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Q13422

- IKZF1_HUMAN

UniProt

Q13422 - IKZF1_HUMAN

Protein

DNA-binding protein Ikaros

Gene

IKZF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. Confers early temporal competence to retinal progenitor cells (RPCs) By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei159 – 1591Required for both pericentromeric heterochromatin localization and complete DNA bindingBy similarity
    Sitei162 – 1621Required for both pericentromeric heterochromatin localization and complete DNA bindingBy similarity
    Sitei188 – 1881Required for both pericentromeric heterochromatin localization and DNA bindingBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri117 – 13923C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri145 – 16723C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri173 – 19523C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri201 – 22424C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri462 – 48423C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri490 – 51425C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. sequence-specific DNA binding Source: Ensembl
    4. sequence-specific DNA binding transcription factor activity Source: Ensembl

    GO - Biological processi

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

    Enzyme and pathway databases

    SignaLinkiQ13422.

    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:IK1, IKAROS, LYF1, ZNFN1A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:13176. IKZF1.

    Subcellular locationi

    Nucleus 1 Publication
    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 By similarity.By similarity
    Isoform Ik2 : 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 By similarity.By similarity
    Isoform Ik6 : Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. pericentric heterochromatin Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in IKZF1 are frequent occurrences (28.6%) in acute lymphoblasic leukemia (ALL). Such alterations or deletions lead to poor prognosis for ALL.
    Chromosomal aberrations involving IKZF1 are a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;7)(q27;p12), with BCL6.

    Organism-specific databases

    Orphaneti317473. Pancytopenia due to IKZF1 mutations.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA37748.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519DNA-binding protein IkarosPRO_0000047094Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei23 – 231PhosphothreonineBy similarity
    Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei63 – 631Phosphoserine1 Publication
    Modified residuei101 – 1011PhosphoserineBy similarity
    Modified residuei140 – 1401PhosphothreonineBy similarity
    Modified residuei168 – 1681PhosphoserineBy similarity
    Modified residuei196 – 1961PhosphoserineBy similarity
    Cross-linki241 – 241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei258 – 2581Phosphoserine1 Publication
    Modified residuei261 – 2611Phosphoserine1 Publication
    Modified residuei295 – 2951PhosphoserineBy similarity
    Modified residuei361 – 3611Phosphoserine2 Publications
    Modified residuei364 – 3641Phosphoserine2 Publications
    Modified residuei389 – 3891PhosphoserineBy similarity
    Modified residuei391 – 3911PhosphoserineBy similarity
    Modified residuei393 – 3931PhosphoserineBy similarity
    Modified residuei397 – 3971PhosphoserineBy similarity
    Modified residuei398 – 3981PhosphothreonineBy similarity

    Post-translational modificationi

    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-295 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 similarity. Phosphorylation at Ser-361 and Ser-364 downstream of SYK induces nuclear translocation.By similarity2 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 By similarity.By similarity
    Polyubiquitinated.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13422.
    PaxDbiQ13422.
    PRIDEiQ13422.

    PTM databases

    PhosphoSiteiQ13422.

    Expressioni

    Tissue specificityi

    Abundantly expressed in thymus, spleen and peripheral blood Leukocytes and lymph nodes. Lower expression in bone marrow and small intestine.

    Gene expression databases

    ArrayExpressiQ13422.
    BgeeiQ13422.
    CleanExiHS_IKZF1.
    GenevestigatoriQ13422.

    Organism-specific databases

    HPAiCAB009247.

    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 By similarity. 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 similarity.By similarity

    Protein-protein interaction databases

    BioGridi115604. 38 interactions.
    IntActiQ13422. 18 interactions.
    MINTiMINT-129252.
    STRINGi9606.ENSP00000331614.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13422.
    SMRiQ13422. Positions 112-259, 460-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni154 – 16310Required for both high-affinity DNA binding and pericentromeric heterochromatin localizationBy similarity
    Regioni180 – 19516Required for both high-affinity DNA binding and pericentromeric heterochromatin localizationBy similarityAdd
    BLAST
    Regioni468 – 4714Required for binding PP1CCBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi373 – 3764Poly-Leu

    Domaini

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

    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 fingeri145 – 16723C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri173 – 19523C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri201 – 22424C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri462 – 48423C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri490 – 51425C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244744.
    HOVERGENiHBG004752.
    InParanoidiQ13422.
    KOiK09220.
    OMAiGDKCLSD.
    PhylomeDBiQ13422.
    TreeFamiTF331189.

    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]
    SMARTiSM00355. ZnF_C2H2. 6 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 5 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform Ik1 (identifier: Q13422-1) [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

    MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD    50
    RVVASNVKVE TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG 100
    SSALSGVGGI RLPNGKLKCD ICGIICIGPN VLMVHKRSHT GERPFQCNQC 150
    GASFTQKGNL LRHIKLHSGE KPFKCHLCNY ACRRRDALTG HLRTHSVGKP 200
    HKCGYCGRSY KQRSSLEEHK ERCHNYLESM GLPGTLYPVI KEETNHSEMA 250
    EDLCKIGSER SLVLDRLASN VAKRKSSMPQ KFLGDKGLSD TPYDSSASYE 300
    KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL 350
    HKPLAEGTPR SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT 400
    ESNNEEQRSG LIYLTNHIAP HARNGLSLKE EHRAYDLLRA ASENSQDALR 450
    VVSTSGEQMK VYKCEHCRVL FLDHVMYTIH MGCHGFRDPF ECNMCGYHSQ 500
    DRYEFSSHIT RGEHRFHMS 519
    Length:519
    Mass (Da):57,528
    Last modified:November 1, 1996 - v1
    Checksum:i7B0129C4E3FE41A8
    GO
    Isoform Ik2 (identifier: Q13422-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:432
    Mass (Da):48,289
    Checksum:iE8E57F8BF5B306E6
    GO
    Isoform Ik3 (identifier: Q13422-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         197-283: Missing.

    Show »
    Length:432
    Mass (Da):47,634
    Checksum:i1093D253341A95E8
    GO
    Isoform Ik4 (identifier: Q13422-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-53: Missing.
         197-283: Missing.

    Show »
    Length:388
    Mass (Da):43,093
    Checksum:i137C942A5278A9F0
    GO
    Isoform Ik5 (identifier: Q13422-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         141-283: Missing.

    Show »
    Length:376
    Mass (Da):41,229
    Checksum:i0B060551CB3E0082
    GO
    Isoform Ik6 (identifier: Q13422-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         54-283: Missing.

    Show »
    Length:289
    Mass (Da):31,989
    Checksum:iEB96A15185C62A18
    GO
    Isoform Ik7 (identifier: Q13422-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         197-238: Missing.

    Show »
    Length:477
    Mass (Da):52,706
    Checksum:iB19FE76450EA40E4
    GO
    Isoform Ikx (identifier: Q13422-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         197-238: Missing.
         260-268: RSLVLDRLA → ISRAGQTSK
         269-519: Missing.

    Show »
    Length:226
    Mass (Da):24,470
    Checksum:i2BB5B70D38F73264
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 122QV → FS in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti214 – 2141S → T in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti245 – 2451N → K in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti296 – 2961Missing in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti298 – 2981S → T in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti352 – 3554KPLA → RRS in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti372 – 3721N → Y in AAB50683. (PubMed:8543809)Curated
    Sequence conflicti420 – 4267PHARNGL → RRAQRV in AAB50683. (PubMed:8543809)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei10 – 5344Missing in isoform Ik4. CuratedVSP_006847Add
    BLAST
    Alternative sequencei54 – 283230Missing in isoform Ik6. CuratedVSP_006849Add
    BLAST
    Alternative sequencei54 – 14087Missing in isoform Ik2. 1 PublicationVSP_006848Add
    BLAST
    Alternative sequencei141 – 283143Missing in isoform Ik5. CuratedVSP_006852Add
    BLAST
    Alternative sequencei197 – 28387Missing in isoform Ik3 and isoform Ik4. CuratedVSP_006850Add
    BLAST
    Alternative sequencei197 – 23842Missing in isoform Ik7 and isoform Ikx. 3 PublicationsVSP_006851Add
    BLAST
    Alternative sequencei260 – 2689RSLVLDRLA → ISRAGQTSK in isoform Ikx. 1 PublicationVSP_053404
    Alternative sequencei269 – 519251Missing in isoform Ikx. 1 PublicationVSP_053405Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40462 mRNA. Translation: AAC50459.1.
    S80876 mRNA. Translation: AAB50683.1.
    AY377974 mRNA. Translation: AAR84585.1.
    AK303586 mRNA. Translation: BAG64603.1.
    BT009836 mRNA. Translation: AAP88838.1.
    AC124014 Genomic DNA. No translation available.
    AC233268 Genomic DNA. No translation available.
    CH471128 Genomic DNA. Translation: EAW60977.1.
    CH471128 Genomic DNA. Translation: EAW60978.1.
    CH471128 Genomic DNA. Translation: EAW60981.1.
    CH236955 Genomic DNA. Translation: EAL23900.1.
    CH471128 Genomic DNA. Translation: EAW60979.1.
    BC018349 mRNA. Translation: AAH18349.1.
    CCDSiCCDS59055.1. [Q13422-7]
    CCDS69299.1. [Q13422-5]
    RefSeqiNP_001207694.1. NM_001220765.2. [Q13422-7]
    NP_001207696.1. NM_001220767.2.
    NP_001207697.1. NM_001220768.2. [Q13422-3]
    NP_001207699.1. NM_001220770.2.
    NP_001207700.1. NM_001220771.2. [Q13422-5]
    NP_001278766.1. NM_001291837.1. [Q13422-7]
    NP_001278767.1. NM_001291838.1. [Q13422-2]
    NP_001278768.1. NM_001291839.1.
    NP_001278769.1. NM_001291840.1. [Q13422-6]
    NP_001278770.1. NM_001291841.1.
    NP_001278771.1. NM_001291842.1.
    NP_001278772.1. NM_001291843.1.
    NP_001278773.1. NM_001291844.1.
    NP_006051.1. NM_006060.5. [Q13422-1]
    UniGeneiHs.435949.
    Hs.488251.
    Hs.731495.

    Genome annotation databases

    EnsembliENST00000331340; ENSP00000331614; ENSG00000185811. [Q13422-1]
    ENST00000343574; ENSP00000342750; ENSG00000185811. [Q13422-2]
    ENST00000346667; ENSP00000340080; ENSG00000185811. [Q13422-6]
    ENST00000349824; ENSP00000342485; ENSG00000185811. [Q13422-5]
    ENST00000357364; ENSP00000349928; ENSG00000185811. [Q13422-3]
    ENST00000359197; ENSP00000352123; ENSG00000185811. [Q13422-7]
    ENST00000438033; ENSP00000396554; ENSG00000185811. [Q13422-2]
    ENST00000439701; ENSP00000413025; ENSG00000185811. [Q13422-7]
    ENST00000440768; ENSP00000401507; ENSG00000185811. [Q13422-8]
    GeneIDi10320.
    KEGGihsa:10320.
    UCSCiuc003tow.4. human. [Q13422-1]
    uc003tox.4. human. [Q13422-7]
    uc003tpa.4. human. [Q13422-6]
    uc011kck.2. human. [Q13422-2]
    uc022acq.1. human. [Q13422-5]
    uc022acs.1. human. [Q13422-4]
    uc022acx.1. human. [Q13422-3]

