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

O95619 (YETS4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
YEATS domain-containing protein 4
Alternative name(s):
Glioma-amplified sequence 41
Short name=Gas41
NuMA-binding protein 1
Short name=NuBI-1
Short name=NuBI1
Gene names
Name:YEATS4
Synonyms:GAS41
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones 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. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Ref.10

Subunit structure

Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. YEATS4 interacts with MLLT10/AF10. YEATS4 may also interact with the SWI/SNF component SMARCB1/BAF47, TACC1 and TACC2, and the nuclear matrix protein NUMA1. Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus Ref.2.

Tissue specificity

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. Ref.2

Sequence similarities

Contains 1 YEATS domain.

Sequence caution

The sequence CAC01935.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGrowth regulation
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainCoiled coil
   Molecular functionChromatin regulator
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H2A acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

mitotic nuclear division

Non-traceable author statement Ref.2. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement Ref.2. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear matrix

Non-traceable author statement Ref.2. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

protein C-terminus binding

Inferred from physical interaction Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: IntAct

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

structural constituent of cytoskeleton

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TACC1O754106EBI-399269,EBI-624237

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227YEATS domain-containing protein 4
PRO_0000066204

Regions

Domain22 – 126105YEATS
Region163 – 22765Interaction with MLLT10
Region168 – 22760Interaction with TACC1
Coiled coil178 – 22649 Potential

Experimental info

Sequence conflict1591R → C in CAC01935. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O95619 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 34C4692B227A7B85

FASTA22726,499
        10         20         30         40         50         60 
MFKRMAEFGP DSGGRVKGVT IVKPIVYGNV ARYFGKKREE DGHTHQWTVY VKPYRNEDMS 

        70         80         90        100        110        120 
AYVKKIQFKL HESYGNPLRV VTKPPYEITE TGWGEFEIII KIFFIDPNER PVTLYHLLKL 

       130        140        150        160        170        180 
FQSDTNAMLG KKTVVSEFYD EMIFQDPTAM MQQLLTTSRQ LTLGAYKHET EFAELEVKTR 

       190        200        210        220 
EKLEAAKKKT SFEIAELKER LKASRETINC LKNEIRKLEE DDQAKDI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel transcription factor-like gene amplified in human glioma including astrocytoma grade I."
Fischer U., Heckel D., Michel A., Janka M., Hulsebos T., Meese E.
Hum. Mol. Genet. 6:1817-1822(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"GAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMA."
Harborth J., Weber K., Osborn M.
J. Biol. Chem. 275:31979-31985(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH NUMA1, TISSUE SPECIFICITY.
[3]"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].
[4]"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].
[5]"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: PROTEIN SEQUENCE OF 5-15; 18-32; 56-64; 120-131; 168-178 AND 217-227, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes in human cells."
Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.
Biochem. J. 363:195-200(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TACC1.
[7]"The MLL fusion partner AF10 binds GAS41, a protein that interacts with the human SWI/SNF complex."
Debernardi S., Bassini A., Jones L.K., Chaplin T., Linder B., de Bruijn D.R.H., Meese E., Young B.D.
Blood 99:275-281(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLLT10 AND SMARCB1.
[8]"Molecular cloning, genomic structure and interactions of the putative breast tumor suppressor TACC2."
Lauffart B., Gangisetty O., Still I.H.
Genomics 81:192-201(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TACC2.
[9]"The highly conserved and multifunctional NuA4 HAT complex."
Doyon Y., Cote J.
Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON NUA4 COMPLEX.
[10]"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 NUA4 COMPLEX, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U61384 mRNA. Translation: AAD12188.1.
AJ245746 mRNA. Translation: CAC01935.1. Different initiation.
AK001413 mRNA. Translation: BAA91678.1.
BC000994 mRNA. Translation: AAH00994.1.
CCDSCCDS8990.1.
RefSeqNP_006521.1. NM_006530.2.
UniGeneHs.4029.

3D structure databases

ProteinModelPortalO95619.
SMRO95619. Positions 13-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113761. 28 interactions.
IntActO95619. 10 interactions.
MINTMINT-3003084.
STRING9606.ENSP00000247843.

PTM databases

PhosphoSiteO95619.

Proteomic databases

MaxQBO95619.
PaxDbO95619.
PeptideAtlasO95619.
PRIDEO95619.

Protocols and materials databases

DNASU8089.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247843; ENSP00000247843; ENSG00000127337.
GeneID8089.
KEGGhsa:8089.
UCSCuc001sux.3. human.

Organism-specific databases

CTD8089.
GeneCardsGC12P069753.
HGNCHGNC:24859. YEATS4.
MIM602116. gene.
neXtProtNX_O95619.
PharmGKBPA134992686.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5033.
HOGENOMHOG000190181.
HOVERGENHBG061271.
InParanoidO95619.
KOK11341.
OrthoDBEOG73FQNN.
PhylomeDBO95619.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressO95619.
BgeeO95619.
CleanExHS_YEATS4.
GenevestigatorO95619.

Family and domain databases

InterProIPR005033. YEATS.
[Graphical view]
PANTHERPTHR23195. PTHR23195. 1 hit.
PfamPF03366. YEATS. 1 hit.
[Graphical view]
PROSITEPS51037. YEATS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi8089.
NextBio30722.
PROO95619.
SOURCESearch...

Entry information

Entry nameYETS4_HUMAN
AccessionPrimary (citable) accession number: O95619
Secondary accession number(s): Q9NQD0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 115 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 12

Human chromosome 12: entries, gene names and cross-references to MIM