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Protein

DNA-binding protein Ikaros

Gene

Ikzf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transcription regulator of hematopoietic cell differentiation. Binds gamma-satellite DNA. Binds with higher affinity to gamma satellite A. Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (terminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta-globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells (By similarity). Confers early temporal competence to retinal progenitor cells (RPCs). Function is isoform-specific and is modulated by dominant-negative inactive isoforms (By similarity).By similarity7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei158Required for both pericentromeric heterochromatin localization and complete DNA binding1
Sitei161Required for both pericentromeric heterochromatin localization and complete DNA binding1
Sitei187Required for both pericentromeric heterochromatin localization and DNA binding1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri117 – 139C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri144 – 166C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri172 – 194C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri200 – 223C2H2-type 4PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri457 – 479C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri488 – 512C2H2-type 6PROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Chromatin regulator, Developmental protein, DNA-binding, Repressor
Biological processCell cycle, Transcription, Transcription regulation
LigandMetal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-binding protein Ikaros
Alternative name(s):
Ikaros family zinc finger protein 1
Lymphoid transcription factor LyF-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ikzf1
Synonyms:Ikaros, Lyf1, Zfpn1a1, Znfn1a1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1342540 Ikzf1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Defects in hemopoietic stem cell activity. Progressive reduction in multipotent CFU-S(14) (colony-forming unit-spleen) progenitors and the earliest erythroid-restricted precursors (BFU-E).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi13S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. 1 Publication1
Mutagenesisi13S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. 1 Publication1
Mutagenesisi23T → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. 1 Publication1
Mutagenesisi23T → D: Decreased binding to gamma satellites A and B by 3-fold. Little change in pericentromeric location. 1 Publication1
Mutagenesisi58K → R: Some loss of sumoylation. Complete loss of sumoylation, increased repressor activity but no change in pericentromeric heterochromatin location; when associated with R-240 and R-459. 1 Publication1
Mutagenesisi63S → A: No change in pericentromeric location. Greatly reduced phosphorylation; when associated with A-384; A-386; A-388; A392 and A-393. No effect on DNA-binding activity. Increased DNA-binding activity; when associated with A-384; A-386; A-388; A-392 and A-393. 2 Publications1
Mutagenesisi63S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 2 Publications1
Mutagenesisi101S → A: Abolishes phosphorylation. No change in pericentromeric location. 1 Publication1
Mutagenesisi101S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 1 Publication1
Mutagenesisi140T → A: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-167 and A-195. 1 Publication1
Mutagenesisi140T → E: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-167 and D-195. 1 Publication1
Mutagenesisi152S → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi153F → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication1
Mutagenesisi154T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi155Q → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi156K → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. 1 Publication1
Mutagenesisi157G → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi158N → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication1
Mutagenesisi159L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi160L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi161R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication1
Mutagenesisi167S → A: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-140 and A-195. 1 Publication1
Mutagenesisi167S → E: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-140 and D-195. 1 Publication1
Mutagenesisi173K → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi178N → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi179Y → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication1
Mutagenesisi180A → L: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi181C → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi182R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi183R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication1
Mutagenesisi184R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi185D → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi186A → L: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi187L → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication1
Mutagenesisi188T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi189G → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi191L → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi192R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi193T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi195S → A: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-140 and A-167. 1 Publication1
Mutagenesisi195S → D: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-140 and E-167. 1 Publication1
Mutagenesisi239K → R: Some loss of sumoylation. Complete loss of sumoylation, increased repressor activity but no change in pericentromeric heterochromatin location.; when associated with R-58 and R-459. 1 Publication1
Mutagenesisi293S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. 1 Publication1
Mutagenesisi293S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. Decreased DNA binding affinity toward TdT by 3-fold. 1 Publication1
Mutagenesisi384S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-386; A-388; A-392 and A-393. and A-392. Further reduction in phosphorylation; when associated with A-63; A-386; A-388; A-392 and A-393. 1 Publication1
Mutagenesisi386S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-388; A-392 and A-393. Further reduction in phosphorylation; when associated with A-63; A-384; A-388; A-392 and A-393. 1 Publication1
Mutagenesisi388S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-392 and A-393. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-392 and A-393. 1 Publication1
Mutagenesisi392S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-388 and A-392. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-386 and A-388. 1 Publication1
Mutagenesisi393T → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-388 and A-392. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-388 and A-392. 1 Publication1
Mutagenesisi424K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi458K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi465 – 467LFL → AFA: Abolishes binding of PP1CC, decreases DNA binding, abolishes pericentromeric location, and results in IKAROS degradation. 1 Publication3

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000470951 – 517DNA-binding protein IkarosAdd BLAST517

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei13Phosphoserine1 Publication1
Modified residuei23Phosphothreonine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei63PhosphoserineCombined sources2 Publications1
Modified residuei101Phosphoserine1 Publication1
Modified residuei140Phosphothreonine1 Publication1
Modified residuei167Phosphoserine1 Publication1
Modified residuei195Phosphoserine1 Publication1
Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei259PhosphoserineBy similarity1
Modified residuei287PhosphoserineBy similarity1
Modified residuei293Phosphoserine1 Publication1
Modified residuei357PhosphoserineBy similarity1
Modified residuei360PhosphoserineBy similarity1
Modified residuei384Phosphoserine1 Publication1
Modified residuei386Phosphoserine1 Publication1
Modified residuei388Phosphoserine1 Publication1
Modified residuei392Phosphoserine1 Publication1
Modified residuei393Phosphothreonine1 Publication1
Modified residuei397PhosphoserineCombined sources1
Modified residuei440PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-357 and Ser-360 downstream of SYK induces nuclear translocation (By similarity). Phosphorylation controls cell-cycle progression from late G1 stage to S stage. Hyperphosphorylated during G2/M phase. Dephosphorylated state during late G1 phase. Phosphorylation on Thr-140 is required for DNA and pericentromeric location during mitosis. CK2 is the main kinase, in vitro. GSK3 and CDK may also contribute to phosphorylation of the C-terminal serine and threonine residues. Phosphorylation on these C-terminal residues reduces the DNA-binding ability. Phosphorylation/dephosphorylation events on Ser-13 and Ser-293 regulate TDT expression during thymocyte differentiation. Dephosphorylation by protein phosphatase 1 regulates stability and pericentromeric heterochromatin location. Phosphorylated in both lymphoid and non-lymphoid tissues.By similarity4 Publications
Sumoylated. Simulataneous sumoylation on the 2 sites results in a loss of both HDAC-dependent and HDAC-independent repression. Has no effect on pericentromeric heterochromatin location. Desumoylated by SENP1.1 Publication
Polyubiquitinated.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q03267

MaxQB - The MaxQuant DataBase

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MaxQBi
Q03267

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q03267

PeptideAtlas

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PeptideAtlasi
Q03267

PRoteomics IDEntifications database

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PRIDEi
Q03267

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q03267

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q03267

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Strongly expressed in T-cells and their progenitors,in B-cells, and in all early embryonic retinal progenitor cells (RPCs). Isoforms V and VI are the predominant isoforms in lymphocytes.3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

First detected in fetal liver and embryonic thymus.1 Publication

Gene expression databases

CleanEx database of gene expression profiles

More...
CleanExi
MM_IKZF1

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer with other IKAROS family members. Interacts with IKZF4 AND IKZF5 (By similarity). Component of the chromatin-remodeling NuRD repressor complex which includes at least HDAC1, HDAC2, RBBP4, RBBP7, IKZF1, MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4. Interacts directly with the CHD4 component of the NuRD complex. Interacts directly with SMARCA4; the interaction associates IKFZ1 with the BAF complex. Interacts with SUMO1; the interaction sumoylates IKAROS, promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform alpha); the interaction promotes sumoylation and reduces transcription repression. Interacts, to a lesser extent, with PIAS3. Interacts with PPP1CC; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with IKZF3.By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Sumo1P631662EBI-908572,EBI-80152

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q03267

Protein interaction database and analysis system

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IntActi
Q03267, 12 interactors

Molecular INTeraction database

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MINTi
Q03267

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000075992

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q03267

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q03267

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni153 – 162Required for both high-affinity DNA binding and pericentromeric heterochromatin localization10
Regioni179 – 194Required for both high-affinity DNA binding and pericentromeric heterochromatin localizationAdd BLAST16
Regioni463 – 466Required for binding PP1CC4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi368 – 371Poly-Leu4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal zinc-fingers 2 and 3 are required for DNA binding as well as for targeting IKFZ1 to pericentromeric heterochromatin.
The C-terminal zinc-finger domain is required for dimerization.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri117 – 139C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri144 – 166C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri172 – 194C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri200 – 223C2H2-type 4PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri457 – 479C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri488 – 512C2H2-type 6PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1721 Eukaryota
COG5048 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000049114

