GATA2_HUMAN
ID GATA2_HUMAN Reviewed; 480 AA.
AC P23769; D3DNB3; Q53YE0; Q96BH0; Q96BH8; Q9BUJ6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Endothelial transcription factor GATA-2;
DE AltName: Full=GATA-binding protein 2;
GN Name=GATA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1714909; DOI=10.1016/s0021-9258(18)98533-9;
RA Lee M.-E., Temizer D.T., Clifford J.A., Quertermous T.;
RT "Cloning of the GATA-binding protein that regulates endothelin-1 gene
RT expression in endothelial cells.";
RL J. Biol. Chem. 266:16188-16192(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Endothelial cell;
RX PubMed=1370462; DOI=10.1016/s0021-9258(18)48426-8;
RA Dorfman D.M., Wilson D.B., Bruns G.A.P., Orkin S.H.;
RT "Human transcription factor GATA-2. Evidence for regulation of
RT preproendothelin-1 gene expression in endothelial cells.";
RL J. Biol. Chem. 267:1279-1285(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-164.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-164.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-164.
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-192, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INTERACTION WITH AR AND CCAR1.
RX PubMed=23887938; DOI=10.1093/nar/gkt644;
RA Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E., Kwon G.Y.,
RA Lee H.M., Kim J.H.;
RT "CCAR1 promotes chromatin loading of androgen receptor (AR) transcription
RT complex by stabilizing the association between AR and GATA2.";
RL Nucleic Acids Res. 41:8526-8536(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-86, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-389, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP VARIANTS IMD21 LEU-254; MET-354 AND TRP-398.
RX PubMed=21670465; DOI=10.1182/blood-2011-05-356352;
RA Hsu A.P., Sampaio E.P., Khan J., Calvo K.R., Lemieux J.E., Patel S.Y.,
RA Frucht D.M., Vinh D.C., Auth R.D., Freeman A.F., Olivier K.N., Uzel G.,
RA Zerbe C.S., Spalding C., Pittaluga S., Raffeld M., Kuhns D.B., Ding L.,
RA Paulson M.L., Marciano B.E., Gea-Banacloche J.C., Orange J.S.,
RA Cuellar-Rodriguez J., Hickstein D.D., Holland S.M.;
RT "Mutations in GATA2 are associated with the autosomal dominant and sporadic
RT monocytopenia and mycobacterial infection (MonoMAC) syndrome.";
RL Blood 118:2653-2655(2011).
RN [13]
RP VARIANTS LMPM PRO-361 AND ARG-373.
RX PubMed=21892158; DOI=10.1038/ng.923;
RA Ostergaard P., Simpson M.A., Connell F.C., Steward C.G., Brice G.,
RA Woollard W.J., Dafou D., Kilo T., Smithson S., Lunt P., Murday V.A.,
RA Hodgson S., Keenan R., Pilz D.T., Martinez-Corral I., Makinen T.,
RA Mortimer P.S., Jeffery S., Trembath R.C., Mansour S.;
RT "Mutations in GATA2 cause primary lymphedema associated with a
RT predisposition to acute myeloid leukemia (Emberger syndrome).";
RL Nat. Genet. 43:929-931(2011).
RN [14]
RP VARIANTS MDS MET-354 AND THR-355 DEL.
RX PubMed=21892162; DOI=10.1038/ng.913;
RA Hahn C.N., Chong C.E., Carmichael C.L., Wilkins E.J., Brautigan P.J.,
RA Li X.C., Babic M., Lin M., Carmagnac A., Lee Y.K., Kok C.H., Gagliardi L.,
RA Friend K.L., Ekert P.G., Butcher C.M., Brown A.L., Lewis I.D., To L.B.,
RA Timms A.E., Storek J., Moore S., Altree M., Escher R., Bardy P.G.,
RA Suthers G.K., D'Andrea R.J., Horwitz M.S., Scott H.S.;
RT "Heritable GATA2 mutations associated with familial myelodysplastic
RT syndrome and acute myeloid leukemia.";
RL Nat. Genet. 43:1012-1017(2011).
CC -!- FUNCTION: Transcriptional activator which regulates endothelin-1 gene
CC expression in endothelial cells. Binds to the consensus sequence 5'-
CC AGATAG-3'.
CC -!- SUBUNIT: Interacts with BRD3 (By similarity). Interacts with AR and
CC CCAR1. {ECO:0000250|UniProtKB:O09100, ECO:0000269|PubMed:23887938}.
