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Q03267

- IKZF1_MOUSE

UniProt

Q03267 - IKZF1_MOUSE

Protein

DNA-binding protein Ikaros

Gene

Ikzf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    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).By similarity7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei158 – 1581Required for both pericentromeric heterochromatin localization and complete DNA binding
    Sitei161 – 1611Required for both pericentromeric heterochromatin localization and complete DNA binding
    Sitei187 – 1871Required for both pericentromeric heterochromatin localization and DNA binding

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri117 – 13923C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri144 – 16623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri172 – 19423C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri200 – 22324C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri457 – 47923C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri488 – 51225C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: MGI
    5. sequence-specific DNA binding Source: MGI
    6. sequence-specific DNA binding transcription factor activity Source: MGI
    7. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: MGI
    2. cell cycle Source: UniProtKB-KW
    3. chromatin modification Source: UniProtKB-KW
    4. forebrain development Source: MGI
    5. gland development Source: MGI
    6. hemopoiesis Source: MGI
    7. lymph node development Source: MGI
    8. natural killer cell differentiation Source: MGI
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    11. Peyer's patch development Source: MGI
    12. positive regulation of multicellular organism growth Source: MGI
    13. positive regulation of neutrophil differentiation Source: MGI
    14. positive regulation of NK T cell differentiation Source: MGI
    15. positive regulation of transcription, DNA-templated Source: MGI
    16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    17. regulation of transcription, DNA-templated Source: MGI
    18. retina development in camera-type eye Source: MGI
    19. T cell differentiation Source: MGI
    20. thymus development Source: MGI
    21. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Developmental protein, Repressor

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-binding protein Ikaros
    Alternative name(s):
    Ikaros family zinc finger protein 1
    Lymphoid transcription factor LyF-1
    Gene namesi
    Name:Ikzf1
    Synonyms:Ikaros, Lyf1, Zfpn1a1, Znfn1a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1342540. Ikzf1.

    Subcellular locationi

    Nucleus 4 Publications
    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.
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: MGI
    3. pericentric heterochromatin Source: MGI
    4. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. 2 Publications
    Mutagenesisi13 – 131S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. 2 Publications
    Mutagenesisi23 – 231T → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. 2 Publications
    Mutagenesisi23 – 231T → D: Decreased binding to gamma satellites A and B by 3-fold. Little change in pericentromeric location. 2 Publications
    Mutagenesisi58 – 581K → 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. 2 Publications
    Mutagenesisi63 – 631S → 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. 3 Publications
    Mutagenesisi63 – 631S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 3 Publications
    Mutagenesisi101 – 1011S → A: Abolishes phosphorylation. No change in pericentromeric location. 2 Publications
    Mutagenesisi101 – 1011S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 2 Publications
    Mutagenesisi140 – 1401T → A: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-167 and A-195. 2 Publications
    Mutagenesisi140 – 1401T → E: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-167 and D-195. 2 Publications
    Mutagenesisi152 – 1521S → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi153 – 1531F → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 2 Publications
    Mutagenesisi154 – 1541T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi155 – 1551Q → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 2 Publications
    Mutagenesisi156 – 1561K → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. 2 Publications
    Mutagenesisi157 – 1571G → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 2 Publications
    Mutagenesisi158 – 1581N → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 2 Publications
    Mutagenesisi159 – 1591L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi160 – 1601L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi161 – 1611R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 2 Publications
    Mutagenesisi167 – 1671S → 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. 2 Publications
    Mutagenesisi167 – 1671S → 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. 2 Publications
    Mutagenesisi173 – 1731K → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi178 – 1781N → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi179 – 1791Y → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 2 Publications
    Mutagenesisi180 – 1801A → L: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 2 Publications
    Mutagenesisi181 – 1811C → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi182 – 1821R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi183 – 1831R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 2 Publications
    Mutagenesisi184 – 1841R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi185 – 1851D → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 2 Publications
    Mutagenesisi186 – 1861A → L: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 2 Publications
    Mutagenesisi187 – 1871L → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 2 Publications
    Mutagenesisi188 – 1881T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi189 – 1891G → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi191 – 1911L → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 2 Publications
    Mutagenesisi192 – 1921R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi193 – 1931T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 2 Publications
    Mutagenesisi195 – 1951S → 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. 2 Publications
    Mutagenesisi195 – 1951S → 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. 2 Publications
    Mutagenesisi239 – 2391K → 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. 2 Publications
    Mutagenesisi293 – 2931S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. 2 Publications
    Mutagenesisi293 – 2931S → 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. 2 Publications
    Mutagenesisi384 – 3841S → 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. 2 Publications
    Mutagenesisi386 – 3861S → 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. 2 Publications
    Mutagenesisi388 – 3881S → 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. 2 Publications
    Mutagenesisi392 – 3921S → 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. 2 Publications
    Mutagenesisi393 – 3931T → 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. 2 Publications
    Mutagenesisi424 – 4241K → R: No effect on sumoylation. 2 Publications
    Mutagenesisi458 – 4581K → R: No effect on sumoylation. 2 Publications
    Mutagenesisi465 – 4673LFL → AFA: Abolishes binding of PP1CC, decreases DNA binding, abolishes pericentromeric location, and results in IKAROS degradation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 517517DNA-binding protein IkarosPRO_0000047095Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphoserine2 Publications
    Modified residuei23 – 231Phosphothreonine2 Publications
    Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei63 – 631Phosphoserine3 Publications
    Modified residuei101 – 1011Phosphoserine2 Publications
    Modified residuei140 – 1401Phosphothreonine2 Publications
    Modified residuei167 – 1671Phosphoserine2 Publications
    Modified residuei195 – 1951Phosphoserine2 Publications
    Cross-linki239 – 239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei259 – 2591PhosphoserineBy similarity
    Modified residuei293 – 2931Phosphoserine2 Publications
    Modified residuei357 – 3571PhosphoserineBy similarity
    Modified residuei360 – 3601PhosphoserineBy similarity
    Modified residuei384 – 3841Phosphoserine2 Publications
    Modified residuei386 – 3861Phosphoserine2 Publications
    Modified residuei388 – 3881Phosphoserine2 Publications
    Modified residuei392 – 3921Phosphoserine2 Publications
    Modified residuei393 – 3931Phosphothreonine2 Publications

