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Protein

Chromatin modification-related protein MEAF6

Gene

Meaf6

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

Functioni

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.
R-MMU-6804758. Regulation of TP53 Activity through Acetylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin modification-related protein MEAF6
Short name:
MYST/Esa1-associated factor 6
Alternative name(s):
Esa1-associated factor 6 homolog
Short name:
Protein EAF6 homolog
Gene namesi
Name:Meaf6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1917338. Meaf6.

Subcellular locationi

  • Nucleusnucleolus By similarity
  • Chromosomecentromerekinetochore By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 191190Chromatin modification-related protein MEAF6PRO_0000272610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei6 – 61N6-acetyllysineCombined sources
Modified residuei69 – 691N6-acetyllysineCombined sources
Modified residuei74 – 741N6-acetyllysineCombined sources
Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei120 – 1201PhosphothreonineCombined sources
Isoform 2 (identifier: Q2VPQ9-2)
Modified residuei182 – 1821PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ2VPQ9.
MaxQBiQ2VPQ9.
PaxDbiQ2VPQ9.
PeptideAtlasiQ2VPQ9.
PRIDEiQ2VPQ9.

PTM databases

iPTMnetiQ2VPQ9.
PhosphoSiteiQ2VPQ9.

Expressioni

Gene expression databases

BgeeiQ2VPQ9.
CleanExiMM_2310005N01RIK.
ExpressionAtlasiQ2VPQ9. baseline and differential.
GenevisibleiQ2VPQ9. MM.

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5 and the subunits EP400, TRRAP, BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A, MORF4L1, MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi213858. 1 interaction.
IntActiQ2VPQ9. 1 interaction.
MINTiMINT-4127483.
STRINGi10090.ENSMUSP00000053543.

Structurei

3D structure databases

ProteinModelPortaliQ2VPQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili11 – 4737Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the EAF6 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3856. Eukaryota.
ENOG4111IAX. LUCA.
GeneTreeiENSGT00390000015257.
InParanoidiQ2VPQ9.
KOiK11344.
OrthoDBiEOG79CZ1M.
TreeFamiTF324130.

Family and domain databases

InterProiIPR015418. Eaf6.
[Graphical view]
PfamiPF09340. NuA4. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2VPQ9-1) [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

        10         20         30         40         50
MAMHNKTAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED
60 70 80 90 100
TQMYGNIIRG WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV
110 120 130 140 150
SALAGVQDQL IEKREPGSGT ESDTSPDFHN QENEPAQEDP EDLDGSVQGV
160 170 180 190
KPQKAASSTS SGSHHSSHKK RKNKNRHRID LKLNKKPRAD Y
Length:191
Mass (Da):21,649
Last modified:January 10, 2006 - v1
Checksum:i4B9EDC2812CFF1FD
GO
Isoform 2 (identifier: Q2VPQ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-191: IDLKLNKKPRADY → MNVSPQTGWHQLHL

Note: No experimental confirmation available.Combined sources
Show »
Length:192
Mass (Da):21,723
Checksum:i2F595123C751C0A3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei179 – 19113IDLKL…PRADY → MNVSPQTGWHQLHL in isoform 2. 1 PublicationVSP_022452Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009177 mRNA. Translation: BAB26123.1.
AL626775 Genomic DNA. Translation: CAM20901.1.
BC108404 mRNA. Translation: AAI08405.1.
CCDSiCCDS18637.1. [Q2VPQ9-2]
CCDS71467.1. [Q2VPQ9-1]
RefSeqiNP_001277630.1. NM_001290701.1. [Q2VPQ9-1]
NP_081586.1. NM_027310.4. [Q2VPQ9-2]
UniGeneiMm.291214.

Genome annotation databases

EnsembliENSMUST00000055213; ENSMUSP00000053543; ENSMUSG00000028863. [Q2VPQ9-2]
ENSMUST00000154689; ENSMUSP00000122288; ENSMUSG00000028863. [Q2VPQ9-1]
GeneIDi70088.
KEGGimmu:70088.
UCSCiuc008urs.2. mouse. [Q2VPQ9-2]
uc008uru.2. mouse. [Q2VPQ9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009177 mRNA. Translation: BAB26123.1.
AL626775 Genomic DNA. Translation: CAM20901.1.
BC108404 mRNA. Translation: AAI08405.1.
CCDSiCCDS18637.1. [Q2VPQ9-2]
CCDS71467.1. [Q2VPQ9-1]
RefSeqiNP_001277630.1. NM_001290701.1. [Q2VPQ9-1]
NP_081586.1. NM_027310.4. [Q2VPQ9-2]
UniGeneiMm.291214.

3D structure databases

ProteinModelPortaliQ2VPQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213858. 1 interaction.
IntActiQ2VPQ9. 1 interaction.
MINTiMINT-4127483.
STRINGi10090.ENSMUSP00000053543.

PTM databases

iPTMnetiQ2VPQ9.
PhosphoSiteiQ2VPQ9.

Proteomic databases

EPDiQ2VPQ9.
MaxQBiQ2VPQ9.
PaxDbiQ2VPQ9.
PeptideAtlasiQ2VPQ9.
PRIDEiQ2VPQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055213; ENSMUSP00000053543; ENSMUSG00000028863. [Q2VPQ9-2]
ENSMUST00000154689; ENSMUSP00000122288; ENSMUSG00000028863. [Q2VPQ9-1]
GeneIDi70088.
KEGGimmu:70088.
UCSCiuc008urs.2. mouse. [Q2VPQ9-2]
uc008uru.2. mouse. [Q2VPQ9-1]

Organism-specific databases

CTDi64769.
MGIiMGI:1917338. Meaf6.

Phylogenomic databases

eggNOGiKOG3856. Eukaryota.
ENOG4111IAX. LUCA.
GeneTreeiENSGT00390000015257.
InParanoidiQ2VPQ9.
KOiK11344.
OrthoDBiEOG79CZ1M.
TreeFamiTF324130.

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.
R-MMU-6804758. Regulation of TP53 Activity through Acetylation.

Miscellaneous databases

ChiTaRSiMeaf6. mouse.
PROiQ2VPQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ2VPQ9.
CleanExiMM_2310005N01RIK.
ExpressionAtlasiQ2VPQ9. baseline and differential.
GenevisibleiQ2VPQ9. MM.

Family and domain databases

InterProiIPR015418. Eaf6.
[Graphical view]
PfamiPF09340. NuA4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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: Jaw and Limb.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-6; LYS-69 AND LYS-74, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEAF6_MOUSE
AccessioniPrimary (citable) accession number: Q2VPQ9
Secondary accession number(s): B1ASC6, Q9D7J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 10, 2006
Last modified: July 6, 2016
This is version 78 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.