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Protein

M-phase phosphoprotein 8

Gene

Mphosph8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. Binds 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase phosphoprotein 8By similarity
Gene namesi
Name:Mphosph8By similarityImported
Synonyms:Mpp8By similarity
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1922589. Mphosph8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 858858M-phase phosphoprotein 8PRO_0000415976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphoserineCombined sources
Modified residuei85 – 851PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei144 – 1441PhosphothreonineCombined sources
Modified residuei149 – 1491Phosphoserine; by CDK1By similarity
Modified residuei164 – 1641Phosphoserine; by CDK1By similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei267 – 2671PhosphoserineCombined sources
Modified residuei271 – 2711PhosphoserineCombined sources
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei318 – 3181PhosphoserineBy similarity
Modified residuei385 – 3851Phosphothreonine; by CDK1By similarity
Modified residuei392 – 3921PhosphoserineBy similarity
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei453 – 4531PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated in M (mitotic) phase. Phosphorylation by CDK1 promotes dissociation from chromatin.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3TYA6.
MaxQBiQ3TYA6.
PaxDbiQ3TYA6.
PRIDEiQ3TYA6.

PTM databases

iPTMnetiQ3TYA6.

Expressioni

Gene expression databases

BgeeiQ3TYA6.
GenevisibleiQ3TYA6. MM.

Interactioni

Subunit structurei

Homodimer. Interacts (via chromo domain) with histone H3K9me3. Has the highest affinity for H3K9me3, and lesser affinity for H3K9me2 and H3K9me1. Component of the HUSH complex; at least composed of FAM208A/TASOR, PPHLN1 and MPHOSPH8. Interacts with DNMT3, EHMT1 and SETDB1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei59 – 591Interaction with histone H3K9me3By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112170.

Structurei

3D structure databases

ProteinModelPortaliQ3TYA6.
SMRiQ3TYA6. Positions 55-115, 568-753.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 11860ChromoPROSITE-ProRule annotationAdd
BLAST
Repeati598 – 62730ANK 1Add
BLAST
Repeati631 – 66030ANK 2Add
BLAST
Repeati664 – 69330ANK 3Add
BLAST
Repeati697 – 72630ANK 4Add
BLAST

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 54Poly-Ala
Compositional biasi152 – 255104Lys-richAdd
BLAST
Compositional biasi330 – 491162Lys-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).By similarity

Sequence similaritiesi

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

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG1911. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00730000111087.
HOGENOMiHOG000290641.
HOVERGENiHBG052503.
InParanoidiQ3TYA6.
OMAiKYQKRHD.
OrthoDBiEOG74FF0B.
TreeFamiTF106394.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF00385. Chromo. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 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]

Sequencei

Sequence statusi: Complete.

Q3TYA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAEEGMS AAALVMSVPD SIGRSPESEG VGAGDEEKDA ATKGTVAVGD
60 70 80 90 100
SEEDGEDVFE VERILDMKCE GGKNLYKVRW KGYTSEDDTW EPEVHLEDCK
110 120 130 140 150
EVLLEFRKKL AENKAKAVRK DIQRLSLNND IFEADSDSDQ QSDTKEDISP
160 170 180 190 200
RKKKKKIKCK EETSPEDLRK KRTKMGKLKD KFKTELESTS EIIGFDVKTK
210 220 230 240 250
KRIWEVKEEL KDSKKPKKDE IKETKELKKA NKRAEVRDLK IKIREDVKEN
260 270 280 290 300
RKTKKERYIE SPLESESPND SLILEDDSED FISDNREENQ NVRSVRDKTA
310 320 330 340 350
QETVQEGIFE KHLDDLISIE EDAGTRVRRK KTKPRKFEEP KEIKKLESTN
360 370 380 390 400
AFLERRAIPK KQRNQDKGIS NLELNKLPSP VFAQTLKSSR LSGEEKSLKS
410 420 430 440 450
PDLAEEEKEK KNEPKGKYQK RYDLDKEEKA RKEPKVLKSF KEIRNAFDLF
460 470 480 490 500
KKTTEEKNDV LENNSKREEI SLDSKIMNDN KTKDKCSLKE KRNTRDETDT
510 520 530 540 550
WAYIAAEGDQ EVSDSVCQTD ETSDGRQPVL SLGMDLQLEW MKLEDFQKHL
560 570 580 590 600
DGEDEPFITT NRIPNNLLRD AVKNGDYIAV KVALNSNEEY NLDQEDSTGM
610 620 630 640 650
TLVMLAAAGG QDDLLRLLIT KGAKVNGRQK NGTTALIHAA EKNFLTTVAI
660 670 680 690 700
LLEAGAFVNV QQSNGETALM KACKRGNSDI VRLVIECGAD CNILSKHQNS
710 720 730 740 750
ALYFAKQCNN VLVYELLKSH LETLSRVAEE TIRDYFESRL ALLEPVFPIA
760 770 780 790 800
CHRLCEGPDF STDFNYMPPQ NMPEGSGVLL FIFHANFLGK DVIARLCGPC
810 820 830 840 850
SVQAVVLNDK FQLPVFLDSH FVYSFSPVAG PNKLFIRLTE APFAKVKLLI