    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

    MaxQBiQ03267.
    PaxDbiQ03267.
    PRIDEiQ03267.

    PTM databases

    PhosphoSiteiQ03267.

    Expressioni

    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

    Developmental stagei

    First detected in fetal liver and embryonic thymus.1 Publication

    Gene expression databases

    CleanExiMM_IKZF1.
    GenevestigatoriQ03267.

    Interactioni

    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. 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.By similarity4 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    IntActiQ03267. 12 interactions.
    MINTiMINT-4098529.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03267.
    SMRiQ03267. Positions 112-219, 455-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni153 – 16210Required for both high-affinity DNA binding and pericentromeric heterochromatin localization
    Regioni179 – 19416Required for both high-affinity DNA binding and pericentromeric heterochromatin localizationAdd
    BLAST
    Regioni463 – 4664Required for binding PP1CC

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi368 – 3714Poly-Leu

    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.

    Sequence similaritiesi

    Contains 6 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri117 – 13923C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri144 – 16623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri172 – 19423C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri200 – 22324C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri457 – 47923C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri488 – 51225C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244744.
    HOGENOMiHOG000049114.
    HOVERGENiHBG004752.
    InParanoidiQ03267.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 3 hits.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 6 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 5 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    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

    MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD    50
    RGMGSNVKVE TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG 100
    SSALSGVGGI RLPNGKLKCD ICGIVCIGPN VLMVHKRSHT ERPFQCNQCG 150
    ASFTQKGNLL RHIKLHSGEK PFKCHLCNYA CRRRDALTGH LRTHSVGKPH 200
    KCGYCGRSYK QRSSLEEHKE RCHNYLESMG LPGVCPVIKE ETNHNEMAED 250
    LCKIGAERSL VLDRLASNVA KRKSSMPQKF LGDKCLSDMP YDSANYEKED 300
    MMTSHVMDQA INNAINYLGA ESLRPLVQTP PGSSEVVPVI SSMYQLHKPP 350
    SDGPPRSNHS AQDAVDNLLL LSKAKSVSSE REASPSNSCQ DSTDTESNAE 400
    EQRSGLIYLT NHINPHARNG LALKEEQRAY EVLRAASENS QDAFRVVSTS 450
    GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG CHGFRDPFEC NMCGYHSQDR 500
    YEFSSHITRG EHRYHLS 517
    Length:517
    Mass (Da):57,336
    Last modified:December 15, 1998 - v2
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2352VC → MY in AAB32250. (PubMed:7935426)Curated
    Sequence conflicti480 – 4823Missing AA sequence (PubMed:7935426)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei53 – 531M → VAYGADGFRDFHAIISDRGM in isoform II and isoform IV. CuratedVSP_006853
    Alternative sequencei54 – 282229Missing in isoform I and isoform II. CuratedVSP_006855Add
    BLAST
    Alternative sequencei54 – 14087Missing in isoform V. 1 PublicationVSP_006854Add
    BLAST
    Alternative sequencei141 – 282142Missing in isoform III and isoform IV. CuratedVSP_006856Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03547 mRNA. Translation: AAA66193.1 .
    S74517 mRNA. Translation: AAB32248.2 . Sequence problems.
    S74518 mRNA. Translation: AAB32249.2 .
    S74708 mRNA. Translation: AAB32250.2 .
    PIRi A56355.
    I59572.
    UniGenei Mm.103545.

    3D structure databases

    ProteinModelPortali Q03267.
    SMRi Q03267. Positions 112-219, 455-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q03267. 12 interactions.
    MINTi MINT-4098529.

    PTM databases

    PhosphoSitei Q03267.

    Proteomic databases

    MaxQBi Q03267.
    PaxDbi Q03267.
    PRIDEi Q03267.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:1342540. Ikzf1.

    Phylogenomic databases

    eggNOGi NOG244744.
    HOGENOMi HOG000049114.
    HOVERGENi HBG004752.
    InParanoidi Q03267.

    Miscellaneous databases

    PROi Q03267.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_IKZF1.
    Genevestigatori Q03267.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 3 hits.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 6 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 5 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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.

    Entry informationi

    Entry nameiIKZF1_MOUSE
    AccessioniPrimary (citable) accession number: Q03267
    Secondary accession number(s): Q64044, Q64045, Q64051
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3