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O35615 (FOG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein ZFPM1
Alternative name(s):
Friend of GATA protein 1
Short name=FOG-1
Short name=Friend of GATA 1
Zinc finger protein multitype 1
Gene names
Name:Zfpm1
Synonyms:Fog, Fog1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length995 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with the N-terminal zinc-finger of GATA1, GATA2 and GATA3. Interacts with corepressor CTBP2; this interaction is however not essential for corepressor activity in erythropoiesis. Interacts with TACC3. Ref.1 Ref.3 Ref.5 Ref.6 Ref.10

Subcellular location

Nucleus Ref.1.

Tissue specificity

Mainly expressed in hematopoietic tissues. Expressed in the spleen, a primary site of hematopoiesis in the adult mouse, as well as in the liver and testis, but not in the heart, brain, lung, kidney, or skeletal muscle. Among hematopoietic cell lines, it is strongly expressed in erythroid and megakaryocytic cell lines. Expressed at low level in several lymphoid and early myeloid cell lines. Not expressed in mast cell and macrophage lines. Expressed in the heart, where it colocalizes with GATA4, GATA5 and GATA6. Ref.1 Ref.8

Developmental stage

First expressed in two extraembryonic mesodermal derivatives, the yolk sac and the allantois in E8.5 embryos. Localized to the embryonic red blood cells within the yolk sac blood islands. Ref.1

Domain

The CCHC-type zinc fingers 1, 5, 6 and 9 bind directly to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC-type zinc finger is essential for the interaction with GATA-type zinc fingers.

Sequence similarities

Belongs to the FOG (Friend of GATA) family.

Contains 4 C2H2-type zinc fingers.

Contains 5 C2HC-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processatrial septum morphogenesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

atrioventricular valve morphogenesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

cardiac muscle tissue morphogenesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

definitive erythrocyte differentiation

Inferred from mutant phenotype Ref.2. Source: MGI

embryonic hemopoiesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

erythrocyte differentiation

Inferred from mutant phenotype PubMed 20010697. Source: MGI

granulocyte differentiation

Inferred from mutant phenotype PubMed 20010697. Source: MGI

heart development

Inferred from mutant phenotype Ref.8. Source: MGI

homeostasis of number of cells

Inferred from mutant phenotype PubMed 20643340. Source: MGI

megakaryocyte development

Inferred from mutant phenotype PubMed 20010697. Source: MGI

megakaryocyte differentiation

Inferred from mutant phenotype Ref.2. Source: MGI

mitral valve formation

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

negative regulation of fat cell differentiation

Inferred from mutant phenotype PubMed 20705609. Source: UniProtKB

negative regulation of interleukin-4 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell differentiation

Inferred from direct assay PubMed 18063754. Source: BHF-UCL

negative regulation of protein binding

Inferred from direct assay PubMed 18063754. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 2906112. Source: MGI

outflow tract morphogenesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

platelet formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: MGI

primitive erythrocyte differentiation

Inferred from mutant phenotype Ref.2. Source: MGI

regulation of chemokine production

Inferred from mutant phenotype PubMed 20643340. Source: MGI

regulation of definitive erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

transcriptional activation by promoter-enhancer looping

Inferred from direct assay PubMed 15644435. Source: BHF-UCL

tricuspid valve formation

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

ventricular septum morphogenesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19654328. Source: MGI

nucleus

Inferred from direct assay PubMed 12213678PubMed 12923059PubMed 19654328. Source: MGI

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

transcriptional repressor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II activating transcription factor binding

Inferred from direct assay Ref.1. 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: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.10. Source: IntAct

transcription corepressor activity

Traceable author statement PubMed 12923059. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tacc3Q9JJ117EBI-4394596,EBI-2553611

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 995995Zinc finger protein ZFPM1
PRO_0000221042

Regions

Zinc finger255 – 27824C2HC-type 1
Zinc finger303 – 32725C2H2-type 1
Zinc finger333 – 35523C2H2-type 2
Zinc finger361 – 38424C2H2-type 3
Zinc finger590 – 61324C2HC-type 2
Zinc finger696 – 71924C2HC-type 3
Zinc finger836 – 85924C2HC-type 4
Zinc finger868 – 89124C2H2-type 4
Zinc finger963 – 98624C2HC-type 5
Region343 – 35412Interaction with TACC3
Region811 – 8177Interaction with CTBP2

Amino acid modifications

Modified residue8031Phosphoserine By similarity
Modified residue9251Phosphoserine Ref.9
Modified residue9271Phosphoserine Ref.9

Experimental info

Mutagenesis2541V → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2551F → A: Impairs interaction with GATA1. Ref.5 Ref.6
Mutagenesis2561P → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2581K → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2591D → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2611G → A: Slightly affects the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2621I → A: Impairs interaction with GATA1. Ref.5 Ref.6
Mutagenesis2631W → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2651R → A: Slightly affects the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2661S → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2671E → A: Slightly affects the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2681R → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2691N → A: Impairs interaction with GATA1. Ref.5 Ref.6
Mutagenesis2711Q → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2741L → A: Slightly affects the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2751L → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2761Y → A: Slightly affects the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2771Y → A: Impairs interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-612; A-718 and/or A-985. Ref.5 Ref.6
Mutagenesis2801S → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis2811R → A: Does not affect the interaction with GATA1. Ref.5 Ref.6
Mutagenesis3341V → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3361L → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3391L → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3401S → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3431T → A: Impairs interaction with TACC3. Ref.6 Ref.10
Mutagenesis3441T → A: Abolishes interaction with TACC3. Ref.6 Ref.10
Mutagenesis3451K → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3461A → D: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3471N → A: Abolishes interaction with TACC3. Ref.6 Ref.10
Mutagenesis3491E → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3501R → A: Abolishes interaction with TACC3. Ref.6 Ref.10
Mutagenesis3521L → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3531K → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3541V → A: Abolishes interaction with TACC3. Ref.6 Ref.10
Mutagenesis3561T → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis3571D → A: No effect on interaction with TACC3. Ref.6 Ref.10
Mutagenesis6121Y → A: Impairs interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-277; A-718 and/or A-985. Ref.5 Ref.6
Mutagenesis6981C → A: Abolishes interaction with GATA1. Ref.3 Ref.6
Mutagenesis7061S → R: Able to partially restore the interaction with the G-205 GATA1 mutant, which is usually unable to interact with ZFPM1. Ref.4 Ref.6
Mutagenesis7181Y → A: Impairs interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-277; A-612 and/or A-985. Ref.5 Ref.6
Mutagenesis7191C → A: Abolishes interaction with GATA1. Ref.3 Ref.6
Mutagenesis7191C → H: Transforms the C2HC-type zinc finger into a C2H2-type, leading to abolition of interaction with GATA1. Ref.3 Ref.6
Mutagenesis811 – 8144PIDL → AIAA: Abolishes interaction with CTBP2. Ref.5 Ref.6
Mutagenesis813 – 8142DL → AS: Abolishes interaction with CTBP2; it however does not abolish the corepressor activity in erythropoiesis. Ref.6
Mutagenesis9851Y → A: Slightly affects the interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-277; A-612 and/or A-718. Ref.5 Ref.6

Secondary structure

....... 995
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35615 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 293255B28151ECB8

FASTA995105,984
        10         20         30         40         50         60 
MSRRKQSNPR QIKRSLRDME AGEEAKAMDS SPKEQEAPDP EAPAIEEPPS PPREDVSPPA 

        70         80         90        100        110        120 
VPAPPESPED PEDMEGQELE MRPQDEEKEE KEEEAAMASP WSGPEELELA LQDGQRCVRA 

       130        140        150        160        170        180 
RLSLTEGLSW GPFYGSIQTR ALSPEREEPG PAVTLMVDES CWLRMLPQVL TEEAANSEIY 

       190        200        210        220        230        240 
RKDDALWCRV TKVVPSGGLL YVRLVTEPHG APRHPVQEPV EPGGLAPVHT DIQLLPQQAG 

       250        260        270        280        290        300 
MASILATAVI NKDVFPCKDC GIWYRSERNL QAHLLYYCAS RQRAGSPVSA TEEKPKETYP 

       310        320        330        340        350        360 
NERVCPFPQC RKSCPSASSL EIHMRSHSGE RPFVCLICLS AFTTKANCER HLKVHTDTLS 

       370        380        390        400        410        420 
GVCHNCGFIS TTRDILYSHL VTNHMVCQPG SKGEIYSPGA GHPAAKLPPD SLAGFQQHSL 

       430        440        450        460        470        480 
MHSPLVPADK APTPSSGLDS KAEVTNGETR VPPQNGGSSE SPAAPRTIKV EAAEEPEATR 

       490        500        510        520        530        540 
ASGPGEPGPQ APSRTPSPHS PNPVRVKTEL SSPTPGSSPG PGELTMAGTL FLPQYVFSPD 

       550        560        570        580        590        600 
AGTTTVPTAP QASEILAKMS ELVHNRLQQG AGSSGAAGTP TGLFSGTKGA TCFECEITFN 

       610        620        630        640        650        660 
NINNFYVHKR LYCSGRRAPE DPPTVRRPKA ATGPARAPAG AAAEPDPSRS SPGPGPREEE 

       670        680        690        700        710        720 
ASGTTTPEAE AAGRGSEGSQ SPGSSVDDAE DDPSRTLCEA CNIRFSRHET YTVHKRYYCA 

       730        740        750        760        770        780 
SRHDPPPRRP PAPTTAPGPA APALTAPPVR TRRRRKLYEL PAAGAPPPAA GPAPVPVVPS 

       790        800        810        820        830        840 
PTAELPSSPR PGSASAGPAP ALSPSPVPDG PIDLSKRPRR QSPDAPTALP ALADYHECTA 

       850        860        870        880        890        900 
CRVSFHSLEA YLAHKKYSCP AAPLRTTALC PYCPPNGRVR GDLVEHLRQA HGLQVAKPAA 

       910        920        930        940        950        960 
SPGAEPRTPA ERAPRDSPDG RAPRSPSPAP ENTPSDPADQ GARTPSKGPP APAPAPGGGG 

