IKZF1
entrez
10320
canonical
uniprot
Q13422
canonical
ensembl
ENSG00000185811
resolver
ensp
ENSP00000331614
resolver
ensp
ENSP00000352123
resolver
ensp
ENSP00000388478
resolver
ensp
ENSP00000396554
resolver
ensp
ENSP00000413025
resolver
ensp
ENSP00000493696
resolver
ensp
ENSP00000494180
resolver
ensp
ENSP00000496655
resolver
ensp
ENSP00000513804
resolver
ensp
ENSP00000513805
resolver
ensp
ENSP00000513806
resolver
ensp
ENSP00000528103
resolver
ensp
ENSP00000528105
resolver
ensp
ENSP00000528106
resolver
ensp
ENSP00000528107
resolver
ensp
ENSP00000528108
resolver
ensp
ENSP00000528109
resolver
ensp
ENSP00000528110
resolver
ensp
ENSP00000528111
resolver
ensp
ENSP00000528112
resolver
ensp
ENSP00000528114
resolver
ensp
ENSP00000528115
resolver
ensp
ENSP00000528117
resolver
ensp
ENSP00000528118
resolver
ensp
ENSP00000528119
resolver
ensp
ENSP00000528120
resolver
ensp
ENSP00000528124
resolver
ensp
ENSP00000641338
resolver
ensp
ENSP00000641339
resolver
enst
ENST00000413698
resolver
enst
ENST00000492782
resolver
enst
ENST00000642219
resolver
enst
ENST00000646110
resolver
enst
ENST00000698574
resolver
enst
ENST00000858048
resolver
enst
ENST00000858050
resolver
enst
ENST00000858052
resolver
enst
ENST00000858059
resolver
enst
ENST00000858065
resolver
genesymbol
IKZF1
resolver
genesymbol_syn
IK1
resolver
genesymbol_syn
IKAROS
resolver
genesymbol_syn
LYF1
resolver
genesymbol_syn
ZNFN1A1
resolver
hgnc
HGNC:13176
resolver
uniprot
A0A2R8Y4D3
resolver
uniprot
A0A2R8YFR0
resolver
uniprot
A0A8V8TNQ0
resolver
uniprot
A4D260
resolver
uniprot
B4E0Z1
resolver
uniprot
C9JTB0
resolver
uniprot
D3DVM5
resolver
uniprot
O00598
resolver
uniprot
Q53XL2
resolver
uniprot
Q69BM4
resolver
uniprot
Q8WVA3
resolver
uniprot
R9R4D9
resolver
uniprot_entry
A0A2R8Y4D3_HUMAN
resolver
uniprot_entry
A0A2R8YFR0_HUMAN
resolver
uniprot_entry
A0A8V8TNQ0_HUMAN
resolver
uniprot_entry
C9JTB0_HUMAN
resolver
uniprot_entry
IKZF1_HUMAN
resolver
uniprot_entry
R9R4D9_HUMAN
resolver
uniprot_sec
A4D260
resolver
uniprot_sec
B4E0Z1
resolver
uniprot_sec
D3DVM5
resolver
uniprot_sec
O00598
resolver
uniprot_sec
Q53XL2
resolver
uniprot_sec
Q69BM4
resolver
uniprot_sec
Q8WVA3
resolver
amino_acid_sequence
MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in IKZF1 are frequent occurrences (28.6%) in acute lymphoblasic leukemia (ALL). Such alterations or deletions lead to poor prognosis for ALL.; DISEASE: Note=Chromosomal aberrations involving IKZF1 are a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;7)(q27;p12), with BCL6.; DISEASE: Immunodeficiency, common variable, 13 (CVID13) [MIM:616873]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. CVID13 is an autosomal dominant disease associated with a striking decrease in B-cell numbers. {ECO:0000269|PubMed:21548011, ECO:0000269|PubMed:26981933}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Transcription regulator of hematopoietic cell differentiation (PubMed:17934067). Binds gamma-satellite DNA (PubMed:17135265, PubMed:19141594). 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 (fikzfterminal 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 (PubMed:10204490). Increases normal apoptosis in adult erythroid cells (By similarity). Confers early temporal competence to retinal progenitor cells (RPCs) (By similarity). Function is isoform-specific and is modulated by dominant-negative inactive isoforms (PubMed:17135265, PubMed:17934067). Recognized by CRBN and is targeted for degradation by DCX (DDB1-CUL4-X-box) E3 protein ligase complex (PubMed:41565821). {ECO:0000250|UniProtKB:Q03267, ECO:0000269|PubMed:10204490, ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:17934067, ECO:0000269|PubMed:19141594, ECO:0000269|PubMed:41565821}.
uniprot
proteins
mass_dalton
57528
uniprot
proteins
mutagenesis
MUTAGEN 159; /note="N->A: Abolishes binding to DNA and has diffuse nuclear localization."; /evidence="ECO:0000269|PubMed:26981933"; MUTAGEN 191; /note="H->R: Abolishes binding to DNA and has diffuse nuclear localization."; /evidence="ECO:0000269|PubMed:26981933
uniprot
proteins
post_translational_modification
PTM: Phosphorylation controls cell-cycle progression from late G(1) stage to S stage. Hyperphosphorylated during G2/M phase. Dephosphorylated state during late G(1) 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. {ECO:0000250, ECO:0000269|PubMed:22106042, ECO:0000269|PubMed:23071339}.; PTM: Sumoylated. Simultaneous 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). {ECO:0000250}.; PTM: Polyubiquitinated. {ECO:0000250}.
uniprot
proteins
protein_family
Ikaros C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
10204490
uniprot
proteins
pubmed
10753856
uniprot
proteins
pubmed
10978333
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17135265
uniprot
proteins
pubmed
17934067
uniprot
proteins
pubmed
19129520
uniprot
proteins
pubmed
19141594
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21548011
uniprot
proteins
pubmed
22106042
uniprot
proteins
pubmed
23071339
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26981933
uniprot
proteins
pubmed
41565821
uniprot
proteins
pubmed
8543809
uniprot
proteins
pubmed
8964602
uniprot
proteins
sequence_length
519
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:21548011, ECO:0000269|PubMed:22106042, ECO:0000269|PubMed:23071339}. 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. {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:22106042}.; SUBCELLULAR LOCATION: [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). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Ik6]: Cytoplasm {ECO:0000250}.
uniprot
proteins