Protein AATF - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9NY61 (AATF_HUMAN)

Last modified July 22, 2008. Version 52. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	560 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Subunit structure	Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May also bind MAPT.
Subcellular location	Nucleus › nucleolus.
Tissue specificity	Ubiquitously expressed. Expressed at high levels in brain, heart, kidney, placenta and thymus.
Post-translational modification	Hyperphosphorylated during the G1/S phase transition.
Sequence similarities	Belongs to the AATF family.
Sequence caution	AAD52016.1 sequence differs from that shown. Reason: Frameshift at positions 355, 365, 487, 498 and 503.

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Ontologies

Keywords
Cellular component	Nucleus
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ATM	Q13315	2	EBI-372428,EBI-495465
ATR	Q13535	1	EBI-372428,EBI-968983
CHEK1	O14757	1	EBI-372428,EBI-974488
CHEK2	O96017	3	EBI-372428,EBI-1180783
MPHOSPH6	Q99547	1	EBI-372428,EBI-373187
RELA	Q04206	2	EBI-372428,EBI-73886

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 560

560

Protein AATF

Regions

Region

273 – 315

POLR2J binding

Region

316 – 372

RB1 binding

Region

373 – 472

100

RB1 and SP1 binding

Compositional bias

96 – 195

100

Glu-rich

Amino acid modifications

Modified residue

203

Phosphoserine

Modified residue

316

Phosphoserine

Modified residue

320

Phosphoserine

Modified residue

321

Phosphoserine

Experimental info

Sequence conflict

2 – 3

AG → GR in AAD52016. Ref.2

Sequence conflict

4 – 5

Missing in AAD52016. Ref.2

Sequence conflict

139

S → T in AAD52016. Ref.2

Sequence conflict

262

L → V in AAD52016. Ref.2

Sequence conflict

272

S → A in AAD52016. Ref.2

Sequence conflict

306

L → V in AAD52016. Ref.2

Sequence conflict

402

D → C in AAD52016. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9NY61-1 [UniParc].

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

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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: 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]	"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].
[4]	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].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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].
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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: Epithelium.
[14]	"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: Epithelium.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases
	AJ249940 mRNA. Translation: CAB57451.2. AF083208 mRNA. Translation: AAD52016.1. Frameshift. AC003103 Genomic DNA. No translation available. CH471199 Genomic DNA. Translation: EAW57575.1. BC000591 mRNA. Translation: AAH00591.1. AF161395 mRNA. Translation: AAF28955.1.
RefSeq	NP_036270.1.
UniGene	Hs.195740
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NY61.
PTM databases
PhosphoSite	Q9NY61.
2-D gel databases
SWISS-2DPAGE	Q9NY61.
Genome annotation databases
Ensembl	ENSG00000108270. Homo sapiens. [Contig view]
GeneID	26574.
KEGG	hsa:26574.
Organism-specific databases
H-InvDB	HIX0013742.
HGNC	HGNC:19235. AATF.
HPA	HPA004940.
MIM	608463. gene.
PharmGKB	PA128395780.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOVERGEN	Q9NY61.
Gene expression databases
ArrayExpress	Q9NY61.
CleanEx	HS_AATF.
Family and domain databases
InterPro	IPR012617. TRAUB. [Graphical view]
Pfam	PF08164. TRAUB. 1 hit. [Graphical view]
ProDom	Q9NY61. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

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Entry information

Entry name

AATF_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	October 1, 2000
Last modified:	July 22, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents