Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99549

- MPP8_HUMAN

UniProt

Q99549 - MPP8_HUMAN

Protein

M-phase phosphoprotein 8

Gene

MPHOSPH8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (01 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in transcriptional regulation. Specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei59 – 591Interaction with histone H3K9me3

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. regulation of DNA methylation Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase phosphoprotein 8
    Alternative name(s):
    Two hybrid-associated protein 3 with RanBPM
    Short name:
    Twa3
    Gene namesi
    Name:MPHOSPH8
    Synonyms:MPP8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:29810. MPHOSPH8.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Detected on heterochromatin. Detected on nucleosomes.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. nuclear heterochromatin Source: UniProtKB
    4. nuclear nucleosome Source: UniProtKB
    5. nucleolus Source: HPA
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801W → A: Abolishes interaction with histone H3K9me3. 1 Publication

    Organism-specific databases

    PharmGKBiPA162396090.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 860860M-phase phosphoprotein 8PRO_0000080244Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei51 – 511Phosphoserine6 Publications
    Modified residuei136 – 1361Phosphoserine5 Publications
    Modified residuei138 – 1381Phosphoserine5 Publications
    Modified residuei149 – 1491Phosphoserine3 Publications
    Modified residuei188 – 1881Phosphoserine2 Publications
    Modified residuei189 – 1891Phosphoserine3 Publications
    Modified residuei192 – 1921Phosphoserine2 Publications
    Modified residuei272 – 2721PhosphoserineSequence Analysis
    Modified residuei319 – 3191Phosphoserine3 Publications
    Modified residuei334 – 3341PhosphothreonineSequence Analysis
    Modified residuei385 – 3851PhosphothreonineSequence Analysis
    Modified residuei392 – 3921Phosphoserine4 Publications
    Modified residuei400 – 4001Phosphoserine2 Publications
    Modified residuei403 – 4031Phosphoserine4 Publications
    Modified residuei454 – 4541Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated in M (mitotic) phase.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99549.
    PaxDbiQ99549.
    PeptideAtlasiQ99549.
    PRIDEiQ99549.

    PTM databases

    PhosphoSiteiQ99549.

    Expressioni

    Gene expression databases

    BgeeiQ99549.
    CleanExiHS_MPHOSPH8.
    GenevestigatoriQ99549.

    Organism-specific databases

    HPAiHPA039701.
    HPA040035.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (via chromo domain) with histone H3K9me3. Has the highest affinity for H3K9me3, and lesser affinity for H3K9me2 and H3K9me1. Interacts with DNMT3, EHMT1 and SETDB1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EHMT1Q9H9B12EBI-2653928,EBI-766087
    HIST1H3DP684315EBI-2653928,EBI-79722
    SETDB1Q150472EBI-2653928,EBI-79691

    Protein-protein interaction databases

    BioGridi120119. 9 interactions.
    IntActiQ99549. 5 interactions.
    MINTiMINT-6943098.
    STRINGi9606.ENSP00000355388.

    Structurei

    Secondary structure

    1
    860
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 7010
    Beta strandi73 – 808
    Helixi85 – 873
    Beta strandi89 – 924
    Helixi93 – 964
    Helixi100 – 11415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LWEX-ray2.05A/B55-116[»]
    3QO2X-ray2.49A/B/C/D55-116[»]
    3R93X-ray2.06A/B/C/D55-116[»]
    3SVMX-ray2.31A55-116[»]
    ProteinModelPortaliQ99549.
    SMRiQ99549. Positions 55-115, 503-806.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99549.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini59 – 11860ChromoPROSITE-ProRule annotationAdd
    BLAST
    Repeati600 – 62930ANK 1Add
    BLAST
    Repeati633 – 66230ANK 2Add
    BLAST
    Repeati666 – 69530ANK 3Add
    BLAST
    Repeati699 – 72830ANK 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni80 – 878Histone H3K9me3 binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi151 – 256106Lys-richAdd
    BLAST

    Domaini

    The chromo domain mediates interaction with methylated 'Lys-9' of histone H3 (H3K9me), with the highest affinity for the trimethylated form (H3K9me3).2 Publications

    Sequence similaritiesi

    Contains 4 ANK repeats.PROSITE-ProRule annotation
    Contains 1 chromo domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000290641.
    HOVERGENiHBG052503.
    InParanoidiQ99549.
    OMAiHKTKENK.
    OrthoDBiEOG74FF0B.
    PhylomeDBiQ99549.
    TreeFamiTF106394.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    [Graphical view]
    PfamiPF00023. Ank. 1 hit.
    PF12796. Ank_2. 1 hit.
    PF00385. Chromo. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 4 hits.
    SM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF54160. SSF54160. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 3 hits.
    PS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99549-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEQVAEGARV TAVPVSAADS TEELAEVEEG VGVVGEDNDA AARGAEAFGD    50
    SEEDGEDVFE VEKILDMKTE GGKVLYKVRW KGYTSDDDTW EPEIHLEDCK 100
    EVLLEFRKKI AENKAKAVRK DIQRLSLNND IFEANSDSDQ QSETKEDTSP 150
    KKKKKKLRQR EEKSPDDLKK KKAKAGKLKD KSKPDLESSL ESLVFDLRTK 200
    KRISEAKEEL KESKKPKKDE VKETKELKKV KKGEIRDLKT KTREDPKENR 250
    KTKKEKFVES QVESESSVLN DSPFPEDDSE GLHSDSREEK QNTKSARERA 300
    GQDMGLEHGF EKPLDSAMSA EEDTDVRGRR KKKTPRKAED TRENRKLENK 350
    NAFLEKKTVP KKQRNQDRSK SAAELEKLMP VSAQTPKGRR LSGEERGLWS 400
    TDSAEEDKET KRNESKEKYQ KRHDSDKEEK GRKEPKGLKT LKEIRNAFDL 450
    FKLTPEEKND VSENNRKREE IPLDFKTIDD HKTKENKQSL KERRNTRDET 500
    DTWAYIAAEG DQEVLDSVCQ ADENSDGRQQ ILSLGMDLQL EWMKLEDFQK 550
    HLDGKDENFA ATDAIPSNVL RDAVKNGDYI TVKVALNSNE EYNLDQEDSS 600
    GMTLVMLAAA GGQDDLLRLL ITKGAKVNGR QKNGTTALIH AAEKNFLTTV 650
    AILLEAGAFV NVQQSNGETA LMKACKRGNS DIVRLVIECG ADCNILSKHQ 700
    NSALHFAKQS NNVLVYDLLK NHLETLSRVA EETIKDYFEA RLALLEPVFP 750
    IACHRLCEGP DFSTDFNYKP PQNIPEGSGI LLFIFHANFL GKEVIARLCG 800
    PCSVQAVVLN DKFQLPVFLD SHFVYSFSPV AGPNKLFIRL TEAPSAKVKL 850
    LIGAYRVQLQ 860
    Length:860
    Mass (Da):97,182
    Last modified:February 1, 2005 - v2
    Checksum:iDD75D14C3DBF5E95
    GO
    Isoform 2 (identifier: Q99549-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         820-860: DSHFVYSFSP...LIGAYRVQLQ → TGSRSVVQAG...GLKMHATTSG

    Show »
    Length:867
    Mass (Da):97,637
    Checksum:i5638702150529EA3
    GO

    Sequence cautioni

    The sequence CAI46172.1 differs from that shown. Reason: Frameshift at positions 248, 255 and 731.
    The sequence AAH46214.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB71284.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti526 – 5305DGRQQ → GEFGI in CAA66912. (PubMed:8885239)Curated
    Sequence conflicti860 – 8601Q → QPNRRDWAEFS in AAH46214. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei820 – 86041DSHFV…RVQLQ → TGSRSVVQAGVQWRGLQLTG VLTSQAQAILPPQPPNYLGL KMHATTSG in isoform 2. 2 PublicationsVSP_031523Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK056785 mRNA. Translation: BAB71284.1. Different initiation.
    AK300258 mRNA. Translation: BAH13245.1.
    AL832864 mRNA. Translation: CAI46172.1. Frameshift.
    AL359457, AL354808 Genomic DNA. Translation: CAI16671.1.
    AL354808, AL359457 Genomic DNA. Translation: CAI41002.1.
    CH471075 Genomic DNA. Translation: EAX08228.1.
    CH471075 Genomic DNA. Translation: EAX08230.1.
    BC003542 mRNA. Translation: AAH03542.2.
    BC046214 mRNA. Translation: AAH46214.1. Different initiation.
    X98259 mRNA. Translation: CAA66912.1.
    CCDSiCCDS9287.1. [Q99549-1]
    RefSeqiNP_059990.2. NM_017520.3. [Q99549-1]
    UniGeneiHs.269654.

    Genome annotation databases

    EnsembliENST00000361479; ENSP00000355388; ENSG00000196199. [Q99549-1]
    ENST00000414242; ENSP00000414663; ENSG00000196199. [Q99549-2]
    GeneIDi54737.
    KEGGihsa:54737.
    UCSCiuc001umg.3. human. [Q99549-2]
    uc001umh.3. human. [Q99549-1]

