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Protein

Chromatin modification-related protein MEAF6

Gene

MEAF6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.3 Publications

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H2A acetylation Source: UniProtKB
  3. histone H3-K14 acetylation Source: UniProtKB
  4. histone H4-K12 acetylation Source: UniProtKB
  5. histone H4-K5 acetylation Source: UniProtKB
  6. histone H4-K8 acetylation Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

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
Short name:
hEAF6
Sarcoma antigen NY-SAR-91
Gene namesi
Name:MEAF6
Synonyms:C1orf149, EAF6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25674. MEAF6.

Subcellular locationi

  1. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  4. NuA4 histone acetyltransferase complex Source: UniProtKB
  5. nucleolus Source: UniProtKB
  6. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MEAF6 may be a cause of endometrial stromal tumors. Translocation t(1;6)(p34;p21) with PHF1.

Organism-specific databases

PharmGKBiPA165751536.

Polymorphism and mutation databases

DMDMi74752760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 191190Chromatin modification-related protein MEAF6PRO_0000272609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Modified residuei69 – 691N6-acetyllysine1 Publication
Modified residuei74 – 741N6-acetyllysine1 Publication
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei120 – 1201Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HAF1.
PaxDbiQ9HAF1.
PRIDEiQ9HAF1.

PTM databases

PhosphoSiteiQ9HAF1.

Expressioni

Gene expression databases

BgeeiQ9HAF1.
CleanExiHS_C1orf149.
ExpressionAtlasiQ9HAF1. baseline and differential.
GenevestigatoriQ9HAF1.

Organism-specific databases

HPAiHPA029599.
HPA029600.

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, KAT7/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 BRPF3.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FXR2P511163EBI-399266,EBI-740459
LDOC1O957513EBI-399266,EBI-740738
PLEKHF2Q9H8W45EBI-399266,EBI-742388
TRIM54Q9BYV23EBI-399266,EBI-2130429

Protein-protein interaction databases

BioGridi122280. 30 interactions.
IntActiQ9HAF1. 9 interactions.
STRINGi9606.ENSP00000362166.

Structurei

3D structure databases

ProteinModelPortaliQ9HAF1.
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

eggNOGiNOG290756.
GeneTreeiENSGT00390000015257.
HOGENOMiHOG000290166.
InParanoidiQ9HAF1.
KOiK11344.
OMAiYQKETEY.
OrthoDBiEOG79CZ1M.
PhylomeDBiQ9HAF1.
TreeFamiTF324130.

Family and domain databases

InterProiIPR015418. Hist_AcTrfase_NuA4_cplx.
[Graphical view]
PfamiPF09340. NuA4. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HAF1-1) [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
MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED
60 70 80 90 100
TQMYGNIIRG WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV
110 120 130 140 150
SALAGVQDQL IEKREPGSGT ESDTSPDFHN QENEPSQEDP EDLDGSVQGV
160 170 180 190
KPQKAASSTS SGSHHSSHKK RKNKNRHRID LKLNKKPRAD Y
Length:191
Mass (Da):21,635
Last modified:March 1, 2001 - v1
Checksum:iC0FBC7566BAAF1F7
GO
Isoform 2 (identifier: Q9HAF1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     178-191: RIDLKLNKKPRADY → SPSGMFDYDFEYVY

Note: No experimental confirmation available.

Show »
Length:191
Mass (Da):21,625
Checksum:i4A46263CF13F3C99
GO
Isoform 3 (identifier: Q9HAF1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     178-178: R → SPSGMFDYDFE

Note: No experimental confirmation available.

Show »
Length:201
Mass (Da):22,755
Checksum:iE30FC55A4AB5EBA0
GO
Isoform 4 (identifier: Q9HAF1-4) [UniParc]FASTAAdd to basket

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

Note: Gene prediction based on EST data.

Show »
Length:192
Mass (Da):21,709
Checksum:i3DC03438B928A5A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AM → RG in AAO65179 (PubMed:12601173).Curated
Sequence conflicti4 – 41H → P in AAZ13760 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei178 – 19114RIDLK…PRADY → SPSGMFDYDFEYVY in isoform 2. 1 PublicationVSP_022450Add
BLAST
Alternative sequencei178 – 1781R → SPSGMFDYDFE in isoform 3. 1 PublicationVSP_022451
Alternative sequencei179 – 19113IDLKL…PRADY → MNVSPKTGWHQLHL in isoform 4. CuratedVSP_047018Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX538212 mRNA. Translation: CAD98071.1.
BX640719 mRNA. Translation: CAE45838.1.
AK021792 mRNA. Translation: BAB13898.1.
DQ099384 mRNA. Translation: AAZ13760.1.
AL034379 Genomic DNA. Translation: CAI20549.1.
AL034379 Genomic DNA. Translation: CAI20550.1.
BC056406 mRNA. Translation: AAH56406.1.
BC016328 mRNA. Translation: AAH16328.1.
AY211926 mRNA. Translation: AAO65179.1.
CCDSiCCDS418.1. [Q9HAF1-3]
CCDS59195.1. [Q9HAF1-4]
CCDS59196.1. [Q9HAF1-1]
RefSeqiNP_001257804.1. NM_001270875.1. [Q9HAF1-1]
NP_001257805.1. NM_001270876.1. [Q9HAF1-4]
NP_073593.2. NM_022756.5. [Q9HAF1-3]
UniGeneiHs.17118.

Genome annotation databases

EnsembliENST00000296214; ENSP00000296214; ENSG00000163875. [Q9HAF1-1]
ENST00000373073; ENSP00000362164; ENSG00000163875. [Q9HAF1-4]
ENST00000373075; ENSP00000362166; ENSG00000163875. [Q9HAF1-3]
ENST00000448519; ENSP00000394966; ENSG00000163875. [Q9HAF1-2]
GeneIDi64769.
KEGGihsa:64769.
UCSCiuc001cbe.2. human. [Q9HAF1-3]
uc001cbg.2. human. [Q9HAF1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX538212 mRNA. Translation: CAD98071.1.
BX640719 mRNA. Translation: CAE45838.1.
AK021792 mRNA. Translation: BAB13898.1.
DQ099384 mRNA. Translation: AAZ13760.1.
AL034379 Genomic DNA. Translation: CAI20549.1.
AL034379 Genomic DNA. Translation: CAI20550.1.
BC056406 mRNA. Translation: AAH56406.1.
BC016328 mRNA. Translation: AAH16328.1.
AY211926 mRNA. Translation: AAO65179.1.
CCDSiCCDS418.1. [Q9HAF1-3]
CCDS59195.1. [Q9HAF1-4]
CCDS59196.1. [Q9HAF1-1]
RefSeqiNP_001257804.1. NM_001270875.1. [Q9HAF1-1]
NP_001257805.1. NM_001270876.1. [Q9HAF1-4]
NP_073593.2. NM_022756.5. [Q9HAF1-3]
UniGeneiHs.17118.

3D structure databases

ProteinModelPortaliQ9HAF1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122280. 30 interactions.
IntActiQ9HAF1. 9 interactions.
STRINGi9606.ENSP00000362166.

PTM databases

PhosphoSiteiQ9HAF1.

Polymorphism and mutation databases

DMDMi74752760.

Proteomic databases

MaxQBiQ9HAF1.
PaxDbiQ9HAF1.
PRIDEiQ9HAF1.

Protocols and materials databases

DNASUi64769.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296214; ENSP00000296214; ENSG00000163875. [Q9HAF1-1]
ENST00000373073; ENSP00000362164; ENSG00000163875. [Q9HAF1-4]
ENST00000373075; ENSP00000362166; ENSG00000163875. [Q9HAF1-3]
ENST00000448519; ENSP00000394966; ENSG00000163875. [Q9HAF1-2]
GeneIDi64769.
KEGGihsa:64769.
UCSCiuc001cbe.2. human. [Q9HAF1-3]
uc001cbg.2. human. [Q9HAF1-1]

Organism-specific databases

CTDi64769.
GeneCardsiGC01M037951.
HGNCiHGNC:25674. MEAF6.
HPAiHPA029599.
HPA029600.
MIMi611001. gene.
neXtProtiNX_Q9HAF1.
PharmGKBiPA165751536.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG290756.
GeneTreeiENSGT00390000015257.
HOGENOMiHOG000290166.
InParanoidiQ9HAF1.
KOiK11344.
OMAiYQKETEY.
OrthoDBiEOG79CZ1M.
PhylomeDBiQ9HAF1.
TreeFamiTF324130.

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

Miscellaneous databases

GeneWikiiC1orf149.
GenomeRNAii64769.
NextBioi35466510.
PROiQ9HAF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAF1.
CleanExiHS_C1orf149.
ExpressionAtlasiQ9HAF1. baseline and differential.
GenevestigatoriQ9HAF1.

Family and domain databases

InterProiIPR015418. Hist_AcTrfase_NuA4_cplx.
[Graphical view]
PfamiPF09340. NuA4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Cerebellum and Fetal brain.
  2. "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 1).
    Tissue: Embryo.
  3. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Li M., Li H., Yang S.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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: Brain and Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-191 (ISOFORM 1).
  7. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
  8. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
  9. "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes."
    Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 280:13665-13670(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
  10. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
    Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
    Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX, IDENTIFICATION IN THE HBO1 COMPLEX, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69 AND LYS-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial stromal sarcoma."
    Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M., Bjerkehagen B., Davidson B., Heim S.
    PLoS ONE 7:E39354-E39354(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PHF1.

Entry informationi

Entry nameiEAF6_HUMAN
AccessioniPrimary (citable) accession number: Q9HAF1
Secondary accession number(s): B1AK64
, Q4F967, Q7Z311, Q86WE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 109 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.