AATF_MOUSE - dbPTM
AATF_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AATF_MOUSE
UniProt AC Q9JKX4
Protein Name Protein AATF
Gene Name Aatf
Organism Mus musculus (Mouse).
Sequence Length 526
Subcellular Localization Nucleus, nucleolus .
Protein Description 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)..
Protein Sequence MAAPQPLALQLEQLLNPRPREADPEADPEEATRARVIDRFDEGEEEKDDLAVSSIRKLAPVSLLDTDKRYSGKTTSRKAWKEDHWEQALPSSSDNEASDEGGSEDGDSEGLGLEEISEDVDEDLEDNKISDEGGSEDGDSEGLGLEEFSEDVEEDLEGEDEEDREEDRNSEDDGVVAAFSSVKVSEEVEKGRAVKNQIALWDQLLEGRIKLQKALLTTNQLPQPDVFPVFKDKGGPEFASALKNSHKALKALLRSLVDLQEELLFQYPDTRHIVNGAKPNTESEEISSEDDELVGEKKKQRKAPPKRKLEMEDYPSFMAKRFADFTIYRNHTLQKWHDKTKLASGKLGKGFGAFERSILTQIDHIMMDKERLLRRTQTKRSAYRVLGKPEPVPEPVAETLPGEPETLPQGPANAHLRDLDEEIFDDDDFYHQLLRELIERKTSSLDPNDQVAMGRQWLAIQKLRSKIRKKVDRKASKGRKLRFHVLSKLLSFMAPIDHTAMSDDARTELFRSLFGQLNPPDADRGK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAPQPLAL
------CCCCCCHHH
28.05-
62PhosphorylationIRKLAPVSLLDTDKR
HHHHCCEEHHCCCCC
23.35-
75PhosphorylationKRYSGKTTSRKAWKE
CCCCCCCCCCHHHHH
29.9851457125
130PhosphorylationDLEDNKISDEGGSED
HHHHCCCCCCCCCCC
31.0825293948
135PhosphorylationKISDEGGSEDGDSEG
CCCCCCCCCCCCCCC
43.2925293948
140PhosphorylationGGSEDGDSEGLGLEE
CCCCCCCCCCCCHHH
38.8125293948
170PhosphorylationDREEDRNSEDDGVVA
HHHHHCCCCCCCHHE
43.2126239621
180PhosphorylationDGVVAAFSSVKVSEE
CCHHEEEECEECCHH
29.5118846507
181PhosphorylationGVVAAFSSVKVSEEV
CHHEEEECEECCHHH
21.3618846507
240PhosphorylationKGGPEFASALKNSHK
CCCHHHHHHHHHHHH
39.18-
281PhosphorylationVNGAKPNTESEEISS
CCCCCCCCCCCCCCC
49.7929138701
283PhosphorylationGAKPNTESEEISSED
CCCCCCCCCCCCCCC
38.1927087446
287PhosphorylationNTESEEISSEDDELV
CCCCCCCCCCCHHHH
30.8427087446
288PhosphorylationTESEEISSEDDELVG
CCCCCCCCCCHHHHC
51.1927087446
314PhosphorylationRKLEMEDYPSFMAKR
CCCCHHCCHHHHHHH
6.3522817900
316PhosphorylationLEMEDYPSFMAKRFA
CCHHCCHHHHHHHHC
22.7922817900
320AcetylationDYPSFMAKRFADFTI
CCHHHHHHHHCCEEE
35.947622843
442PhosphorylationRELIERKTSSLDPND
HHHHHHHCCCCCCCC
29.7525338131

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of AATF_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AATF_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AATF_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGD1_MOUSEMaged1physical
17488777

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AATF_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-288, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-288, ANDMASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-288, ANDMASS SPECTROMETRY.

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