AP2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP2A_MOUSE
• UniProt AC: P34056
• Protein Name: Transcription factor AP-2-alpha
• Gene Name: Tfap2a
• Organism: Mus musculus (Mouse).
• Sequence Length: 437
• Subcellular Localization: Nucleus.
• Protein Description: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region..
• Protein Sequence: MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALGSGLGDLPIHSLPHAIEDVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVARKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNSAKSSDKEEKHRK

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
119	Phosphorylation	RGLPHQLSGLDPRRD CCCCHHHCCCCCCCC	30.64	101546439
185	Phosphorylation	GPVSLSKSNSNAVSA CCCCCCCCCCCCCEE	41.96	23375375
187	Phosphorylation	VSLSKSNSNAVSAIP CCCCCCCCCCCEEEE	33.00	6371355
219	Phosphorylation	CSVPGRLSLLSSTSK EECCCCCHHCCCCCC	26.38	51163007
223	Phosphorylation	GRLSLLSSTSKYKVT CCCHHCCCCCCEEEE	36.35	22006019
225	Phosphorylation	LSLLSSTSKYKVTVA CHHCCCCCCEEEEHH	35.62	29514104
230	Phosphorylation	STSKYKVTVAEVQRR CCCCEEEEHHHHHHH	15.17	-
239	Phosphorylation	AEVQRRLSPPECLNA HHHHHHCCCHHHHCH	36.28	22817900
258	Phosphorylation	GVLRRAKSKNGGRSL HHHHHHHHCCCCHHH	30.30	10049257
263	Methylation	AKSKNGGRSLREKLD HHHCCCCHHHHHHHH	33.64	-
287	Phosphorylation	RRKAANVTLLTSLVE CHHHCCEEEEEHHHH	18.83	27180971
290	Phosphorylation	AANVTLLTSLVEGEA HCCEEEEEHHHHCCH	24.11	27180971
291	Phosphorylation	ANVTLLTSLVEGEAV CCEEEEEHHHHCCHH	30.32	27180971
420	Phosphorylation	YLSNNPNSHTDNSAK HHHCCCCCCCCCCCC	29.08	29514104
425	Phosphorylation	PNSHTDNSAKSSDKE CCCCCCCCCCCCCHH	39.62	28576409

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
219	S	Phosphorylation	Kinase	AMPKA2	Q8BRK8	PSP
239	S	Phosphorylation	Kinase	PKA	-	Uniprot
258	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
10	K	Sumoylation	Sumoylated on Lys-10; which inhibits transcriptional activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AP2A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AP2D_MOUSE	Tfap2d	physical	20211142
CITE2_MOUSE	Cited2	physical	11694877
BRE1A_MOUSE	Rnf20	physical	24374663

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.