Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9HAF1 (EAF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MEAF6
Synonyms:C1orf149, EAF6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.12

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Nucleusnucleolus Ref.12.

Involvement in disease

A chromosomal aberration involving MEAF6 may be a cause of endometrial stromal tumors. Translocation t(1;6)(p34;p21) with PHF1. Ref.17

Sequence similarities

Belongs to the EAF6 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainCoiled coil
   Molecular functionActivator
Chromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H2A acetylation

Inferred from direct assay Ref.8. Source: UniProtKB

histone H3-K14 acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

histone H4-K12 acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMOZ/MORF histone acetyltransferase complex

Inferred from direct assay Ref.10Ref.12. Source: UniProtKB

NuA4 histone acetyltransferase complex

Inferred from direct assay Ref.8Ref.10. Source: UniProtKB

centrosome

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay Ref.12. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16189514PubMed 19060904. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FXR2P511163EBI-399266,EBI-740459

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HAF1-1)

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.
Isoform 2 (identifier: Q9HAF1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     178-191: RIDLKLNKKPRADY → SPSGMFDYDFEYVY
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HAF1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     178-178: R → SPSGMFDYDFE
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9HAF1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     179-191: IDLKLNKKPRADY → MNVSPKTGWHQLHL
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 191190Chromatin modification-related protein MEAF6
PRO_0000272609

Regions

Coiled coil11 – 4737 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue61N6-acetyllysine By similarity
Modified residue691N6-acetyllysine Ref.14
Modified residue741N6-acetyllysine Ref.14
Modified residue1181Phosphoserine Ref.13
Modified residue1201Phosphothreonine Ref.13

Natural variations

Alternative sequence178 – 19114RIDLK…PRADY → SPSGMFDYDFEYVY in isoform 2.
VSP_022450
Alternative sequence1781R → SPSGMFDYDFE in isoform 3.
VSP_022451
Alternative sequence179 – 19113IDLKL…PRADY → MNVSPKTGWHQLHL in isoform 4.
VSP_047018

Experimental info

Sequence conflict2 – 32AM → RG in AAO65179. Ref.6
Sequence conflict41H → P in AAZ13760. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C0FBC7566BAAF1F7

FASTA19121,635
        10         20         30         40         50         60 
MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG 

        70         80         90        100        110        120 
WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT 

       130        140        150        160        170        180 
ESDTSPDFHN QENEPSQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHRID 

       190 
LKLNKKPRAD Y 

« Hide

Isoform 2 [UniParc].

Checksum: 4A46263CF13F3C99
Show »

FASTA19121,625
Isoform 3 [UniParc].

Checksum: E30FC55A4AB5EBA0
Show »

FASTA20122,755
Isoform 4 [UniParc].

Checksum: 3DC03438B928A5A3
Show »

FASTA19221,709

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Immunomic analysis of human sarcoma."
Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.
Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes."
Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J.
Mol. Cell. Biol. 28:6828-6843(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS418.1. [Q9HAF1-3]
CCDS59195.1. [Q9HAF1-4]
CCDS59196.1. [Q9HAF1-1]
RefSeqNP_001257804.1. NM_001270875.1. [Q9HAF1-1]
NP_001257805.1. NM_001270876.1. [Q9HAF1-4]
NP_073593.2. NM_022756.5. [Q9HAF1-3]
UniGeneHs.17118.

3D structure databases

ProteinModelPortalQ9HAF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122280. 21 interactions.
IntActQ9HAF1. 7 interactions.
STRING9606.ENSP00000362166.

PTM databases

PhosphoSiteQ9HAF1.

Polymorphism databases

DMDM74752760.

Proteomic databases

MaxQBQ9HAF1.
PaxDbQ9HAF1.
PRIDEQ9HAF1.

Protocols and materials databases

DNASU64769.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296214; ENSP00000296214; ENSG00000163875. [Q9HAF1-1]
ENST00000373073; ENSP00000362164; ENSG00000163875. [Q9HAF1-4]
ENST00000373075; ENSP00000362166; ENSG00000163875. [Q9HAF1-3]
ENST00000448519; ENSP00000394966; ENSG00000163875. [Q9HAF1-2]
GeneID64769.
KEGGhsa:64769.
UCSCuc001cbe.2. human. [Q9HAF1-3]
uc001cbg.2. human. [Q9HAF1-1]

Organism-specific databases

CTD64769.
GeneCardsGC01M037951.
HGNCHGNC:25674. MEAF6.
HPAHPA029599.
HPA029600.
MIM611001. gene.
neXtProtNX_Q9HAF1.
PharmGKBPA165751536.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290756.
HOGENOMHOG000290166.
KOK11344.
OMAATAGKAN.
OrthoDBEOG79CZ1M.
PhylomeDBQ9HAF1.
TreeFamTF324130.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ9HAF1.
BgeeQ9HAF1.
CleanExHS_C1orf149.
GenevestigatorQ9HAF1.

Family and domain databases

InterProIPR015418. Hist_AcTrfase_NuA4_cplx.
[Graphical view]
PfamPF09340. NuA4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiC1orf149.
GenomeRNAi64769.
NextBio35466510.
PROQ9HAF1.
SOURCESearch...

Entry information

Entry nameEAF6_HUMAN
AccessionPrimary (citable) accession number: Q9HAF1
Secondary accession number(s): B1AK64 expand/collapse secondary AC list , Q4F967, Q7Z311, Q86WE3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM