Protein AATF

Protein-coding gene in the species Homo sapiens
AATF
Identifiers
AliasesAATF, BFR2, CHE-1, CHE1, DED, Apoptosis-antagonizing transcription factor, apoptosis antagonizing transcription factor
External IDsOMIM: 608463; MGI: 1929608; HomoloGene: 40811; GeneCards: AATF; OMA:AATF - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for AATF
Genomic location for AATF
Band17q12Start36,948,925 bp[1]
End37,056,871 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for AATF
Genomic location for AATF
Band11|11 CStart84,422,855 bp[2]
End84,513,522 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • granulocyte

  • corpus callosum

  • Achilles tendon

  • tibial arteries

  • blood

  • skin of leg

  • bone marrow

  • body of pancreas

  • sural nerve
Top expressed in
  • morula

  • epiblast

  • embryo

  • tail of embryo

  • genital tubercle

  • primary oocyte

  • yolk sac

  • endothelial cell of lymphatic vessel

  • spermatocyte

  • embryo
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein domain specific binding
  • DNA-binding transcription factor activity
  • leucine zipper domain binding
  • protein binding
  • tau protein binding
  • RNA binding
  • protein kinase binding
Cellular component
  • cytoplasm
  • Golgi apparatus
  • nucleus
  • nucleolus
Biological process
  • embryonic cleavage
  • ribosome biogenesis
  • negative regulation of apoptotic process
  • cellular response to DNA damage stimulus
  • positive regulation of transcription, DNA-templated
  • cell adhesion
  • negative regulation of amyloid precursor protein biosynthetic process
  • regulation of mitotic cell cycle
  • negative regulation of superoxide anion generation
  • negative regulation of reactive oxygen species metabolic process
  • positive regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

26574

56321

Ensembl

ENSG00000275700
ENSG00000276072

ENSMUSG00000018697

UniProt

Q9NY61

Q9JKX4

RefSeq (mRNA)

NM_012138

NM_019816

RefSeq (protein)

NP_036270

NP_062790

Location (UCSC)Chr 17: 36.95 – 37.06 MbChr 11: 84.42 – 84.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein AATF, also known as apoptosis-antagonizing transcription factor is a protein that in humans is encoded by the AATF gene.[5][6][7]

Function

The protein encoded by this gene was identified on the basis of its interaction with MAP3K12/DLK, a protein kinase known to be involved in the induction of cell apoptosis. This gene product contains a leucine zipper, which is a characteristic motif of transcription factors, and was shown to exhibit strong transactivation activity when fused to Gal4 DNA binding domain. Overexpression of this gene interfered with MAP3K12 induced apoptosis.[7]

Interactions

Protein AATF has been shown to interact with:

References

  1. ^ a b c ENSG00000276072 GRCh38: Ensembl release 89: ENSG00000275700, ENSG00000276072 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018697 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lindfors K, Halttunen T, Huotari P, Nupponen N, Vihinen M, Visakorpi T, Mäki M, Kainulainen H (Sep 2000). "Identification of novel transcription factor-like gene from human intestinal cells". Biochemical and Biophysical Research Communications. 276 (2): 660–6. doi:10.1006/bbrc.2000.3480. PMID 11027528.
  6. ^ a b c Fanciulli M, Bruno T, Di Padova M, De Angelis R, Iezzi S, Iacobini C, Floridi A, Passananti C (May 2000). "Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb". FASEB Journal. 14 (7): 904–12. doi:10.1096/fasebj.14.7.904. PMID 10783144. S2CID 43175069.
  7. ^ a b "Entrez Gene: AATF apoptosis antagonizing transcription factor".
  8. ^ Guo Q, Xie J (Feb 2004). "AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4". The Journal of Biological Chemistry. 279 (6): 4596–603. doi:10.1074/jbc.M309811200. PMID 14627703.
  9. ^ 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 (Nov 2002). "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb". Cancer Cell. 2 (5): 387–99. doi:10.1016/s1535-6108(02)00182-4. PMID 12450794.
  10. ^ 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 (Sep 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry. 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.

Further reading

  • Page G, Lödige I, Kögel D, Scheidtmann KH (Nov 1999). "AATF, a novel transcription factor that interacts with Dlk/ZIP kinase and interferes with apoptosis". FEBS Letters. 462 (1–2): 187–91. doi:10.1016/S0014-5793(99)01529-X. PMID 10580117. S2CID 6061613.
  • Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (Jan 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • Scherl A, Couté Y, Déon C, Callé A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ (Nov 2002). "Functional proteomic analysis of human nucleolus". Molecular Biology of the Cell. 13 (11): 4100–9. doi:10.1091/mbc.E02-05-0271. PMC 133617. PMID 12429849.
  • 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 (Nov 2002). "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb". Cancer Cell. 2 (5): 387–99. doi:10.1016/S1535-6108(02)00182-4. PMID 12450794.
  • 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 (Sep 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry. 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.
  • Guo Q, Xie J (Feb 2004). "AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4". The Journal of Biological Chemistry. 279 (6): 4596–603. doi:10.1074/jbc.M309811200. PMID 14627703.
  • 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 (Dec 2003). "Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons. Modulation during neuronal apoptosis". Molecular and Cellular Neurosciences. 24 (4): 1038–50. doi:10.1016/j.mcn.2003.08.002. hdl:2108/56917. PMID 14697667. S2CID 35111183.
  • Burgdorf S, Leister P, Scheidtmann KH (Apr 2004). "TSG101 interacts with apoptosis-antagonizing transcription factor and enhances androgen receptor-mediated transcription by promoting its monoubiquitination". The Journal of Biological Chemistry. 279 (17): 17524–34. doi:10.1074/jbc.M313703200. PMID 14761944.
  • Xie J, Guo Q (Jun 2004). "AATF protects neural cells against oxidative damage induced by amyloid beta-peptide". Neurobiology of Disease. 16 (1): 150–7. doi:10.1016/j.nbd.2004.02.003. PMID 15207272. S2CID 53204920.
  • Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (Jan 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (Apr 2006). "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
  • Kaul D, Mehrotra A (Mar 2007). "Functional characterization of AATF transcriptome in human leukemic cells". Molecular and Cellular Biochemistry. 297 (1–2): 215–20. doi:10.1007/s11010-006-9317-1. PMID 17006618. S2CID 8612000.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

  • v
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(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies
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  • t
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