CC -!- INTERACTION:
CC P23769; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2806671, EBI-10173507;
CC P23769; Q92793: CREBBP; NbExp=2; IntAct=EBI-2806671, EBI-81215;
CC P23769; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2806671, EBI-3867333;
CC P23769; Q13643: FHL3; NbExp=5; IntAct=EBI-2806671, EBI-741101;
CC P23769; Q08379: GOLGA2; NbExp=4; IntAct=EBI-2806671, EBI-618309;
CC P23769; Q6A162: KRT40; NbExp=3; IntAct=EBI-2806671, EBI-10171697;
CC P23769; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-2806671, EBI-10172052;
CC P23769; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-2806671, EBI-1052037;
CC P23769; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-2806671, EBI-10241252;
CC P23769; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-2806671, EBI-18395721;
CC P23769; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-2806671, EBI-9996449;
CC P23769; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-2806671, EBI-18394498;
CC P23769; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-2806671, EBI-10261141;
CC P23769; Q99750: MDFI; NbExp=4; IntAct=EBI-2806671, EBI-724076;
CC P23769; P35548: MSX2; NbExp=3; IntAct=EBI-2806671, EBI-6447480;
CC P23769; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-2806671, EBI-945833;
CC P23769; P86479: PRR20C; NbExp=3; IntAct=EBI-2806671, EBI-10172814;
CC P23769; P25788: PSMA3; NbExp=4; IntAct=EBI-2806671, EBI-348380;
CC P23769; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-2806671, EBI-740343;
CC P23769; Q13485: SMAD4; NbExp=5; IntAct=EBI-2806671, EBI-347263;
CC P23769; P17947: SPI1; NbExp=4; IntAct=EBI-2806671, EBI-2293548;
CC P23769; Q13077: TRAF1; NbExp=3; IntAct=EBI-2806671, EBI-359224;
CC P23769; P36406: TRIM23; NbExp=4; IntAct=EBI-2806671, EBI-740098;
CC P23769; P25801: Lmo2; Xeno; NbExp=3; IntAct=EBI-2806671, EBI-3903256;
CC P23769-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-21856389, EBI-25837549;
CC P23769-2; P22607: FGFR3; NbExp=3; IntAct=EBI-21856389, EBI-348399;
CC P23769-2; P28799: GRN; NbExp=3; IntAct=EBI-21856389, EBI-747754;
CC P23769-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-21856389, EBI-396669;
CC P23769-2; O76024: WFS1; NbExp=3; IntAct=EBI-21856389, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23769-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23769-2; Sequence=VSP_041126;
CC -!- TISSUE SPECIFICITY: Endothelial cells.
CC -!- DISEASE: Immunodeficiency 21 (IMD21) [MIM:614172]: An immunodeficiency
CC disease characterized by profoundly decreased or absent monocytes, B-
CC lymphocytes, natural killer lymphocytes, and circulating and tissue
CC dendritic cells, with little or no effect on T-cell numbers. Clinical
CC features of DCML include susceptibility to disseminated non-tuberculous
CC mycobacterial infections, papillomavirus infections, opportunistic
CC fungal infections, and pulmonary alveolar proteinosis. Bone marrow
CC hypocellularity and dysplasia of myeloid, erythroid, and megakaryocytic
CC lineages are present in most patients, as are karyotypic abnormalities,
CC including monosomy 7 and trisomy 8. This syndrome links susceptibility
CC to mycobacterial, viral, and fungal infections with malignancy and can
CC be transmitted in an autosomal dominant pattern.
CC {ECO:0000269|PubMed:21670465}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Lymphedema, primary, with myelodysplasia (LMPM) [MIM:614038]:
CC A chronic disabling condition characterized by swelling of the
CC extremities due to altered lymphatic flow, associated with
CC myelodysplasia. Patients with lymphedema suffer from recurrent local
CC infections, and physical impairment. {ECO:0000269|PubMed:21892158}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous
CC group of closely related clonal hematopoietic disorders. All are
CC characterized by a hypercellular or hypocellular bone marrow with
CC impaired morphology and maturation, dysplasia of the myeloid,
CC megakaryocytic and/or erythroid lineages, and peripheral blood
CC cytopenias resulting from ineffective blood cell production. Included
CC diseases are: refractory anemia (RA), refractory anemia with ringed
CC sideroblasts (RARS), refractory anemia with excess blasts (RAEB),
CC refractory cytopenia with multilineage dysplasia and ringed
CC sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a
CC myelodysplastic/myeloproliferative disease. MDS is considered a
CC premalignant condition in a subgroup of patients that often progresses
CC to acute myeloid leukemia (AML). {ECO:0000269|PubMed:21892162}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35869.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GATA2ID44160ch3q21.html";
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DR EMBL; M68891; AAA35868.1; -; mRNA.
DR EMBL; M77810; AAA35869.1; ALT_SEQ; mRNA.
DR EMBL; BT006671; AAP35317.1; -; mRNA.
