FOXA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FOXA2_HUMAN
• UniProt AC: Q9Y261
• Protein Name: Hepatocyte nuclear factor 3-beta
• Gene Name: FOXA2
• Organism: Homo sapiens (Human).
• Sequence Length: 457
• Subcellular Localization: Nucleus . Cytoplasm . Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner; in response to insulin signaling via AKT1 is exported from the nucleus.
• Protein Description: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation..
• Protein Sequence: MLGAVKMEGHEPSDWSSYYAEPEGYSSVSNMNAGLGMNGMNTYMSMSAAAMGSGSGNMSAGSMNMSSYVGAGMSPSLAGMSPGAGAMAGMGGSAGAAGVAGMGPHLSPSLSPLGGQAAGAMGGLAPYANMNSMSPMYGQAGLSRARDPKTYRRSYTHAKPPYSYISLITMAIQQSPNKMLTLSEIYQWIMDLFPFYRQNQQRWQNSIRHSLSFNDCFLKVPRSPDKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKCEKQLALKEAAGAAGSGKKAAAGAQASQAQLGEAAGPASETPAGTESPHSSASPCQEHKRGGLGELKGTPAAALSPPEPAPSPGQQQQAAAHLLGPPHHPGLPPEAHLKPEHHYAFNHPFSINNLMSSEQQHHHSHHHHQPHKMDLKAYEQVMHYPGYGSPMPGSLAMGPVTNKTGLDASPLAADTSYYQGVYSRPIMNSS

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
3 (in isoform 2)	Phosphorylation	-	27.33	24043423
5 (in isoform 2)	Phosphorylation	-	6.02	24043423
6	Acetylation	--MLGAVKMEGHEPS --CCCCCCCCCCCCC	30.60	67205201
6 (in isoform 2)	Phosphorylation	-	30.60	24043423
107	Phosphorylation	AGMGPHLSPSLSPLG CCCCCCCCCCCCCCC	14.92	22196886
111	Phosphorylation	PHLSPSLSPLGGQAA CCCCCCCCCCCHHHC	23.55	22196886
156	Phosphorylation	KTYRRSYTHAKPPYS CCCCCCCCCCCCCCH	19.32	14500912
212	Phosphorylation	NSIRHSLSFNDCFLK HHHHHHCCCCCCEEE	25.64	23312004
223	Phosphorylation	CFLKVPRSPDKPGKG CEEECCCCCCCCCCC	31.23	26657352
248	Phosphorylation	NMFENGCYLRRQKRF CCCCCCEEHHHHHCH	12.49	-
256	Acetylation	LRRQKRFKCEKQLAL HHHHHCHHCHHHHHH	45.58	19830003
259	Acetylation	QKRFKCEKQLALKEA HHCHHCHHHHHHHHH	61.14	55166807
264	Acetylation	CEKQLALKEAAGAAG CHHHHHHHHHHCCCC	39.43	19830013
274	Acetylation	AGAAGSGKKAAAGAQ HCCCCCCHHHHHHHH	40.72	7298009
275	Acetylation	GAAGSGKKAAAGAQA CCCCCCHHHHHHHHH	46.94	7298019
283	Phosphorylation	AAAGAQASQAQLGEA HHHHHHHHHHHHHHH	17.61	25999147
295	Phosphorylation	GEAAGPASETPAGTE HHHCCCCCCCCCCCC	45.17	29116813
297	Phosphorylation	AAGPASETPAGTESP HCCCCCCCCCCCCCC	18.88	29116813
301	Phosphorylation	ASETPAGTESPHSSA CCCCCCCCCCCCCCC	35.08	26657352
303	Phosphorylation	ETPAGTESPHSSASP CCCCCCCCCCCCCCC	27.96	30206219
306	Phosphorylation	AGTESPHSSASPCQE CCCCCCCCCCCCCHH	30.86	29116813
307	Phosphorylation	GTESPHSSASPCQEH CCCCCCCCCCCCHHH	29.72	30206219
309	Phosphorylation	ESPHSSASPCQEHKR CCCCCCCCCCHHHCC	28.31	30206219
338	Phosphorylation	SPPEPAPSPGQQQQA CCCCCCCCCCHHHHH	43.71	26657352
436	Phosphorylation	NKTGLDASPLAADTS CCCCCCCCCCCCCCC	21.80	28348404
457	Phosphorylation	SRPIMNSS------- CCCCCCCC-------	38.96	-

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
107	S	Phosphorylation	Kinase	CHUK	O15111	GPS
111	S	Phosphorylation	Kinase	CHUK	O15111	GPS
156	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
156	T	Phosphorylation	Phosphorylation on Thr-156 abolishes binding to target promoters and subsequent transcription activation upon insulin stimulation.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FOXA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HNF6_HUMAN	ONECUT1	physical	12509444
TLE1_HUMAN	TLE1	physical	10748198
HXD13_HUMAN	HOXD13	physical	25609649
SATB2_HUMAN	SATB2	physical	25609649
DSRAD_HUMAN	ADAR	physical	25609649
GDE_HUMAN	AGL	physical	25609649
DACH1_HUMAN	DACH1	physical	25609649
FOXN2_HUMAN	FOXN2	physical	25609649
HXB13_HUMAN	HOXB13	physical	25609649
NACC1_HUMAN	NACC1	physical	25609649
SALL1_HUMAN	SALL1	physical	25609649

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.