YEATS domain-containing protein 4 - Homo sapiens (Human)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
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 HTATIP/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 EAF6. 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.6 Ref.7 Ref.8
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.

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Ontologies

Keywords
Biological process	Growth regulation Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
Molecular function	Chromatin regulator
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW mitosis Ref.2 Non-traceable author statement. Source: UniProtKB positive regulation of transcription, DNA-dependent Ref.2 Non-traceable author statement. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Ref.10 Inferred from direct assay. Source: UniProtKB nuclear matrix Ref.2 Non-traceable author statement. Source: UniProtKB
Molecular function	protein C-terminus binding Ref.2 Inferred from physical interaction. Source: UniProtKB structural constituent of cytoskeleton Ref.2 Non-traceable author statement. Source: UniProtKB transcription factor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
TACC1	O75410	3	EBI-399269,EBI-624237

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 227

227

YEATS domain-containing protein 4

PRO_0000066204

Regions

Domain

22 – 126

105

YEATS

Region

163 – 227

65

Interaction with MLLT10

Region

168 – 227

60

Interaction with TACC1

Coiled coil

178 – 226

49

Potential

Experimental info

Sequence conflict

159

1

R → C in CAC01935. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O95619-1 [UniParc].

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

227

26,499

        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

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References

	« Hide 'large scale' referencesShow '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: 9302258] [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: 10913114] [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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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: 15489334] [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: 12963728] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-15; 18-32; 56-64; 120-131; 168-178 AND 217-227, IDENTIFICATION IN NUA4 COMPLEX, 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: 11903063] [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: 11756182] [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: 12620397] [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: 15196461] [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: 14966270] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U61384 mRNA. Translation: AAD12188.1. AJ245746 mRNA. Translation: CAC01935.1. Different initiation. AK001413 mRNA. Translation: BAA91678.1. BC000994 mRNA. Translation: AAH00994.1.
IPI	IPI00008536.
RefSeq	NP_006521.1.
UniGene	Hs.4029
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O95619. 8 interactions.
Proteomic databases
PeptideAtlas	O95619.
PRIDE	O95619.
Genome annotation databases
Ensembl	ENSG00000127337. Homo sapiens. [Contig view]
GeneID	8089.
KEGG	hsa:8089.
Organism-specific databases
GeneCards	GC12P068040.
H-InvDB	HIX0019068.
HGNC	HGNC:24859. YEATS4.
MIM	602116. gene.
Orphanet	360. Glioblastoma.
PharmGKB	PA134992686.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O95619.
HOVERGEN	O95619.
OMA	O95619. HESYANP.
Gene expression databases
ArrayExpress	O95619.
Bgee	O95619.
CleanEx	HS_YEATS4.
GermOnline	ENSG00000127337. Homo sapiens.
Family and domain databases
InterPro	IPR005033. YEATS. [Graphical view]
PANTHER	PTHR23195. YEATS. 1 hit.
Pfam	PF03366. YEATS. 1 hit. [Graphical view]
PROSITE	PS51037. YEATS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	30722.
SOURCE	Search...

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Entry information

Entry name

YETS4_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents