Q13422 (IKZF1_HUMAN) 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:	IK1, IKAROS, LYF1, ZNFN1A1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	519 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. Confers early temporal competence to retinal progenitor cells (RPCs) By similarity. Ref.8
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 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. Ref.8 Ref.9
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 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. Isoform Ik6: Cytoplasm By similarity.
Tissue specificity	Abundantly expressed in thymus, spleen and peripheral blood Leukocytes and lymph nodes. Lower expression in bone marrow and small intestine.
Domain	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.
Post-translational modification	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. 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. Polyubiquitinated By similarity.
Involvement in disease	Defects in IKZF1 are frequent occurrences (28.6%) in acute lymphoblasic leukemia (ALL). Such alterations or deletions lead to poor prognosis for ALL.
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 Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara Peyer's patch development Inferred from electronic annotation. Source: Compara T cell differentiation Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW forebrain development Inferred from electronic annotation. Source: Compara gland development Inferred from electronic annotation. Source: Compara lymph node development Inferred from electronic annotation. Source: Compara mesoderm development Traceable author statement Ref.2. Source: ProtInc natural killer cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of NK T cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara positive regulation of neutrophil differentiation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara retina development in camera-type eye Inferred from electronic annotation. Source: Compara thymus development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centromeric heterochromatin Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Traceable author statement Ref.2. Source: ProtInc sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform Ik1 (identifier: Q13422-1)

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 Ik2 (identifier: Q13422-2)

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

Isoform Ik3 (identifier: Q13422-3)

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

Isoform Ik4 (identifier: Q13422-4)

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

Isoform Ik5 (identifier: Q13422-5)

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

Isoform Ik6 (identifier: Q13422-6)

