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Protein

M-phase phosphoprotein 8

Gene

Mphosph8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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:Mphosph8Imported
Synonyms:Mpp8By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi1305133. Mphosph8.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity

  • Note: Detected on heterochromatin. Dissociates from chromatin during interphase and early mitosis. Detected on nucleosomes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004159771 – 851M-phase phosphoprotein 8Add BLAST851

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51PhosphoserineBy similarity1
Modified residuei85PhosphoserineBy similarity1
Modified residuei136PhosphoserineBy similarity1
Modified residuei144PhosphothreonineBy similarity1
Modified residuei149Phosphoserine; by CDK1By similarity1
Modified residuei164Phosphoserine; by CDK1By similarity1
Modified residuei188PhosphoserineBy similarity1
Modified residuei263PhosphoserineBy similarity1
Modified residuei267PhosphoserineBy similarity1
Modified residuei274PhosphoserineBy similarity1
Modified residuei313PhosphoserineBy similarity1
Modified residuei379Phosphothreonine; by CDK1By similarity1
Modified residuei386PhosphoserineBy similarity1
Modified residuei394PhosphoserineBy similarity1
Modified residuei447PhosphothreonineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiG3V8T1.
PRIDEiG3V8T1.

PTM databases

iPTMnetiG3V8T1.
PhosphoSitePlusiG3V8T1.

Expressioni

Gene expression databases

BgeeiENSRNOG00000032888.
GenevisibleiG3V8T1. RN.

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

STRINGi10116.ENSRNOP00000040476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini59 – 118ChromoPROSITE-ProRule annotationAdd BLAST60
Repeati591 – 620ANK 1Add BLAST30
Repeati624 – 653ANK 2Add BLAST30
Repeati657 – 686ANK 3Add BLAST30
Repeati690 – 719ANK 4Add BLAST30

Region

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi152 – 478Lys-richAdd BLAST327

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.
InParanoidiG3V8T1.
OrthoDBiEOG091G02M0.

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.

G3V8T1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATEENMS VAALVMSVPD NIGRSPEVEG GGAAGEEKDA ATKGTVAVGD
60 70 80 90 100
SEEDGEDVFE VERILDMKCE GGKNLYKVRW KGYTSDDDTW EPEVHLEDCK
110 120 130 140 150
EVLLEFRKKV AENKAKAVRK DIQKLSLNND IFEADSDIDQ QGDTKEDTSP
160 170 180 190 200
RKKKKKIKYK EDKSPDDLRK KRAKMGKLKD KFKTELESTS EILGFDVKTK
210 220 230 240 250
KRILEVKEEL KDSKKPKKDE IKETKKTKRA DIRDLKIKIR EDVKDNRKTK
260 270 280 290 300
KERYIDSPLE SESPNDSFTL EDESEDFLSD NKEKQNVRTA KDKTGQDTVQ
310 320 330 340 350
ESIFEKHLDD LISIEEAGTR VRRKKKQPRK FEEPKEIKKL ENTNNFLERK
360 370 380 390 400
MIPKKQRNQD KGRSNPELSK LPSPVFAQTM KSLRLSGEEK GLKSSDLAEE
410 420 430 440 450
EKERKNEPKE KYQKRYDFDK EEKARKEPKG LKSFKEIRNA FDLFKKTAEE
460 470 480 490 500
KNDLENNSKR EEISLDYKIT HDNKTKDKCS LREERNTRDE TDTWAYIAAE
510 520 530 540 550
GDQEVSDSVC QTDESSDGKQ PILSLGMDLQ LEWMKLEDFQ KHLDGEDEPF
560 570 580 590 600
ITANRIPSNL LRDAVKNGDY IAVKVALNSN EEYNLDQEDS TGMTLVMLAA
610 620 630 640 650
AGGQDDLLRL LITKGAKVNG RQKNGTTALI HAAEKNFLTT VAILLEAGAF
660 670 680 690 700
VNVQQSNGET ALMKACKRGN SDIVRLVIEC GADCNILSKH QNSALYFAKQ
710 720 730 740 750
CNNVLVYELL KSHLETLSRV AEETIRDYFE SRLALLEPVF PIACHRLCEG
760 770 780 790 800
PDFSTDFNYM PPQNMPEGSG VLLFIFHANF LGKDVIARLC GPCSVQAVVL
810 820 830 840 850
NDKFQLPVFL DSHFVYSFSP VAGPNKLFIR LTEAPFAKVK LLIGAYRVQL

Q
Length:851
Mass (Da):96,784
Last modified:November 16, 2011 - v1
Checksum:iA5DFDBCC343479A3
GO

Sequence cautioni

The sequence AAH99116 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474049 Genomic DNA. Translation: EDM14330.1.
BC099116 mRNA. Translation: AAH99116.1. Different initiation.
RefSeqiNP_001017375.2. NM_001017375.2.
UniGeneiRn.42579.

Genome annotation databases

EnsembliENSRNOT00000028145; ENSRNOP00000028145; ENSRNOG00000051238.
GeneIDi290270.
KEGGirno:290270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474049 Genomic DNA. Translation: EDM14330.1.
BC099116 mRNA. Translation: AAH99116.1. Different initiation.
RefSeqiNP_001017375.2. NM_001017375.2.
UniGeneiRn.42579.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040476.

PTM databases

iPTMnetiG3V8T1.
PhosphoSitePlusiG3V8T1.

Proteomic databases

PaxDbiG3V8T1.
PRIDEiG3V8T1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028145; ENSRNOP00000028145; ENSRNOG00000051238.
GeneIDi290270.
KEGGirno:290270.

Organism-specific databases

CTDi54737.
RGDi1305133. Mphosph8.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG1911. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00730000111087.
HOGENOMiHOG000290641.
InParanoidiG3V8T1.
OrthoDBiEOG091G02M0.

Miscellaneous databases

PROiG3V8T1.

Gene expression databases

BgeeiENSRNOG00000032888.
GenevisibleiG3V8T1. RN.

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_RAT
AccessioniPrimary (citable) accession number: G3V8T1
Secondary accession number(s): Q4KLM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: November 16, 2011
Last modified: November 2, 2016
This is version 35 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. 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.