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Q03267 (IKZF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-binding protein Ikaros
Alternative name(s):
Ikaros family zinc finger protein 1
Lymphoid transcription factor LyF-1
Gene names
Name:Ikzf1
Synonyms:Ikaros, Lyf1, Zfpn1a1, Znfn1a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

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. Component of the BAF (SWI/SNF) gene activator complex which includes ACTB, ARID1A, ARID1B, IKZF1, ARID1A, ARID1B, SMARCA2, SMARCA4 and at least one BAF subunit. Interacts directly with the SMARCA4 component of 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. Ref.3 Ref.6 Ref.9 Ref.13

Subcellular location

Nucleus. Note: In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events. Ref.5 Ref.7 Ref.12 Ref.13

Isoform V: Nucleus. Note: In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events. Ref.5 Ref.7 Ref.12 Ref.13

Isoform I: Cytoplasm Ref.5 Ref.7 Ref.12 Ref.13.

Tissue specificity

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. Ref.1 Ref.2 Ref.11

Developmental stage

First detected in fetal liver and embryonic thymus. Ref.1

Domain

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.

Post-translational modification

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. Ref.7 Ref.8 Ref.12 Ref.13

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. Ref.9

Polyubiquitinated.

Disruption phenotype

Defects in hemopoietic stem cell activity. Progressive reduction in multipotent CFU-S14 (colony-forming unit-spleen) progenitors and the earliest erythroid-restricted precursors (BFU-E). Ref.4

Sequence similarities

Belongs to the Ikaros C2H2-type zinc-finger protein family.

Contains 6 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Developmental protein
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 7923373. Source: MGI

Peyer's patch development

Inferred from mutant phenotype PubMed 7923373. Source: MGI

T cell differentiation

Inferred from mutant phenotype PubMed 7923373. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

forebrain development

Inferred from mutant phenotype PubMed 15841184PubMed 16467156. Source: MGI

gland development

Inferred from mutant phenotype PubMed 16467156. Source: MGI

hemopoiesis

Inferred from mutant phenotype PubMed 11805317. Source: MGI

lymph node development

Inferred from mutant phenotype PubMed 7923373. Source: MGI

natural killer cell differentiation

Inferred from mutant phenotype PubMed 7923373. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12617992. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18804520. Source: UniProtKB

positive regulation of NK T cell differentiation

Inferred from mutant phenotype PubMed 10366784. Source: MGI

positive regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 16467156. Source: MGI

positive regulation of neutrophil differentiation

Inferred from mutant phenotype PubMed 12406904. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15841184PubMed 16467156. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 7969165. Source: MGI

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 11805317. Source: MGI

retina development in camera-type eye

Inferred from mutant phenotype Ref.11. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 7923373. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentromeric heterochromatin

Inferred from direct assay Ref.9. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 12617992PubMed 16467156PubMed 7969165. Source: MGI

transcription factor complex

Traceable author statement PubMed 11805317. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 11805317PubMed 15841184PubMed 7969165. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 10218586PubMed 9560339. Source: MGI

sequence-specific DNA binding

Inferred from mutant phenotype PubMed 7923373. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 7969165. Source: MGI

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18804520. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sumo1P631662EBI-908572,EBI-80152

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform VI (identifier: Q03267-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform I (identifier: Q03267-2)

The sequence of this isoform differs from the canonical sequence as follows:
     54-282: Missing.
Isoform II (identifier: Q03267-3)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: M → VAYGADGFRDFHAIISDRGM
     54-282: Missing.
Isoform III (identifier: Q03267-4)

The sequence of this isoform differs from the canonical sequence as follows:
     141-282: Missing.
Isoform IV (identifier: Q03267-5)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: M → VAYGADGFRDFHAIISDRGM
     141-282: Missing.
Isoform V (identifier: Q03267-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517DNA-binding protein Ikaros
PRO_0000047095