GAYRVQLQ
Length:858
Mass (Da):97,467
Last modified:October 11, 2005 - v1
Checksum:i17C90A836A416964
GO

Sequence cautioni

The sequence AAI45701.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581K → E in BAE35129 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK158773 mRNA. Translation: BAE34657.1.
AK159495 mRNA. Translation: BAE35129.1.
AC154731 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36192.1.
BC145700 mRNA. Translation: AAI45701.1. Different initiation.
CCDSiCCDS49504.1.
RefSeqiNP_076262.2. NM_023773.2.
UniGeneiMm.152466.

Genome annotation databases

EnsembliENSMUST00000116468; ENSMUSP00000112170; ENSMUSG00000079184.
GeneIDi75339.
KEGGimmu:75339.
UCSCiuc011zmc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK158773 mRNA. Translation: BAE34657.1.
AK159495 mRNA. Translation: BAE35129.1.
AC154731 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36192.1.
BC145700 mRNA. Translation: AAI45701.1. Different initiation.
CCDSiCCDS49504.1.
RefSeqiNP_076262.2. NM_023773.2.
UniGeneiMm.152466.

3D structure databases

ProteinModelPortaliQ3TYA6.
SMRiQ3TYA6. Positions 55-115, 568-753.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112170.

PTM databases

iPTMnetiQ3TYA6.

Proteomic databases

EPDiQ3TYA6.
MaxQBiQ3TYA6.
PaxDbiQ3TYA6.
PRIDEiQ3TYA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000116468; ENSMUSP00000112170; ENSMUSG00000079184.
GeneIDi75339.
KEGGimmu:75339.
UCSCiuc011zmc.1. mouse.

Organism-specific databases

CTDi54737.
MGIiMGI:1922589. Mphosph8.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG1911. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00730000111087.
HOGENOMiHOG000290641.
HOVERGENiHBG052503.
InParanoidiQ3TYA6.
OMAiKYQKRHD.
OrthoDBiEOG74FF0B.
TreeFamiTF106394.

Miscellaneous databases

ChiTaRSiMphosph8. mouse.
PROiQ3TYA6.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TYA6.
GenevisibleiQ3TYA6. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF00385. Chromo. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Visual cortex.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    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.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-85; SER-136; SER-138; THR-144; SER-267 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Pancreas, Spleen and Testis.
  7. "Mitotic phosphorylation of MPP8 by cyclin-dependent kinases regulates chromatin dissociation."
    Nishigaki M., Kawada Y., Misaki T., Murata K., Goshima T., Hirokawa T., Yamada C., Shimada M., Nakanishi M.
    Biochem. Biophys. Res. Commun. 432:654-659(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMPP8_MOUSE
AccessioniPrimary (citable) accession number: Q3TYA6
Secondary accession number(s): A6H600, Q3TWY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.