P17679 (GATA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Erythroid transcription factor

Alternative name(s):
Eryf1
GATA-binding factor 1
Short name=GATA-1
Short name=GF-1
NF-E1 DNA-binding protein

Gene names

Name:	Gata1
Synonyms:	Gf-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells. Ref.8 Ref.9 Ref.10 Ref.13 Ref.16
Subunit structure	May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1 By similarity. Interacts with GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner. Interacts with LMCD1. Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo. Interacts with BRD3. Ref.7 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18
Subcellular location	Nucleus Ref.16.
Tissue specificity	Erythrocytes. Expressed (at protein level) in liver. Ref.1 Ref.10
Developmental stage	Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo. Ref.10
Domain	The two fingers are functionally distinct and cooperate to achieve specific, stable DNA binding. The first finger is necessary only for full specificity and stability of binding, whereas the second one is required for binding.
Post-translational modification	Highly phosphorylated on serine residues. Phosphorylation on Ser-310 is enhanced on erythroid differentiation. Phosphorylation on Ser-142 promotes sumoylation on Lys-137 By similarity. Ref.9 Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on transcriptional activity. Ref.13 Acetylated on Lys-233, Lys-245 Lys-246 by EP300 By similarity. Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro. Acetylation does not affect DNA-binding in vitro but is essential to induce erythroid differentiation and for binding chromatin in vivo.
Sequence similarities	Contains 2 GATA-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative initiation
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	basophil differentiation Inferred from electronic annotation. Source: Compara cell-cell signaling Inferred from mutant phenotype PubMed 15005853. Source: MGI cellular response to thyroid hormone stimulus Inferred from electronic annotation. Source: Compara dendritic cell differentiation Inferred from direct assay PubMed 17505015. Source: MGI embryonic hemopoiesis Inferred from mutant phenotype PubMed 9576834. Source: MGI eosinophil fate commitment Inferred from electronic annotation. Source: Compara erythrocyte development Inferred from electronic annotation. Source: Compara erythrocyte differentiation Inferred from direct assay PubMed 9427697. Source: MGI in utero embryonic development Inferred from mutant phenotype PubMed 9576834. Source: MGI male gonad development Inferred from electronic annotation. Source: Compara megakaryocyte differentiation Inferred from direct assay PubMed 9427697. Source: MGI negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of bone mineralization Inferred from mutant phenotype PubMed 15005853. Source: MGI negative regulation of cell proliferation Inferred from mutant phenotype PubMed 9233806. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 17505015. Source: MGI negative regulation of transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara platelet aggregation Inferred from mutant phenotype PubMed 15701726. Source: BHF-UCL platelet formation Inferred from electronic annotation. Source: Compara positive regulation of erythrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of osteoblast proliferation Inferred from mutant phenotype PubMed 15005853. Source: MGI positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype PubMed 15701726. Source: BHF-UCL regulation of definitive erythrocyte differentiation Inferred from direct assay PubMed 12200364. Source: BHF-UCL regulation of glycoprotein biosynthetic process Inferred from mutant phenotype PubMed 15701726. Source: BHF-UCL transcriptional activation by promoter-enhancer looping Inferred from direct assay PubMed 15644435. Source: BHF-UCL
Cellular_component	nuclear membrane Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 15613485PubMed 17505015PubMed 7924983Ref.10PubMed 9787185. Source: MGI transcription factor complex Inferred from electronic annotation. Source: Compara transcriptional repressor complex Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding, bending Inferred from direct assay PubMed 21436399. Source: MGI RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 7896801. Source: MGI RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from electronic annotation. Source: Compara RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 19398553PubMed 8195185PubMed 9230307PubMed 9427697. Source: MGI chromatin binding Inferred from direct assay PubMed 17505015PubMed 19011221. Source: MGI enhancer sequence-specific DNA binding Inferred from direct assay PubMed 20855530. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay PubMed 8195185Ref.10PubMed 9787185. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Lmo2	P25801	5	EBI-3903251,EBI-3903256

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P17679-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P17679-2)

Also known as: GATA-1s;

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Note: Produced by alternative initiation at Met-84 of isoform 1. Less effective than isoform 1 in its ability to transactivate target genes.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 413

