dbPTM

AP2C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AP2C_HUMAN
UniProt AC	Q92754
Protein Name	Transcription factor AP-2 gamma
Gene Name	TFAP2C
Organism	Homo sapiens (Human).
Sequence Length	450
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. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer..
Protein Sequence	MLWKITDNVKYEEDCEDRHDGSSNGNPRVPHLSSAGQHLYSPAPPLSHTGVAEYQPPPYFPPPYQQLAYSQSADPYSHLGEAYAAAINPLHQPAPTGSQQQAWPGRQSQEGAGLPSHHGRPAGLLPHLSGLEAGAVSARRDAYRRSDLLLPHAHALDAAGLAENLGLHDMPHQMDEVQNVDDQHLLLHDQTVIRKGPISMTKNPLNLPCQKELVGAVMNPTEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAAHVTLLTSLVEGEAVHLARDFAYVCEAEFPSKPVAEYLTRPHLGGRNEMAARKNMLLAAQQLCKEFTELLSQDRTPHGTSRLAPVLETNIQNCLSHFSLITHGFGSQAICAAVSALQNYIKEALIVIDKSYMNPGDQSPADSNKTLEKMEKHRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Sumoylation	WKITDNVKYEEDCED CEECCCCCCCCCCCC	53.88	-
10	Sumoylation	WKITDNVKYEEDCED CEECCCCCCCCCCCC	53.88	-
11	Phosphorylation	KITDNVKYEEDCEDR EECCCCCCCCCCCCC	21.92	22210691
22	Phosphorylation	CEDRHDGSSNGNPRV CCCCCCCCCCCCCCC	27.04	22210691
42	Ubiquitination	AGQHLYSPAPPLSHT CCCCCCCCCCCCCCC	34.92	-
70	Ubiquitination	PYQQLAYSQSADPYS HHHHHCCCCCCCCCC	16.44	-
72	Ubiquitination	QQLAYSQSADPYSHL HHHCCCCCCCCCCHH	28.79	-
112	Ubiquitination	GRQSQEGAGLPSHHG CCCCCCCCCCCCCCC	18.65	-
115	Ubiquitination	SQEGAGLPSHHGRPA CCCCCCCCCCCCCCC	30.60	-
202	Ubiquitination	KGPISMTKNPLNLPC CCCCCCCCCCCCCCC	48.18	29967540
211	Ubiquitination	PLNLPCQKELVGAVM CCCCCCHHHHHCCCC	60.78	21963094
232	Phosphorylation	CSVPGRLSLLSSTSK ECCCCCHHHCCCCCC	26.38	51163003
235	Phosphorylation	PGRLSLLSSTSKYKV CCCHHHCCCCCCEEE	36.54	25159151
236	Phosphorylation	GRLSLLSSTSKYKVT CCHHHCCCCCCEEEE	36.35	29255136
237	Phosphorylation	RLSLLSSTSKYKVTV CHHHCCCCCCEEEEH	26.34	29255136
238	Phosphorylation	LSLLSSTSKYKVTVA HHHCCCCCCEEEEHH	35.62	30576142
239	Ubiquitination	SLLSSTSKYKVTVAE HHCCCCCCEEEEHHH	49.53	21963094
241	Ubiquitination	LSSTSKYKVTVAEVQ CCCCCCEEEEHHHHH	34.86	22817900
252	Phosphorylation	AEVQRRLSPPECLNA HHHHHHCCCHHHHCH	36.28	22617229
260	Phosphorylation	PPECLNASLLGGVLR CHHHHCHHHHHHHHH	24.05	24732914
271	Phosphorylation	GVLRRAKSKNGGRSL HHHHHHHHCCCCHHH	30.30	10049255
281	Ubiquitination	GGRSLREKLDKIGLN CCHHHHHHHHHHCCC	56.40	-
284	Ubiquitination	SLREKLDKIGLNLPA HHHHHHHHHCCCCCC	49.46	-
434	Phosphorylation	YMNPGDQSPADSNKT HCCCCCCCCCCHHHH	27.13	30278072
438	Phosphorylation	GDQSPADSNKTLEKM CCCCCCCHHHHHHHH	42.19	24732914
440	Acetylation	QSPADSNKTLEKMEK CCCCCHHHHHHHHHH	59.44	26051181
441	Phosphorylation	SPADSNKTLEKMEKH CCCCHHHHHHHHHHH	44.38	26074081
444	Acetylation	DSNKTLEKMEKHRK- CHHHHHHHHHHHCC-	56.31	26051181
444	Ubiquitination	DSNKTLEKMEKHRK- CHHHHHHHHHHHCC-	56.31	-
447	Ubiquitination	KTLEKMEKHRK---- HHHHHHHHHCC----	45.25	-

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
252	S	Phosphorylation	Kinase	PKA	-	Uniprot

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 AP2C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYC_HUMAN	MYC	genetic	22371483
KDM5B_HUMAN	KDM5B	genetic	22371483
MYC_HUMAN	MYC	physical	22371483
KDM5B_HUMAN	KDM5B	physical	22371483
UBC9_HUMAN	UBE2I	physical	12072434
ERBB4_HUMAN	ERBB4	physical	20943952

Drug and Disease Associations

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

Regulatory Network of AP2C_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-434, AND MASSSPECTROMETRY.	18669648 [Abstract]
Sumoylation
Reference	PubMed
"Transcription factor AP-2 interacts with the SUMO-conjugating enzymeUBC9 and is sumolated in vivo."; Eloranta J.J., Hurst H.C.; J. Biol. Chem. 277:30798-30804(2002). Cited for: INTERACTION WITH UBE2I, AND SUMOYLATION AT LYS-10.	12072434 [Abstract]

show