    Polymorphism databases

    DMDMi3913926.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40462 mRNA. Translation: AAC50459.1 .
    S80876 mRNA. Translation: AAB50683.1 .
    AY377974 mRNA. Translation: AAR84585.1 .
    AK303586 mRNA. Translation: BAG64603.1 .
    BT009836 mRNA. Translation: AAP88838.1 .
    AC124014 Genomic DNA. No translation available.
    AC233268 Genomic DNA. No translation available.
    CH471128 Genomic DNA. Translation: EAW60977.1 .
    CH471128 Genomic DNA. Translation: EAW60978.1 .
    CH471128 Genomic DNA. Translation: EAW60981.1 .
    CH236955 Genomic DNA. Translation: EAL23900.1 .
    CH471128 Genomic DNA. Translation: EAW60979.1 .
    BC018349 mRNA. Translation: AAH18349.1 .
    CCDSi CCDS59055.1. [Q13422-7 ]
    CCDS69299.1. [Q13422-5 ]
    RefSeqi NP_001207694.1. NM_001220765.2. [Q13422-7 ]
    NP_001207696.1. NM_001220767.2.
    NP_001207697.1. NM_001220768.2. [Q13422-3 ]
    NP_001207699.1. NM_001220770.2.
    NP_001207700.1. NM_001220771.2. [Q13422-5 ]
    NP_001278766.1. NM_001291837.1. [Q13422-7 ]
    NP_001278767.1. NM_001291838.1. [Q13422-2 ]
    NP_001278768.1. NM_001291839.1.
    NP_001278769.1. NM_001291840.1. [Q13422-6 ]
    NP_001278770.1. NM_001291841.1.
    NP_001278771.1. NM_001291842.1.
    NP_001278772.1. NM_001291843.1.
    NP_001278773.1. NM_001291844.1.
    NP_006051.1. NM_006060.5. [Q13422-1 ]
    UniGenei Hs.435949.
    Hs.488251.
    Hs.731495.

    3D structure databases

    ProteinModelPortali Q13422.
    SMRi Q13422. Positions 112-259, 460-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115604. 38 interactions.
    IntActi Q13422. 18 interactions.
    MINTi MINT-129252.
    STRINGi 9606.ENSP00000331614.

    PTM databases

    PhosphoSitei Q13422.

    Polymorphism databases

    DMDMi 3913926.

    Proteomic databases

    MaxQBi Q13422.
    PaxDbi Q13422.
    PRIDEi Q13422.

    Protocols and materials databases

    DNASUi 10320.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331340 ; ENSP00000331614 ; ENSG00000185811 . [Q13422-1 ]
    ENST00000343574 ; ENSP00000342750 ; ENSG00000185811 . [Q13422-2 ]
    ENST00000346667 ; ENSP00000340080 ; ENSG00000185811 . [Q13422-6 ]
    ENST00000349824 ; ENSP00000342485 ; ENSG00000185811 . [Q13422-5 ]
    ENST00000357364 ; ENSP00000349928 ; ENSG00000185811 . [Q13422-3 ]
    ENST00000359197 ; ENSP00000352123 ; ENSG00000185811 . [Q13422-7 ]
    ENST00000438033 ; ENSP00000396554 ; ENSG00000185811 . [Q13422-2 ]
    ENST00000439701 ; ENSP00000413025 ; ENSG00000185811 . [Q13422-7 ]
    ENST00000440768 ; ENSP00000401507 ; ENSG00000185811 . [Q13422-8 ]
    GeneIDi 10320.
    KEGGi hsa:10320.
    UCSCi uc003tow.4. human. [Q13422-1 ]
    uc003tox.4. human. [Q13422-7 ]
    uc003tpa.4. human. [Q13422-6 ]
    uc011kck.2. human. [Q13422-2 ]
    uc022acq.1. human. [Q13422-5 ]
    uc022acs.1. human. [Q13422-4 ]
    uc022acx.1. human. [Q13422-3 ]

    Organism-specific databases

    CTDi 10320.
    GeneCardsi GC07P050343.
    HGNCi HGNC:13176. IKZF1.
    HPAi CAB009247.
    MIMi 603023. gene.
    neXtProti NX_Q13422.
    Orphaneti 317473. Pancytopenia due to IKZF1 mutations.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBi PA37748.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244744.
    HOVERGENi HBG004752.
    InParanoidi Q13422.
    KOi K09220.
    OMAi GDKCLSD.
    PhylomeDBi Q13422.
    TreeFami TF331189.

