Q9NY61 (AATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein AATF

Alternative name(s):
Apoptosis-antagonizing transcription factor
Rb-binding protein Che-1

Gene names

Name:	AATF
Synonyms:	CHE1, DED
ORF Names:	HSPC277

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	560 AA.
Sequence status	Complete.
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	Nucleus › nucleolus Ref.9.
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
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

Keywords
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: Compara embryonic cleavage Inferred from electronic annotation. Source: Compara negative regulation of amyloid precursor protein biosynthetic process Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype Ref.13. Source: UniProtKB negative regulation of superoxide anion generation Inferred from direct assay Ref.13. Source: UniProtKB nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 18049476. Source: UniProtKB regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from expression pattern PubMed 18049476. Source: UniProtKB ribosome biogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay. Source: HPA cytoplasm Inferred from direct assay Ref.12Ref.13. Source: UniProtKB focal adhesion Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA
Molecular_function	sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 10580117. Source: UniProtKB
Complete GO annotation...

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
	Chain	1 – 560	560	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	203	1	Phosphoserine Ref.8 Ref.16 Ref.17
	Modified residue	316	1	Phosphoserine Ref.8 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	320	1	Phosphoserine Ref.8 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	321	1	Phosphoserine Ref.8 Ref.14 Ref.15 Ref.16 Ref.17
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

	Sequence		Length	Mass (Da)
	Q9NY61 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EC493EF3B4C3A199	FASTA	560	63,133
	10 20 30 40 50 60 MAGPQPLALQ LEQLLNPRPS EADPEADPEE ATAARVIDRF DEGEDGEGDF LVVGSIRKLA 70 80 90 100 110 120 SASLLDTDKR YCGKTTSRKA WNEDHWEQTL PGSSDEEISD EEGSGDEDSE GLGLEEYDED 130 140 150 160 170 180 DLGAAEEQEC GDHRESKKSR SHSAKTPGFS VQSISDFEKF TKGMDDLGSS EEEEDEESGM 190 200 210 220 230 240 EEGDDAEDSQ GESEEDRAGD RNSEDDGVVM TFSSVKVSEE VEKGRAVKNQ IALWDQLLEG 250 260 270 280 290 300 RIKLQKALLT TNQLPQPDVF PLFKDKGGPE FSSALKNSHK ALKALLRSLV GLQEELLFQY 310 320 330 340 350 360 PDTRYLVDGT KPNAGSEEIS SEDDELVEEK KQQRRRVPAK RKLEMEDYPS FMAKRFADFT 370 380 390 400 410 420 VYRNRTLQKW HDKTKLASGK LGKGFGAFER SILTQIDHIL MDKERLLRRT QTKRSVYRVL 430 440 450 460 470 480 GKPEPAAQPV PESLPGEPEI LPQAPANAHL KDLDEEIFDD DDFYHQLLRE LIERKTSSLD 490 500 510 520 530 540 PNDQVAMGRQ WLAIQKLRSK IHKKVDRKAS KGRKLRFHVL SKLLSFMAPI DHTTMNDDAR 550 560 TELYRSLFGQ LHPPDEGHGD

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 AND SER-321, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 AND SER-321, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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	9606.ENSP00000225402.
PTM databases
PhosphoSite	Q9NY61.
Polymorphism databases
DMDM	71152211.
2D gel databases
SWISS-2DPAGE	Q9NY61.
Proteomic databases
PaxDb	Q9NY61.
PRIDE	Q9NY61.
Protocols and materials databases
DNASU	26574.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000225402; ENSP00000225402; ENSG00000108270.
GeneID	26574.
KEGG	hsa:26574.
UCSC	uc002hni.3. human.
Organism-specific databases
CTD	26574.
GeneCards	GC17P035306.
HGNC	HGNC:19235. AATF.
HPA	HPA004940.
MIM	608463. gene.
neXtProt	NX_Q9NY61.
PharmGKB	PA128395780.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG270454.
HOGENOM	HOG000007555.
HOVERGEN	HBG080805.
InParanoid	Q9NY61.
KO	K14782.
OMA	DKGGPEF.
OrthoDB	EOG41NTM1.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
Bgee	Q9NY61.
CleanEx	HS_AATF.
Genevestigator	Q9NY61.
Family and domain databases
InterPro	IPR025160. AATF. IPR012617. AATF_C. [Graphical view]
Pfam	PF13339. AATF-Che1. 1 hit. PF08164. TRAUB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AATF. human.
GenomeRNAi	26574.
NextBio	48910.
SOURCE	Search...

Entry information

Entry name

AATF_HUMAN

Accession

Primary (citable) accession number: Q9NY61
Secondary accession number(s): A6NCJ6 , B3KQ26, Q9P0A4, Q9UNX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete 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.