AATF_RAT
ID AATF_RAT Reviewed; 523 AA.
AC Q9QYW0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein AATF;
DE AltName: Full=Apoptosis-antagonizing transcription factor;
GN Name=Aatf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DAPK3, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=10580117; DOI=10.1016/s0014-5793(99)01529-x;
RA Page G., Loedige I., Kogel D., Scheidtmann K.H.;
RT "AATF -- a novel transcription factor that interacts with Dlk/ZIP kinase
RT and interferes with apoptosis.";
RL FEBS Lett. 462:187-191(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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, AND INTERACTION WITH TSG101.
RX PubMed=14761944; DOI=10.1074/jbc.m313703200;
RA Burgdorf S., Leister P., Scheidtmann K.H.;
RT "TSG101 interacts with apoptosis-antagonizing transcription factor and
RT enhances androgen receptor-mediated transcription by promoting its
RT monoubiquitination.";
RL J. Biol. Chem. 279:17524-17534(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-284 AND SER-285, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. May negatively regulate
CC the pro-apoptotic activity of DAPK3/ZIPK. Can act cooperatively with
CC TSG101 to stimulate AR mediated transcription activation (By
CC similarity). May negatively regulate the pro-apoptotic activity of
CC DAPK3/ZIPK. Can act cooperatively with TSG101 to stimulate AR mediated
CC transcription activation. {ECO:0000250, ECO:0000269|PubMed:14761944}.
CC -!- SUBUNIT: Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130 and SP1 (By
CC similarity). Binds DAPK3/ZIPK and TSG101. May also bind MAPT.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10580117}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10580117}.
CC -!- SIMILARITY: Belongs to the AATF family. {ECO:0000305}.
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DR EMBL; AJ238717; CAB59426.1; -; mRNA.
DR EMBL; BC078769; AAH78769.1; -; mRNA.
DR RefSeq; NP_446172.1; NM_053720.1.
DR AlphaFoldDB; Q9QYW0; -.
DR SMR; Q9QYW0; -.
DR BioGRID; 250358; 6.
DR MINT; Q9QYW0; -.
DR STRING; 10116.ENSRNOP00000000258; -.
DR iPTMnet; Q9QYW0; -.
DR PhosphoSitePlus; Q9QYW0; -.
DR jPOST; Q9QYW0; -.
DR PaxDb; Q9QYW0; -.
DR PRIDE; Q9QYW0; -.
DR Ensembl; ENSRNOT00000000258; ENSRNOP00000000258; ENSRNOG00000002778.
DR GeneID; 114512; -.
DR KEGG; rno:114512; -.
DR CTD; 26574; -.
DR RGD; 620685; Aatf.
DR eggNOG; KOG2773; Eukaryota.
DR GeneTree; ENSGT00390000000288; -.
DR HOGENOM; CLU_018299_1_2_1; -.
DR InParanoid; Q9QYW0; -.
DR OMA; LINFMAP; -.
DR OrthoDB; 794860at2759; -.
DR PhylomeDB; Q9QYW0; -.
DR TreeFam; TF324341; -.
DR PRO; PR:Q9QYW0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002778; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q9QYW0; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0043522; F:leucine zipper domain binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0048156; F:tau protein binding; IPI:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0040016; P:embryonic cleavage; ISO:RGD.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:RGD.
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; Apoptosis; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT CHAIN 2..523
FT /note="Protein AATF"
FT /id="PRO_0000056618"
FT REGION 13..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..279
FT /note="Binds POLR2J"
FT /evidence="ECO:0000250"
FT REGION 273..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..335
FT /note="Binds RB1"
FT /evidence="ECO:0000250"
FT REGION 336..435
FT /note="Binds RB1 and SP1"
FT /evidence="ECO:0000250"
FT REGION 447..523
FT /note="Binds to TSG101"
FT COMPBIAS 18..40
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 100..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..305
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 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY61"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 523 AA; 59497 MW; B66C0FA591FB5FB4 CRC64;
MAELQPLALQ LEQLLNPRPR EADPEADPEE ATRARVIDRF DEGEEEEDDL PVSSIRKLAP
VSLLDTDKRY SGKTTSRKAW KEDHWDQTLP SSSDNEIPDE GGSEAGDSEG LEELSEDVEE
DLEDNEIPDE GGSEDGDSEG LEEEISEDVE EDLEGEDEED REEDRNSEDD GVVMAFSGVK
VSEEVEKGRA VKNQIALWDQ LLEGRIKLQK ALLTTNQLPQ PDVFPVFKDK GGPEFASALK
NSHKALKALL RSLVDLQEEL LFQYPDTRYL VKGTKPNAES EEISSEDDEL VGEKKKQRKA
PPKRKLEMED YPSFMAKRSA DFTVYRNRTL QKWHDKTKLA SGKLGKGFGA FERSILTQID
HILMDKERLL RRTQTKRSAY RVLGKPEPVP EPVAETLPGE PESLPQVPAN AHLKDLDEEI
FDDDDFYHQL LRELIERKTS SLDPNDQVAM GRQWLAIQKL RSKIRKKVDR KASKGRKLRF
HVLSKLLSFM APIDHTAMND EARTELYRSL FGQLNRLDAD HGQ
