Q03267 (IKZF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-binding protein Ikaros

Alternative name(s):
Ikaros family zinc finger protein 1
Lymphoid transcription factor LyF-1

Gene names

Name:	Ikzf1
Synonyms:	Ikaros, Lyf1, Zfpn1a1, Znfn1a1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription regulator of hematopoietic cell differentiation. Binds gamma-satellite DNA. Binds with higher affinity to gamma satellite A. Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (terminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta-globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells By similarity. Confers early temporal competence to retinal progenitor cells (RPCs). Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Subunit structure	Heterodimer with other IKAROS family members. Interacts with IKZF4 AND IKZF5 By similarity. Component of the chromatin-remodeling NuRD repressor complex which includes at least HDAC1, HDAC2, RBBP4, RBBP7, IKZF1, MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4. Interacts directly with the CHD4 component of the NuRD complex. Component of the BAF (SWI/SNF) gene activator complex which includes ACTB, ARID1A, ARID1B, IKZF1, ARID1A, ARID1B, SMARCA2, SMARCA4 and at least one BAF subunit. Interacts directly with the SMARCA4 component of the BAF complex. Interacts with SUMO1; the interaction sumoylates IKAROS, promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform alpha); the interaction promotes sumoylation and reduces transcription repression. Interacts, to a lesser extent, with PIAS3. Interacts with PPP1CC; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with IKZF3. Ref.3 Ref.6 Ref.9 Ref.13
Subcellular location	Nucleus. Note: In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events. Ref.5 Ref.7 Ref.12 Ref.13 Isoform V: Nucleus. Note: In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events. Ref.5 Ref.7 Ref.12 Ref.13 Isoform I: Cytoplasm Ref.5 Ref.7 Ref.12 Ref.13.
Tissue specificity	Strongly expressed in T-cells and their progenitors,in B-cells, and in all early embryonic retinal progenitor cells (RPCs). Isoforms V and VI are the predominant isoforms in lymphocytes. Ref.1 Ref.2 Ref.11
Developmental stage	First detected in fetal liver and embryonic thymus. Ref.1
Domain	The N-terminal zinc-fingers 2 and 3 are required for DNA binding as well as for targeting IKFZ1 to pericentromeric heterochromatin. The C-terminal zinc-finger domain is required for dimerization.
Post-translational modification	Phosphorylation at Ser-357 and Ser-360 downstream of SYK induces nuclear translocation By similarity. Phosphorylation controls cell-cycle progression from late G1 stage to S stage. Hyperphosphorylated during G2/M phase. Dephosphorylated state during late G1 phase. Phosphorylation on Thr-140 is required for DNA and pericentromeric location during mitosis. CK2 is the main kinase, in vitro. GSK3 and CDK may also contribute to phosphorylation of the C-terminal serine and threonine residues. Phosphorylation on these C-terminal residues reduces the DNA-binding ability. Phosphorylation/dephosphorylation events on Ser-13 and Ser-293 regulate TDT expression during thymocyte differentiation. Dephosphorylation by protein phosphatase 1 regulates stability and pericentromeric heterochromatin location. Phosphorylated in both lymphoid and non-lymphoid tissues. Ref.7 Ref.8 Ref.12 Ref.13 Sumoylated. Simulataneous sumoylation on the 2 sites results in a loss of both HDAC-dependent and HDAC-independent repression. Has no effect on pericentromeric heterochromatin location. Desumoylated by SENP1. Ref.9 Polyubiquitinated.
Disruption phenotype	Defects in hemopoietic stem cell activity. Progressive reduction in multipotent CFU-S14 (colony-forming unit-spleen) progenitors and the earliest erythroid-restricted precursors (BFU-E). Ref.4
Sequence similarities	Belongs to the Ikaros C2H2-type zinc-finger protein family. Contains 6 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Chromatin regulator Developmental protein Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from mutant phenotype PubMed 7923373. Source: MGI Peyer's patch development Inferred from mutant phenotype PubMed 7923373. Source: MGI T cell differentiation Inferred from mutant phenotype PubMed 7923373. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW forebrain development Inferred from mutant phenotype PubMed 15841184PubMed 16467156. Source: MGI gland development Inferred from mutant phenotype PubMed 16467156. Source: MGI lymph node development Inferred from mutant phenotype PubMed 7923373. Source: MGI natural killer cell differentiation Inferred from mutant phenotype PubMed 7923373. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12617992. Source: MGI positive regulation of NK T cell differentiation Inferred from mutant phenotype PubMed 10366784. Source: MGI positive regulation of multicellular organism growth Inferred from mutant phenotype PubMed 16467156. Source: MGI positive regulation of neutrophil differentiation Inferred from mutant phenotype PubMed 12406904. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 15841184PubMed 16467156. Source: MGI retina development in camera-type eye Inferred from mutant phenotype Ref.11. Source: MGI thymus development Inferred from mutant phenotype PubMed 7923373. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centromeric heterochromatin Inferred from direct assay Ref.9. Source: MGI cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell transcription factor complex Traceable author statement PubMed 11805317. Source: MGI
Molecular_function	sequence-specific DNA binding Inferred from mutant phenotype PubMed 7923373. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 7969165. Source: MGI transcription regulatory region DNA binding Inferred from direct assay PubMed 18804520. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sumo1	P63166	2	EBI-908572,EBI-80152

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform VI (identifier: Q03267-1)

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

Isoform I (identifier: Q03267-2)

The sequence of this isoform differs from the canonical sequence as follows:
     54-282: Missing.

Isoform II (identifier: Q03267-3)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: M → VAYGADGFRDFHAIISDRGM
     54-282: Missing.

Isoform III (identifier: Q03267-4)

The sequence of this isoform differs from the canonical sequence as follows:
     141-282: Missing.

Isoform IV (identifier: Q03267-5)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: M → VAYGADGFRDFHAIISDRGM
     141-282: Missing.

Isoform V (identifier: Q03267-6)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 517	517	DNA-binding protein Ikaros		PRO_0000047095
Regions
	Zinc finger	117 – 139	23	C2H2-type 1
	Zinc finger	144 – 166	23	C2H2-type 2
	Zinc finger	172 – 194	23	C2H2-type 3
	Zinc finger	200 – 223	24	C2H2-type 4
	Zinc finger	457 – 479	23	C2H2-type 5
	Zinc finger	488 – 512	25	C2H2-type 6
	Region	153 – 162	10	Required for both high-affinity DNA binding and pericentromeric heterochromatin localization
	Region	179 – 194	16	Required for both high-affinity DNA binding and pericentromeric heterochromatin localization
	Region	463 – 466	4	Required for binding PP1CC
	Compositional bias	368 – 371	4	Poly-Leu
Sites
	Site	158	1	Required for both pericentromeric heterochromatin localization and complete DNA binding
	Site	161	1	Required for both pericentromeric heterochromatin localization and complete DNA binding
	Site	187	1	Required for both pericentromeric heterochromatin localization and DNA binding
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.12
	Modified residue	23	1	Phosphothreonine Ref.12
	Modified residue	63	1	Phosphoserine Ref.8 Ref.12
	Modified residue	101	1	Phosphoserine Ref.12
	Modified residue	140	1	Phosphothreonine Ref.7
	Modified residue	167	1	Phosphoserine Ref.7
	Modified residue	195	1	Phosphoserine Ref.7
	Modified residue	259	1	Phosphoserine By similarity
	Modified residue	293	1	Phosphoserine Ref.12
	Modified residue	357	1	Phosphoserine By similarity
	Modified residue	360	1	Phosphoserine By similarity
	Modified residue	384	1	Phosphoserine Ref.8
	Modified residue	386	1	Phosphoserine Ref.8
	Modified residue	388	1	Phosphoserine Ref.8
	Modified residue	392	1	Phosphoserine Ref.8
	Modified residue	393	1	Phosphothreonine Ref.8
	Cross-link	58		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
	Cross-link	239		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Natural variations
	Alternative sequence	53	1	M → VAYGADGFRDFHAIISDRGM in isoform II and isoform IV.		VSP_006853
	Alternative sequence	54 – 282	229	Missing in isoform I and isoform II.		VSP_006855
	Alternative sequence	54 – 140	87	Missing in isoform V.		VSP_006854
	Alternative sequence	141 – 282	142	Missing in isoform III and isoform IV.		VSP_006856
Experimental info
	Mutagenesis	13	1	S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. Ref.12
	Mutagenesis	13	1	S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. Ref.12
	Mutagenesis	23	1	T → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Ref.12
	Mutagenesis	23	1	T → D: Decreased binding to gamma satellites A and B by 3-fold. Little change in pericentromeric location. Ref.12
	Mutagenesis	58	1	K → R: Some loss of sumoylation. Complete loss of sumoylation, increased repressor activity but no change in pericentromeric heterochromatin location; when associated with R-240 and R-459. Ref.9
	Mutagenesis	63	1	S → A: No change in pericentromeric location. Greatly reduced phosphorylation; when associated with A-384; A-386; A-388; A392 and A-393. No effect on DNA-binding activity. Increased DNA-binding activity; when associated with A-384; A-386; A-388; A-392 and A-393. Ref.8 Ref.12
	Mutagenesis	63	1	S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. Ref.8 Ref.12
	Mutagenesis	101	1	S → A: Abolishes phosphorylation. No change in pericentromeric location. Ref.12
	Mutagenesis	101	1	S → D: No change in binding to gamma satellites A and B. No change in pericentromeric location. Ref.12
	Mutagenesis	140	1	T → A: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-167 and A-195. Ref.7
	Mutagenesis	140	1	T → E: Abolishes phosphorylation, DNA binding and pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-167 and D-195. Ref.7
	Mutagenesis	152	1	S → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	153	1	F → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. Ref.5
	Mutagenesis	154	1	T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	155	1	Q → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
	Mutagenesis	156	1	K → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Ref.5
	Mutagenesis	157	1	G → A: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
	Mutagenesis	158	1	N → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. Ref.5
	Mutagenesis	159	1	L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	160	1	L → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	161	1	R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. Ref.5
	Mutagenesis	167	1	S → A: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-140 and A-195. Ref.7
	Mutagenesis	167	1	S → E: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-140 and D-195. Ref.7
	Mutagenesis	173	1	K → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	178	1	N → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	179	1	Y → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. Ref.5
	Mutagenesis	180	1	A → L: Loss of pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
	Mutagenesis	181	1	C → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	182	1	R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	183	1	R → A: Disrupts pericentromeric heterochromatin location. Partial cytoplasmic location. Abolishes DNA binding. Ref.5
	Mutagenesis	184	1	R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	185	1	D → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
	Mutagenesis	186	1	A → L: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
	Mutagenesis	187	1	L → A: Loss of pericentromeric heterochromatin location. Abolishes DNA binding. Ref.5
	Mutagenesis	188	1	T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	189	1	G → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	191	1	L → A: No effect on pericentromeric heterochromatin location. Disrupted DNA binding. Ref.5
	Mutagenesis	192	1	R → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	193	1	T → A: No effect on pericentromeric heterochromatin location. No change in DNA binding. Ref.5
	Mutagenesis	195	1	S → A: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with A-140 and A-167. Ref.7
	Mutagenesis	195	1	S → D: Abolishes phosphorylation, no effect on DNA binding nor on pericentromeric location. Loss of DNA binding and pericentromeric location; when associated with E-140 and E-167. Ref.7
	Mutagenesis	239	1	K → R: Some loss of sumoylation. Complete loss of sumoylation, increased repressor activity but no change in pericentromeric heterochromatin location.; when associated with R-58 and R-459. Ref.9
	Mutagenesis	293	1	S → A: Abolishes phosphorylation. No change in binding to gamma satellites A and B. No change in pericentromeric location. Increased DNA binding affinity toward TDT. Ref.12
	Mutagenesis	293	1	S → D: Decreased binding to gamma satellite A by 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear location. Decreased DNA binding affinity toward TdT by 3-fold. Ref.12
	Mutagenesis	384	1	S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-386; A-388; A-392 and A-393. and A-392. Further reduction in phosphorylation; when associated with A-63; A-386; A-388; A-392 and A-393. Ref.8
	Mutagenesis	386	1	S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-388; A-392 and A-393. Further reduction in phosphorylation; when associated with A-63; A-384; A-388; A-392 and A-393. Ref.8
	Mutagenesis	388	1	S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-392 and A-393. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-392 and A-393. Ref.8
	Mutagenesis	392	1	S → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-388 and A-392. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-386 and A-388. Ref.8
	Mutagenesis	393	1	T → A: Significantly reduced phosphorylation and 2- to 3-fold increase in ability to arrest in G(1); when associated with A-384; A-386; A-388 and A-392. Further reduction in phosphorylation; when associated with A-63; A-384; A-386; A-388 and A-392. Ref.8
