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Protein

YEATS domain-containing protein 4

Gene

YEATS4

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 (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.1 Publication

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • protein C-terminus binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

  • chromatin organization Source: Reactome
  • histone H2A acetylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of growth Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
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 namesi
Name:YEATS4
Synonyms:GAS41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24859. YEATS4.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • cytoplasm Source: HPA
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992686.

Polymorphism and mutation databases

BioMutaiYEATS4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227YEATS domain-containing protein 4PRO_0000066204Add
BLAST

Proteomic databases

MaxQBiO95619.
PaxDbiO95619.
PeptideAtlasiO95619.
PRIDEiO95619.

PTM databases

PhosphoSiteiO95619.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.1 Publication

Gene expression databases

BgeeiO95619.
CleanExiHS_YEATS4.
ExpressionAtlasiO95619. baseline and differential.
GenevisibleiO95619. HS.

Interactioni

Subunit structurei

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 NUMA1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TACC1O754106EBI-399269,EBI-624237

Protein-protein interaction databases

BioGridi113761. 58 interactions.
IntActiO95619. 10 interactions.
MINTiMINT-3003084.
STRINGi9606.ENSP00000247843.

Structurei

3D structure databases

ProteinModelPortaliO95619.
SMRiO95619. Positions 13-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 126105YEATSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 22765Interaction with MLLT10Add
BLAST
Regioni168 – 22760Interaction with TACC1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili178 – 22649Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 YEATS domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5033.
GeneTreeiENSGT00530000063543.
HOGENOMiHOG000190181.
HOVERGENiHBG061271.
InParanoidiO95619.
KOiK11341.
OrthoDBiEOG73FQNN.
PhylomeDBiO95619.

Family and domain databases

InterProiIPR005033. YEATS.
[Graphical view]
PANTHERiPTHR23195. PTHR23195. 1 hit.
PfamiPF03366. YEATS. 1 hit.
[Graphical view]
PROSITEiPS51037. YEATS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRMAEFGP DSGGRVKGVT IVKPIVYGNV ARYFGKKREE DGHTHQWTVY
60 70 80 90 100
VKPYRNEDMS AYVKKIQFKL HESYGNPLRV VTKPPYEITE TGWGEFEIII
110 120 130 140 150
KIFFIDPNER PVTLYHLLKL FQSDTNAMLG KKTVVSEFYD EMIFQDPTAM
160 170 180 190 200
MQQLLTTSRQ LTLGAYKHET EFAELEVKTR EKLEAAKKKT SFEIAELKER
210 220
LKASRETINC LKNEIRKLEE DDQAKDI
Length:227
Mass (Da):26,499
Last modified:May 1, 1999 - v1
Checksum:i34C4692B227A7B85
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591R → C in CAC01935 (PubMed:10913114).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61384 mRNA. Translation: AAD12188.1.
AJ245746 mRNA. Translation: CAC01935.1. Different initiation.
AK001413 mRNA. Translation: BAA91678.1.
BC000994 mRNA. Translation: AAH00994.1.
CCDSiCCDS8990.1.
RefSeqiNP_001287879.1. NM_001300950.1.
NP_006521.1. NM_006530.3.
UniGeneiHs.4029.

Genome annotation databases

EnsembliENST00000247843; ENSP00000247843; ENSG00000127337.
GeneIDi8089.
KEGGihsa:8089.
UCSCiuc001sux.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61384 mRNA. Translation: AAD12188.1.
AJ245746 mRNA. Translation: CAC01935.1. Different initiation.
AK001413 mRNA. Translation: BAA91678.1.
BC000994 mRNA. Translation: AAH00994.1.
CCDSiCCDS8990.1.
RefSeqiNP_001287879.1. NM_001300950.1.
NP_006521.1. NM_006530.3.
UniGeneiHs.4029.

3D structure databases

ProteinModelPortaliO95619.
SMRiO95619. Positions 13-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113761. 58 interactions.
IntActiO95619. 10 interactions.
MINTiMINT-3003084.
STRINGi9606.ENSP00000247843.

PTM databases

PhosphoSiteiO95619.

Polymorphism and mutation databases

BioMutaiYEATS4.

Proteomic databases

MaxQBiO95619.
PaxDbiO95619.
PeptideAtlasiO95619.
PRIDEiO95619.

Protocols and materials databases

DNASUi8089.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247843; ENSP00000247843; ENSG00000127337.
GeneIDi8089.
KEGGihsa:8089.
UCSCiuc001sux.3. human.

Organism-specific databases

CTDi8089.
GeneCardsiGC12P069753.
HGNCiHGNC:24859. YEATS4.
MIMi602116. gene.
neXtProtiNX_O95619.
PharmGKBiPA134992686.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5033.
GeneTreeiENSGT00530000063543.
HOGENOMiHOG000190181.
HOVERGENiHBG061271.
InParanoidiO95619.
KOiK11341.
OrthoDBiEOG73FQNN.
PhylomeDBiO95619.

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

Miscellaneous databases

GenomeRNAii8089.
NextBioi30722.
PROiO95619.
SOURCEiSearch...

Gene expression databases

BgeeiO95619.
CleanExiHS_YEATS4.
ExpressionAtlasiO95619. baseline and differential.
GenevisibleiO95619. HS.

Family and domain databases

InterProiIPR005033. YEATS.
[Graphical view]
PANTHERiPTHR23195. PTHR23195. 1 hit.
PfamiPF03366. YEATS. 1 hit.
[Graphical view]
PROSITEiPS51037. YEATS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYETS4_HUMAN
AccessioniPrimary (citable) accession number: O95619
Secondary accession number(s): Q9NQD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 124 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.