    Polymorphism databases

    DMDMi93204602.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK056785 mRNA. Translation: BAB71284.1 . Different initiation.
    AK300258 mRNA. Translation: BAH13245.1 .
    AL832864 mRNA. Translation: CAI46172.1 . Frameshift.
    AL359457 , AL354808 Genomic DNA. Translation: CAI16671.1 .
    AL354808 , AL359457 Genomic DNA. Translation: CAI41002.1 .
    CH471075 Genomic DNA. Translation: EAX08228.1 .
    CH471075 Genomic DNA. Translation: EAX08230.1 .
    BC003542 mRNA. Translation: AAH03542.2 .
    BC046214 mRNA. Translation: AAH46214.1 . Different initiation.
    X98259 mRNA. Translation: CAA66912.1 .
    CCDSi CCDS9287.1. [Q99549-1 ]
    RefSeqi NP_059990.2. NM_017520.3. [Q99549-1 ]
    UniGenei Hs.269654.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LWE X-ray 2.05 A/B 55-116 [» ]
    3QO2 X-ray 2.49 A/B/C/D 55-116 [» ]
    3R93 X-ray 2.06 A/B/C/D 55-116 [» ]
    3SVM X-ray 2.31 A 55-116 [» ]
    ProteinModelPortali Q99549.
    SMRi Q99549. Positions 55-115, 503-806.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120119. 9 interactions.
    IntActi Q99549. 5 interactions.
    MINTi MINT-6943098.
    STRINGi 9606.ENSP00000355388.

    Chemistry

    ChEMBLi CHEMBL1741210.

    PTM databases

    PhosphoSitei Q99549.

    Polymorphism databases

    DMDMi 93204602.

    Proteomic databases

    MaxQBi Q99549.
    PaxDbi Q99549.
    PeptideAtlasi Q99549.
    PRIDEi Q99549.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361479 ; ENSP00000355388 ; ENSG00000196199 . [Q99549-1 ]
    ENST00000414242 ; ENSP00000414663 ; ENSG00000196199 . [Q99549-2 ]
    GeneIDi 54737.
    KEGGi hsa:54737.
    UCSCi uc001umg.3. human. [Q99549-2 ]
    uc001umh.3. human. [Q99549-1 ]

    Organism-specific databases

    CTDi 54737.
    GeneCardsi GC13P020208.
    H-InvDB HIX0171874.
    HGNCi HGNC:29810. MPHOSPH8.
    HPAi HPA039701.
    HPA040035.
    MIMi 611626. gene.
    neXtProti NX_Q99549.
    PharmGKBi PA162396090.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000290641.
    HOVERGENi HBG052503.
    InParanoidi Q99549.
    OMAi HKTKENK.
    OrthoDBi EOG74FF0B.
    PhylomeDBi Q99549.
    TreeFami TF106394.

    Miscellaneous databases

    ChiTaRSi MPHOSPH8. human.
    EvolutionaryTracei Q99549.
    GeneWikii MPHOSPH8.
    GenomeRNAii 54737.
    NextBioi 57325.
    PROi Q99549.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99549.
    CleanExi HS_MPHOSPH8.
    Genevestigatori Q99549.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    [Graphical view ]
    Pfami PF00023. Ank. 1 hit.
    PF12796. Ank_2. 1 hit.
    PF00385. Chromo. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 4 hits.
    SM00298. CHROMO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF54160. SSF54160. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 3 hits.
    PS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-860 (ISOFORM 1).
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lymph node.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Pancreas and PNS.
    6. "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 228-532 (ISOFORMS 1/2), SUBCELLULAR LOCATION, PHOSPHORYLATION.
      Tissue: Lymphoblast.
    7. "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-51; SER-319 AND SER-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-138; SER-149 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-51; SER-136; SER-138; SER-149; SER-188; SER-189; SER-192 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion."
      Kokura K., Sun L., Bedford M.T., Fang J.
      EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HISTONE H3K9ME3; DNMT3A; EHMT1 AND SETDB1, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-80.
    13. "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-51; SER-136; SER-138; SER-392; SER-400; SER-403 AND THR-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-51; SER-136; SER-138; SER-319; SER-392 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding."
      Chang Y., Horton J.R., Bedford M.T., Zhang X., Cheng X.
      J. Mol. Biol. 408:807-814(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 55-116 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE, DOMAIN CHROMO, SUBUNIT.
    17. "MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a."
      Chang Y., Sun L., Kokura K., Horton J.R., Fukuda M., Espejo A., Izumi V., Koomen J.M., Bedford M.T., Zhang X., Shinkai Y., Fang J., Cheng X.
      Nat. Commun. 2:533-533(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 55-116 IN COMPLEX WITH DNMT3A.
    18. "Structural basis for specific binding of human MPP8 chromodomain to histone H3 methylated at lysine 9."
      Li J., Li Z., Ruan J., Xu C., Tong Y., Pan P.W., Tempel W., Crombet L., Min J., Zang J.
      PLoS ONE 6:E25104-E25104(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 55-116 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE, DOMAIN CHROMO, SUBUNIT.

    Entry informationi

    Entry nameiMPP8_HUMAN
    AccessioniPrimary (citable) accession number: Q99549
    Secondary accession number(s): B7Z6F9
    , Q5JPE5, Q5JTQ0, Q86TK3, Q96MK4, Q9BTP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 117 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3