Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00004159761 – 858M-phase phosphoprotein 8Add BLAST858

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51PhosphoserineCombined sources1
Modified residuei85PhosphoserineCombined sources1
Modified residuei136PhosphoserineCombined sources1
Modified residuei138PhosphoserineCombined sources1
Modified residuei144PhosphothreonineCombined sources1
Modified residuei149Phosphoserine; by CDK1By similarity1
Modified residuei164Phosphoserine; by CDK1By similarity1
Modified residuei188PhosphoserineBy similarity1
Modified residuei267PhosphoserineCombined sources1
Modified residuei271PhosphoserineCombined sources1
Modified residuei278PhosphoserineBy similarity1
Modified residuei318PhosphoserineBy similarity1
Modified residuei385Phosphothreonine; by CDK1By similarity1
Modified residuei392PhosphoserineBy similarity1
Modified residuei400PhosphoserineBy similarity1
Modified residuei453PhosphothreonineBy similarity1

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.
PeptideAtlasiQ3TYA6.
PRIDEiQ3TYA6.

PTM databases

iPTMnetiQ3TYA6.
PhosphoSitePlusiQ3TYA6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000079184.
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)DescriptionActionsGraphical viewLength
Sitei59Interaction with histone H3K9me3By similarity1

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112170.

Structurei

3D structure databases

ProteinModelPortaliQ3TYA6.
SMRiQ3TYA6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini59 – 118ChromoPROSITE-ProRule annotationAdd BLAST60
Repeati598 – 627ANK 1Add BLAST30
Repeati631 – 660ANK 2Add BLAST30
Repeati664 – 693ANK 3Add BLAST30
Repeati697 – 726ANK 4Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 87Histone H3K9me3 bindingBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 5Poly-Ala4
Compositional biasi152 – 255Lys-richAdd BLAST104
Compositional biasi330 – 491Lys-richAdd BLAST162

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.
OrthoDBiEOG091G02M0.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti158K → E in BAE35129 (PubMed:16141072).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112170.

PTM databases

iPTMnetiQ3TYA6.
PhosphoSitePlusiQ3TYA6.

Proteomic databases

EPDiQ3TYA6.
MaxQBiQ3TYA6.
PaxDbiQ3TYA6.
PeptideAtlasiQ3TYA6.
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.
OrthoDBiEOG091G02M0.
TreeFamiTF106394.

Miscellaneous databases

ChiTaRSiMphosph8. mouse.
PROiQ3TYA6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000079184.
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...

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: November 2, 2016
This is version 100 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.