ID AATF_HUMAN Reviewed; 560 AA. AC Q9NY61; A6NCJ6; B3KQ26; Q9P0A4; Q9UNX5; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 184. DE RecName: Full=Protein AATF; DE AltName: Full=Apoptosis-antagonizing transcription factor; DE AltName: Full=Rb-binding protein Che-1; GN Name=AATF {ECO:0000312|HGNC:HGNC:19235}; Synonyms=CHE1, DED; GN ORFNames=HSPC277; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=11027528; DOI=10.1006/bbrc.2000.3480; RA Lindfors K., Halttunen T., Huotari P., Nupponen N., Vihinen M., RA Visakorpi T., Maki M., Kainulainen H.; RT "Identification of novel transcription factor-like gene from human RT intestinal cells."; RL Biochem. Biophys. Res. Commun. 276:660-666(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR2J AND RB1, AND TISSUE RP SPECIFICITY. RC TISSUE=Skeletal muscle; RX PubMed=10783144; DOI=10.1096/fasebj.14.7.904; RA Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S., Iacobini C., RA Floridi A., Passananti C.; RT "Identification of a novel partner of RNA polymerase II subunit 11, Che-1, RT which interacts with and affects the growth suppression function of Rb."; RL FASEB J. 14:904-912(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 361-560. RC TISSUE=Umbilical cord blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, PHOSPHORYLATION AT THE G1/S TRANSITION, AND INTERACTION WITH RB1; RP RBL1 AND RBL2. RX PubMed=12450794; DOI=10.1016/s1535-6108(02)00182-4; RA Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M., Corbi N., RA Libri V., Benassi B., Mattei E., Chersi A., Soddu S., Floridi A., RA Passananti C., Fanciulli M.; RT "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by RT Rb."; RL Cancer Cell 2:387-399(2002). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [10] RP FUNCTION, AND INTERACTION WITH SP1. RX PubMed=12847090; DOI=10.1074/jbc.m306694200; RA Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., RA Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M.; RT "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 RT from the p21WAF1/CIP1 promoter."; RL J. Biol. Chem. 278:36496-36504(2003). RN [11] RP INTERACTION WITH MAPT. RX PubMed=14697667; DOI=10.1016/j.mcn.2003.08.002; RA Barbato C., Corbi N., Canu N., Fanciulli M., Serafino A., Ciotti M., RA Libri V., Bruno T., Amadoro G., De Angelis R., Calissano P., Passananti C.; RT "Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons. RT Modulation during neuronal apoptosis."; RL Mol. Cell. Neurosci. 24:1038-1050(2003). RN [12] RP FUNCTION, AND INTERACTION WITH PAWR. RX PubMed=14627703; DOI=10.1074/jbc.m309811200; RA Guo Q., Xie J.; RT "AATF inhibits aberrant production of amyloid beta peptide 1-42 by RT interacting directly with Par-4."; RL J. Biol. Chem. 279:4596-4603(2004). RN [13] RP FUNCTION. RX PubMed=15207272; DOI=10.1016/j.nbd.2004.02.003; RA Xie J., Guo Q.; RT "AATF protects neural cells against oxidative damage induced by amyloid RT beta-peptide."; RL Neurobiol. Dis. 16:150-157(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 AND RP SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 AND RP SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-63; SER-150; SER-155; RP SER-203 AND SER-273, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). 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 (PubMed:34516797). May function as a CC general inhibitor of the histone deacetylase HDAC1. Binding to the CC pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading CC to activation of E2F target genes and cell cycle progression. CC Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter CC leads to increased expression of this CDK inhibitor and blocks cell CC cycle progression. Also antagonizes PAWR mediated induction of aberrant CC amyloid peptide production in Alzheimer disease (presenile and senile CC dementia), although the molecular basis for this phenomenon has not CC been described to date. {ECO:0000269|PubMed:12450794, CC ECO:0000269|PubMed:12847090, ECO:0000269|PubMed:14627703, CC ECO:0000269|PubMed:15207272, ECO:0000269|PubMed:34516797}. 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 (PubMed:34516797). Interacts with POLR2J, RB1/RB, RBL1/P107 and CC RBL2/P130 (PubMed:12450794, PubMed:10783144). Interacts with PAWR and CC SP1 (PubMed:12847090, PubMed:14627703). May also bind MAPT CC (PubMed:14697667). {ECO:0000269|PubMed:10783144, CC ECO:0000269|PubMed:12450794, ECO:0000269|PubMed:12847090, CC ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:14697667, CC ECO:0000269|PubMed:34516797}. CC -!- INTERACTION: CC Q9NY61; P05067: APP; NbExp=3; IntAct=EBI-372428, EBI-77613; CC Q9NY61; Q13315: ATM; NbExp=3; IntAct=EBI-372428, EBI-495465; CC Q9NY61; O96017: CHEK2; NbExp=4; IntAct=EBI-372428, EBI-1180783; CC Q9NY61; Q92830: KAT2A; NbExp=4; IntAct=EBI-372428, EBI-477622; CC Q9NY61; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-372428, EBI-743811; CC Q9NY61; Q8NEJ9: NGDN; NbExp=4; IntAct=EBI-372428, EBI-9995414; CC Q9NY61; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-372428, EBI-9090282; CC Q9NY61; P63000: RAC1; NbExp=3; IntAct=EBI-372428, EBI-413628; CC Q9NY61; Q04206: RELA; NbExp=3; IntAct=EBI-372428, EBI-73886; CC Q9NY61; P08047: SP1; NbExp=2; IntAct=EBI-372428, EBI-298336; CC Q9NY61; O75478: TADA2A; NbExp=4; IntAct=EBI-372428, EBI-742268; CC Q9NY61; Q86TJ2: TADA2B; NbExp=4; IntAct=EBI-372428, EBI-2512219; CC Q9NY61; O75528: TADA3; NbExp=2; IntAct=EBI-372428, EBI-473249; CC Q9NY61; Q6ZWQ9: Myl12a; Xeno; NbExp=3; IntAct=EBI-372428, EBI-8034418; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, CC ECO:0000269|PubMed:34516797}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high levels in CC brain, heart, kidney, placenta and thymus. CC {ECO:0000269|PubMed:10783144, ECO:0000269|PubMed:11027528}. CC -!- PTM: Hyperphosphorylated during the G1/S phase transition. CC -!- SIMILARITY: Belongs to the AATF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD52016.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/534/AATF"; 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; AJ249940; CAB57451.2; -; mRNA. DR EMBL; AF083208; AAD52016.1; ALT_FRAME; mRNA. DR EMBL; AK057229; BAG51888.1; -; mRNA. DR EMBL; AC003103; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471199; EAW57575.1; -; Genomic_DNA. DR EMBL; BC000591; AAH00591.1; -; mRNA. DR EMBL; AF161395; AAF28955.1; -; mRNA. DR CCDS; CCDS32632.1; -. DR RefSeq; NP_036270.1; NM_012138.3. DR PDB; 5W6A; X-ray; 1.74 A; E/F=539-547. DR PDB; 7MQ8; EM; 3.60 A; NN=1-560. DR PDB; 7MQ9; EM; 3.87 A; NN=1-560. DR PDBsum; 5W6A; -. DR PDBsum; 7MQ8; -. DR PDBsum; 7MQ9; -. DR AlphaFoldDB; Q9NY61; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR SMR; Q9NY61; -. DR BioGRID; 117743; 361. DR ComplexPortal; CPX-2511; Small ribosomal subunit processome. DR CORUM; Q9NY61; -. DR ELM; Q9NY61; -. DR IntAct; Q9NY61; 66. DR MINT; Q9NY61; -. DR STRING; 9606.ENSP00000477848; -. DR GlyGen; Q9NY61; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9NY61; -. DR MetOSite; Q9NY61; -. DR PhosphoSitePlus; Q9NY61; -. DR SwissPalm; Q9NY61; -. DR BioMuta; AATF; -. DR DMDM; 71152211; -. DR EPD; Q9NY61; -. DR jPOST; Q9NY61; -. DR MassIVE; Q9NY61; -. DR MaxQB; Q9NY61; -. DR PaxDb; 9606-ENSP00000477848; -. DR PeptideAtlas; Q9NY61; -. DR ProteomicsDB; 83181; -. DR Pumba; Q9NY61; -. DR TopDownProteomics; Q9NY61; -. DR Antibodypedia; 72876; 425 antibodies from 37 providers. DR DNASU; 26574; -. DR Ensembl; ENST00000619387.5; ENSP00000477848.1; ENSG00000275700.6. DR