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Q9NY61 (AATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Nucleusnucleolus 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 componentNucleus
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from expression pattern PubMed 18049476. Source: UniProtKB

embryonic cleavage

Inferred from electronic annotation. Source: Ensembl

negative regulation of amyloid precursor protein biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of reactive oxygen species metabolic process

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of superoxide anion generation

Inferred from direct assay Ref.13. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

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: Ensembl

ribosome biogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

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

nucleus

Inferred from direct assay PubMed 10580117Ref.9Ref.12Ref.13. Source: UniProtKB

   Molecular_functionleucine zipper domain binding

Inferred from physical interaction PubMed 10580117Ref.12. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2. Source: UniProtKB

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

ATMQ133153EBI-372428,EBI-495465
CHEK2O960174EBI-372428,EBI-1180783
Myl12aQ6ZWQ93EBI-372428,EBI-8034418From a different organism.
RELAQ042063EBI-372428,EBI-73886

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 560559Protein AATF
PRO_0000056616

Regions

Region273 – 31543POLR2J binding
Region316 – 37257RB1 binding
Region373 – 472100RB1 and SP1 binding
Compositional bias96 – 195100Glu-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue2031Phosphoserine Ref.8 Ref.17 Ref.18
Modified residue3161Phosphoserine Ref.8 Ref.14 Ref.16 Ref.17 Ref.18
Modified residue3201Phosphoserine Ref.8 Ref.14 Ref.16 Ref.17 Ref.18
Modified residue3211Phosphoserine Ref.8 Ref.14 Ref.16 Ref.17 Ref.18

Experimental info

Sequence conflict2 – 32AG → GR in AAD52016. Ref.2
Sequence conflict4 – 52Missing in AAD52016. Ref.2
Sequence conflict1391S → T in AAD52016. Ref.2
Sequence conflict2621L → V in AAD52016. Ref.2
Sequence conflict2721S → A in AAD52016. Ref.2
Sequence conflict3061L → V in AAD52016. Ref.2
Sequence conflict4021D → C in AAD52016. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NY61 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EC493EF3B4C3A199

FASTA56063,133
        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 

« Hide

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] [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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS32632.1.
RefSeqNP_036270.1. NM_012138.3.
UniGeneHs.195740.

3D structure databases

ProteinModelPortalQ9NY61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117743. 33 interactions.
IntActQ9NY61. 16 interactions.
MINTMINT-131397.
STRING9606.ENSP00000225402.

PTM databases

PhosphoSiteQ9NY61.

Polymorphism databases

DMDM71152211.

2D gel databases

SWISS-2DPAGEQ9NY61.

Proteomic databases

MaxQBQ9NY61.
PaxDbQ9NY61.
PRIDEQ9NY61.

Protocols and materials databases

DNASU26574.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225402; ENSP00000225402; ENSG00000108270.
GeneID26574.
KEGGhsa:26574.
UCSCuc002hni.3. human.

Organism-specific databases

CTD26574.
GeneCardsGC17P035306.
HGNCHGNC:19235. AATF.
HPAHPA004940.
MIM608463. gene.
neXtProtNX_Q9NY61.
PharmGKBPA128395780.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270454.
HOGENOMHOG000007555.
HOVERGENHBG080805.
InParanoidQ9NY61.
KOK14782.
OMAQLHPPDE.
OrthoDBEOG7VDXQ2.
PhylomeDBQ9NY61.
TreeFamTF324341.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9NY61.
BgeeQ9NY61.
CleanExHS_AATF.
GenevestigatorQ9NY61.

Family and domain databases

InterProIPR025160. AATF.
IPR012617. AATF_C.
[Graphical view]
PfamPF13339. AATF-Che1. 1 hit.
PF08164. TRAUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAATF. human.
GeneWikiApoptosis-antagonizing_transcription_factor.
GenomeRNAi26574.
NextBio48910.
PROQ9NY61.
SOURCESearch...

Entry information

Entry nameAATF_HUMAN
AccessionPrimary (citable) accession number: Q9NY61
Secondary accession number(s): A6NCJ6 expand/collapse secondary AC list , B3KQ26, Q9P0A4, Q9UNX5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM