dbPTM

AP2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AP2A_HUMAN
UniProt AC	P05549
Protein Name	Transcription factor AP-2-alpha
Gene Name	TFAP2A
Organism	Homo sapiens (Human).
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	MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Acetylation	WKLTDNIKYEDCEDR CCCCCCCCCCCCCCC	49.17	26051181
10	Ubiquitination	WKLTDNIKYEDCEDR CCCCCCCCCCCCCCC	49.17	29967540
10	Sumoylation	WKLTDNIKYEDCEDR CCCCCCCCCCCCCCC	49.17	12072434
73	Phosphorylation	YPQSQDPYSHVNDPY CCCCCCCCCCCCCCC	21.50	46164837
102	Phosphorylation	GWPGQRQSQESGLLH CCCCCHHCCCCCCCC	37.80	28555341
119	Phosphorylation	RGLPHQLSGLDPRRD CCCCHHHCCCCCCCC	30.64	27251275
147	Ubiquitination	LSSGLGDLSIHSLPH HCCCCCCCCCCCCCH	5.00	21963094
171	Ubiquitination	DPGINIPDQTVIKKG CCCCCCCCCCEEECC	53.65	29967540
173	Ubiquitination	GINIPDQTVIKKGPV CCCCCCCCEEECCCC	31.42	29967540
176	Ubiquitination	IPDQTVIKKGPVSLS CCCCCEEECCCCCCC	47.55	21963094
177	Sumoylation	PDQTVIKKGPVSLSK CCCCEEECCCCCCCC	58.27	-
177	Ubiquitination	PDQTVIKKGPVSLSK CCCCEEECCCCCCCC	58.27	29967540
177	Sumoylation	PDQTVIKKGPVSLSK CCCCEEECCCCCCCC	58.27	28112733
178	Ubiquitination	DQTVIKKGPVSLSKS CCCEEECCCCCCCCC	23.88	22817900
180	Ubiquitination	TVIKKGPVSLSKSNS CEEECCCCCCCCCCC	14.16	29967540
181	Phosphorylation	VIKKGPVSLSKSNSN EEECCCCCCCCCCCC	30.02	18669648
183	Phosphorylation	KKGPVSLSKSNSNAV ECCCCCCCCCCCCCC	26.91	18669648
184	Sumoylation	KGPVSLSKSNSNAVS CCCCCCCCCCCCCCE	59.97	28112733
184	Ubiquitination	KGPVSLSKSNSNAVS CCCCCCCCCCCCCCE	59.97	29967540
185	Phosphorylation	GPVSLSKSNSNAVSA CCCCCCCCCCCCCEE	41.96	25159151
187	Phosphorylation	VSLSKSNSNAVSAIP CCCCCCCCCCCEEEE	33.00	25159151
191	Ubiquitination	KSNSNAVSAIPINKD CCCCCCCEEEECCCC	20.33	21963094
191	Phosphorylation	KSNSNAVSAIPINKD CCCCCCCEEEECCCC	20.33	28787133
193	Ubiquitination	NSNAVSAIPINKDNL CCCCCEEEECCCCCC	2.47	21963094
197	Ubiquitination	VSAIPINKDNLFGGV CEEEECCCCCCCCCC	49.03	21963094
197	Acetylation	VSAIPINKDNLFGGV CEEEECCCCCCCCCC	49.03	26051181
213	Phosphorylation	NPNEVFCSVPGRLSL CCCCCEEECCCCCHH	21.63	29514088
219	Phosphorylation	CSVPGRLSLLSSTSK EECCCCCHHCCCCCC	26.38	51163003
220	Ubiquitination	SVPGRLSLLSSTSKY ECCCCCHHCCCCCCE	6.78	21963094
222	Ubiquitination	PGRLSLLSSTSKYKV CCCCHHCCCCCCEEE	36.54	21963094
222	Phosphorylation	PGRLSLLSSTSKYKV CCCCHHCCCCCCEEE	36.54	25159151
223	Phosphorylation	GRLSLLSSTSKYKVT CCCHHCCCCCCEEEE	36.35	29255136
224	Phosphorylation	RLSLLSSTSKYKVTV CCHHCCCCCCEEEEH	26.34	29255136
224	Ubiquitination	RLSLLSSTSKYKVTV CCHHCCCCCCEEEEH	26.34	22817900
225	Phosphorylation	LSLLSSTSKYKVTVA CHHCCCCCCEEEEHH	35.62	25159151
226	Ubiquitination	SLLSSTSKYKVTVAE HHCCCCCCEEEEHHH	49.53	21963094
226	Acetylation	SLLSSTSKYKVTVAE HHCCCCCCEEEEHHH	49.53	26051181
228	Ubiquitination	LSSTSKYKVTVAEVQ CCCCCCEEEEHHHHH	34.86	22817900
239	Phosphorylation	AEVQRRLSPPECLNA HHHHHHCCCHHHHCH	36.28	22617229
242	Ubiquitination	QRRLSPPECLNASLL HHHCCCHHHHCHHHH	55.83	21963094
247	Phosphorylation	PPECLNASLLGGVLR CHHHHCHHHHHHHHH	24.05	24732914
258	Phosphorylation	GVLRRAKSKNGGRSL HHHHHHHHCCCCHHH	30.30	18845787
265	Ubiquitination	SKNGGRSLREKLDKI HCCCCHHHHHHHHHH	8.69	33845483
267	Ubiquitination	NGGRSLREKLDKIGL CCCHHHHHHHHHHCC	64.36	33845483
268	Ubiquitination	GGRSLREKLDKIGLN CCHHHHHHHHHHCCC	56.40	-
271	Ubiquitination	SLREKLDKIGLNLPA HHHHHHHHHCCCCCC	49.46	21963094
273	Ubiquitination	REKLDKIGLNLPAGR HHHHHHHCCCCCCCC	17.79	33845483
276	Ubiquitination	LDKIGLNLPAGRRKA HHHHCCCCCCCCHHH	3.55	29967540
278	Ubiquitination	KIGLNLPAGRRKAAN HHCCCCCCCCHHHCC	27.56	29967540
279	Ubiquitination	IGLNLPAGRRKAANV HCCCCCCCCHHHCCE	28.17	21963094
282	Ubiquitination	NLPAGRRKAANVTLL CCCCCCHHHCCEEEE	50.95	29967540
308	Ubiquitination	ARDFGYVCETEFPAK HHHHCCEECCCCCHH	3.94	21963094
309	Ubiquitination	RDFGYVCETEFPAKA HHHCCEECCCCCHHH	41.13	32015554
310	Ubiquitination	DFGYVCETEFPAKAV HHCCEECCCCCHHHH	37.49	22817900
311	Ubiquitination	FGYVCETEFPAKAVA HCCEECCCCCHHHHH	27.60	32015554
315	Ubiquitination	CETEFPAKAVAEFLN ECCCCCHHHHHHHHH	43.56	21987572
317	Ubiquitination	TEFPAKAVAEFLNRQ CCCCHHHHHHHHHHH	5.30	32015554
326	Phosphorylation	EFLNRQHSDPNEQVT HHHHHHCCCCCHHHH	46.56	18845787
329	Ubiquitination	NRQHSDPNEQVTRKN HHHCCCCCHHHHHHH	58.27	29967540
331	Ubiquitination	QHSDPNEQVTRKNML HCCCCCHHHHHHHHH	48.82	29967540
333	Phosphorylation	SDPNEQVTRKNMLLA CCCCHHHHHHHHHHH	35.30	26074081
335	Ubiquitination	PNEQVTRKNMLLATK CCHHHHHHHHHHHHH	37.03	29967540
360	Ubiquitination	AQDRSPLGNSRPNPI HCCCCCCCCCCCCCC	33.19	21987572
397	Ubiquitination	AVCAAVTALQNYLTE HHHHHHHHHHHHHHH	10.68	21987572
405	Ubiquitination	LQNYLTEALKAMDKM HHHHHHHHHHHHHHH	14.77	29967540
407	Ubiquitination	NYLTEALKAMDKMYL HHHHHHHHHHHHHHH	49.03	29967540
411	Ubiquitination	EALKAMDKMYLSNNP HHHHHHHHHHHHCCC	19.16	29967540
427	Acetylation	SHTDNNAKSSDKEEK CCCCCCCCCCCHHHH	53.25	26051181
428	Phosphorylation	HTDNNAKSSDKEEKH CCCCCCCCCCHHHHH	41.16	50565743
429	Phosphorylation	TDNNAKSSDKEEKHR CCCCCCCCCHHHHHC	52.58	41595205
431	Acetylation	NNAKSSDKEEKHRK- CCCCCCCHHHHHCC-	70.49	26051181