413

Erythroid transcription factor

PRO_0000083398

Regions

Zinc finger

204 – 228

25

GATA-type 1

Zinc finger

258 – 282

25

GATA-type 2

Region

203 – 222

20

Required for interaction with ZFPM1 By similarity

Amino acid modifications

Modified residue

26

1

Phosphoserine Ref.9

Modified residue

49

1

Phosphoserine Ref.9

Modified residue

72

1

Phosphoserine Ref.9

Modified residue

142

1

Phosphoserine Ref.9

Modified residue

178

1

Phosphoserine Ref.9

Modified residue

187

1

Phosphoserine

Modified residue

233

1

N6-acetyllysine; by EP300 By similarity

Modified residue

245

1

N6-acetyllysine; by EP300 By similarity

Modified residue

246

1

N6-acetyllysine; by CREBBP Ref.12

Modified residue

246

1

N6-acetyllysine; by EP300 By similarity

Modified residue

252

1

N6-acetyllysine; by CREBBP Ref.12

Modified residue

308

1

N6-acetyllysine Ref.7

Modified residue

310

1

Phosphoserine Ref.9

Modified residue

312

1

N6-acetyllysine; by CREBBP Ref.7 Ref.12

Modified residue

314

1

N6-acetyllysine Ref.7

Modified residue

315

1

N6-acetyllysine Ref.7

Cross-link

137

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence

1 – 83

83

Missing in isoform 2.

VSP_041452

Experimental info

Mutagenesis

26

1

S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9

Mutagenesis

49

1

S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9

Mutagenesis

72

1

S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9

Mutagenesis

137

1

K → R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. Ref.13

Mutagenesis

142

1

S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9

Mutagenesis

178

1

S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9

Mutagenesis

187

1

S → A: Loss of phosphorylation of the chymotryptic peptide.

Mutagenesis

203

1

E → V: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11

Mutagenesis

204

1

C → R: Disrupts interaction with ZFPM1 and binding to DNA. Ref.11

Mutagenesis

205

1

V → G: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11

Mutagenesis

205

1

V → M: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11

Mutagenesis

207

1

C → G, R or W: Disrupts interaction with ZFPM1. Ref.8 Ref.11

Mutagenesis

207

1

C → P: Stability of binding to DNA reduced. Ref.8 Ref.11

Mutagenesis

208

1

G → E or V: Disrupts interaction with ZFPM1 and binding to DNA. Ref.11

Mutagenesis

218

1

D → G or V: No effect on interaction with ZFPM1. Ref.11

Mutagenesis

222

1

H → R: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11

Mutagenesis

224

1

L → P: Disrupts interaction with ZFPM1 and binding to DNA. Ref.11

Mutagenesis

225

1

C → R, S or Y: Disrupts interaction with ZFPM1. Ref.11

Mutagenesis

228

1

C → R or S: Disrupts interaction with ZFPM1. Ref.11

Mutagenesis

230

1

L → F: Stability of binding to DNA reduced. Ref.8

Mutagenesis

233

1

K → E: No effect on interaction with ZFPM1. Ref.11

Mutagenesis

245 – 246

2

KK → AA: No effect on DNA binding. Reduces acetylation. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 312-A--A-316. Abrogates ability to induce erythroid differentiation; when associated with 312-A--A-316. Reduces binding to CREBBP; when associated with 312-A--A-316. Disrupts stable association with chromatin; when associated with 312-A--A-316.

Mutagenesis

245 – 246

2

KK → RR: No effect on DNA binding.

Mutagenesis

261

1

C → P: Abolishes DNA-binding. Ref.8

Mutagenesis

284

1

L → F: Binds to DNA with reduced affinity. Ref.8

Mutagenesis

310

1

S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9

Mutagenesis

312 – 316

5

KGKKK → AGAAA: No effect on DNA binding. Reduces acetylation. Reduces binding to CREBBP. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 245-A-A-246. Abrogates ability to induce erythroid differentiation; when associated with 245-A-A-246. Reduces binding to CREBBP; when associated with 245-A-A-246. Disrupts stable association with chromatin; when associated with 245-A-A-246. Ref.12 Ref.16

Mutagenesis

312 – 316

5

KGKKK → RGRRR: No effect on DNA binding. Ref.12 Ref.16

Sequence conflict

29

1

D → G in AAH52653. Ref.5

Sequence conflict

129

1

N → S in AAH52653. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

413

Helix Strand Turn

Details...

