AATF_HUMAN
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 03-AUG-2022, entry version 175.
DE RecName: Full=Protein AATF;
DE AltName: Full=Apoptosis-antagonizing transcription factor;
DE AltName: Full=Rb-binding protein Che-1;
GN Name=AATF; Synonyms=CHE1, DED; 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).
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. Also antagonizes PAWR
CC mediated induction of aberrant amyloid peptide production in Alzheimer
CC disease (presenile and senile dementia), although the molecular basis
CC for this phenomenon has not been described to date.
CC {ECO:0000269|PubMed:12450794, ECO:0000269|PubMed:12847090,
CC ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:15207272}.
CC -!- SUBUNIT: Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May
CC also bind MAPT.
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 -!- 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="http://atlasgeneticsoncology.org/Genes/AATFID534ch17q11.html";
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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 SMR; Q9NY61; -.
DR BioGRID; 117743; 203.
DR CORUM; Q9NY61; -.
DR ELM; Q9NY61; -.
DR IntAct; Q9NY61; 66.
DR MINT; Q9NY61; -.
DR STRING; 9606.ENSP00000477848; -.
DR GlyGen; Q9NY61; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NY61; -.
DR MetOSite; Q9NY61; -.
DR PhosphoSitePlus; Q9NY61; -.
DR BioMuta; AATF; -.
DR DMDM; 71152211; -.
DR SWISS-2DPAGE; Q9NY61; -.
DR EPD; Q9NY61; -.
DR jPOST; Q9NY61; -.
DR MassIVE; Q9NY61; -.
DR MaxQB; Q9NY61; -.
DR PaxDb; Q9NY61; -.
DR PeptideAtlas; Q9NY61; -.
DR PRIDE; Q9NY61; -.
DR ProteomicsDB; 83181; -.
DR TopDownProteomics; Q9NY61; -.
DR Antibodypedia; 72876; 356 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 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; LINFMAP; -.
DR OrthoDB; 794860at2759; -.
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; 586 hits in 1089 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 99 other tissues.
DR ExpressionAtlas; Q9NY61; baseline and differential.
DR Genevisible; Q9NY61; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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: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:cellular response to DNA damage stimulus; 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:0042254; P:ribosome biogenesis; IEA:Ensembl.
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 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