DR EMBL; AK314826; BAG37347.1; -; mRNA.
DR EMBL; AC080005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79313.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79314.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79315.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79316.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79317.1; -; Genomic_DNA.
DR EMBL; BC002557; AAH02557.1; -; mRNA.
DR EMBL; BC015613; AAH15613.1; -; mRNA.
DR EMBL; BC015577; AAH15577.1; -; mRNA.
DR EMBL; BC018988; AAH18988.1; -; mRNA.
DR EMBL; BC051272; AAH51272.1; -; mRNA.
DR EMBL; BC051342; AAH51342.1; -; mRNA.
DR CCDS; CCDS3049.1; -. [P23769-1]
DR CCDS; CCDS46903.1; -. [P23769-2]
DR PIR; A40815; A40815.
DR PIR; A41782; A41782.
DR RefSeq; NP_001139133.1; NM_001145661.1. [P23769-1]
DR RefSeq; NP_001139134.1; NM_001145662.1. [P23769-2]
DR RefSeq; NP_116027.2; NM_032638.4. [P23769-1]
DR PDB; 5O9B; NMR; -; A=343-391.
DR PDB; 6ZFV; NMR; -; A=291-334.
DR PDBsum; 5O9B; -.
DR PDBsum; 6ZFV; -.
DR AlphaFoldDB; P23769; -.
DR SMR; P23769; -.
DR BioGRID; 108894; 213.
DR DIP; DIP-29711N; -.
DR IntAct; P23769; 170.
DR STRING; 9606.ENSP00000345681; -.
DR ChEMBL; CHEMBL4523206; -.
DR iPTMnet; P23769; -.
DR PhosphoSitePlus; P23769; -.
DR BioMuta; GATA2; -.
DR DMDM; 229462971; -.
DR EPD; P23769; -.
DR jPOST; P23769; -.
DR MassIVE; P23769; -.
DR MaxQB; P23769; -.
DR PaxDb; P23769; -.
DR PeptideAtlas; P23769; -.
DR PRIDE; P23769; -.
DR ProteomicsDB; 54160; -. [P23769-1]
DR ProteomicsDB; 54161; -. [P23769-2]
DR Antibodypedia; 788; 497 antibodies from 37 providers.
DR DNASU; 2624; -.
DR Ensembl; ENST00000341105.7; ENSP00000345681.2; ENSG00000179348.12. [P23769-1]
DR Ensembl; ENST00000430265.6; ENSP00000400259.2; ENSG00000179348.12. [P23769-2]
DR Ensembl; ENST00000487848.5; ENSP00000417074.1; ENSG00000179348.12. [P23769-1]
DR GeneID; 2624; -.
DR KEGG; hsa:2624; -.
DR MANE-Select; ENST00000341105.7; ENSP00000345681.2; NM_032638.5; NP_116027.2.
DR UCSC; uc003ekm.4; human. [P23769-1]
DR CTD; 2624; -.
DR DisGeNET; 2624; -.
DR GeneCards; GATA2; -.
DR HGNC; HGNC:4171; GATA2.
DR HPA; ENSG00000179348; Low tissue specificity.
DR MalaCards; GATA2; -.
DR MIM; 137295; gene.
DR MIM; 614038; phenotype.
DR MIM; 614172; phenotype.
DR MIM; 614286; phenotype.
DR neXtProt; NX_P23769; -.
DR OpenTargets; ENSG00000179348; -.
DR Orphanet; 3226; Deafness-lymphedema-leukemia syndrome.
DR Orphanet; 319465; Inherited acute myeloid leukemia.
DR Orphanet; 228423; Monocytopenia with susceptibility to infections.
DR Orphanet; 98827; Unclassified myelodysplastic syndrome.
DR PharmGKB; PA28585; -.
DR VEuPathDB; HostDB:ENSG00000179348; -.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000156315; -.
DR HOGENOM; CLU_027524_1_0_1; -.
DR InParanoid; P23769; -.
DR OMA; WTVSPFT; -.
DR OrthoDB; 1240204at2759; -.
DR PhylomeDB; P23769; -.
DR TreeFam; TF315391; -.
DR PathwayCommons; P23769; -.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P23769; -.
DR SIGNOR; P23769; -.
DR BioGRID-ORCS; 2624; 32 hits in 1109 CRISPR screens.
DR ChiTaRS; GATA2; human.
DR GeneWiki; GATA2; -.
DR GenomeRNAi; 2624; -.
DR Pharos; P23769; Tbio.
DR PRO; PR:P23769; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P23769; protein.
DR Bgee; ENSG00000179348; Expressed in seminal vesicle and 197 other tissues.
DR ExpressionAtlas; P23769; baseline and differential.