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	PRKAA2	P54646	GPS
239	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
239	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
239	S	Phosphorylation	Kinase	PKA	-	Uniprot
258	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
258	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
326	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
326	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
429	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
429	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
10	K	Sumoylation		12072434
Sumoylated on Lys-10; which inhibits transcriptional activity.

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 AP2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	12226108
APC_HUMAN	APC	physical	15331612
CTNB1_HUMAN	CTNNB1	physical	15331612
DEK_HUMAN	DEK	physical	12595566
CITE2_HUMAN	CITED2	physical	12586840
MYC_HUMAN	MYC	physical	7729426
YBOX1_HUMAN	YBX1	physical	9830047
TYY1_HUMAN	YY1	physical	15870067
NPM_HUMAN	NPM1	physical	17318229
UBC9_HUMAN	UBE2I	physical	12072434
AURKA_HUMAN	AURKA	physical	21829699
EPN1_HUMAN	EPN1	physical	15809337
KCTD1_HUMAN	KCTD1	physical	19115315
SRA1_HUMAN	SRA1	physical	20398657
DAB2_HUMAN	DAB2	physical	22323290
KCD15_HUMAN	KCTD15	physical	23382213
MKRN3_HUMAN	MKRN3	physical	25416956
GSTO2_HUMAN	GSTO2	physical	25416956
EPN1_HUMAN	EPN1	physical	16497222
AP2D_HUMAN	TFAP2D	physical	26186194
ACOT1_HUMAN	ACOT1	physical	26186194
AAPK2_HUMAN	PRKAA2	physical	22561688
CSK2B_HUMAN	CSNK2B	physical	21777522
ERBB4_HUMAN	ERBB4	physical	20943952
AP2C_HUMAN	TFAP2C	physical	20459791
CFTR_RAT	Cftr	physical	20351096
XRCC6_HUMAN	XRCC6	physical	19906305
XRCC5_HUMAN	XRCC5	physical	19906305
TF65_HUMAN	RELA	physical	19074833
SP1_HUMAN	SP1	physical	19074833
NPM_HUMAN	NPM1	physical	19074833
NFKB1_HUMAN	NFKB1	physical	19074833
AP2B_HUMAN	TFAP2B	physical	18843039
AP2B1_HUMAN	AP2B1	physical	18843039
AP1M2_HUMAN	AP1M2	physical	18843039
ACOT1_HUMAN	ACOT1	physical	28514442
P53_HUMAN	TP53	physical	16288208

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
113620	Branchiooculofacial syndrome (BOFS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AP2A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-239, ANDMASS SPECTROMETRY.	18669648 [Abstract]

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