Regions

Zinc finger117 – 13923C2H2-type 1
Zinc finger144 – 16623C2H2-type 2
Zinc finger172 – 19423C2H2-type 3
Zinc finger200 – 22324C2H2-type 4
Zinc finger457 – 47923C2H2-type 5
Zinc finger488 – 51225C2H2-type 6
Region153 – 16210Required for both high-affinity DNA binding and pericentromeric heterochromatin localization
Region179 – 19416Required for both high-affinity DNA binding and pericentromeric heterochromatin localization
Region463 – 4664Required for binding PP1CC
Compositional bias368 – 3714Poly-Leu

Sites

Site1581Required for both pericentromeric heterochromatin localization and complete DNA binding
Site1611Required for both pericentromeric heterochromatin localization and complete DNA binding
Site1871Required for both pericentromeric heterochromatin localization and DNA binding

Amino acid modifications

Modified residue131Phosphoserine Ref.12
Modified residue231Phosphothreonine Ref.12
Modified residue631Phosphoserine Ref.8 Ref.12
Modified residue1011Phosphoserine Ref.12
Modified residue1401Phosphothreonine Ref.7
Modified residue1671Phosphoserine Ref.7
Modified residue1951Phosphoserine Ref.7
Modified residue2591Phosphoserine By similarity
Modified residue2931Phosphoserine Ref.12
Modified residue3571Phosphoserine By similarity
Modified residue3601Phosphoserine By similarity
Modified residue3841Phosphoserine Ref.8
Modified residue3861Phosphoserine Ref.8
Modified residue3881Phosphoserine Ref.8
Modified residue3921Phosphoserine Ref.8
Modified residue3931Phosphothreonine Ref.8
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Natural variations

Alternative sequence531M → VAYGADGFRDFHAIISDRGM in isoform II and isoform IV.
VSP_006853
Alternative sequence54 – 282229Missing in isoform I and isoform II.
VSP_006855
Alternative sequence54 – 14087Missing in isoform V.
VSP_006854
Alternative sequence141 – 282142Missing in isoform III and isoform IV.
VSP_006856

Experimental info

Mutagenesis131S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. Ref.12
Mutagenesis131S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. Ref.12
Mutagenesis231T → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Ref.12
Mutagenesis231T → D: Decreased binding to gamma satellites A and B by 3-fold. Little change in pericentromeric location. Ref.12
Mutagenesis581K → 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. Ref.9
Mutagenesis631S → 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. Ref.8 Ref.12
Mutagenesis631S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. Ref.8 Ref.12
Mutagenesis1011S → A: Abolishes phosphorylation. No change in pericentromeric location. Ref.12
Mutagenesis1011S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. Ref.12
Mutagenesis1401T → A: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-167 and A-195. Ref.7
Mutagenesis1401T → E: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-167 and D-195. Ref.7
Mutagenesis1521S → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1531F → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. Ref.5
Mutagenesis1541T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1551Q → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
Mutagenesis1561K → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Ref.5
Mutagenesis1571G → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
Mutagenesis1581N → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. Ref.5
Mutagenesis1591L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1601L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1611R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. Ref.5
Mutagenesis1671S → 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. Ref.7
Mutagenesis1671S → 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. Ref.7
Mutagenesis1731K → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1781N → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1791Y → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. Ref.5
Mutagenesis1801A → L: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
Mutagenesis1811C → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1821R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1831R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. Ref.5
Mutagenesis1841R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1851D → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
Mutagenesis1861A → L: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
Mutagenesis1871L → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. Ref.5
Mutagenesis1881T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1891G → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1911L → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
Mutagenesis1921R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1931T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
Mutagenesis1951S → 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. Ref.7
Mutagenesis1951S → 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. Ref.7
Mutagenesis2391K → 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. Ref.9
Mutagenesis2931S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. Ref.12
Mutagenesis2931S → 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. Ref.12
Mutagenesis3841S → 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. Ref.8
Mutagenesis3861S → 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. Ref.8
Mutagenesis3881S → 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. Ref.8
Mutagenesis3921S → 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. Ref.8
Mutagenesis3931T → 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. Ref.8
Mutagenesis4241K → R: No effect on sumoylation. Ref.9
Mutagenesis4581K → R: No effect on sumoylation. Ref.9
Mutagenesis465 – 4673LFL → AFA: Abolishes binding of PP1CC, decreases DNA binding, abolishes pericentromeric location, and results in IKAROS degradation. Ref.13
Sequence conflict234 – 2352VC → MY in AAB32250. Ref.2
Sequence conflict480 – 4823Missing AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform VI [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 1052B8E76AF24287