Ensembl; ENST00000620004.2; ENSP00000481894.1; ENSG00000276072.2. DR GeneID; 26574; -. DR KEGG; hsa:26574; -. DR MANE-Select; ENST00000619387.5; ENSP00000477848.1; NM_012138.4; NP_036270.1. DR UCSC; uc002hni.3; human. DR AGR; HGNC:19235; -. DR CTD; 26574; -. DR DisGeNET; 26574; -. DR GeneCards; AATF; -. DR HGNC; HGNC:19235; AATF. DR HPA; ENSG00000275700; Low tissue specificity. DR MIM; 608463; gene. DR neXtProt; NX_Q9NY61; -. DR OpenTargets; ENSG00000275700; -. DR PharmGKB; PA128395780; -. DR VEuPathDB; HostDB:ENSG00000275700; -. DR eggNOG; KOG2773; Eukaryota. DR GeneTree; ENSGT00390000000288; -. DR HOGENOM; CLU_018299_1_2_1; -. DR InParanoid; Q9NY61; -. DR OMA; RRIRYHV; -. DR OrthoDB; 26012at2759; -. DR PhylomeDB; Q9NY61; -. DR TreeFam; TF324341; -. DR PathwayCommons; Q9NY61; -. DR Reactome; R-HSA-193648; NRAGE signals death through JNK. DR SignaLink; Q9NY61; -. DR SIGNOR; Q9NY61; -. DR BioGRID-ORCS; 26574; 615 hits in 1168 CRISPR screens. DR ChiTaRS; AATF; human. DR GeneWiki; Apoptosis-antagonizing_transcription_factor; -. DR GenomeRNAi; 26574; -. DR Pharos; Q9NY61; Tbio. DR PRO; PR:Q9NY61; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9NY61; Protein. DR Bgee; ENSG00000275700; Expressed in monocyte and 100 other cell types or tissues. DR ExpressionAtlas; Q9NY61; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl. DR GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0048156; F:tau protein binding; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl. DR GO; GO:0006974; P:DNA damage response; IEP:UniProtKB. DR GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl. DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0032929; P:negative regulation of superoxide anion generation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. 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 SWISS-2DPAGE; Q9NY61; -. DR Genevisible; Q9NY61; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..560 FT /note="Protein AATF" FT /id="PRO_0000056616" FT REGION 76..208 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 273..315 FT /note="POLR2J binding" FT REGION 309..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..372 FT /note="RB1 binding" FT REGION 373..472 FT /note="RB1 and SP1 binding" FT COMPBIAS 76..91 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 94..126 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 127..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..193 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 150 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 273 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT CONFLICT 2..3 FT /note="AG -> GR (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" FT CONFLICT 4..5 FT /note="Missing (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="S -> T (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="L -> V (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="S -> A (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="L -> V (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="D -> C (in Ref. 2; AAD52016)" FT /evidence="ECO:0000305" SQ SEQUENCE 560 AA; 63133 MW; EC493EF3B4C3A199 CRC64; MAGPQPLALQ LEQLLNPRPS EADPEADPEE ATAARVIDRF DEGEDGEGDF LVVGSIRKLA SASLLDTDKR YCGKTTSRKA WNEDHWEQTL PGSSDEEISD EEGSGDEDSE GLGLEEYDED DLGAAEEQEC GDHRESKKSR SHSAKTPGFS VQSISDFEKF TKGMDDLGSS EEEEDEESGM EEGDDAEDSQ GESEEDRAGD RNSEDDGVVM TFSSVKVSEE VEKGRAVKNQ IALWDQLLEG RIKLQKALLT TNQLPQPDVF PLFKDKGGPE FSSALKNSHK ALKALLRSLV GLQEELLFQY PDTRYLVDGT KPNAGSEEIS SEDDELVEEK KQQRRRVPAK RKLEMEDYPS FMAKRFADFT VYRNRTLQKW HDKTKLASGK LGKGFGAFER SILTQIDHIL MDKERLLRRT QTKRSVYRVL GKPEPAAQPV PESLPGEPEI LPQAPANAHL KDLDEEIFDD DDFYHQLLRE LIERKTSSLD PNDQVAMGRQ WLAIQKLRSK IHKKVDRKAS KGRKLRFHVL SKLLSFMAPI DHTTMNDDAR TELYRSLFGQ LHPPDEGHGD //