AATF_MOUSE
ID AATF_MOUSE Reviewed; 526 AA.
AC Q9JKX4; Q7TQN1; Q8C5Q2; Q99P89;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein AATF;
DE AltName: Full=Apoptosis-antagonizing transcription factor;
DE AltName: Full=Rb-binding protein Che-1;
DE AltName: Full=Traube protein;
GN Name=Aatf; Synonyms=Che1, Trb;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11071758; DOI=10.1006/dbio.2000.9915;
RA Thomas T., Voss A.K., Petrou P., Gruss P.;
RT "The murine gene, Traube, is essential for the growth of preimplantation
RT embryos.";
RL Dev. Biol. 227:324-342(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24 (ISOFORMS 1/2), NUCLEOTIDE
RP SEQUENCE [MRNA] OF 1-265 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=SWR/J; TISSUE=Testis;
RX PubMed=14636992; DOI=10.1016/s0378-1119(03)00834-5;
RA Monaco L., Passananti C., Fanciulli M.;
RT "Genomic structure and transcriptional regulation of Che-1, a novel partner
RT of Rb.";
RL Gene 321:57-63(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-287 AND SER-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a general inhibitor of the histone
CC deacetylase HDAC1. Binding to the pocket region of RB1 may displace
CC HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes
CC and cell cycle progression. Conversely, displacement of HDAC1 from SP1
CC bound to the CDKN1A promoter leads to increased expression of this CDK
CC inhibitor and blocks cell cycle progression (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May
CC also bind MAPT (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11071758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JKX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JKX4-2; Sequence=VSP_014897, VSP_014898;
CC Name=3;
CC IsoId=Q9JKX4-3; Sequence=VSP_014899, VSP_014900;
CC -!- TISSUE SPECIFICITY: Expressed in adrenal gland, brain (Purkinje cells),
CC heart, kidney, liver, lung, muscle, ovary and testis (at the protein
CC level). {ECO:0000269|PubMed:11071758, ECO:0000269|PubMed:14636992}.
CC -!- DEVELOPMENTAL STAGE: Expressed uniformly throughout the embryo until
CC 10.5 dpc. From 11.5 dpc, the relative expression level increases in the
CC liver, hind brain, spinal cord, dorsal root ganglia, and the posterior
CC commissure. {ECO:0000269|PubMed:11071758}.
CC -!- SIMILARITY: Belongs to the AATF family. {ECO:0000305}.
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DR EMBL; AF222801; AAF26745.1; -; mRNA.
DR EMBL; AK077789; BAC37011.1; -; mRNA.
DR EMBL; AL603708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025080; AAH25080.1; -; mRNA.
DR EMBL; AF322223; AAK07639.1; -; Genomic_DNA.
DR EMBL; AY306199; AAP73747.1; -; mRNA.
DR CCDS; CCDS25186.1; -. [Q9JKX4-1]
DR RefSeq; NP_062790.1; NM_019816.1. [Q9JKX4-1]
DR AlphaFoldDB; Q9JKX4; -.
DR SMR; Q9JKX4; -.
DR BioGRID; 207901; 59.
DR STRING; 10090.ENSMUSP00000018841; -.
DR iPTMnet; Q9JKX4; -.
DR PhosphoSitePlus; Q9JKX4; -.
DR EPD; Q9JKX4; -.
DR jPOST; Q9JKX4; -.
DR MaxQB; Q9JKX4; -.
DR PaxDb; Q9JKX4; -.
DR PeptideAtlas; Q9JKX4; -.
DR PRIDE; Q9JKX4; -.
DR ProteomicsDB; 286017; -. [Q9JKX4-1]
DR ProteomicsDB; 286018; -. [Q9JKX4-2]
DR ProteomicsDB; 286019; -. [Q9JKX4-3]
DR Antibodypedia; 72876; 356 antibodies from 37 providers.
DR DNASU; 56321; -.
DR Ensembl; ENSMUST00000018841; ENSMUSP00000018841; ENSMUSG00000018697. [Q9JKX4-1]
DR GeneID; 56321; -.
DR KEGG; mmu:56321; -.
