372240.
    STRINGi9606.ENSP00000258169.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99547.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi116 – 13318Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi32 – 354Poly-Glu

    Sequence similaritiesi

    Belongs to the MPP6 family.Curated

    Phylogenomic databases

    eggNOGiNOG256213.
    HOGENOMiHOG000007728.
    HOVERGENiHBG031714.
    InParanoidiQ99547.
    KOiK12593.
    OMAiNGDITPI.
    PhylomeDBiQ99547.
    TreeFamiTF323810.

    Family and domain databases

    InterProiIPR019324. MPP6.
    [Graphical view]
    PANTHERiPTHR13582. PTHR13582. 1 hit.
    PfamiPF10175. MPP6. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99547-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAERKTRLS KNLLRMKFMQ RGLDSETKKQ LEEEEKKIIS EEHWYLDLPE    50
    LKEKESFIIE EQSFLLCEDL LYGRMSFRGF NPEVEKLMLQ MNAKHKAEEV 100
    EDETVELDVS DEEMARRYET LVGTIGKKFA RKRDHANYEE DENGDITPIK 150
    AKKMFLKPQD 160
    Length:160
    Mass (Da):19,024
    Last modified:May 18, 2010 - v2
    Checksum:i506D5274C839BD7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81R → K in CAA66916. (PubMed:8885239)Curated
    Sequence conflicti8 – 81R → K in BAG36847. (PubMed:14702039)Curated
    Sequence conflicti8 – 81R → K in AAH05242. (PubMed:15489334)Curated
    Sequence conflicti8 – 81R → K in AAH11020. (PubMed:15489334)Curated
    Sequence conflicti8 – 81R → K in AAH31017. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581I → V.
    Corresponds to variant rs2303267 [ dbSNP | Ensembl ].
    VAR_056150

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98263 mRNA. Translation: CAA66916.1.
    AK314163 mRNA. Translation: BAG36847.1.
    AC138304 Genomic DNA. No translation available.
    BC005242 mRNA. Translation: AAH05242.1.
    BC011020 mRNA. Translation: AAH11020.1.
    BC031017 mRNA. Translation: AAH31017.1.
    CCDSiCCDS10937.1.
    RefSeqiNP_005783.2. NM_005792.2.
    UniGeneiHs.344400.

    Genome annotation databases

    EnsembliENST00000258169; ENSP00000258169; ENSG00000135698.
    GeneIDi10200.
    KEGGihsa:10200.
    UCSCiuc002fgw.3. human.

    Polymorphism databases

    DMDMi296438296.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98263 mRNA. Translation: CAA66916.1 .
    AK314163 mRNA. Translation: BAG36847.1 .
    AC138304 Genomic DNA. No translation available.
    BC005242 mRNA. Translation: AAH05242.1 .
    BC011020 mRNA. Translation: AAH11020.1 .
    BC031017 mRNA. Translation: AAH31017.1 .
    CCDSi CCDS10937.1.
    RefSeqi NP_005783.2. NM_005792.2.
    UniGenei Hs.344400.

    3D structure databases

    ProteinModelPortali Q99547.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115495. 14 interactions.
    IntActi Q99547. 27 interactions.
    MINTi MINT-1372240.
    STRINGi 9606.ENSP00000258169.

    PTM databases

    PhosphoSitei Q99547.

    Polymorphism databases

    DMDMi 296438296.

    Proteomic databases

    MaxQBi Q99547.
    PaxDbi Q99547.
    PRIDEi Q99547.

    Protocols and materials databases

    DNASUi 10200.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258169 ; ENSP00000258169 ; ENSG00000135698 .
    GeneIDi 10200.
    KEGGi hsa:10200.
    UCSCi uc002fgw.3. human.

    Organism-specific databases

    CTDi 10200.
    GeneCardsi GC16M082181.
    H-InvDB HIX0013281.
    HGNCi HGNC:7214. MPHOSPH6.
    HPAi CAB003674.
    HPA026948.
    MIMi 605500. gene.
    neXtProti NX_Q99547.
    PharmGKBi PA30920.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256213.
    HOGENOMi HOG000007728.
    HOVERGENi HBG031714.
    InParanoidi Q99547.
    KOi K12593.
    OMAi NGDITPI.
    PhylomeDBi Q99547.
    TreeFami TF323810.

    Miscellaneous databases

    GeneWikii MPHOSPH6.
    GenomeRNAii 10200.
    NextBioi 38606.
    PROi Q99547.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99547.
    Bgeei Q99547.
    CleanExi HS_MPHOSPH6.
    HS_MPP6.
    Genevestigatori Q99547.

    Family and domain databases

    InterProi IPR019324. MPP6.
    [Graphical view ]
    PANTHERi PTHR13582. PTHR13582. 1 hit.
    Pfami PF10175. MPP6. 1 hit.
    [Graphical view ]
    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].
      Tissue: Lymphoblast.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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, Lung and Urinary bladder.
    5. "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
      Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
      Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "A protein interaction framework for human mRNA degradation."
      Lehner B., Sanderson C.M.
      Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP18.
    7. "MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation."
      Schilders G., Raijmakers R., Raats J.M., Pruijn G.J.
      Nucleic Acids Res. 33:6795-6804(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, RNA-BINDING, SUBCELLULAR LOCATION.
    8. "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 THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing."
      Schilders G., van Dijk E., Pruijn G.J.M.
      Nucleic Acids Res. 35:2564-2572(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EXOSC10 AND SKIV2L2.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-110 AND THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, SUBCELLULAR LOCATION.
    14. "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
      Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
      EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "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 THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMPH6_HUMAN
    AccessioniPrimary (citable) accession number: Q99547
    Secondary accession number(s): B2RAF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 125 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 16
      Human chromosome 16: 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