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Q9NY61 (AATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. 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)
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 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
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.18
Modified residue2031Phosphoserine Ref.8 Ref.14 Ref.15 Ref.16
Modified residue3161Phosphoserine Ref.8 Ref.15 Ref.17 Ref.18 Ref.19
Modified residue3201Phosphoserine Ref.8 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19
Modified residue3211Phosphoserine Ref.8 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19

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: 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. 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: 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. 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: 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. 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: 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.
IPIIPI00302238.
RefSeqNP_036270.1. NM_012138.3.
UniGeneHs.195740.

3D structure databases

ProteinModelPortalQ9NY61.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NY61. 14 interactions.
MINTMINT-131397.
STRINGQ9NY61.

PTM databases

PhosphoSiteQ9NY61.

Polymorphism databases

DMDM71152211.

2D gel databases

SWISS-2DPAGEQ9NY61.

Proteomic databases

PRIDEQ9NY61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225402; ENSP00000225402; ENSG00000108270.
GeneID26574.
KEGGhsa:26574.
UCSCuc002hni.1. human.

Organism-specific databases

CTD26574.
GeneCardsGC17P035306.
H-InvDBHIX0013742.
HGNCHGNC:19235. AATF.
HPAHPA004940.
MIM608463. gene.
neXtProtNX_Q9NY61.
PharmGKBPA128395780.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17989.
GeneTreeENSGT00390000000288.
HOGENOMHBG607920.
HOVERGENHBG080805.
InParanoidQ9NY61.
OMAKDKGGPE.
OrthoDBEOG41NTM1.
PhylomeDBQ9NY61.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9NY61.
BgeeQ9NY61.
CleanExHS_AATF.
GenevestigatorQ9NY61.

Family and domain databases

InterProIPR012617. TRAUB.
[Graphical view]
KOK14782.
PfamPF08164. TRAUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio48910.
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: January 25, 2012
This is version 85 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

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