DR UCSC; uc007kqm.1; mouse. [Q9JKX4-1]
DR UCSC; uc007kqn.1; mouse. [Q9JKX4-3]
DR CTD; 26574; -.
DR MGI; MGI:1929608; Aatf.
DR VEuPathDB; HostDB:ENSMUSG00000018697; -.
DR eggNOG; KOG2773; Eukaryota.
DR GeneTree; ENSGT00390000000288; -.
DR HOGENOM; CLU_018299_1_2_1; -.
DR InParanoid; Q9JKX4; -.
DR OMA; LINFMAP; -.
DR OrthoDB; 794860at2759; -.
DR PhylomeDB; Q9JKX4; -.
DR TreeFam; TF324341; -.
DR BioGRID-ORCS; 56321; 25 hits in 78 CRISPR screens.
DR ChiTaRS; Aatf; mouse.
DR PRO; PR:Q9JKX4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JKX4; protein.
DR Bgee; ENSMUSG00000018697; Expressed in ectoplacental cone and 264 other tissues.
DR Genevisible; Q9JKX4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0040016; P:embryonic cleavage; IMP:MGI.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:MGI.
DR InterPro; IPR025160; AATF.
DR InterPro; IPR039223; AATF/Bfr2.
DR InterPro; IPR012617; AATF_C.
DR PANTHER; PTHR15565; PTHR15565; 1.
DR Pfam; PF13339; AATF-Che1; 1.
DR Pfam; PF08164; TRAUB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT CHAIN 2..526
FT /note="Protein AATF"
FT /id="PRO_0000056617"
FT REGION 13..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..282
FT /note="Binds POLR2J"
FT /evidence="ECO:0000250"
FT REGION 274..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..338
FT /note="Binds RB1"
FT /evidence="ECO:0000250"
FT REGION 339..438
FT /note="Binds RB1 and SP1"
FT /evidence="ECO:0000250"
FT REGION 388..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 84
FT /note="H -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14636992"
FT /id="VSP_014897"
FT VAR_SEQ 85..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14636992"
FT /id="VSP_014898"
FT VAR_SEQ 433..458
FT /note="LLRELIERKTSSLDPNDQVAMGRQWL -> VRLFLSFLCYNKPGVCILEPLI
FT VSSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014899"
FT VAR_SEQ 459..526
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014900"
FT CONFLICT 2..3
FT /note="AA -> GR (in Ref. 5; AAP73747)"
FT /evidence="ECO:0000305"
FT CONFLICT 4..5
FT /note="Missing (in Ref. 5; AAP73747)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> K (in Ref. 5; AAP73747)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="E -> K (in Ref. 5; AAP73747)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="K -> Q (in Ref. 5; AAP73747)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="D -> G (in Ref. 5; AAP73747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59482 MW; 8AD2A8396F521DCF CRC64;
MAAPQPLALQ LEQLLNPRPR EADPEADPEE ATRARVIDRF DEGEEEKDDL AVSSIRKLAP
VSLLDTDKRY SGKTTSRKAW KEDHWEQALP SSSDNEASDE GGSEDGDSEG LGLEEISEDV
DEDLEDNKIS DEGGSEDGDS EGLGLEEFSE DVEEDLEGED EEDREEDRNS EDDGVVAAFS
SVKVSEEVEK GRAVKNQIAL WDQLLEGRIK LQKALLTTNQ LPQPDVFPVF KDKGGPEFAS
ALKNSHKALK ALLRSLVDLQ EELLFQYPDT RHIVNGAKPN TESEEISSED DELVGEKKKQ
RKAPPKRKLE MEDYPSFMAK RFADFTIYRN HTLQKWHDKT KLASGKLGKG FGAFERSILT
QIDHIMMDKE RLLRRTQTKR SAYRVLGKPE PVPEPVAETL PGEPETLPQG PANAHLRDLD
EEIFDDDDFY HQLLRELIER KTSSLDPNDQ VAMGRQWLAI QKLRSKIRKK VDRKASKGRK
LRFHVLSKLL SFMAPIDHTA MSDDARTELF RSLFGQLNPP DADRGK