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

Isoform Ik7 (identifier: Q13422-7)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 519	519	DNA-binding protein Ikaros		PRO_0000047094
Regions
	Zinc finger	117 – 139	23	C2H2-type 1
	Zinc finger	145 – 167	23	C2H2-type 2
	Zinc finger	173 – 195	23	C2H2-type 3
	Zinc finger	201 – 224	24	C2H2-type 4
	Zinc finger	462 – 484	23	C2H2-type 5
	Zinc finger	490 – 514	25	C2H2-type 6
	Region	154 – 163	10	Required for both high-affinity DNA binding and pericentromeric heterochromatin localization By similarity
	Region	180 – 195	16	Required for both high-affinity DNA binding and pericentromeric heterochromatin localization By similarity
	Region	468 – 471	4	Required for binding PP1CC By similarity
	Compositional bias	373 – 376	4	Poly-Leu
Sites
	Site	159	1	Required for both pericentromeric heterochromatin localization and complete DNA binding By similarity
	Site	162	1	Required for both pericentromeric heterochromatin localization and complete DNA binding By similarity
	Site	188	1	Required for both pericentromeric heterochromatin localization and DNA binding By similarity
Amino acid modifications
	Modified residue	13	1	Phosphoserine By similarity
	Modified residue	23	1	Phosphothreonine By similarity
	Modified residue	63	1	Phosphoserine Ref.12
	Modified residue	101	1	Phosphoserine By similarity
	Modified residue	168	1	Phosphoserine By similarity
	Modified residue	196	1	Phosphoserine By similarity
	Modified residue	258	1	Phosphoserine Ref.12
	Modified residue	261	1	Phosphoserine Ref.12
	Modified residue	296	1	Phosphoserine By similarity
	Modified residue	361	1	Phosphoserine Ref.12
	Modified residue	364	1	Phosphoserine Ref.12
	Modified residue	389	1	Phosphoserine By similarity
	Modified residue	391	1	Phosphoserine By similarity
	Modified residue	393	1	Phosphoserine By similarity
	Modified residue	397	1	Phosphoserine By similarity
	Modified residue	398	1	Phosphothreonine By similarity
	Cross-link	58		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	241		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	10 – 53	44	Missing in isoform Ik4.		VSP_006847
	Alternative sequence	54 – 283	230	Missing in isoform Ik6.		VSP_006849
	Alternative sequence	54 – 140	87	Missing in isoform Ik2.		VSP_006848
	Alternative sequence	141 – 283	143	Missing in isoform Ik5.		VSP_006852
	Alternative sequence	197 – 283	87	Missing in isoform Ik3 and isoform Ik4.		VSP_006850
	Alternative sequence	197 – 238	42	Missing in isoform Ik7.		VSP_006851
Experimental info
	Sequence conflict	11 – 12	2	QV → FS in AAB50683. Ref.2
	Sequence conflict	214	1	S → T in AAB50683. Ref.2
	Sequence conflict	245	1	N → K in AAB50683. Ref.2
	Sequence conflict	296	1	Missing in AAB50683. Ref.2
	Sequence conflict	298	1	S → T in AAB50683. Ref.2
	Sequence conflict	352 – 355	4	KPLA → RRS in AAB50683. Ref.2
	Sequence conflict	372	1	N → Y in AAB50683. Ref.2
	Sequence conflict	420 – 426	7	PHARNGL → RRAQRV in AAB50683. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Ik1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7B0129C4E3FE41A8	FASTA	519	57,528
	10 20 30 40 50 60 MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE 70 80 90 100 110 120 TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 130 140 150 160 170 180 ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY 190 200 210 220 230 240 ACRRRDALTG HLRTHSVGKP HKCGYCGRSY KQRSSLEEHK ERCHNYLESM GLPGTLYPVI 250 260 270 280 290 300 KEETNHSEMA EDLCKIGSER SLVLDRLASN VAKRKSSMPQ KFLGDKGLSD TPYDSSASYE 310 320 330 340 350 360 KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL HKPLAEGTPR 370 380 390 400 410 420 SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT ESNNEEQRSG LIYLTNHIAP 430 440 450 460 470 480 HARNGLSLKE EHRAYDLLRA ASENSQDALR VVSTSGEQMK VYKCEHCRVL FLDHVMYTIH 490 500 510 MGCHGFRDPF ECNMCGYHSQ DRYEFSSHIT RGEHRFHMS
