Details for: MPHOSPH8

Gene ID: 54737

Symbol: MPHOSPH8

Ensembl ID: ENSG00000196199

Description: M-phase phosphoprotein 8

Associated with

Other Information

Genular Protein ID: 3899365820

Symbol: MPP8_HUMAN

Name: M-phase phosphoprotein 8

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8885239

Title: Identification of novel M phase phosphoproteins by expression cloning.

PubMed ID: 8885239

DOI: 10.1091/mbc.7.9.1455

PubMed ID: 12559565

Title: A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM.

PubMed ID: 12559565

DOI: 10.1016/s0378-1119(02)01153-8

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20871592

Title: Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion.

PubMed ID: 20871592

DOI: 10.1038/emboj.2010.239

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23416073

Title: Mitotic phosphorylation of MPP8 by cyclin-dependent kinases regulates chromatin dissociation.

PubMed ID: 23416073

DOI: 10.1016/j.bbrc.2013.02.027

PubMed ID: 23532874

Title: Humanin binds MPP8: mapping interaction sites of the peptide and protein.

PubMed ID: 23532874

DOI: 10.1002/psc.2500

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26022416

Title: Epigenetic silencing by the HUSH complex mediates position-effect variegation in human cells.

PubMed ID: 26022416

DOI: 10.1126/science.aaa7227

PubMed ID: 28581500

Title: Hyperactivation of HUSH complex function by Charcot-Marie-Tooth disease mutation in MORC2.

PubMed ID: 28581500

DOI: 10.1038/ng.3878

PubMed ID: 29211708

Title: Selective silencing of euchromatic L1s revealed by genome-wide screens for L1 regulators.

PubMed ID: 29211708

DOI: 10.1038/nature25179

PubMed ID: 30487602

Title: NP220 mediates silencing of unintegrated retroviral DNA.

PubMed ID: 30487602

DOI: 10.1038/s41586-018-0750-6

PubMed ID: 21419134

Title: Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding.

PubMed ID: 21419134

DOI: 10.1016/j.jmb.2011.03.018

PubMed ID: 22086334

Title: MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a.

PubMed ID: 22086334

DOI: 10.1038/ncomms1549

PubMed ID: 22022377

Title: Structural basis for specific binding of human MPP8 chromodomain to histone H3 methylated at lysine 9.

PubMed ID: 22022377

DOI: 10.1371/journal.pone.0025104

Sequence Information:

  • Length: 860
  • Mass: 97182
  • Checksum: DD75D14C3DBF5E95
  • Sequence:
  • MEQVAEGARV TAVPVSAADS TEELAEVEEG VGVVGEDNDA AARGAEAFGD SEEDGEDVFE 
    VEKILDMKTE GGKVLYKVRW KGYTSDDDTW EPEIHLEDCK EVLLEFRKKI AENKAKAVRK 
    DIQRLSLNND IFEANSDSDQ QSETKEDTSP KKKKKKLRQR EEKSPDDLKK KKAKAGKLKD 
    KSKPDLESSL ESLVFDLRTK KRISEAKEEL KESKKPKKDE VKETKELKKV KKGEIRDLKT 
    KTREDPKENR KTKKEKFVES QVESESSVLN DSPFPEDDSE GLHSDSREEK QNTKSARERA 
    GQDMGLEHGF EKPLDSAMSA EEDTDVRGRR KKKTPRKAED TRENRKLENK NAFLEKKTVP 
    KKQRNQDRSK SAAELEKLMP VSAQTPKGRR LSGEERGLWS TDSAEEDKET KRNESKEKYQ 
    KRHDSDKEEK GRKEPKGLKT LKEIRNAFDL FKLTPEEKND VSENNRKREE IPLDFKTIDD 
    HKTKENKQSL KERRNTRDET DTWAYIAAEG DQEVLDSVCQ ADENSDGRQQ ILSLGMDLQL 
    EWMKLEDFQK HLDGKDENFA ATDAIPSNVL RDAVKNGDYI TVKVALNSNE EYNLDQEDSS 
    GMTLVMLAAA GGQDDLLRLL ITKGAKVNGR QKNGTTALIH AAEKNFLTTV AILLEAGAFV 
    NVQQSNGETA LMKACKRGNS DIVRLVIECG ADCNILSKHQ NSALHFAKQS NNVLVYDLLK 
    NHLETLSRVA EETIKDYFEA RLALLEPVFP IACHRLCEGP DFSTDFNYKP PQNIPEGSGI 
    LLFIFHANFL GKEVIARLCG PCSVQAVVLN DKFQLPVFLD SHFVYSFSPV AGPNKLFIRL 
    TEAPSAKVKL LIGAYRVQLQ

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.