    Enzyme and pathway databases

    SignaLinki Q13422.

    Miscellaneous databases

    ChiTaRSi IKZF1. human.
    GeneWikii IKZF1.
    GenomeRNAii 10320.
    NextBioi 39123.
    PROi Q13422.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13422.
    Bgeei Q13422.
    CleanExi HS_IKZF1.
    Genevestigatori Q13422.

    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 ]
    SMARTi SM00355. ZnF_C2H2. 6 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 5 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of hIk-1, a cDNA encoding a human homologue of mouse Ikaros/LyF-1."
      Nietfeld W., Meyerhans A.
      Immunol. Lett. 49:139-141(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Bone marrow.
    2. "The Ikaros gene encodes a family of lymphocyte-restricted zinc finger DNA binding proteins, highly conserved in human and mouse."
      Molnar A., Wu P., Largespada D.A., Vortkamp A., Scherer S., Copeland N.G., Jenkins N.A., Bruns G., Georgopoulos K.
      J. Immunol. 156:585-592(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Molecular misreading is involved in generation of Ikaros diversity."
      Sanchez-Tapia E.M., Rodriguez R.E., Gonzalez-Sarmiento R.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IKX).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK2).
      Tissue: Thymus.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
      Tissue: Lymph.
    10. "Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes."
      Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.
      Immunity 10:345-355(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NURD COMPLEX, IDENTIFICATION IN THE BAF COMPLEX, INTERACTION WITH SMARCA4 AND CHD4, FUNCTION.
    11. "The Ikaros gene, a central regulator of lymphoid differentiation, fuses to the BCL6 gene as a result of t(3;7)(q27;p12) translocation in a patient with diffuse large B-cell lymphoma."
      Hosokawa Y., Maeda Y., Ichinohasama R., Miura I., Taniwaki M., Seto M.
      Blood 95:2719-2721(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, CHROMOSOMAL TRANSLOCATION WITH BCL6.
    12. "Eos and pegasus, two members of the Ikaros family of proteins with distinct DNA binding activities."
      Perdomo J., Holmes M., Chong B., Crossley M.
      J. Biol. Chem. 275:38347-38354(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKZF4 AND IKZF5.
    13. "Human gamma-satellite DNA maintains open chromatin structure and protects a transgene from epigenetic silencing."
      Kim J.-H., Ebersole T., Kouprina N., Noskov V.N., Ohzeki J.-I., Masumoto H., Mravinac B., Sullivan B.A., Pavlicek A., Dovat S., Pack S.D., Kwon Y.-W., Flanagan P.T., Loukinov D., Lobanenkov V., Larionov V.
      Genome Res. 19:533-544(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    14. Cited for: INVOLVEMENT IN ACUTE LYMPHOBLASIC LEUKEMIA.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-258; SER-261; SER-361 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Serine phosphorylation by SYK is critical for nuclear localization and transcription factor function of Ikaros."
      Uckun F.M., Ma H., Zhang J., Ozer Z., Dovat S., Mao C., Ishkhanian R., Goodman P., Qazi S.
      Proc. Natl. Acad. Sci. U.S.A. 109:18072-18077(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-361 AND SER-364 BY SYK, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiIKZF1_HUMAN
    AccessioniPrimary (citable) accession number: Q13422
    Secondary accession number(s): A4D260
    , B4E0Z1, D3DVM5, O00598, Q53XL2, Q69BM4, Q8WVA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3