FASTA51757,336
        10         20         30         40         50         60 
MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGMGSNVKVE 

        70         80         90        100        110        120 
TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 

       130        140        150        160        170        180 
ICGIVCIGPN VLMVHKRSHT ERPFQCNQCG ASFTQKGNLL RHIKLHSGEK PFKCHLCNYA 

       190        200        210        220        230        240 
CRRRDALTGH LRTHSVGKPH KCGYCGRSYK QRSSLEEHKE RCHNYLESMG LPGVCPVIKE 

       250        260        270        280        290        300 
ETNHNEMAED LCKIGAERSL VLDRLASNVA KRKSSMPQKF LGDKCLSDMP YDSANYEKED 

       310        320        330        340        350        360 
MMTSHVMDQA INNAINYLGA ESLRPLVQTP PGSSEVVPVI SSMYQLHKPP SDGPPRSNHS 

       370        380        390        400        410        420 
AQDAVDNLLL LSKAKSVSSE REASPSNSCQ DSTDTESNAE EQRSGLIYLT NHINPHARNG 

       430        440        450        460        470        480 
LALKEEQRAY EVLRAASENS QDAFRVVSTS GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG 

       490        500        510 
CHGFRDPFEC NMCGYHSQDR YEFSSHITRG EHRYHLS 

« Hide

Isoform I [UniParc].

Checksum: 71C89A7297190EDB
Show »

FASTA28831,989
Isoform II [UniParc].

Checksum: E644C2B323032538
Show »

FASTA30734,038
Isoform III [UniParc].

Checksum: 436E72D7B71477B1
Show »

FASTA37541,200
Isoform IV [UniParc].

Checksum: B6F496262B04D9F3
Show »

FASTA39443,250
Isoform V [UniParc].

Checksum: 56F4672C0F124FF1
Show »

FASTA43048,125

References

[1]"Ikaros, an early lymphoid-specific transcription factor and a putative mediator for T cell commitment."
Georgopoulos K., Moore D.D., Derfler B.
Science 258:808-812(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V), FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Embryo.
[2]"The lymphoid transcription factor LyF-1 is encoded by specific, alternatively spliced mRNAs derived from the Ikaros gene."
Hahm K., Ernst P., Lo K., Kim G.S., Turck C., Smale S.T.
Mol. Cell. Biol. 14:7111-7123(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[3]"Aiolos, a lymphoid restricted transcription factor that interacts with Ikaros to regulate lymphocyte differentiation."
Morgan B., Sun L., Avitahl N., Andrikopoulos K., Ikeda T., Gonzales E., Wu P., Neben S., Georgopoulos K.
EMBO J. 16:2004-2013(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKZF3.
[4]"Defects in hemopoietic stem cell activity in Ikaros mutant mice."
Nichogiannopoulou A., Trevisan M., Neben S., Friedrich C., Georgopoulos K.
J. Exp. Med. 190:1201-1214(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Targeting of Ikaros to pericentromeric heterochromatin by direct DNA binding."
Cobb B.S., Morales-Alcelay S., Kleiger G., Brown K.E., Fisher A.G., Smale S.T.
Genes Dev. 14:2146-2160(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-152; PHE-153; THR-154; GLN-155; LYS-156; GLY-157; ASN-158; LEU-159; LEU-160; ARG-161; LYS-173; ASN-178; TYR-179; ALA-180; CYS-181; ARG-182; ARG-183; ARG-184; ASP-185; ALA-186; LEU-187; THR-188; GLY-189; LEU-191; ARG-192 AND THR-193.
[6]"An ikaros-containing chromatin-remodeling complex in adult-type erythroid cells."
O'Neill D.W., Schoetz S.S., Lopez R.A., Castle M., Rabinowitz L., Shor E., Krawchuk D., Goll M.G., Renz M., Seelig H.P., Han S., Seong R.H., Park S.D., Agalioti T., Munshi N., Thanos D., Erdjument-Bromage H., Tempst P., Bank A.
Mol. Cell. Biol. 20:7572-7582(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NURD COMPLEX, IDENTIFICATION IN THE BAF COMPLEX, INTERACTION WITH CHD4, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"A common mechanism for mitotic inactivation of C2H2 zinc finger DNA-binding domains."
Dovat S., Ronni T., Russell D., Ferrini R., Cobb B.S., Smale S.T.
Genes Dev. 16:2985-2990(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-140; SER-167 AND SER-195, SUBCELLULAR LOCATION, DNA-BINDING, MUTAGENESIS OF THR-140; SER-167 AND SER-195.
[8]"Phosphorylation controls Ikaros's ability to negatively regulate the G(1)-S transition."
Gomez-del Arco P., Maki K., Georgopoulos K.
Mol. Cell. Biol. 24:2797-2807(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-63; SER-384; SER-386; SER-388; SER-392 AND THR-393, DNA-BINDING, FUNCTION, MUTAGENESIS OF SER-63; SER-384; SER-386; SER-388; SER-392 AND THR-393.
[9]"Ikaros SUMOylation: switching out of repression."
Gomez-del Arco P., Koipally J., Georgopoulos K.
Mol. Cell. Biol. 25:2688-2697(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-58 AND LYS-239, INTERACTION WITH SUMO1; PIAS2; PIAS3 AND SMARCA4, FUNCTION, MUTAGENESIS OF LYS-58; LYS-239; LYS-424 AND LYS-458.
[10]"Ikaros increases normal apoptosis in adult erythroid cells."
Pulte D., Lopez R.A., Baker S.T., Ward M., Ritchie E., Richardson C.A., O'Neill D.W., Bank A.
Am. J. Hematol. 81:12-18(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Ikaros confers early temporal competence to mouse retinal progenitor cells."
Elliott J., Jolicoeur C., Ramamurthy V., Cayouette M.
Neuron 60:26-39(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Recruitment of ikaros to pericentromeric heterochromatin is regulated by phosphorylation."
Gurel Z., Ronni T., Ho S., Kuchar J., Payne K.J., Turk C.W., Dovat S.
J. Biol. Chem. 283:8291-8300(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-13; THR-23; SER-63; SER-101 AND SER-293, FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-13; THR-23; SER-63; SER-101 AND SER-293.
[13]"Ikaros stability and pericentromeric localization are regulated by protein phosphatase 1."
Popescu M., Gurel Z., Ronni T., Song C., Hung K.Y., Payne K.J., Dovat S.
J. Biol. Chem. 284:13869-13880(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1CC, PHOSPHORYLATION, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF 465-LEU--LEU-467.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L03547 mRNA. Translation: AAA66193.1.
S74517 mRNA. Translation: AAB32248.2. Sequence problems.
S74518 mRNA. Translation: AAB32249.2.
S74708 mRNA. Translation: AAB32250.2.
PIRA56355.
I59572.
UniGeneMm.103545.

3D structure databases

ProteinModelPortalQ03267.
SMRQ03267. Positions 112-219, 455-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ03267. 12 interactions.
MINTMINT-4098529.

PTM databases

PhosphoSiteQ03267.

Proteomic databases

MaxQBQ03267.
PaxDbQ03267.
PRIDEQ03267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1342540. Ikzf1.

Phylogenomic databases

eggNOGNOG244744.
HOGENOMHOG000049114.
HOVERGENHBG004752.
InParanoidQ03267.

Gene expression databases

CleanExMM_IKZF1.
GenevestigatorQ03267.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 3 hits.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ03267.
SOURCESearch...

Entry information

Entry nameIKZF1_MOUSE
AccessionPrimary (citable) accession number: Q03267
Secondary accession number(s): Q64044, Q64045, Q64051
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: December 15, 1998
Last modified: June 11, 2014
This is version 128 of the entry and version 2 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

MGD cross-references

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