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004752

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q03267

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type

Pfam protein domain database

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Pfami
View protein in Pfam
PF00096 zf-C2H2, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00355 ZnF_C2H2, 6 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57667 SSF57667, 3 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 5 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform VI (identifier: Q03267-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD
60 70 80 90 100
RGMGSNVKVE TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG
110 120 130 140 150
SSALSGVGGI RLPNGKLKCD ICGIVCIGPN VLMVHKRSHT ERPFQCNQCG
160 170 180 190 200
ASFTQKGNLL RHIKLHSGEK PFKCHLCNYA CRRRDALTGH LRTHSVGKPH
210 220 230 240 250
KCGYCGRSYK QRSSLEEHKE RCHNYLESMG LPGVCPVIKE ETNHNEMAED
260 270 280 290 300
LCKIGAERSL VLDRLASNVA KRKSSMPQKF LGDKCLSDMP YDSANYEKED
310 320 330 340 350
MMTSHVMDQA INNAINYLGA ESLRPLVQTP PGSSEVVPVI SSMYQLHKPP
360 370 380 390 400
SDGPPRSNHS AQDAVDNLLL LSKAKSVSSE REASPSNSCQ DSTDTESNAE
410 420 430 440 450
EQRSGLIYLT NHINPHARNG LALKEEQRAY EVLRAASENS QDAFRVVSTS
460 470 480 490 500
GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG CHGFRDPFEC NMCGYHSQDR
510
YEFSSHITRG EHRYHLS
Length:517
Mass (Da):57,336
Last modified:December 15, 1998 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1052B8E76AF24287
GO
Isoform I (identifier: Q03267-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-282: Missing.

Show »
Length:288
Mass (Da):31,989
Checksum:i71C89A7297190EDB
GO
Isoform II (identifier: Q03267-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: M → VAYGADGFRDFHAIISDRGM
     54-282: Missing.

Show »
Length:307
Mass (Da):34,038
Checksum:iE644C2B323032538
GO
Isoform III (identifier: Q03267-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-282: Missing.

Show »
Length:375
Mass (Da):41,200
Checksum:i436E72D7B71477B1
GO
Isoform IV (identifier: Q03267-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: M → VAYGADGFRDFHAIISDRGM
     141-282: Missing.

Show »
Length:394
Mass (Da):43,250
Checksum:iB6F496262B04D9F3
GO
Isoform V (identifier: Q03267-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-140: Missing.

Show »
Length:430
Mass (Da):48,125
Checksum:i56F4672C0F124FF1
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G5E8H3G5E8H3_MOUSE
DNA-binding protein Ikaros
Ikzf1 Zfpn1a1, mCG_3994
515Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SWU0Q5SWU0_MOUSE
DNA-binding protein Ikaros
Ikzf1 Zfpn1a1, mCG_3994
428Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SWT9Q5SWT9_MOUSE
DNA-binding protein Ikaros
Ikzf1
535Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q8C9X3Q8C9X3_MOUSE
DNA-binding protein Ikaros
Ikzf1 Zfpn1a1
198Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SWT7Q5SWT7_MOUSE
DNA-binding protein Ikaros
Ikzf1
79Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SWT6Q5SWT6_MOUSE
DNA-binding protein Ikaros
Ikzf1
18Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti234 – 235VC → MY in AAB32250 (PubMed:7935426).Curated2
Sequence conflicti480 – 482Missing AA sequence (PubMed:7935426).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00685353M → VAYGADGFRDFHAIISDRGM in isoform II and isoform IV. Curated1
Alternative sequenceiVSP_00685554 – 282Missing in isoform I and isoform II. CuratedAdd BLAST229
Alternative sequenceiVSP_00685454 – 140Missing in isoform V. 1 PublicationAdd BLAST87
Alternative sequenceiVSP_006856141 – 282Missing in isoform III and isoform IV. CuratedAdd BLAST142

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L03547 mRNA Translation: AAA66193.1
S74517 mRNA Translation: AAB32248.2 Sequence problems.
S74518 mRNA Translation: AAB32249.2
S74708 mRNA Translation: AAB32250.2

Protein sequence database of the Protein Information Resource

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PIRi
A56355
I59572

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.103545

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03547 mRNA Translation: AAA66193.1
S74517 mRNA Translation: AAB32248.2 Sequence problems.
S74518 mRNA Translation: AAB32249.2
S74708 mRNA Translation: AAB32250.2
PIRiA56355
I59572
UniGeneiMm.103545

3D structure databases

ProteinModelPortaliQ03267
SMRiQ03267
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiQ03267
IntActiQ03267, 12 interactors
MINTiQ03267
STRINGi10090.ENSMUSP00000075992

PTM databases

iPTMnetiQ03267
PhosphoSitePlusiQ03267

Proteomic databases

EPDiQ03267
MaxQBiQ03267
PaxDbiQ03267
PeptideAtlasiQ03267
PRIDEiQ03267

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1342540 Ikzf1

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
HOGENOMiHOG000049114
HOVERGENiHBG004752
InParanoidiQ03267

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q03267

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

CleanExiMM_IKZF1

Family and domain databases

InterProiView protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 6 hits
SUPFAMiSSF57667 SSF57667, 3 hits
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 5 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIKZF1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q03267
Secondary accession number(s): Q64044, Q64045, Q64051
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: December 15, 1998
Last modified: November 7, 2018
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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