Turn

205 – 207

3

Helix

226 – 235

10

Turn

259 – 261

3

Helix

280 – 289

10

Helix

295 – 297

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: BB627A92700D557A	FASTA	413	42,674
	10 20 30 40 50 60 MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP NAATAAASAL 70 80 90 100 110 120 AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK TALYPASTVC PSHEDAPSQA 130 140 150 160 170 180 LEDQEGKSNN TFLDTLKTER LSPDLLTLGT ALPASLPVTG SAYGGADFPS PFFSPTGSPL 190 200 210 220 230 240 SSAAYSSPKF HGSLPLAPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP 250 260 270 280 290 300 LIRPKKRMIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD 310 320 330 340 350 360 GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA SGLALGTAGT 370 380 390 400 410 AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP TTSSTSVIAP LSS
	Isoform 2 (GATA-1s) [UniParc]. Checksum: 8BF1F251EB8E47A1	FASTA	330	34,188
	10 20 30 40 50 60 MEGIPGGSPY ASWAYGKTAL YPASTVCPSH EDAPSQALED QEGKSNNTFL DTLKTERLSP 70 80 90 100 110 120 DLLTLGTALP ASLPVTGSAY GGADFPSPFF SPTGSPLSSA AYSSPKFHGS LPLAPCEARE 130 140 150 160 170 180 CVNCGATATP LWRRDRTGHY LCNACGLYHK MNGQNRPLIR PKKRMIVSKR AGTQCTNCQT 190 200 210 220 230 240 TTTTLWRRNA SGDPVCNACG LYFKLHQVNR PLTMRKDGIQ TRNRKASGKG KKKRGSNLAG 250 260 270 280 290 300 AGAAEGPAGG FMVVAGSSSS GNCGEVASGL ALGTAGTAHL YQGLGPVVLS GPVSHLMPFP 310 320 330 GPLLGSPTTS FPTGPAPTTS STSVIAPLSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNA for the major DNA-binding protein of the erythroid lineage through expression in mammalian cells." Tsai S.-F., Martin D.I.K., Zon L.I., D'Andrea A.D., Wong G.W., Orkin S.H. Nature 339:446-451(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY. Tissue: Erythrocyte.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Liver.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6NCr. Tissue: Hematopoietic stem cell.
[6]	Todokoro K., Chiba T., Kuramochi S., Ikawa Y. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73. Strain: BALB/c.
[7]	"Bromodomain protein Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes." Lamonica J.M., Deng W., Kadauke S., Campbell A.E., Gamsjaeger R., Wang H., Cheng Y., Billin A.N., Hardison R.C., Mackay J.P., Blobel G.A. Proc. Natl. Acad. Sci. U.S.A. 108:E159-E168(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH BRD3, ACETYLATION AT LYS-308; LYS-312; LYS-314 AND LYS-315, MASS SPECTROMETRY.
[8]	"Transcriptional activation and DNA binding by the erythroid factor GF-1/NF-E1/Eryf 1." Martin D.I.K., Orkin S.H. Genes Dev. 4:1886-1898(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ZINC FINGERS, MUTAGENESIS OF CYS-207; LEU-230; CYS-261 AND LEU-284.
[9]	"Phosphorylation of the erythroid transcription factor GATA-1." Crossley M., Orkin S.H. J. Biol. Chem. 269:16589-16596(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-26; SER-49; SER-72; SER-142; SER-178 AND SER-310, FUNCTION, MUTAGENESIS OF SER-26; SER-49; SER-72; SER-142; SER-178 AND SER-310.
[10]	"Alternative translation initiation site usage results in two functionally distinct forms of the GATA-1 transcription factor." Calligaris R., Bottardi S., Cogoi S., Apezteguia I., Santoro C. Proc. Natl. Acad. Sci. U.S.A. 92:11598-11602(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE INITIATION (ISOFORM 2), FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[11]	"Use of altered specificity mutants to probe a specific protein-protein interaction in differentiation: the GATA-1:FOG complex." Crispino J.D., Lodish M.B., MacKay J.P., Orkin S.H. Mol. Cell 3:219-228(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLU-203; CYS-204; VAL-205; CYS-207; GLY-208; ASP-218; HIS-222; LEU-224; CYS-225; CYS-228 AND LYS-233.
[12]	"CREB-Binding protein acetylates hematopoietic transcription factor GATA-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) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CREBBP, ACETYLATION AT LYS-246; LYS-252 AND LYS-312, MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316.
[13]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-137, INTERACTION WITH PIAS4, FUNCTION, MUTAGENESIS OF LYS-137.
[14]	"GATA-1 forms distinct activating and repressive complexes in erythroid cells." Rodriguez P., Bonte E., Krijgsveld J., Kolodziej K.E., Guyot B., Heck A.J.R., Vyas P., de Boer E., Grosveld F., Strouboulis J. EMBO J. 24:2354-2366(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GFI1B.
[15]	"LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6 function by inhibiting DNA binding." Rath N., Wang Z., Lu M.M., Morrisey E.E. Mol. Cell. Biol. 25:8864-8873(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LMCD1.
[16]	"Acetylation of GATA-1 is required for chromatin occupancy." Lamonica J.M., Vakoc C.R., Blobel G.A. Blood 108:3736-3738(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316.
[17]	"The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG." Kowalski K., Czolij R., King G.F., Crossley M., Mackay J.P. J. Biomol. NMR 13:249-262(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 200-243.
[18]	"Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3." Gamsjaeger R., Webb S.R., Lamonica J.M., Billin A., Blobel G.A., Mackay J.P. Mol. Cell. Biol. 31:2632-2640(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 308-320 IN COMPLEX WITH BRD3, INTERACTION WITH BRD3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15763 mRNA. Translation: CAA33769.1.
AK146915 mRNA. Translation: BAE27527.1.
AL670169 Genomic DNA. Translation: CAM17247.1.
CH466638 Genomic DNA. Translation: EDL33938.1.
X57530 Genomic DNA. Translation: CAA40751.1.
BC052653 mRNA. Translation: AAH52653.1.

