Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei158Required for both pericentromeric heterochromatin localization and complete DNA binding1
Sitei161Required for both pericentromeric heterochromatin localization and complete DNA binding1
Sitei187Required for both pericentromeric heterochromatin localization and DNA binding1

Regions

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

GO - Molecular functioni

  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • poly-pyrimidine tract binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding Source: MGI
  • transcription factor activity, sequence-specific DNA binding 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
  • establishment of protein localization Source: MGI
  • 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 gene expression 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 RNA polymerase II transcriptional preinitiation complex assembly Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription elongation from RNA polymerase II promoter 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
Proteomesi
  • UP000000589 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
  • nuclear pericentric heterochromatin Source: MGI
  • nucleus Source: MGI
  • pericentric heterochromatin Source: MGI
  • protein complex Source: MGI
  • protein-DNA 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)DescriptionActionsGraphical viewLength
Mutagenesisi13S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. 1 Publication1
Mutagenesisi13S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. 1 Publication1
Mutagenesisi23T → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. 1 Publication1
Mutagenesisi23T → D: Decreased binding to gamma satellites A and B by 3-fold. Little change in pericentromeric location. 1 Publication1
Mutagenesisi58K → R: Some loss of sumoylation. Complete loss of sumoylation, increased repressor activity but no change in pericentromeric heterochromatin location; when associated with R-240 and R-459. 1 Publication1
Mutagenesisi63S → A: No change in pericentromeric location. Greatly reduced phosphorylation; when associated with A-384; A-386; A-388; A392 and A-393. No effect on DNA-binding activity. Increased DNA-binding activity; when associated with A-384; A-386; A-388; A-392 and A-393. 2 Publications1
Mutagenesisi63S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 2 Publications1
Mutagenesisi101S → A: Abolishes phosphorylation. No change in pericentromeric location. 1 Publication1
Mutagenesisi101S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. 1 Publication1
Mutagenesisi140T → A: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-167 and A-195. 1 Publication1
Mutagenesisi140T → E: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-167 and D-195. 1 Publication1
Mutagenesisi152S → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi153F → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication1
Mutagenesisi154T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi155Q → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi156K → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. 1 Publication1
Mutagenesisi157G → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi158N → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication1
Mutagenesisi159L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi160L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi161R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication1
Mutagenesisi167S → A: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-140 and A-195. 1 Publication1
Mutagenesisi167S → E: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-140 and D-195. 1 Publication1
Mutagenesisi173K → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi178N → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi179Y → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication1
Mutagenesisi180A → L: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi181C → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi182R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi183R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. 1 Publication1
Mutagenesisi184R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi185D → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi186A → L: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi187L → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. 1 Publication1
Mutagenesisi188T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi189G → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi191L → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. 1 Publication1
Mutagenesisi192R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi193T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. 1 Publication1
Mutagenesisi195S → A: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-140 and A-167. 1 Publication1
Mutagenesisi195S → D: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-140 and E-167. 1 Publication1
Mutagenesisi239K → R: Some loss of sumoylation. Complete loss of sumoylation, increased repressor activity but no change in pericentromeric heterochromatin location.; when associated with R-58 and R-459. 1 Publication1
Mutagenesisi293S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. 1 Publication1
Mutagenesisi293S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. Decreased DNA binding affinity toward TdT by 3-fold. 1 Publication1
Mutagenesisi384S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-386; A-388; A-392 and A-393. and A-392. Further reduction in phosphorylation; when associated with A-63; A-386; A-388; A-392 and A-393. 1 Publication1
Mutagenesisi386S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-388; A-392 and A-393. Further reduction in phosphorylation; when associated with A-63; A-384; A-388; A-392 and A-393. 1 Publication1
Mutagenesisi388S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-392 and A-393. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-392 and A-393. 1 Publication1
Mutagenesisi392S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-388 and A-392. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-386 and A-388. 1 Publication1
Mutagenesisi393T → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-388 and A-392. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-388 and A-392. 1 Publication1
Mutagenesisi424K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi458K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi465 – 467LFL → AFA: Abolishes binding of PP1CC, decreases DNA binding, abolishes pericentromeric location, and results in IKAROS degradation. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000470951 – 517DNA-binding protein IkarosAdd BLAST517

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13Phosphoserine1 Publication1
Modified residuei23Phosphothreonine1 Publication1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei63PhosphoserineCombined sources2 Publications1
Modified residuei101Phosphoserine1 Publication1
Modified residuei140Phosphothreonine1 Publication1
Modified residuei167Phosphoserine1 Publication1
Modified residuei195Phosphoserine1 Publication1
Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei259PhosphoserineBy similarity1
Modified residuei287PhosphoserineBy similarity1
Modified residuei293Phosphoserine1 Publication1
Modified residuei357PhosphoserineBy similarity1
Modified residuei360PhosphoserineBy similarity1
Modified residuei384Phosphoserine1 Publication1
Modified residuei386Phosphoserine1 Publication1
Modified residuei388Phosphoserine1 Publication1
Modified residuei392Phosphoserine1 Publication1
Modified residuei393Phosphothreonine1 Publication1
Modified residuei397PhosphoserineCombined sources1
Modified residuei440PhosphoserineCombined sources1

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

EPDiQ03267.
MaxQBiQ03267.
PaxDbiQ03267.
PeptideAtlasiQ03267.
PRIDEiQ03267.

PTM databases

iPTMnetiQ03267.
PhosphoSitePlusiQ03267.

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

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ03267.
SMRiQ03267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni153 – 162Required for both high-affinity DNA binding and pericentromeric heterochromatin localization10
Regioni179 – 194Required for both high-affinity DNA binding and pericentromeric heterochromatin localizationAdd BLAST16
Regioni463 – 466Required for binding PP1CC4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi368 – 371Poly-Leu4

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
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. 1 hit.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti234 – 235VC → MY in AAB32250 (PubMed:7935426).Curated2
Sequence conflicti480 – 482Missing AA sequence (PubMed:7935426).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00685353M → VAYGADGFRDFHAIISDRGM in isoform II and isoform IV. Curated1
Alternative sequenceiVSP_00685554 – 282Missing in isoform I and isoform II. CuratedAdd BLAST229
Alternative sequenceiVSP_00685454 – 140Missing in isoform V. 1 PublicationAdd BLAST87
Alternative sequenceiVSP_006856141 – 282Missing in isoform III and isoform IV. CuratedAdd BLAST142

Sequence databases

Select the link destinations:
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ03267.
PhosphoSitePlusiQ03267.

Proteomic databases

EPDiQ03267.
MaxQBiQ03267.
PaxDbiQ03267.
PeptideAtlasiQ03267.
PRIDEiQ03267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1342540. Ikzf1.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
HOGENOMiHOG000049114.
HOVERGENiHBG004752.
InParanoidiQ03267.

Miscellaneous databases

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. 1 hit.
[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...

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: November 2, 2016
This is version 145 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

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 one 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.