       970        980        990 
GHRYCRLCNI RFSSLSTFIA HKKYYCSSHA AEHVK 

« Hide

References

« Hide 'large scale' references
[1]"FOG, a multitype zinc finger protein, acts as a cofactor for transcription factor GATA-1 in erythroid and megakaryocytic differentiation."
Tsang A.P., Visvader J.E., Turner C.A., Fujiwara Y., Yu C., Weiss M.J., Crossley M., Orkin S.H.
Cell 90:109-119(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH GATA1; GATA2 AND GATA3.
Tissue: Erythroleukemia.
[2]"Failure of megakaryopoiesis and arrested erythropoiesis in mice lacking the GATA-1 transcriptional cofactor FOG."
Tsang A.P., Fujiwara Y., Hom D.B., Orkin S.H.
Genes Dev. 12:1176-1188(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"Key residues characteristic of GATA N-fingers are recognized by FOG."
Fox A.H., Kowalski K., King G.F., Mackay J.P., Crossley M.
J. Biol. Chem. 273:33595-33603(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GATA1, MUTAGENESIS OF CYS-698 AND CYS-719.
[4]"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: FUNCTION, MUTAGENESIS OF SER-706.
[5]"Transcriptional cofactors of the FOG family interact with GATA proteins by means of multiple zinc fingers."
Fox A.H., Liew C., Holmes M., Kowalski K., Mackay J., Crossley M.
EMBO J. 18:2812-2822(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GATA1 AND CTBP2, MUTAGENESIS OF VAL-254; PHE-255; PRO-256; LYS-258; ASP-259; GLY-261; ILE-262; TRP-263; ARG-265; SER-266; GLU-267; ARG-268; ASN-269; GLN-271; LEU-274; LEU-275; TYR-276; TYR-277; SER-280; ARG-281; 811-PRO--LEU-814; TYR-612; TYR-718 AND TYR-985.
[6]"Interaction between FOG-1 and the corepressor C-terminal binding protein is dispensable for normal erythropoiesis in vivo."
Katz S.G., Cantor A.B., Orkin S.H.
Mol. Cell. Biol. 22:3121-3128(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTBP2, MUTAGENESIS OF 813-ASP-LEU-814.
[7]"Control of megakaryocyte-specific gene expression by GATA-1 and FOG-1: role of Ets transcription factors."
Wang X., Crispino J.D., Letting D.L., Nakazawa M., Poncz M., Blobel G.A.
EMBO J. 21:5225-5234(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Endothelial lineage-mediated loss of the GATA cofactor Friend of GATA 1 impairs cardiac development."
Katz S.G., Williams A., Yang J., Fujiwara Y., Tsang A.P., Epstein J.A., Orkin S.H.
Proc. Natl. Acad. Sci. U.S.A. 100:14030-14035(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-925 AND SER-927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"A classic zinc finger from Friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3."
Simpson R.J.Y., Yi Lee S.H., Bartle N., Sum E.Y., Visvader J.E., Matthews J.M., Mackay J.P., Crossley M.
J. Biol. Chem. 279:39789-39797(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 328-360, INTERACTION WITH TACC3, MUTAGENESIS OF VAL-334; LEU-336; LEU-339; SER-340; THR-343; THR-344; LYS-345; ALA-346; ASN-347; GLU-349; ARG-350; LEU-352; LYS-353; VAL-354; THR-356 AND ASP-357.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006492 mRNA. Translation: AAC53292.1.
CCDSCCDS22733.1.
RefSeqNP_033595.1. NM_009569.3.
XP_006530914.1. XM_006530851.1.
UniGeneMm.3105.
Mm.390068.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRKNMR-A328-360[»]
ProteinModelPortalO35615.
SMRO35615. Positions 251-418, 582-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204687. 11 interactions.
DIPDIP-48414N.
IntActO35615. 3 interactions.
MINTMINT-6613139.
STRING10090.ENSMUSP00000058037.

PTM databases

PhosphoSiteO35615.

Proteomic databases

PaxDbO35615.
PRIDEO35615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054052; ENSMUSP00000058037; ENSMUSG00000049577.
GeneID22761.
KEGGmmu:22761.
UCSCuc009nsj.1. mouse.

Organism-specific databases

CTD161882.
MGIMGI:1095400. Zfpm1.

Phylogenomic databases

eggNOGNOG146797.
GeneTreeENSGT00530000063823.
HOGENOMHOG000112626.
HOVERGENHBG101018.
InParanoidO35615.
KOK17441.
OMAKLYELHA.
OrthoDBEOG74TWXR.
PhylomeDBO35615.
TreeFamTF331342.

Gene expression databases

ArrayExpressO35615.
BgeeO35615.
CleanExMM_ZFPM1.
GenevestigatorO35615.

Family and domain databases

Gene3D3.30.160.60. 2 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 9 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO35615.
NextBio303277.
PROO35615.
SOURCESearch...

Entry information

Entry nameFOG1_MOUSE
AccessionPrimary (citable) accession number: O35615
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot