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Q99549

- MPP8_HUMAN

UniProt

Q99549 - MPP8_HUMAN

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Protein

M-phase phosphoprotein 8

Gene
MPHOSPH8, MPP8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Synonyms:MPP8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:29810. MPHOSPH8.

Subcellular locationi

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

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
Complete GO annotation...

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 – 511Phosphoserine5 Publications
Modified residuei136 – 1361Phosphoserine4 Publications
Modified residuei138 – 1381Phosphoserine4 Publications
Modified residuei149 – 1491Phosphoserine2 Publications
Modified residuei188 – 1881Phosphoserine1 Publication
Modified residuei189 – 1891Phosphoserine2 Publications
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei272 – 2721Phosphoserine Reviewed prediction
Modified residuei319 – 3191Phosphoserine2 Publications
Modified residuei334 – 3341Phosphothreonine Reviewed prediction
Modified residuei385 – 3851Phosphothreonine Reviewed prediction
Modified residuei392 – 3921Phosphoserine3 Publications
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine3 Publications
Modified residuei454 – 4541Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated in M (mitotic) phase.1 Publication

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 SETDB1.3 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.

Miscellaneous databases

EvolutionaryTraceiQ99549.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 11860ChromoAdd
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.
Contains 1 chromo domain.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei820 – 86041DSHFV…RVQLQ → TGSRSVVQAGVQWRGLQLTG VLTSQAQAILPPQPPNYLGL KMHATTSG in isoform 2. VSP_031523Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5305DGRQQ → GEFGI in CAA66912. 1 Publication
Sequence conflicti860 – 8601Q → QPNRRDWAEFS in AAH46214. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 116 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

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