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Protein

DNA-binding protein Ikaros

Gene

Ikzf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)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

  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: MGI
  • sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding transcription factor activity Source: MGI
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • amacrine cell differentiation Source: MGI
  • B cell differentiation Source: MGI
  • cell cycle Source: UniProtKB-KW
  • chromatin modification Source: UniProtKB-KW
  • erythrocyte differentiation Source: UniProtKB
  • forebrain development Source: MGI
  • gland development Source: MGI
  • hemopoiesis Source: MGI
  • lymph node development Source: MGI
  • lymphocyte differentiation Source: UniProtKB
  • natural killer cell differentiation Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • Peyer's patch development Source: MGI
  • positive regulation of B cell differentiation Source: MGI
  • positive regulation of multicellular organism growth Source: MGI
  • positive regulation of neutrophil differentiation Source: MGI
  • positive regulation of NK T cell differentiation Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • retina development in camera-type eye Source: MGI
  • retinal bipolar neuron differentiation Source: MGI
  • T cell differentiation Source: MGI
  • thymus development Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1342540. Ikzf1.

Subcellular locationi

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

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: MGI
  • pericentric heterochromatin Source: MGI
  • protein complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

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. 1 Publication
Mutagenesisi13 – 131S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. 1 Publication
Mutagenesisi23 – 231T → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. 1 Publication
Mutagenesisi23 – 231T → D: Decreased binding to gamma satellites A and B by 3-fold. Little change in pericentromeric location. 1 Publication
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. 1 Publication
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. 2 Publications
Mutagenesisi63 – 631S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 2 Publications
Mutagenesisi101 – 1011S → A: Abolishes phosphorylation. No change in pericentromeric location. 1 Publication
Mutagenesisi101 – 1011S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 1 Publication
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. 1 Publication
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. 1 Publication
Mutagenesisi152 – 1521S → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi153 – 1531F → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication
Mutagenesisi154 – 1541T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi155 – 1551Q → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication
Mutagenesisi156 – 1561K → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. 1 Publication
Mutagenesisi157 – 1571G → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication
Mutagenesisi158 – 1581N → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication
Mutagenesisi159 – 1591L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi160 – 1601L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi161 – 1611R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication
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. 1 Publication
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. 1 Publication
Mutagenesisi173 – 1731K → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi178 – 1781N → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi179 – 1791Y → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication
Mutagenesisi180 – 1801A → L: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication
Mutagenesisi181 – 1811C → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi182 – 1821R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi183 – 1831R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication
Mutagenesisi184 – 1841R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi185 – 1851D → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication
Mutagenesisi186 – 1861A → L: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication
Mutagenesisi187 – 1871L → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication
Mutagenesisi188 – 1881T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi189 – 1891G → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi191 – 1911L → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication
Mutagenesisi192 – 1921R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
Mutagenesisi193 – 1931T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
Mutagenesisi424 – 4241K → R: No effect on sumoylation. 1 Publication
Mutagenesisi458 – 4581K → R: No effect on sumoylation. 1 Publication
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 – 131Phosphoserine1 Publication
Modified residuei23 – 231Phosphothreonine1 Publication
Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei63 – 631Phosphoserine2 Publications
Modified residuei101 – 1011Phosphoserine1 Publication
Modified residuei140 – 1401Phosphothreonine1 Publication
Modified residuei167 – 1671Phosphoserine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication
Cross-linki239 – 239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei259 – 2591PhosphoserineBy similarity
Modified residuei293 – 2931Phosphoserine1 Publication
Modified residuei357 – 3571PhosphoserineBy similarity
Modified residuei360 – 3601PhosphoserineBy similarity
Modified residuei384 – 3841Phosphoserine1 Publication
Modified residuei386 – 3861Phosphoserine1 Publication
Modified residuei388 – 3881Phosphoserine1 Publication
Modified residuei392 – 3921Phosphoserine1 Publication
Modified residuei393 – 3931Phosphothreonine1 Publication
Modified residuei440 – 4401PhosphoserineBy similarity

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.

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.
STRINGi10090.ENSMUSP00000075992.

Structurei

3D structure databases

ProteinModelPortaliQ03267.
SMRiQ03267. Positions 112-219, 455-489.
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. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD
60 70 80 90 100
RGMGSNVKVE TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG
110 120 130 140 150
SSALSGVGGI RLPNGKLKCD ICGIVCIGPN VLMVHKRSHT ERPFQCNQCG
160 170 180 190 200
ASFTQKGNLL RHIKLHSGEK PFKCHLCNYA CRRRDALTGH LRTHSVGKPH
210 220 230 240 250
KCGYCGRSYK QRSSLEEHKE RCHNYLESMG LPGVCPVIKE ETNHNEMAED
260 270 280 290 300
LCKIGAERSL VLDRLASNVA KRKSSMPQKF LGDKCLSDMP YDSANYEKED
310 320 330 340 350
MMTSHVMDQA INNAINYLGA ESLRPLVQTP PGSSEVVPVI SSMYQLHKPP
360 370 380 390 400
SDGPPRSNHS AQDAVDNLLL LSKAKSVSSE REASPSNSCQ DSTDTESNAE
410 420 430 440 450
EQRSGLIYLT NHINPHARNG LALKEEQRAY EVLRAASENS QDAFRVVSTS
460 470 480 490 500
GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG CHGFRDPFEC NMCGYHSQDR
510
YEFSSHITRG EHRYHLS
Length:517
Mass (Da):57,336
Last modified:December 15, 1998 - v2
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:
EMBLi
GenBanki
DDBJi
Links Updated
L03547 mRNA. Translation: AAA66193.1.
S74517 mRNA. Translation: AAB32248.2. Sequence problems.
S74518 mRNA. Translation: AAB32249.2.
S74708 mRNA. Translation: AAB32250.2.
PIRiA56355.
I59572.
UniGeneiMm.103545.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ03267.
SMRiQ03267. Positions 112-219, 455-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ03267. 12 interactions.
MINTiMINT-4098529.
STRINGi10090.ENSMUSP00000075992.

PTM databases

PhosphoSiteiQ03267.

Proteomic databases

MaxQBiQ03267.
PaxDbiQ03267.
PRIDEiQ03267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1342540. Ikzf1.

Phylogenomic databases

eggNOGiNOG244744.
HOGENOMiHOG000049114.
HOVERGENiHBG004752.
InParanoidiQ03267.

Miscellaneous databases

PROiQ03267.
SOURCEiSearch...

Gene expression databases

CleanExiMM_IKZF1.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.