dbPTM

GATA6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GATA6_HUMAN
UniProt AC	Q92908
Protein Name	Transcription factor GATA-6
Gene Name	GATA6
Organism	Homo sapiens (Human).
Sequence Length	595
Subcellular Localization	Nucleus .
Protein Description	Transcriptional activator. [PubMed: 19666519]
Protein Sequence	MALTDGGWCLPKRFGAAGADASDSRAFPAREPSTPPSPISSSSSSCSRGGERGPGGASNCGTPQLDTEAAAGPPARSLLLSSYASHPFGAPHGPSAPGVAGPGGNLSSWEDLLLFTDLDQAATASKLLWSSRGAKLSPFAPEQPEEMYQTLAALSSQGPAAYDGAPGGFVHSAAAAAAAAAAASSPVYVPTTRVGSMLPGLPYHLQGSGSGPANHAGGAGAHPGWPQASADSPPYGSGGGAAGGGAAGPGGAGSAAAHVSARFPYSPSPPMANGAAREPGGYAAAGSGGAGGVSGGGSSLAAMGGREPQYSSLSAARPLNGTYHHHHHHHHHHPSPYSPYVGAPLTPAWPAGPFETPVLHSLQSRAGAPLPVPRGPSADLLEDLSESRECVNCGSIQTPLWRRDGTGHYLCNACGLYSKMNGLSRPLIKPQKRVPSSRRLGLSCANCHTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQTRKRKPKNINKSKTCSGNSNNSIPMTPTSTSSNSDDCSKNTSPTTQPTASGAGAPVMTGAGESTNPENSELKYSGQDGLYIGVSLASPAEVTSSVRPDSWCALALA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Phosphorylation	AGADASDSRAFPARE CCCCCCCCCCCCCCC	24.02	22985185
33	Phosphorylation	AFPAREPSTPPSPIS CCCCCCCCCCCCCCC	49.12	22617229
34	Phosphorylation	FPAREPSTPPSPISS CCCCCCCCCCCCCCC	50.35	26657352
37	Phosphorylation	REPSTPPSPISSSSS CCCCCCCCCCCCCCC	35.75	26657352
40	Phosphorylation	STPPSPISSSSSSCS CCCCCCCCCCCCCCC	27.79	27794612
41	Phosphorylation	TPPSPISSSSSSCSR CCCCCCCCCCCCCCC	34.65	27794612
42	Phosphorylation	PPSPISSSSSSCSRG CCCCCCCCCCCCCCC	27.70	22468782
43	Phosphorylation	PSPISSSSSSCSRGG CCCCCCCCCCCCCCC	28.37	27794612
44	Phosphorylation	SPISSSSSSCSRGGE CCCCCCCCCCCCCCC	36.99	22468782
45	Phosphorylation	PISSSSSSCSRGGER CCCCCCCCCCCCCCC	20.33	27794612
47	Phosphorylation	SSSSSSCSRGGERGP CCCCCCCCCCCCCCC	35.59	27794612
58	Phosphorylation	ERGPGGASNCGTPQL CCCCCCCCCCCCCCC	35.61	21815630
62	Phosphorylation	GGASNCGTPQLDTEA CCCCCCCCCCCCHHH	15.29	28985074
120	Phosphorylation	LLFTDLDQAATASKL HCCCCHHHHHHHHHH	39.95	18669648
122	Phosphorylation	FTDLDQAATASKLLW CCCHHHHHHHHHHHH	9.69	18669648
188	Phosphorylation	AAASSPVYVPTTRVG HHHCCCEEECCCCCC	12.23	-
265	Phosphorylation	HVSARFPYSPSPPMA CHHCCCCCCCCCCCC	30.42	29978859
266	Phosphorylation	VSARFPYSPSPPMAN HHCCCCCCCCCCCCC	21.09	18669648
268	Phosphorylation	ARFPYSPSPPMANGA CCCCCCCCCCCCCCC	35.38	8975704
282	Phosphorylation	AAREPGGYAAAGSGG CCCCCCCCCCCCCCC	10.05	19702290
287	Phosphorylation	GGYAAAGSGGAGGVS CCCCCCCCCCCCCCC	29.35	28555341
290 (in isoform 2)	Phosphorylation	-	18.32	-
374	Methylation	GAPLPVPRGPSADLL CCCCCCCCCCCHHHH	70.64	-
377	Phosphorylation	LPVPRGPSADLLEDL CCCCCCCCHHHHHHH	36.92	26657352
395	Phosphorylation	RECVNCGSIQTPLWR CCCCCCCCCCCCCEE	17.45	28555341
409	Phosphorylation	RRDGTGHYLCNACGL ECCCCCCHHHHHHHH	17.81	-
429	Sumoylation	GLSRPLIKPQKRVPS CCCCCCCCCCCCCCC	49.42	28112733
436	Phosphorylation	KPQKRVPSSRRLGLS CCCCCCCCHHCCCCC	33.35	22496350
437	Phosphorylation	PQKRVPSSRRLGLSC CCCCCCCHHCCCCCC	18.49	22496350
473	Sumoylation	NACGLYMKLHGVPRP HHHHHHHHHHCCCCC	24.63	28112733
484	Sumoylation	VPRPLAMKKEGIQTR CCCCHHHHHHCCCCC	41.91	-
484	Sumoylation	VPRPLAMKKEGIQTR CCCCHHHHHHCCCCC	41.91	28112733
515	Phosphorylation	SNNSIPMTPTSTSSN CCCCCCCCCCCCCCC	20.33	27251275
523	Phosphorylation	PTSTSSNSDDCSKNT CCCCCCCCCCCCCCC	36.45	-
530	Phosphorylation	SDDCSKNTSPTTQPT CCCCCCCCCCCCCCC	39.56	25159151
531	Phosphorylation	DDCSKNTSPTTQPTA CCCCCCCCCCCCCCC	29.64	25159151
533	Phosphorylation	CSKNTSPTTQPTASG CCCCCCCCCCCCCCC	37.52	26657352
534	Phosphorylation	SKNTSPTTQPTASGA CCCCCCCCCCCCCCC	35.62	21712546
537	Phosphorylation	TSPTTQPTASGAGAP CCCCCCCCCCCCCCC	24.52	23403867
539	Phosphorylation	PTTQPTASGAGAPVM CCCCCCCCCCCCCEE	31.49	23403867
547	Phosphorylation	GAGAPVMTGAGESTN CCCCCEECCCCCCCC	24.90	23403867
552	Phosphorylation	VMTGAGESTNPENSE EECCCCCCCCCCCCC	32.35	23403867
553	Phosphorylation	MTGAGESTNPENSEL ECCCCCCCCCCCCCC	50.95	23403867
558	Phosphorylation	ESTNPENSELKYSGQ CCCCCCCCCCEECCC	42.52	23403867

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
37	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
120	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
266	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
266	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
290	S	Phosphorylation	Kinase	AKT2	P31751	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GATA6_HUMAN !!

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 GATA6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EP300_HUMAN	EP300	physical	10851229
KLF2_HUMAN	KLF2	physical	11375995
SP1_HUMAN	SP1	physical	14988427
SP1_HUMAN	SP1	physical	21076612
IMA4_HUMAN	KPNA3	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
217095	Conotruncal heart malformations (CTHM)
614475	Atrial septal defect 9 (ASD9)
187500	Tetralogy of Fallot (TOF)
614474	Atrioventricular septal defect 5 (AVSD5)
600001	Pancreatic agenesis and congenital heart defects (PACHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GATA6_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-266 AND SER-268, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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 THR-534, AND MASSSPECTROMETRY.	19413330 [Abstract]