GATA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GATA1_MOUSE
• UniProt AC: P17679
• Protein Name: Erythroid transcription factor
• Gene Name: Gata1
• Organism: Mus musculus (Mouse).
• 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 (By similarity)..
• Protein Sequence: MDFPGLGALGTSEPLPQFVDSALVSSPSDSTGFFSSGPEGLDAASSSTSPNAATAAASALAYYREAEAYRHSPVFQVYPLLNSMEGIPGGSPYASWAYGKTALYPASTVCPSHEDAPSQALEDQEGKSNNTFLDTLKTERLSPDLLTLGTALPASLPVTGSAYGGADFPSPFFSPTGSPLSSAAYSSPKFHGSLPLAPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSNLAGAGAAEGPAGGFMVVAGSSSSGNCGEVASGLALGTAGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTTSFPTGPAPTTSSTSVIAPLSS

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	VDSALVSSPSDSTGF HHHHHCCCCCCCCCC	22.42	22817900
49	Phosphorylation	DAASSSTSPNAATAA CCCCCCCCHHHHHHH	20.36	22817900
69	Phosphorylation	YYREAEAYRHSPVFQ HHHHHHHHHCCCHHH	10.60	26643407
72	Phosphorylation	EAEAYRHSPVFQVYP HHHHHHCCCHHHHHH	17.48	26643407
78	Phosphorylation	HSPVFQVYPLLNSME CCCHHHHHHHHHCCC	4.20	26643407
131	Phosphorylation	QEGKSNNTFLDTLKT CCCCCCCCHHHHHHH	29.80	22817900
137	Sumoylation	NTFLDTLKTERLSPD CCHHHHHHHHCCCCC	50.89	15173587
137	Sumoylation	NTFLDTLKTERLSPD CCHHHHHHHHCCCCC	50.89	-
138	Phosphorylation	TFLDTLKTERLSPDL CHHHHHHHHCCCCCH	29.47	21189417
142	Phosphorylation	TLKTERLSPDLLTLG HHHHHCCCCCHHHHC	23.69	22817900
163	Phosphorylation	LPVTGSAYGGADFPS CCCCCCCCCCCCCCC	20.14	21189417
178	Phosphorylation	PFFSPTGSPLSSAAY CCCCCCCCCCCCHHH	25.75	22817900
187	Phosphorylation	LSSAAYSSPKFHGSL CCCHHHCCCCCCCCC	21.31	22817900
233	Acetylation	NACGLYHKMNGQNRP HHHHHHHHHCCCCCC	22.09	-
245	Acetylation	NRPLIRPKKRMIVSK CCCCCCCCCCEEEEC	43.07	10207073
246	Acetylation	RPLIRPKKRMIVSKR CCCCCCCCCEEEECC	50.29	10207073
252	Acetylation	KKRMIVSKRAGTQCT CCCEEEECCCCCCCC	35.06	10207073
287	Acetylation	NACGLYFKLHQVNRP HHHHHEEEEEECCCC	31.35	10207073
299	Acetylation	NRPLTMRKDGIQTRN CCCCEECCCCCCCCC	49.86	10207073
308	Acetylation	GIQTRNRKASGKGKK CCCCCCCCCCCCCCC	50.91	21536911
310	Phosphorylation	QTRNRKASGKGKKKR CCCCCCCCCCCCCCC	44.03	16204311
312	Acetylation	RNRKASGKGKKKRGS CCCCCCCCCCCCCCC	66.13	10207073
314	Acetylation	RKASGKGKKKRGSNL CCCCCCCCCCCCCCC	59.62	21536911
315	Acetylation	KASGKGKKKRGSNLA CCCCCCCCCCCCCCC	57.27	21536911
316	Acetylation	ASGKGKKKRGSNLAG CCCCCCCCCCCCCCC	66.53	10207073

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	P63085	GPS
26	S	Phosphorylation	Kinase	ERK1	P27361	PSP
26	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
178	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
310	S	Phosphorylation	Kinase	AKT1	P31749	PSP
310	S	Phosphorylation	Kinase	AKT1	P31750	PSP
310	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS

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).	15173587
137	K	Phosphorylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	15173587
137	K	Sumoylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	15173587
137	K	Sumoylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	15173587
142	S	Phosphorylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	8206977
142	S	Phosphorylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	8206977
142	S	Sumoylation	Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).	8206977
142	S	Sumoylation	Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4.	8206977
233	K	Acetylation	Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity).	10078204
245	K	Acetylation	Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity).	10207073
246	K	Acetylation	Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity).	10207073
246	K	Acetylation	Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro.	10207073
252	K	Acetylation	Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro.	10207073
310	S	Phosphorylation	Phosphorylation on Ser-310 is enhanced on erythroid differentiation.	8206977
312	K	Acetylation	Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro.	21536911

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CREB1_MOUSE	Creb1	physical	17226765
SPI1_MOUSE	Spi1	physical	20211142
FOG1_MOUSE	Zfpm1	physical	15920471
LDB1_MOUSE	Ldb1	physical	15920471
TAL1_MOUSE	Tal1	physical	15920471
GFI1B_MOUSE	Gfi1b	physical	15920471
CHD4_MOUSE	Chd4	physical	15920471
MTA2_MOUSE	Mta2	physical	15920471
HDAC1_MOUSE	Hdac1	physical	15920471
HDAC2_MOUSE	Hdac2	physical	15920471
RBBP7_MOUSE	Rbbp7	physical	15920471
RBBP4_MOUSE	Rbbp4	physical	15920471
MBD2_MOUSE	Mbd2	physical	15920471
MBD3_MOUSE	Mbd3	physical	15920471
SMCA5_MOUSE	Smarca5	physical	15920471
PIAS4_HUMAN	PIAS4	physical	15173587

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"CREB-Binding protein acetylates hematopoietic transcription factorGATA-1 at functionally important sites.";
Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.;
Mol. Cell. Biol. 19:3496-3505(1999).
Cited for: INTERACTION WITH CREBBP, ACETYLATION AT LYS-246; LYS-252 AND LYS-312,AND MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316.
PubMed: 10207073

Phosphorylation

"Phosphorylation of the erythroid transcription factor GATA-1.";
Crossley M., Orkin S.H.;
J. Biol. Chem. 269:16589-16596(1994).
Cited for: PHOSPHORYLATION AT SER-26; SER-49; SER-72; SER-142; SER-178 ANDSER-310, FUNCTION, AND MUTAGENESIS OF SER-26; SER-49; SER-72; SER-142;SER-178 AND SER-310.
PubMed: 8206977

Sumoylation

"Modification of the erythroid transcription factor GATA-1 by SUMO-1.";
Collavin L., Gostissa M., Avolio F., Secco P., Ronchi A., Santoro C.,Del Sal G.;
Proc. Natl. Acad. Sci. U.S.A. 101:8870-8875(2004).
Cited for: SUMOYLATION AT LYS-137, INTERACTION WITH PIAS4, FUNCTION, ANDMUTAGENESIS OF LYS-137.
PubMed: 15173587