Q9NY61 (AATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein AATF Alternative name(s): Apoptosis-antagonizing transcription factor Rb-binding protein Che-1 | ||||||
| Gene names |
| ||||||
| Organism | Homo sapiens (Human) | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 560 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date. Ref.8 Ref.10 Ref.12 Ref.13 |
| Subunit structure | Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May also bind MAPT. |
| Subcellular location | |
| Tissue specificity | Ubiquitously expressed. Expressed at high levels in brain, heart, kidney, placenta and thymus. Ref.1 Ref.2 |
| Post-translational modification | Hyperphosphorylated during the G1/S phase transition. Ref.8 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 |
| Sequence similarities | Belongs to the AATF family. |
| Sequence caution | The sequence AAD52016.1 differs from that shown. Reason: Frameshift at positions 355, 365, 487, 498 and 503. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ATM | Q13315 | 3 | EBI-372428,EBI-495465 | |
| CHEK2 | O96017 | 4 | EBI-372428,EBI-1180783 | |
| RELA | Q04206 | 3 | EBI-372428,EBI-73886 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 560 | 559 | Protein AATF | PRO_0000056616 | |||||
Regions | |||||||||
| Region | 273 – 315 | 43 | POLR2J binding | ||||||
| Region | 316 – 372 | 57 | RB1 binding | ||||||
| Region | 373 – 472 | 100 | RB1 and SP1 binding | ||||||
| Compositional bias | 96 – 195 | 100 | Glu-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.18 | ||||||
| Modified residue | 203 | 1 | Phosphoserine Ref.8 Ref.14 Ref.15 Ref.16 | ||||||
| Modified residue | 316 | 1 | Phosphoserine Ref.8 Ref.15 Ref.17 Ref.18 Ref.19 | ||||||
| Modified residue | 320 | 1 | Phosphoserine Ref.8 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 | ||||||
| Modified residue | 321 | 1 | Phosphoserine Ref.8 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 | ||||||
Experimental info | |||||||||
| Sequence conflict | 2 – 3 | 2 | AG → GR in AAD52016. Ref.2 | ||||||
| Sequence conflict | 4 – 5 | 2 | Missing in AAD52016. Ref.2 | ||||||
| Sequence conflict | 139 | 1 | S → T in AAD52016. Ref.2 | ||||||
| Sequence conflict | 262 | 1 | L → V in AAD52016. Ref.2 | ||||||
| Sequence conflict | 272 | 1 | S → A in AAD52016. Ref.2 | ||||||
| Sequence conflict | 306 | 1 | L → V in AAD52016. Ref.2 | ||||||
| Sequence conflict | 402 | 1 | D → C in AAD52016. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Identification of novel transcription factor-like gene from human intestinal cells." Lindfors K., Halttunen T., Huotari P., Nupponen N., Vihinen M., Visakorpi T., Maki M., Kainulainen H. Biochem. Biophys. Res. Commun. 276:660-666(2000) [PubMed: 11027528] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. |
| [2] | "Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb." Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S., Iacobini C., Floridi A., Passananti C. FASEB J. 14:904-912(2000) [PubMed: 10783144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR2J AND RB1, TISSUE SPECIFICITY. Tissue: Skeletal muscle. |
| [3] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
| [4] | "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. Nusbaum C.Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin. |
| [7] | "Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 361-560. Tissue: Umbilical cord blood. |
| [8] | "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb." Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M., Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S., Floridi A., Passananti C., Fanciulli M. Cancer Cell 2:387-399(2002) [PubMed: 12450794] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THE G1/S TRANSITION, INTERACTION WITH RB1; RBL1 AND RBL2. |
| [9] | "Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed: 12429849] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma. |
| [10] | "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter." Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M. J. Biol. Chem. 278:36496-36504(2003) [PubMed: 12847090] [Abstract] Cited for: FUNCTION, INTERACTION WITH SP1. |
| [11] | "Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons. Modulation during neuronal apoptosis." Barbato C., Corbi N., Canu N., Fanciulli M., Serafino A., Ciotti M., Libri V., Bruno T., Amadoro G., De Angelis R., Calissano P., Passananti C. Mol. Cell. Neurosci. 24:1038-1050(2003) [PubMed: 14697667] [Abstract] Cited for: INTERACTION WITH MAPT. |
| [12] | "AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4." Guo Q., Xie J. J. Biol. Chem. 279:4596-4603(2004) [PubMed: 14627703] [Abstract] Cited for: FUNCTION, INTERACTION WITH PAWR. |
| [13] | "AATF protects neural cells against oxidative damage induced by amyloid beta-peptide." Xie J., Guo Q. Neurobiol. Dis. 16:150-157(2004) [PubMed: 15207272] [Abstract] Cited for: FUNCTION. |
| [14] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma. |
| [16] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [19] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ249940 mRNA. Translation: CAB57451.2. AF083208 mRNA. Translation: AAD52016.1. Frameshift. AK057229 mRNA. Translation: BAG51888.1. AC003103 Genomic DNA. No translation available. CH471199 Genomic DNA. Translation: EAW57575.1. BC000591 mRNA. Translation: AAH00591.1. AF161395 mRNA. Translation: AAF28955.1. |
| IPI | IPI00302238. |
| RefSeq | NP_036270.1. NM_012138.3. |
| UniGene | Hs.195740. |
3D structure databases | |
| ProteinModelPortal | Q9NY61. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9NY61. 14 interactions. |
| MINT | MINT-131397. |
| STRING | Q9NY61. |
PTM databases | |
| PhosphoSite | Q9NY61. |
Polymorphism databases | |
| DMDM | 71152211. |
2D gel databases | |
| SWISS-2DPAGE | Q9NY61. |
Proteomic databases | |
| PRIDE | Q9NY61. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000225402; ENSP00000225402; ENSG00000108270. |
| GeneID | 26574. |
| KEGG | hsa:26574. |
| UCSC | uc002hni.1. human. |
Organism-specific databases | |
| CTD | 26574. |
| GeneCards | GC17P035306. |
| H-InvDB | HIX0013742. |
| HGNC | HGNC:19235. AATF. |
| HPA | HPA004940. |
| MIM | 608463. gene. |
| neXtProt | NX_Q9NY61. |
| PharmGKB | PA128395780. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG17989. |
| GeneTree | ENSGT00390000000288. |
| HOGENOM | HBG607920. |
| HOVERGEN | HBG080805. |
| InParanoid | Q9NY61. |
| OMA | KDKGGPE. |
| OrthoDB | EOG41NTM1. |
| PhylomeDB | Q9NY61. |
Enzyme and pathway databases | |
| Reactome | REACT_111102. Signal Transduction. |
Gene expression databases | |
| ArrayExpress | Q9NY61. |
| Bgee | Q9NY61. |
| CleanEx | HS_AATF. |
| Genevestigator | Q9NY61. |
Family and domain databases | |
| InterPro | IPR012617. TRAUB. [Graphical view] |
| KO | K14782. |
| Pfam | PF08164. TRAUB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 48910. |
| SOURCE | Search... |
Entry information
| Entry name | AATF_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NY61 Secondary accession number(s): A6NCJ6 Q9UNX5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with