Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9JKX4 (AATF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·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
Traube protein
Gene names
Name:Aatf
Synonyms:Che1, Trb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length526 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 By similarity.

Subunit structure

Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May also bind MAPT By similarity.

Subcellular location

Nucleusnucleolus Ref.1.

Tissue specificity

Expressed in adrenal gland, brain (Purkinje cells), heart, kidney, liver, lung, muscle, ovary and testis (at the protein level). Ref.1 Ref.5

Developmental stage

Expressed uniformly throughout the embryo until E10.5. From E11.5, the relative expression level increases in the liver, hind brain, spinal cord, dorsal root ganglia, and the posterior commissure. Ref.1

Sequence similarities

Belongs to the AATF family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from mutant phenotype Ref.1. Source: MGI

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

embryonic cleavage

Inferred from mutant phenotype Ref.1. Source: MGI

negative regulation of amyloid precursor protein biosynthetic process

Inferred from direct assay PubMed 14627703. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: MGI

ribosome biogenesis

Inferred from mutant phenotype Ref.1. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 14627703. Source: MGI

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay Ref.1. Source: MGI

nucleus

Inferred from direct assay Ref.1PubMed 14627703. Source: MGI

   Molecular_functionsequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JKX4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JKX4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     84-84: H → P
     85-199: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9JKX4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     433-458: LLRELIERKTSSLDPNDQVAMGRQWL → VRLFLSFLCYNKPGVCILEPLIVSSG
     459-526: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 526525Protein AATF
PRO_0000056617

Regions

Region240 – 28243Binds POLR2J By similarity
Region283 – 33856Binds RB1 By similarity
Region339 – 438100Binds RB1 and SP1 By similarity
Compositional bias96 – 17176Glu-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1701Phosphoserine By similarity
Modified residue2831Phosphoserine By similarity
Modified residue2871Phosphoserine Ref.6
Modified residue2881Phosphoserine Ref.6

Natural variations

Alternative sequence841H → P in isoform 2.
VSP_014897
Alternative sequence85 – 199115Missing in isoform 2.
VSP_014898
Alternative sequence433 – 45826LLREL…GRQWL → VRLFLSFLCYNKPGVCILEP LIVSSG in isoform 3.
VSP_014899
Alternative sequence459 – 52668Missing in isoform 3.
VSP_014900

Experimental info

Sequence conflict2 – 32AA → GR in AAP73747. Ref.5
Sequence conflict4 – 52Missing in AAP73747. Ref.5
Sequence conflict451E → K in AAP73747. Ref.5
Sequence conflict2371E → K in AAP73747. Ref.5
Sequence conflict2471K → Q in AAP73747. Ref.5
Sequence conflict2581D → G in AAP73747. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8AD2A8396F521DCF

FASTA52659,482
        10         20         30         40         50         60 
MAAPQPLALQ LEQLLNPRPR EADPEADPEE ATRARVIDRF DEGEEEKDDL AVSSIRKLAP 

        70         80         90        100        110        120 
VSLLDTDKRY SGKTTSRKAW KEDHWEQALP SSSDNEASDE GGSEDGDSEG LGLEEISEDV 

       130        140        150        160        170        180 
DEDLEDNKIS DEGGSEDGDS EGLGLEEFSE DVEEDLEGED EEDREEDRNS EDDGVVAAFS 

       190        200        210        220        230        240 
SVKVSEEVEK GRAVKNQIAL WDQLLEGRIK LQKALLTTNQ LPQPDVFPVF KDKGGPEFAS 

       250        260        270        280        290        300 
ALKNSHKALK ALLRSLVDLQ EELLFQYPDT RHIVNGAKPN TESEEISSED DELVGEKKKQ 

       310        320        330        340        350        360 
RKAPPKRKLE MEDYPSFMAK RFADFTIYRN HTLQKWHDKT KLASGKLGKG FGAFERSILT 

       370        380        390        400        410        420 
QIDHIMMDKE RLLRRTQTKR SAYRVLGKPE PVPEPVAETL PGEPETLPQG PANAHLRDLD 

       430        440        450        460        470        480 
EEIFDDDDFY HQLLRELIER KTSSLDPNDQ VAMGRQWLAI QKLRSKIRKK VDRKASKGRK 

       490        500        510        520 
LRFHVLSKLL SFMAPIDHTA MSDDARTELF RSLFGQLNPP DADRGK 

« Hide

Isoform 2 [UniParc].

Checksum: 9BFB0EF9774F70ED
Show »

FASTA41147,085
Isoform 3 [UniParc].

Checksum: D390D787E8B3612A
Show »

FASTA45851,506

References

« Hide 'large scale' references
[1]"The murine gene, Traube, is essential for the growth of preimplantation embryos."
Thomas T., Voss A.K., Petrou P., Gruss P.
Dev. Biol. 227:324-342(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Genomic structure and transcriptional regulation of Che-1, a novel partner of Rb."
Monaco L., Passananti C., Fanciulli M.
Gene 321:57-63(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-265 (ISOFORM 2), TISSUE SPECIFICITY.
Strain: Swiss.
Tissue: Testis.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222801 mRNA. Translation: AAF26745.1.
AK077789 mRNA. Translation: BAC37011.1.
AL603708, AL672252 Genomic DNA. Translation: CAI25418.1.
AL672252, AL603708 Genomic DNA. Translation: CAI26153.1.
BC025080 mRNA. Translation: AAH25080.1.
AF322223 Genomic DNA. Translation: AAK07639.1.
AY306199 mRNA. Translation: AAP73747.1.
RefSeqNP_062790.1. NM_019816.1.
UniGeneMm.257482.

3D structure databases

ProteinModelPortalQ9JKX4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207901. 2 interactions.
IntActQ9JKX4. 1 interaction.
MINTMINT-4130159.

PTM databases

PhosphoSiteQ9JKX4.

Proteomic databases

PaxDbQ9JKX4.
PRIDEQ9JKX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018841; ENSMUSP00000018841; ENSMUSG00000018697. [Q9JKX4-1]
GeneID56321.
KEGGmmu:56321.
UCSCuc007kqm.1. mouse. [Q9JKX4-1]
uc007kqn.1. mouse. [Q9JKX4-3]

Organism-specific databases

CTD26574.
MGIMGI:1929608. Aatf.

Phylogenomic databases

eggNOGNOG270454.
GeneTreeENSGT00390000000288.
HOGENOMHOG000007555.
HOVERGENHBG080805.
InParanoidQ9JKX4.
KOK14782.
OMAEDYPSFM.
OrthoDBEOG7VDXQ2.
PhylomeDBQ9JKX4.
TreeFamTF324341.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

BgeeQ9JKX4.
CleanExMM_AATF.
GenevestigatorQ9JKX4.

Family and domain databases

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

Other

NextBio312286.
PROQ9JKX4.
SOURCESearch...

Entry information

Entry nameAATF_MOUSE
AccessionPrimary (citable) accession number: Q9JKX4
Secondary accession number(s): Q7TQN1, Q8C5Q2, Q99P89
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot