GATA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GATA1_HUMAN
• UniProt AC: P15976
• Protein Name: Erythroid transcription factor
• Gene Name: GATA1
• Organism: Homo sapiens (Human).
• Sequence Length: 413
• Subcellular Localization: Nucleus.
• Protein Description: Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS. [PubMed: 24245781]
• Protein Sequence: MEFPGLGSLGTSEPLPQFVDPALVSSTPESGVFFPSGPEGLDAAASSTAPSTATAAAAALAYYRDAEAYRHSPVFQVYPLLNCMEGIPGGSPYAGWAYGKTGLYPASTVCPTREDSPPQAVEDLDGKGSTSFLETLKTERLSPDLLTLGPALPSSLPVPNSAYGGPDFSSTFFSPTGSPLNSAAYSSPKLRGTLPLPPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRLIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLGGTGAAEGPAGGFMVVAGGSGSGNCGEVASGLTLGPPGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTGSFPTGPMPPTTSTTVVAPLSS

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
26	Phosphorylation	VDPALVSSTPESGVF CCHHHCCCCCCCCCC	40.27	20101202
72	Phosphorylation	DAEAYRHSPVFQVYP CHHHHHCCCHHHHHH	17.48	8206977
78	Phosphorylation	HSPVFQVYPLLNCME CCCHHHHHHHHHHHC	4.20	17360941
91	Phosphorylation	MEGIPGGSPYAGWAY HCCCCCCCCCCCCCC	22.20	-
101	Phosphorylation	AGWAYGKTGLYPAST CCCCCCCCCEEECCC	28.23	23186163
104	Phosphorylation	AYGKTGLYPASTVCP CCCCCCEEECCCCCC	9.71	23186163
107	Phosphorylation	KTGLYPASTVCPTRE CCCEEECCCCCCCCC	19.50	23186163
108	Phosphorylation	TGLYPASTVCPTRED CCEEECCCCCCCCCC	28.38	23186163
112	Phosphorylation	PASTVCPTREDSPPQ ECCCCCCCCCCCCCC	41.38	23401153
116	Phosphorylation	VCPTREDSPPQAVED CCCCCCCCCCCCHHH	33.45	23401153
129	Phosphorylation	EDLDGKGSTSFLETL HHCCCCCCHHHHHHH	25.10	25262027
130	Phosphorylation	DLDGKGSTSFLETLK HCCCCCCHHHHHHHH	31.97	23401153
131	Phosphorylation	LDGKGSTSFLETLKT CCCCCCHHHHHHHHH	29.54	23917254
135	Phosphorylation	GSTSFLETLKTERLS CCHHHHHHHHHCCCC	35.38	23186163
137	Sumoylation	TSFLETLKTERLSPD HHHHHHHHHCCCCCC	56.62	16371476
137	Sumoylation	TSFLETLKTERLSPD HHHHHHHHHCCCCCC	56.62	-
142	Phosphorylation	TLKTERLSPDLLTLG HHHHCCCCCCCEECC	23.69	16371476
161	Phosphorylation	SSLPVPNSAYGGPDF CCCCCCCCCCCCCCC	19.46	-
178	Phosphorylation	TFFSPTGSPLNSAAY CCCCCCCCCCCCCHH	28.79	20101202
187	Phosphorylation	LNSAAYSSPKLRGTL CCCCHHCCCCCCCCC	17.24	8206977
223	Phosphorylation	RRDRTGHYLCNACGL CCCCCCCHHHHHHHH	17.81	17360941
231	Phosphorylation	LCNACGLYHKMNGQN HHHHHHHHHHHCCCC	5.67	17360941
233	Acetylation	NACGLYHKMNGQNRP HHHHHHHHHCCCCCC	22.09	9859997
245	Acetylation	NRPLIRPKKRLIVSK CCCCCCCCCEEEEEC	40.45	9859997
246	Acetylation	RPLIRPKKRLIVSKR CCCCCCCCEEEEECC	55.94	9859997
251	Phosphorylation	PKKRLIVSKRAGTQC CCCEEEEECCCCCCC	14.94	26434776
252	Acetylation	KKRLIVSKRAGTQCT CCEEEEECCCCCCCC	35.06	-
256	Phosphorylation	IVSKRAGTQCTNCQT EEECCCCCCCCCCCC	21.34	26552605
259	Phosphorylation	KRAGTQCTNCQTTTT CCCCCCCCCCCCCCC	29.25	26552605
263	Phosphorylation	TQCTNCQTTTTTLWR CCCCCCCCCCCCCCC	28.45	26552605
264	Phosphorylation	QCTNCQTTTTTLWRR CCCCCCCCCCCCCCC	9.03	26552605
265	Phosphorylation	CTNCQTTTTTLWRRN CCCCCCCCCCCCCCC	22.59	26552605
266	Phosphorylation	TNCQTTTTTLWRRNA CCCCCCCCCCCCCCC	20.14	26552605
267	Phosphorylation	NCQTTTTTLWRRNAS CCCCCCCCCCCCCCC	23.41	26552605
285	Phosphorylation	VCNACGLYYKLHQVN CHHHHHHHHHHHHCC	5.48	17360941
286	Phosphorylation	CNACGLYYKLHQVNR HHHHHHHHHHHHCCC	16.47	-
304	Phosphorylation	MRKDGIQTRNRKASG ECCCCCCCCCCCCCC	28.17	-
308	Acetylation	GIQTRNRKASGKGKK CCCCCCCCCCCCCCC	50.91	-
310	Phosphorylation	QTRNRKASGKGKKKR CCCCCCCCCCCCCCC	44.03	16107690
312	Acetylation	RNRKASGKGKKKRGS CCCCCCCCCCCCCCC	66.13	60831
314	Acetylation	RKASGKGKKKRGSSL CCCCCCCCCCCCCCC	59.62	61375
315	Acetylation	KASGKGKKKRGSSLG CCCCCCCCCCCCCCC	57.27	89149
316	Acetylation	ASGKGKKKRGSSLGG CCCCCCCCCCCCCCC	66.53	89155
319	Phosphorylation	KGKKKRGSSLGGTGA CCCCCCCCCCCCCCC	26.82	-
320	Phosphorylation	GKKKRGSSLGGTGAA CCCCCCCCCCCCCCC	33.58	-
324	Phosphorylation	RGSSLGGTGAAEGPA CCCCCCCCCCCCCCC	23.11	-

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
26	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
26	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
161	S	Phosphorylation	Kinase	PAK5	Q9P286	PSP
170	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
170	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
174	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
174	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
176	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
176	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
187	S	Phosphorylation	Kinase	PAK5	Q9P286	PSP
310	S	Phosphorylation	Kinase	AKT1	P31749	PSP
310	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
310	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
137	K	Phosphorylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	16371476
137	K	Phosphorylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	16371476
137	K	Sumoylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	16371476
137	K	Sumoylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	16371476
142	S	Phosphorylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	16371476
142	S	Phosphorylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	16371476
142	S	Sumoylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	16371476
142	S	Sumoylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	16371476
233	K	Acetylation	Acetylated on Lys-233, Lys-245 Lys-246 by EP300.	9859997
245	K	Acetylation	Acetylated on Lys-233, Lys-245 Lys-246 by EP300.	9859997
246	K	Acetylation	Acetylated on Lys-233, Lys-245 Lys-246 by EP300.	9859997
310	S	Phosphorylation	Phosphorylation on Ser-310 is enhanced on erythroid differentiation.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GATA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FOG2_HUMAN	ZFPM2	physical	10438528
HDAC1_HUMAN	HDAC1	physical	14668799
HDAC3_HUMAN	HDAC3	physical	14668799
HDAC4_HUMAN	HDAC4	physical	14668799
HDAC5_HUMAN	HDAC5	physical	14668799
FLI1_HUMAN	FLI1	physical	12724402
ARI1A_HUMAN	ARID1A	physical	11018012
SMCA4_HUMAN	SMARCA4	physical	11018012
SMRC2_HUMAN	SMARCC2	physical	11018012
SMRC1_HUMAN	SMARCC1	physical	11018012
SMRD1_HUMAN	SMARCD1	physical	11018012
SMCE1_HUMAN	SMARCE1	physical	11018012
SNF5_HUMAN	SMARCB1	physical	11018012
ZBT16_HUMAN	ZBTB16	physical	12242665
RBTN2_HUMAN	LMO2	physical	7568177
FLI1_HUMAN	FLI1	physical	12556498
MED14_HUMAN	MED14	physical	17132730
MED17_HUMAN	MED17	physical	17132730
MED1_HUMAN	MED1	physical	17132730
FOG1_HUMAN	ZFPM1	physical	19513100
TAF7_HUMAN	TAF7	physical	20211142
TRI25_HUMAN	TRIM25	physical	20211142
ZBT22_HUMAN	ZBTB22	physical	20211142
RAI1_HUMAN	RAI1	physical	20211142
TRI29_HUMAN	TRIM29	physical	20211142
ZZZ3_HUMAN	ZZZ3	physical	20211142
TX1B3_HUMAN	TAX1BP3	physical	20211142
SKI_HUMAN	SKI	physical	15542823
HSPB1_HUMAN	HSPB1	physical	20410505
CEBPE_HUMAN	CEBPE	physical	12202480
SPI1_HUMAN	SPI1	physical	12202480
SRA1_HUMAN	SRA1	physical	20398657
HSP74_HUMAN	HSPA4	physical	17167422
SPIB_HUMAN	SPIB	physical	10364157
FLI1_HUMAN	FLI1	physical	10364157
AAPK1_HUMAN	PRKAA1	physical	21988832
HXA1_HUMAN	HOXA1	physical	25416956
AAKB2_HUMAN	PRKAB2	physical	25416956
FRS3_HUMAN	FRS3	physical	25416956
RADIL_HUMAN	RADIL	physical	25416956
KRA92_HUMAN	KRTAP9-2	physical	25416956
FBF1_HUMAN	FBF1	physical	25416956
HEXI2_HUMAN	HEXIM2	physical	25416956
CCD24_HUMAN	CCDC24	physical	25416956
DHX36_HUMAN	DHX36	physical	26186194
TRIP6_HUMAN	TRIP6	physical	26186194
HEMGN_HUMAN	HEMGN	physical	24740910
EP300_HUMAN	EP300	physical	24740910
PML_HUMAN	PML	physical	24255919
TRIP6_HUMAN	TRIP6	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 300367: X-linked dyserythropoietic anemia and thrombocytopenia (XDAT)
• 314050: Thrombocytopenia with beta-thalassemia, X-linked (XLTT)
• 300835: Anemia without thrombocytopenia, X-linked (XLAWT)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.;
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
Cited for: SUMOYLATION AT LYS-137, PHOSPHORYLATION AT SER-142, AND MUTAGENESIS OFLYS-137 AND SER-142.
PubMed: 16371476

Sumoylation

"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.;
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
Cited for: SUMOYLATION AT LYS-137, PHOSPHORYLATION AT SER-142, AND MUTAGENESIS OFLYS-137 AND SER-142.
PubMed: 16371476