IPI

IPI00111277.
IPI01019208.

PIR

S04655.

RefSeq

NP_032115.1. NM_008089.2.

UniGene

Mm.335973.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GNF	NMR	-	A	200-243	[»]
1Y0J	NMR	-	A	200-243	[»]
2L5E	NMR	-	B	308-320	[»]
2L6Y	NMR	-	A	200-238	[»]
2L6Z	NMR	-	A	200-238	[»]
3VD6	X-ray	1.98	C	200-318	[»]
3VEK	X-ray	2.63	C/F	200-318	[»]

ProteinModelPortal

P17679.

SMR

P17679. Positions 200-310.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40883N.

IntAct

P17679. 4 interactions.

MINT

MINT-94735.

STRING

10090.ENSMUSP00000033502.

PTM databases

PhosphoSite

P17679.

Proteomic databases

PRIDE

P17679.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162.

GeneID

14460.

KEGG

mmu:14460.

Organism-specific databases

CTD

2623.

MGI

MGI:95661. Gata1.

Phylogenomic databases

eggNOG

COG5641.

GeneTree

ENSGT00550000074470.

HOGENOM

HOG000047701.

HOVERGEN

HBG051705.

InParanoid

P17679.

KO

K09182.

OrthoDB

EOG4QNMWM.

Gene expression databases

ArrayExpress

P17679.

Bgee

P17679.

CleanEx

MM_GATA1.

Genevestigator

P17679.

GermOnline

ENSMUSG00000031162. Mus musculus.

Family and domain databases

Gene3D

3.30.50.10. 2 hits.

InterPro

IPR016374. TF_GATA-1/2/3.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Pfam

PF00320. GATA. 2 hits.
[Graphical view]

PIRSF

PIRSF003027. TF_GATA-1/2/3. 1 hit.

PRINTS

PR00619. GATAZNFINGER.

SMART

SM00401. ZnF_GATA. 2 hits.
[Graphical view]

PROSITE

PS00344. GATA_ZN_FINGER_1. 2 hits.
PS50114. GATA_ZN_FINGER_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P17679.

NextBio

286092.

SOURCE

Search...

Entry information

Entry name

GATA1_MOUSE

Accession

Primary (citable) accession number: P17679
Secondary accession number(s): Q3UIH9, Q7TMX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program