DR Genevisible; P23769; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0021533; P:cell differentiation in hindbrain; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0001709; P:cell fate determination; IEA:Ensembl.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IEA:Ensembl.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0035854; P:eosinophil fate commitment; IDA:BHF-UCL.
DR GO; GO:0097154; P:GABAergic neuron differentiation; IEA:Ensembl.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:1903444; P:negative regulation of brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0070345; P:negative regulation of fat cell proliferation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IDA:MGI.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000977; P:regulation of forebrain neuron differentiation; IEA:Ensembl.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:Ensembl.
DR GO; GO:0010725; P:regulation of primitive erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0033993; P:response to lipid; IEA:Ensembl.
DR GO; GO:0060872; P:semicircular canal development; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR GO; GO:0061042; P:vascular wound healing; IMP:BHF-UCL.
DR GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IEA:Ensembl.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR029522; GATA-2.
DR InterPro; IPR016374; TF_GATA-2/3.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR PANTHER; PTHR10071:SF149; PTHR10071:SF149; 1.
DR Pfam; PF00320; GATA; 2.
DR PIRSF; PIRSF003027; TF_GATA-1/2/3; 1.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Disease variant;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phagocytosis; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..480
FT /note="Endothelial transcription factor GATA-2"
FT /id="PRO_0000083403"
FT ZN_FING 295..319
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 349..373
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 119..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 340..353
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041126"
FT VARIANT 164
FT /note="A -> T (in dbSNP:rs2335052)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_055004"
FT VARIANT 235
FT /note="T -> N (in dbSNP:rs35079193)"
FT /id="VAR_055005"
FT VARIANT 254
FT /note="P -> L (in IMD21; dbSNP:rs387906630)"
FT /evidence="ECO:0000269|PubMed:21670465"
FT /id="VAR_066405"
FT VARIANT 354
FT /note="T -> M (in IMD21 and MDS; dbSNP:rs387906631)"
FT /evidence="ECO:0000269|PubMed:21670465,
FT ECO:0000269|PubMed:21892162"
FT /id="VAR_066406"
FT VARIANT 355
FT /note="Missing (in MDS)"
FT /evidence="ECO:0000269|PubMed:21892162"
FT /id="VAR_066643"
FT VARIANT 361
FT /note="R -> P (in LMPM)"
FT /evidence="ECO:0000269|PubMed:21892158"
FT /id="VAR_066644"
FT VARIANT 373
FT /note="C -> R (in LMPM; dbSNP:rs387906633)"
FT /evidence="ECO:0000269|PubMed:21892158"
FT /id="VAR_066645"
FT VARIANT 398
FT /note="R -> W (in IMD21; dbSNP:rs387906629)"
FT /evidence="ECO:0000269|PubMed:21670465"
FT /id="VAR_066407"
FT CONFLICT 9
FT /note="R -> G (in Ref. 1; AAA35868)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..21
FT /note="QH -> HD (in Ref. 1; AAA35868)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..39
FT /note="QL -> HV (in Ref. 1; AAA35868)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="R -> A (in Ref. 1; AAA35868)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="G -> S (in Ref. 1; AAA35868)"
FT /evidence="ECO:0000305"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6ZFV"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6ZFV"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:6ZFV"
FT HELIX 317..322
FT /evidence="ECO:0007829|PDB:6ZFV"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:6ZFV"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:5O9B"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:5O9B"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:5O9B"
SQ SEQUENCE 480 AA; 50500 MW; C879CC932C355E6A CRC64;
MEVAPEQPRW MAHPAVLNAQ HPDSHHPGLA HNYMEPAQLL PPDEVDVFFN HLDSQGNPYY
ANPAHARARV SYSPAHARLT GGQMCRPHLL HSPGLPWLDG GKAALSAAAA HHHNPWTVSP
FSKTPLHPSA AGGPGGPLSV YPGAGGGSGG GSGSSVASLT PTAAHSGSHL FGFPPTPPKE
VSPDPSTTGA ASPASSSAGG SAARGEDKDG VKYQVSLTES MKMESGSPLR PGLATMGTQP
ATHHPIPTYP SYVPAAAHDY SSGLFHPGGF LGGPASSFTP KQRSKARSCS EGRECVNCGA
TATPLWRRDG TGHYLCNACG LYHKMNGQNR PLIKPKRRLS AARRAGTCCA NCQTTTTTLW
RRNANGDPVC NACGLYYKLH NVNRPLTMKK EGIQTRNRKM SNKSKKSKKG AECFEELSKC
MQEKSSPFSA AALAGHMAPV GHLPPFSHSG HILPTPTPIH PSSSLSFGHP HPSSMVTAMG