	Mutagenesis	424	1	K → R: No effect on sumoylation. Ref.9
	Mutagenesis	458	1	K → R: No effect on sumoylation. Ref.9
	Mutagenesis	465 – 467	3	LFL → AFA: Abolishes binding of PP1CC, decreases DNA binding, abolishes pericentromeric location, and results in IKAROS degradation. Ref.13
	Sequence conflict	234 – 235	2	VC → MY in AAB32250. Ref.2
	Sequence conflict	480 – 482	3	Missing AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform VI [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 1052B8E76AF24287	FASTA	517	57,336
	10 20 30 40 50 60 MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGMGSNVKVE 70 80 90 100 110 120 TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 130 140 150 160 170 180 ICGIVCIGPN VLMVHKRSHT ERPFQCNQCG ASFTQKGNLL RHIKLHSGEK PFKCHLCNYA 190 200 210 220 230 240 CRRRDALTGH LRTHSVGKPH KCGYCGRSYK QRSSLEEHKE RCHNYLESMG LPGVCPVIKE 250 260 270 280 290 300 ETNHNEMAED LCKIGAERSL VLDRLASNVA KRKSSMPQKF LGDKCLSDMP YDSANYEKED 310 320 330 340 350 360 MMTSHVMDQA INNAINYLGA ESLRPLVQTP PGSSEVVPVI SSMYQLHKPP SDGPPRSNHS 370 380 390 400 410 420 AQDAVDNLLL LSKAKSVSSE REASPSNSCQ DSTDTESNAE EQRSGLIYLT NHINPHARNG 430 440 450 460 470 480 LALKEEQRAY EVLRAASENS QDAFRVVSTS GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG 490 500 510 CHGFRDPFEC NMCGYHSQDR YEFSSHITRG EHRYHLS
	Isoform I [UniParc]. Checksum: 71C89A7297190EDB	FASTA	288	31,989
	10 20 30 40 50 60 MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGMDKCLSDM 70 80 90 100 110 120 PYDSANYEKE DMMTSHVMDQ AINNAINYLG AESLRPLVQT PPGSSEVVPV ISSMYQLHKP 130 140 150 160 170 180 PSDGPPRSNH SAQDAVDNLL LLSKAKSVSS EREASPSNSC QDSTDTESNA EEQRSGLIYL 190 200 210 220 230 240 TNHINPHARN GLALKEEQRA YEVLRAASEN SQDAFRVVST SGEQLKVYKC EHCRVLFLDH 250 260 270 280 VMYTIHMGCH GCHGFRDPFE CNMCGYHSQD RYEFSSHITR GEHRYHLS
	Isoform II [UniParc]. Checksum: E644C2B323032538	FASTA	307	34,038
	10 20 30 40 50 60 MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGVAYGADGF 70 80 90 100 110 120 RDFHAIISDR GMDKCLSDMP YDSANYEKED MMTSHVMDQA INNAINYLGA ESLRPLVQTP 130 140 150 160 170 180 PGSSEVVPVI SSMYQLHKPP SDGPPRSNHS AQDAVDNLLL LSKAKSVSSE REASPSNSCQ 190 200 210 220 230 240 DSTDTESNAE EQRSGLIYLT NHINPHARNG LALKEEQRAY EVLRAASENS QDAFRVVSTS 250 260 270 280 290 300 GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG CHGFRDPFEC NMCGYHSQDR YEFSSHITRG EHRYHLS
	Isoform III [UniParc]. Checksum: 436E72D7B71477B1	FASTA	375	41,200
	10 20 30 40 50 60 MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGMGSNVKVE 70 80 90 100 110 120 TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 130 140 150 160 170 180 ICGIVCIGPN VLMVHKRSHT DKCLSDMPYD SANYEKEDMM TSHVMDQAIN NAINYLGAES 190 200 210 220 230 240 LRPLVQTPPG SSEVVPVISS MYQLHKPPSD GPPRSNHSAQ DAVDNLLLLS KAKSVSSERE 250 260 270 280 290 300 ASPSNSCQDS TDTESNAEEQ RSGLIYLTNH INPHARNGLA LKEEQRAYEV LRAASENSQD 310 320 330 340 350 360 AFRVVSTSGE QLKVYKCEHC RVLFLDHVMY TIHMGCHGCH GFRDPFECNM CGYHSQDRYE 370 FSSHITRGEH RYHLS
	Isoform IV [UniParc]. Checksum: B6F496262B04D9F3	FASTA	394	43,250
	10 20 30 40 50 60 MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGVAYGADGF 70 80 90 100 110 120 RDFHAIISDR GMGSNVKVET QSDEENGRAC EMNGEECAED LRMLDASGEK MNGSHRDQGS 130 140 150 160 170 180 SALSGVGGIR LPNGKLKCDI CGIVCIGPNV LMVHKRSHTD KCLSDMPYDS ANYEKEDMMT 190 200 210 220 230 240 SHVMDQAINN AINYLGAESL RPLVQTPPGS SEVVPVISSM YQLHKPPSDG PPRSNHSAQD 250 260 270 280 290 300 AVDNLLLLSK AKSVSSEREA SPSNSCQDST DTESNAEEQR SGLIYLTNHI NPHARNGLAL 310 320 330 340 350 360 KEEQRAYEVL RAASENSQDA FRVVSTSGEQ LKVYKCEHCR VLFLDHVMYT IHMGCHGCHG 370 380 390 FRDPFECNMC GYHSQDRYEF SSHITRGEHR YHLS
	Isoform V [UniParc]. Checksum: 56F4672C0F124FF1	FASTA	430	48,125
	10 20 30 40 50 60 MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGMERPFQCN 70 80 90 100 110 120 QCGASFTQKG NLLRHIKLHS GEKPFKCHLC NYACRRRDAL TGHLRTHSVG KPHKCGYCGR 130 140 150 160 170 180 SYKQRSSLEE HKERCHNYLE SMGLPGVCPV IKEETNHNEM AEDLCKIGAE RSLVLDRLAS 190 200 210 220 230 240 NVAKRKSSMP QKFLGDKCLS DMPYDSANYE KEDMMTSHVM DQAINNAINY LGAESLRPLV 250 260 270 280 290 300 QTPPGSSEVV PVISSMYQLH KPPSDGPPRS NHSAQDAVDN LLLLSKAKSV SSEREASPSN 310 320 330 340 350 360 SCQDSTDTES NAEEQRSGLI YLTNHINPHA RNGLALKEEQ RAYEVLRAAS ENSQDAFRVV 370 380 390 400 410 420 STSGEQLKVY KCEHCRVLFL DHVMYTIHMG CHGCHGFRDP FECNMCGYHS QDRYEFSSHI 430 TRGEHRYHLS

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	L03547 mRNA. Translation: AAA66193.1. S74517 mRNA. Translation: AAB32248.2. Sequence problems. S74518 mRNA. Translation: AAB32249.2. S74708 mRNA. Translation: AAB32250.2.
IPI	IPI00116369. IPI00130283. IPI00223005. IPI00223008. IPI00223010. IPI00223011.
PIR	A56355. I59572.
UniGene	Mm.103545.
3D structure databases
ProteinModelPortal	Q03267.
SMR	Q03267. Positions 118-219, 455-507.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q03267. 11 interactions.
MINT	MINT-4098529.
PTM databases
PhosphoSite	Q03267.
Proteomic databases
PaxDb	Q03267.
PRIDE	Q03267.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:1342540. Ikzf1.
Phylogenomic databases
eggNOG	NOG244744.
HOGENOM	HOG000049114.
HOVERGEN	HBG004752.
InParanoid	Q03267.
Gene expression databases
CleanEx	MM_IKZF1.
Genevestigator	Q03267.
GermOnline	ENSMUSG00000018654. Mus musculus.
Family and domain databases
Gene3D	3.30.160.60. 4 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF00096. zf-C2H2. 3 hits. [Graphical view]
SMART	SM00355. ZnF_C2H2. 6 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 5 hits. PS50157. ZINC_FINGER_C2H2_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

IKZF1_MOUSE

Accession

Primary (citable) accession number: Q03267
Secondary accession number(s): Q64044, Q64045, Q64051

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	December 15, 1998
Last modified:	May 29, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program