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 24-JAN-2024, entry version 164. 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: Part of the small subunit (SSU) processome, first precursor CC of the small eukaryotic ribosomal subunit. During the assembly of the CC SSU processome in the nucleolus, many ribosome biogenesis factors, an CC RNA chaperone and ribosomal proteins associate with the nascent pre- CC rRNA and work in concert to generate RNA folding, modifications, CC rearrangements and cleavage as well as targeted degradation of pre- CC ribosomal RNA by the RNA exosome. May function as a general inhibitor CC of the histone deacetylase HDAC1. Binding to the pocket region of RB1 CC may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F CC target genes and cell cycle progression. Conversely, displacement of CC HDAC1 from SP1 bound to the CDKN1A promoter leads to increased CC expression of this CDK inhibitor and blocks cell cycle progression. CC Also antagonizes PAWR mediated induction of aberrant amyloid peptide CC production in Alzheimer disease (presenile and senile dementia), CC although the molecular basis for this phenomenon has not been described CC to date. {ECO:0000250|UniProtKB:Q9NY61}. CC -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. CC Interacts with POLR2J, RB1/RB, RBL1/P107 and RBL2/P130. Interacts with CC PAWR and SP1. May also bind MAPT. {ECO:0000250|UniProtKB:Q9NY61}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000018841; -. DR PeptideAtlas; Q9JKX4; -. DR ProteomicsDB; 286017; -. [Q9JKX4-1] DR ProteomicsDB; 286018; -. [Q9JKX4-2] DR ProteomicsDB; 286019; -. [Q9JKX4-3] DR Pumba; Q9JKX4; -. DR Antibodypedia; 72876; 425 antibodies from 37 providers. DR DNASU; 56321; -. DR Ensembl; ENSMUST00000018841.3; ENSMUSP00000018841.3; ENSMUSG00000018697.15. [Q9JKX4-1] DR GeneID; 56321; -. DR KEGG; mmu:56321; -. DR UCSC; uc007kqm.1; mouse. [Q9JKX4-1] DR UCSC; uc007kqn.1; mouse. [Q9JKX4-3] DR AGR; MGI:1929608; -. 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; RRIRYHV; -. DR OrthoDB; 26012at2759; -. DR PhylomeDB; Q9JKX4; -. DR TreeFam; TF324341; -. DR BioGRID-ORCS; 56321; 25 hits in 83 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 267 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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:0032040; C:small-subunit processome; ISS:UniProtKB. 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:DNA damage response; 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:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB. 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; AATF PROTEIN APOPTOSIS ANTAGONIZING TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR15565:SF0; PROTEIN AATF; 1. DR Pfam; PF13339; AATF-Che1; 1. DR Pfam; PF08164; TRAUB; 1. DR Genevisible; Q9JKX4; MM. 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 //