	Isoform Ik2 [UniParc]. Checksum: E8E57F8BF5B306E6	FASTA	432	48,289
	10 20 30 40 50 60 MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVGERPFQC 70 80 90 100 110 120 NQCGASFTQK GNLLRHIKLH SGEKPFKCHL CNYACRRRDA LTGHLRTHSV GKPHKCGYCG 130 140 150 160 170 180 RSYKQRSSLE EHKERCHNYL ESMGLPGTLY PVIKEETNHS EMAEDLCKIG SERSLVLDRL 190 200 210 220 230 240 ASNVAKRKSS MPQKFLGDKG LSDTPYDSSA SYEKENEMMK SHVMDQAINN AINYLGAESL 250 260 270 280 290 300 RPLVQTPPGG SEVVPVISPM YQLHKPLAEG TPRSNHSAQD SAVENLLLLS KAKLVPSERE 310 320 330 340 350 360 ASPSNSCQDS TDTESNNEEQ RSGLIYLTNH IAPHARNGLS LKEEHRAYDL LRAASENSQD 370 380 390 400 410 420 ALRVVSTSGE QMKVYKCEHC RVLFLDHVMY TIHMGCHGFR DPFECNMCGY HSQDRYEFSS 430 HITRGEHRFH MS
	Isoform Ik3 [UniParc]. Checksum: 1093D253341A95E8	FASTA	432	47,634
	10 20 30 40 50 60 MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE 70 80 90 100 110 120 TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 130 140 150 160 170 180 ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY 190 200 210 220 230 240 ACRRRDALTG HLRTHSGDKG LSDTPYDSSA SYEKENEMMK SHVMDQAINN AINYLGAESL 250 260 270 280 290 300 RPLVQTPPGG SEVVPVISPM YQLHKPLAEG TPRSNHSAQD SAVENLLLLS KAKLVPSERE 310 320 330 340 350 360 ASPSNSCQDS TDTESNNEEQ RSGLIYLTNH IAPHARNGLS LKEEHRAYDL LRAASENSQD 370 380 390 400 410 420 ALRVVSTSGE QMKVYKCEHC RVLFLDHVMY TIHMGCHGFR DPFECNMCGY HSQDRYEFSS 430 HITRGEHRFH MS
	Isoform Ik4 [UniParc]. Checksum: 137C942A5278A9F0	FASTA	388	43,093
	10 20 30 40 50 60 MDADEGQDMA SNVKVETQSD EENGRACEMN GEECAEDLRM LDASGEKMNG SHRDQGSSAL 70 80 90 100 110 120 SGVGGIRLPN GKLKCDICGI ICIGPNVLMV HKRSHTGERP FQCNQCGASF TQKGNLLRHI 130 140 150 160 170 180 KLHSGEKPFK CHLCNYACRR RDALTGHLRT HSGDKGLSDT PYDSSASYEK ENEMMKSHVM 190 200 210 220 230 240 DQAINNAINY LGAESLRPLV QTPPGGSEVV PVISPMYQLH KPLAEGTPRS NHSAQDSAVE 250 260 270 280 290 300 NLLLLSKAKL VPSEREASPS NSCQDSTDTE SNNEEQRSGL IYLTNHIAPH ARNGLSLKEE 310 320 330 340 350 360 HRAYDLLRAA SENSQDALRV VSTSGEQMKV YKCEHCRVLF LDHVMYTIHM GCHGFRDPFE 370 380 CNMCGYHSQD RYEFSSHITR GEHRFHMS
	Isoform Ik5 [UniParc]. Checksum: 0B060551CB3E0082	FASTA	376	41,229
	10 20 30 40 50 60 MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE 70 80 90 100 110 120 TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 130 140 150 160 170 180 ICGIICIGPN VLMVHKRSHT GDKGLSDTPY DSSASYEKEN EMMKSHVMDQ AINNAINYLG 190 200 210 220 230 240 AESLRPLVQT PPGGSEVVPV ISPMYQLHKP LAEGTPRSNH SAQDSAVENL LLLSKAKLVP 250 260 270 280 290 300 SEREASPSNS CQDSTDTESN NEEQRSGLIY LTNHIAPHAR NGLSLKEEHR AYDLLRAASE 310 320 330 340 350 360 NSQDALRVVS TSGEQMKVYK CEHCRVLFLD HVMYTIHMGC HGFRDPFECN MCGYHSQDRY 370 EFSSHITRGE HRFHMS
	Isoform Ik6 [UniParc]. Checksum: EB96A15185C62A18	FASTA	289	31,989
	10 20 30 40 50 60 MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVGDKGLSD 70 80 90 100 110 120 TPYDSSASYE KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL 130 140 150 160 170 180 HKPLAEGTPR SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT ESNNEEQRSG 190 200 210 220 230 240 LIYLTNHIAP HARNGLSLKE EHRAYDLLRA ASENSQDALR VVSTSGEQMK VYKCEHCRVL 250 260 270 280 FLDHVMYTIH MGCHGFRDPF ECNMCGYHSQ DRYEFSSHIT RGEHRFHMS
	Isoform Ik7 [UniParc]. Checksum: B19FE76450EA40E4	FASTA	477	52,706
	10 20 30 40 50 60 MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE 70 80 90 100 110 120 TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD 130 140 150 160 170 180 ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY 190 200 210 220 230 240 ACRRRDALTG HLRTHSVIKE ETNHSEMAED LCKIGSERSL VLDRLASNVA KRKSSMPQKF 250 260 270 280 290 300 LGDKGLSDTP YDSSASYEKE NEMMKSHVMD QAINNAINYL GAESLRPLVQ TPPGGSEVVP 310 320 330 340 350 360 VISPMYQLHK PLAEGTPRSN HSAQDSAVEN LLLLSKAKLV PSEREASPSN SCQDSTDTES 370 380 390 400 410 420 NNEEQRSGLI YLTNHIAPHA RNGLSLKEEH RAYDLLRAAS ENSQDALRVV STSGEQMKVY 430 440 450 460 470 KCEHCRVLFL DHVMYTIHMG CHGFRDPFEC NMCGYHSQDR YEFSSHITRG EHRFHMS

References

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[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]	"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.
[4]	"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).
[5]	"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].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"Deletion of IKZF1 and prognosis in acute lymphoblastic leukemia." Mullighan C.G., Su X., Zhang J., Radtke I., Phillips L.A., Miller C.B., Ma J., Liu W., Cheng C., Schulman B.A., Harvey R.C., Chen I.-M., Clifford R.J., Carroll W.L., Reaman G., Bowman W.P., Devidas M., Gerhard D.S. , Yang W., Relling M.V., Shurtleff S.A., Campana D., Borowitz M.J., Pui C.H., Smith M., Hunger S.P., Willman C.L., Downing J.R. N. Engl. J. Med. 360:470-480(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ACUTE LYMPHOBLASIC LEUKEMIA.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	U40462 mRNA. Translation: AAC50459.1. S80876 mRNA. Translation: AAB50683.1. AK303586 mRNA. Translation: BAG64603.1. BT009836 mRNA. Translation: AAP88838.1. 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.
IPI	IPI00013232. IPI00216387. IPI00216388. IPI00216389. IPI00216390. IPI00216391. IPI00216392.
RefSeq	NP_001207694.1. NM_001220765.1. NP_001207695.1. NM_001220766.1. NP_001207696.1. NM_001220767.1. NP_001207697.1. NM_001220768.1. NP_001207698.1. NM_001220769.1. NP_001207699.1. NM_001220770.1. NP_001207700.1. NM_001220771.1. NP_001207701.1. NM_001220772.1. NP_001207702.1. NM_001220773.1. NP_001207703.1. NM_001220774.1. NP_001207704.1. NM_001220775.1. NP_001207705.1. NM_001220776.1. NP_006051.1. NM_006060.4.
UniGene	Hs.435949. Hs.488251. Hs.731495.
3D structure databases
ProteinModelPortal	Q13422.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13422. 5 interactions.
STRING	9606.ENSP00000331614.
PTM databases
PhosphoSite	Q13422.
Polymorphism databases
DMDM	3913926.
Proteomic databases
PaxDb	Q13422.
PRIDE	Q13422.
Protocols and materials databases
DNASU	10320.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331340; ENSP00000331614; ENSG00000185811. ENST00000343574; ENSP00000342750; ENSG00000185811. ENST00000346667; ENSP00000340080; ENSG00000185811. ENST00000349824; ENSP00000342485; ENSG00000185811. ENST00000357364; ENSP00000349928; ENSG00000185811. ENST00000359197; ENSP00000352123; ENSG00000185811. ENST00000438033; ENSP00000396554; ENSG00000185811. ENST00000439701; ENSP00000413025; ENSG00000185811.
GeneID	10320.
KEGG	hsa:10320.
UCSC	uc003tow.4. human. uc003tox.4. human. uc003tpa.4. human. uc011kck.2. human. uc022acq.1. human. uc022acs.1. human. uc022acx.1. human.
Organism-specific databases
CTD	10320.
GeneCards	GC07P050343.
HGNC	HGNC:13176. IKZF1.
HPA	CAB009247.
MIM	603023. gene.
neXtProt	NX_Q13422.
PharmGKB	PA37748.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG244744.
HOVERGEN	HBG004752.
InParanoid	Q13422.
KO	K09220.
OMA	GDKCLSD.
PhylomeDB	Q13422.
Enzyme and pathway databases
Pathway_Interaction_DB	nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
Gene expression databases
ArrayExpress	Q13422.
Bgee	Q13422.
CleanEx	HS_IKZF1.
Genevestigator	Q13422.
GermOnline	ENSG00000185811. Homo sapiens.
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]
SMART	SM00355. ZnF_C2H2. 6 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 5 hits. PS50157. ZINC_FINGER_C2H2_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	IKZF1. human.
GenomeRNAi	10320.
NextBio	39123.
SOURCE	Search...

Entry information

Entry name

IKZF1_HUMAN

Accession

Primary (citable) accession number: Q13422
Secondary accession number(s): A4D260 , B4E0Z1, D3DVM5, O00598, Q53XL2, Q8WVA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.