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Q13422 (IKZF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Protein existenceEvidence 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.10

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.10 Ref.12

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. Ref.17

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. Ref.17

Isoform Ik6: Cytoplasm By similarity Ref.17.

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. Phosphorylation at Ser-361 and Ser-364 downstream of SYK induces nuclear translocation. Ref.17

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.

Chromosomal aberrations involving IKZF1 are a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;7)(q27;p12), with BCL6.

Sequence similarities

Belongs to the Ikaros C2H2-type zinc-finger protein family.

Contains 6 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Developmental protein
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

Peyer's patch development

Inferred from electronic annotation. Source: Ensembl

T cell differentiation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

gland development

Inferred from electronic annotation. Source: Ensembl

lymph node development

Inferred from electronic annotation. Source: Ensembl

mesoderm development

Traceable author statement Ref.2. Source: ProtInc

natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of NK T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of neutrophil differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

thymus development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentromeric heterochromatin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Traceable author statement Ref.2. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 8 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.
Isoform Ikx (identifier: Q13422-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519DNA-binding protein Ikaros
PRO_0000047094

Regions

Zinc finger117 – 13923C2H2-type 1
Zinc finger145 – 16723C2H2-type 2
Zinc finger173 – 19523C2H2-type 3
Zinc finger201 – 22424C2H2-type 4
Zinc finger462 – 48423C2H2-type 5
Zinc finger490 – 51425C2H2-type 6
Region154 – 16310Required for both high-affinity DNA binding and pericentromeric heterochromatin localization By similarity
Region180 – 19516Required for both high-affinity DNA binding and pericentromeric heterochromatin localization By similarity
Region468 – 4714Required for binding PP1CC By similarity
Compositional bias373 – 3764Poly-Leu

Sites

Site1591Required for both pericentromeric heterochromatin localization and complete DNA binding By similarity
Site1621Required for both pericentromeric heterochromatin localization and complete DNA binding By similarity
Site1881Required for both pericentromeric heterochromatin localization and DNA binding By similarity

Amino acid modifications

Modified residue131Phosphoserine By similarity
Modified residue231Phosphothreonine By similarity
Modified residue631Phosphoserine Ref.15
Modified residue1011Phosphoserine By similarity
Modified residue1401Phosphothreonine By similarity
Modified residue1681Phosphoserine By similarity
Modified residue1961Phosphoserine By similarity
Modified residue2581Phosphoserine Ref.15
Modified residue2611Phosphoserine Ref.15
Modified residue2951Phosphoserine By similarity
Modified residue3611Phosphoserine Ref.15 Ref.17
Modified residue3641Phosphoserine Ref.15 Ref.17
Modified residue3891Phosphoserine By similarity
Modified residue3911Phosphoserine By similarity
Modified residue3931Phosphoserine By similarity
Modified residue3971Phosphoserine By similarity
Modified residue3981Phosphothreonine By similarity
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence10 – 5344Missing in isoform Ik4.
VSP_006847
Alternative sequence54 – 283230Missing in isoform Ik6.
VSP_006849
Alternative sequence54 – 14087Missing in isoform Ik2.
VSP_006848
Alternative sequence141 – 283143Missing in isoform Ik5.
VSP_006852
Alternative sequence197 – 28387Missing in isoform Ik3 and isoform Ik4.
VSP_006850
Alternative sequence197 – 23842Missing in isoform Ik7 and isoform Ikx.
VSP_006851
Alternative sequence260 – 2689RSLVLDRLA → ISRAGQTSK in isoform Ikx.
VSP_053404
Alternative sequence269 – 519251Missing in isoform Ikx.
VSP_053405

Experimental info

Sequence conflict11 – 122QV → FS in AAB50683. Ref.2
Sequence conflict2141S → T in AAB50683. Ref.2
Sequence conflict2451N → K in AAB50683. Ref.2
Sequence conflict2961Missing in AAB50683. Ref.2
Sequence conflict2981S → T in AAB50683. Ref.2
Sequence conflict352 – 3554KPLA → RRS in AAB50683. Ref.2
Sequence conflict3721N → Y in AAB50683. Ref.2
Sequence conflict420 – 4267PHARNGL → RRAQRV in AAB50683. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Ik1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7B0129C4E3FE41A8

FASTA51957,528
        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 

« Hide

Isoform Ik2 [UniParc].

Checksum: E8E57F8BF5B306E6
Show »

FASTA43248,289
Isoform Ik3 [UniParc].

Checksum: 1093D253341A95E8
Show »

FASTA43247,634
Isoform Ik4 [UniParc].

Checksum: 137C942A5278A9F0
Show »

FASTA38843,093
Isoform Ik5 [UniParc].

Checksum: 0B060551CB3E0082
Show »

FASTA37641,229
Isoform Ik6 [UniParc].

Checksum: EB96A15185C62A18
Show »

FASTA28931,989
Isoform Ik7 [UniParc].

Checksum: B19FE76450EA40E4
Show »

FASTA47752,706
Isoform Ikx [UniParc].

Checksum: 2BB5B70D38F73264
Show »

FASTA22624,470

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40462 mRNA. Translation: AAC50459.1.
S80876 mRNA. Translation: AAB50683.1.
AY377974 mRNA. Translation: AAR84585.1.
AK303586 mRNA. Translation: BAG64603.1.
BT009836 mRNA. Translation: AAP88838.1.
AC124014 Genomic DNA. No translation available.
AC233268 Genomic DNA. No translation available.
CH471128 Genomic DNA. Translation: EAW60977.1.
CH471128 Genomic DNA. Translation: EAW60978.1.
CH471128 Genomic DNA. Translation: EAW60981.1.
CH236955 Genomic DNA. Translation: EAL23900.1.
CH471128 Genomic DNA. Translation: EAW60979.1.
BC018349 mRNA. Translation: AAH18349.1.
RefSeqNP_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.
UniGeneHs.435949.
Hs.488251.
Hs.731495.

3D structure databases

ProteinModelPortalQ13422.
SMRQ13422. Positions 112-248, 460-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115604. 37 interactions.
IntActQ13422. 18 interactions.
MINTMINT-129252.
STRING9606.ENSP00000331614.

PTM databases

PhosphoSiteQ13422.

Polymorphism databases

DMDM3913926.

Proteomic databases

PaxDbQ13422.
PRIDEQ13422.

Protocols and materials databases

DNASU10320.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331340; ENSP00000331614; ENSG00000185811. [Q13422-1]
ENST00000343574; ENSP00000342750; ENSG00000185811. [Q13422-2]
ENST00000346667; ENSP00000340080; ENSG00000185811. [Q13422-6]
ENST00000349824; ENSP00000342485; ENSG00000185811. [Q13422-5]
ENST00000357364; ENSP00000349928; ENSG00000185811. [Q13422-3]
ENST00000359197; ENSP00000352123; ENSG00000185811. [Q13422-7]
ENST00000438033; ENSP00000396554; ENSG00000185811. [Q13422-2]
ENST00000439701; ENSP00000413025; ENSG00000185811. [Q13422-7]
ENST00000440768; ENSP00000401507; ENSG00000185811. [Q13422-8]
GeneID10320.
KEGGhsa:10320.
UCSCuc003tow.4. human. [Q13422-1]
uc003tox.4. human. [Q13422-7]
uc003tpa.4. human. [Q13422-6]
uc011kck.2. human. [Q13422-2]
uc022acq.1. human. [Q13422-5]
uc022acs.1. human. [Q13422-4]
uc022acx.1. human. [Q13422-3]

Organism-specific databases

CTD10320.
GeneCardsGC07P050343.
HGNCHGNC:13176. IKZF1.
HPACAB009247.
MIM603023. gene.
neXtProtNX_Q13422.
Orphanet317473. Pancytopenia due to IKZF1 mutations.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA37748.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244744.
HOVERGENHBG004752.
InParanoidQ13422.
KOK09220.
OMAGDKCLSD.
PhylomeDBQ13422.
TreeFamTF331189.

Enzyme and pathway databases

SignaLinkQ13422.

Gene expression databases

ArrayExpressQ13422.
BgeeQ13422.
CleanExHS_IKZF1.
GenevestigatorQ13422.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIKZF1. human.
GeneWikiIKZF1.
GenomeRNAi10320.
NextBio39123.
PROQ13422.
SOURCESearch...

Entry information

Entry nameIKZF1_HUMAN
AccessionPrimary (citable) accession number: Q13422
Secondary accession number(s): A4D260 expand/collapse secondary AC list , B4E0Z1, D3DVM5, O00598, Q53XL2, Q69BM4, Q8WVA3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM