YETS4_MOUSE
ID YETS4_MOUSE Reviewed; 227 AA.
AC Q9CR11; Q9CW86;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=YEATS domain-containing protein 4 {ECO:0000305};
DE AltName: Full=Glioma-amplified sequence 41 homolog {ECO:0000303|PubMed:29900004};
DE Short=Gas41 {ECO:0000303|PubMed:29900004};
GN Name=Yeats4 {ECO:0000312|MGI:MGI:1927224};
GN Synonyms=Gas41 {ECO:0000303|PubMed:29900004};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=29900004; DOI=10.1038/s41421-018-0027-0;
RA Hsu C.C., Zhao D., Shi J., Peng D., Guan H., Li Y., Huang Y., Wen H.,
RA Li W., Li H., Shi X.;
RT "Gas41 links histone acetylation to H2A.Z deposition and maintenance of
RT embryonic stem cell identity.";
RL Cell Discov. 4:28-28(2018).
CC -!- FUNCTION: Chromatin reader component of the NuA4 histone
CC acetyltransferase (HAT) complex, a complex involved in transcriptional
CC activation of select genes principally by acetylation of nucleosomal
CC histones H4 and H2A (By similarity). Specifically recognizes and binds
CC acylated histone H3, with a preference for histone H3 diacetylated at
CC 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated
CC at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac) (By similarity). Also
CC able to recognize and bind crotonylated histone H3 (By similarity). May
CC also recognize and bind histone H3 succinylated at 'Lys-122'
CC (H3K122succ); additional evidences are however required to confirm this
CC result in vivo (By similarity). Plays a key role in histone variant
CC H2AZ1/H2A.Z deposition into specific chromatin regions: recognizes and
CC binds H3K14ac and H3K27ac on the promoters of actively transcribed
CC genes and recruits NuA4-related complex to deposit H2AZ1/H2A.Z (By
CC similarity). H2AZ1/H2A.Z deposition is required for maintenance of
CC embryonic stem cell (PubMed:29900004). {ECO:0000250|UniProtKB:O95619,
CC ECO:0000269|PubMed:29900004}.
CC -!- SUBUNIT: Component of numerous complexes with chromatin remodeling and
CC histone acetyltransferase activity. Component of the NuA4 histone
CC acetyltransferase complex which contains the catalytic subunit
CC KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A,
CC MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6.
CC The NuA4 complex interacts with MYC and the adenovirus E1A protein.
CC Component of a NuA4-related complex which contains EP400, TRRAP/PAF400,
CC SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
CC ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Interacts with MLLT10/AF10. Also
CC interacts with the SWI/SNF component SMARCB1/BAF47, TACC1 and TACC2,
CC and the nuclear matrix protein NUMA1. {ECO:0000250|UniProtKB:O95619}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376}.
CC -!- DOMAIN: The YEATS domain specifically recognizes and binds acylated
CC histones, with a preference for histone H3 diacetylated at 'Lys-14' and
CC 'Lys-27' (H3K14ac and H3K27ac). {ECO:0000250|UniProtKB:O95619}.
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DR EMBL; AK002839; BAB22396.1; -; mRNA.
DR EMBL; AK012096; BAB28027.1; -; mRNA.
DR EMBL; AK010522; BAB27003.1; -; mRNA.
DR EMBL; BC020043; AAH20043.1; -; mRNA.
DR CCDS; CCDS24191.1; -.
DR RefSeq; NP_080846.1; NM_026570.4.
DR AlphaFoldDB; Q9CR11; -.
DR SMR; Q9CR11; -.
DR BioGRID; 211018; 4.
DR ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q9CR11; 4.
DR MINT; Q9CR11; -.
DR STRING; 10090.ENSMUSP00000020382; -.
DR iPTMnet; Q9CR11; -.
DR PhosphoSitePlus; Q9CR11; -.
DR EPD; Q9CR11; -.
DR MaxQB; Q9CR11; -.
DR PaxDb; Q9CR11; -.
DR PeptideAtlas; Q9CR11; -.
DR PRIDE; Q9CR11; -.
DR ProteomicsDB; 299620; -.
DR Antibodypedia; 16961; 401 antibodies from 32 providers.
DR DNASU; 64050; -.
DR Ensembl; ENSMUST00000020382; ENSMUSP00000020382; ENSMUSG00000020171.
DR GeneID; 64050; -.
DR KEGG; mmu:64050; -.
DR UCSC; uc007hcx.2; mouse.
DR CTD; 8089; -.
DR MGI; MGI:1927224; Yeats4.
DR VEuPathDB; HostDB:ENSMUSG00000020171; -.
DR eggNOG; KOG3149; Eukaryota.
DR GeneTree; ENSGT00940000155811; -.
DR HOGENOM; CLU_051385_3_0_1; -.
DR InParanoid; Q9CR11; -.
DR OMA; PYHNEDM; -.
DR OrthoDB; 1482359at2759; -.
DR PhylomeDB; Q9CR11; -.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 64050; 26 hits in 73 CRISPR screens.
DR PRO; PR:Q9CR11; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CR11; protein.
DR Bgee; ENSMUSG00000020171; Expressed in dorsal pancreas and 259 other tissues.
DR ExpressionAtlas; Q9CR11; baseline and differential.
DR Genevisible; Q9CR11; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0140030; F:modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Coiled coil; Growth regulation; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..227
FT /note="YEATS domain-containing protein 4"
FT /id="PRO_0000066205"
FT DOMAIN 15..158
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 93..97
FT /note="Diacetylated histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:O95619"
FT REGION 163..227
FT /note="Interaction with MLLT10"
FT /evidence="ECO:0000250"
FT REGION 168..227
FT /note="Interaction with TACC1"
FT /evidence="ECO:0000250"
FT COILED 178..226
FT /evidence="ECO:0000255"
FT SITE 73
FT /note="Interacts with diacetylated histone H3"
FT /evidence="ECO:0000250|UniProtKB:O95619"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95619"
SQ SEQUENCE 227 AA; 26530 MW; 34C46937527A7B85 CRC64;
MFKRMAEFGP DSGGRVKGVT IVKPIVYGNV ARYFGKKREE DGHTHQWTVY VKPYRNEDMS
AYVKKIQFKL HESYGNPLRV VTKPPYEITE TGWGEFEIII KIFFIDPNER PVTLYHLLKL
FQSDTNAMLG KKTVVSEFYD EMIFQDPTAM MQQLLTTSRQ LTLGAYKHET EFAELEVKTR
EKLEAAKKKT SFEIAELKER LKASRETINC LKNEIRKLEE DDQTKDI
