IKZF2_HUMAN
ID IKZF2_HUMAN Reviewed; 526 AA.
AC Q9UKS7; Q53YJ5; Q6PQC5; Q6PQC6; Q6PQC7; Q6PQC8; Q6PQD0; Q6PQD1; Q8N6S1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Zinc finger protein Helios;
DE AltName: Full=Ikaros family zinc finger protein 2;
GN Name=IKZF2; Synonyms=HELIOS, ZNFN1A2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10541817; DOI=10.1007/s002510050696;
RA Hosokawa Y., Maeda Y., Seto M.;
RT "Human Helios, an Ikaros-related zinc finger DNA binding protein: cDNA
RT cloning and tissue expression pattern.";
RL Immunogenetics 50:106-108(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7 AND 8), AND
RP ALTERNATIVE SPLICING.
RA Lopez-Segura V., Gonzalez-Sarmiento R.;
RT "Molecular characterization of new Helios isoforms.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH IKZF4 AND IKZF5.
RX PubMed=10978333; DOI=10.1074/jbc.m005457200;
RA Perdomo J., Holmes M., Chong B., Crossley M.;
RT "Eos and pegasus, two members of the Ikaros family of proteins with
RT distinct DNA binding activities.";
RL J. Biol. Chem. 275:38347-38354(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-78 AND SER-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-442, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-442 AND LYS-448,
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-95 (ISOFORMS 2; 4 AND 7), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Associates with Ikaros at centromeric heterochromatin.
CC -!- SUBUNIT: Interacts with IKZF4 AND IKZF5. {ECO:0000269|PubMed:10978333}.
CC -!- INTERACTION:
CC Q9UKS7; P29972: AQP1; NbExp=3; IntAct=EBI-3893057, EBI-745213;
CC Q9UKS7; P56545: CTBP2; NbExp=3; IntAct=EBI-3893057, EBI-741533;
CC Q9UKS7; P56545-3: CTBP2; NbExp=3; IntAct=EBI-3893057, EBI-10171902;
CC Q9UKS7; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-3893057, EBI-2341787;
CC Q9UKS7; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-3893057, EBI-3957603;
CC Q9UKS7-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-11536241, EBI-11955057;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q9UKS7-1; Sequence=Displayed;
CC Name=2; Synonyms=Helios 1v;
CC IsoId=Q9UKS7-2; Sequence=VSP_006845;
CC Name=3; Synonyms=Helios del(Ex3,4);
CC IsoId=Q9UKS7-3; Sequence=VSP_055347, VSP_055348;
CC Name=4; Synonyms=Helios del(Ex6)v;
CC IsoId=Q9UKS7-4; Sequence=VSP_006845, VSP_055350;
CC Name=5; Synonyms=Helios 1+2a,2b, Helios 1v+2a, Helios del(Ex3)+2a;
CC IsoId=Q9UKS7-5; Sequence=VSP_055345, VSP_055346;
CC Name=6; Synonyms=Helios 1+5a, Helios 1+5a,5b;
CC IsoId=Q9UKS7-6; Sequence=VSP_055351, VSP_055352;
CC Name=7; Synonyms=Helios del(Ex5)v;
CC IsoId=Q9UKS7-7; Sequence=VSP_006845, VSP_055349;
CC Name=8; Synonyms=Helios S;
CC IsoId=Q9UKS7-8; Sequence=VSP_055344;
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IKZF2ID42885ch2q34.html";
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DR EMBL; AF130863; AAF09441.1; -; mRNA.
DR EMBL; AY587062; AAS99855.1; -; mRNA.
DR EMBL; AY587064; AAS99857.1; -; mRNA.
DR EMBL; AY587065; AAS99858.1; -; mRNA.
DR EMBL; AY587066; AAS99859.1; -; mRNA.
DR EMBL; AY587067; AAS99860.1; -; mRNA.
DR EMBL; AY587068; AAS99861.1; -; mRNA.
DR EMBL; AY587069; AAS99862.1; -; mRNA.
DR EMBL; AY587070; AAS99863.1; -; mRNA.
DR EMBL; AY587071; AAS99864.1; -; mRNA.
DR EMBL; AY587072; AAS99865.1; -; mRNA.
DR EMBL; BC028936; AAH28936.1; -; mRNA.
DR CCDS; CCDS2395.1; -. [Q9UKS7-1]
DR CCDS; CCDS46507.1; -. [Q9UKS7-2]
DR RefSeq; NP_001072994.1; NM_001079526.1. [Q9UKS7-2]
DR RefSeq; NP_057344.2; NM_016260.2. [Q9UKS7-1]
DR RefSeq; XP_005246441.1; XM_005246384.4. [Q9UKS7-1]
DR RefSeq; XP_005246442.1; XM_005246385.3. [Q9UKS7-1]
DR RefSeq; XP_011509116.1; XM_011510814.2.
DR RefSeq; XP_016859078.1; XM_017003589.1.
DR RefSeq; XP_016859079.1; XM_017003590.1.
DR PDB; 7LPS; X-ray; 3.78 A; C/F/I/L=136-164.
DR PDBsum; 7LPS; -.
DR AlphaFoldDB; Q9UKS7; -.
DR BMRB; Q9UKS7; -.
DR SMR; Q9UKS7; -.
DR BioGRID; 116485; 25.
DR IntAct; Q9UKS7; 13.
DR MINT; Q9UKS7; -.
DR STRING; 9606.ENSP00000412869; -.
DR GlyGen; Q9UKS7; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9UKS7; -.
DR PhosphoSitePlus; Q9UKS7; -.
DR BioMuta; IKZF2; -.
DR DMDM; 116242509; -.
DR EPD; Q9UKS7; -.
DR jPOST; Q9UKS7; -.
DR MassIVE; Q9UKS7; -.
DR MaxQB; Q9UKS7; -.
DR PaxDb; Q9UKS7; -.
DR PeptideAtlas; Q9UKS7; -.
DR PRIDE; Q9UKS7; -.
DR ProteomicsDB; 84844; -. [Q9UKS7-1]
DR ProteomicsDB; 84845; -. [Q9UKS7-2]
DR Antibodypedia; 34212; 369 antibodies from 39 providers.
DR DNASU; 22807; -.
DR Ensembl; ENST00000374319.8; ENSP00000363439.4; ENSG00000030419.17. [Q9UKS7-2]
DR Ensembl; ENST00000374326.7; ENSP00000363446.3; ENSG00000030419.17. [Q9UKS7-5]
DR Ensembl; ENST00000412444.5; ENSP00000413680.1; ENSG00000030419.17. [Q9UKS7-5]
DR Ensembl; ENST00000431520.5; ENSP00000396253.1; ENSG00000030419.17. [Q9UKS7-6]
DR Ensembl; ENST00000434687.6; ENSP00000412869.1; ENSG00000030419.17. [Q9UKS7-1]
DR Ensembl; ENST00000439848.5; ENSP00000389548.1; ENSG00000030419.17. [Q9UKS7-3]
DR Ensembl; ENST00000453575.5; ENSP00000411444.1; ENSG00000030419.17. [Q9UKS7-5]
DR GeneID; 22807; -.
DR KEGG; hsa:22807; -.
DR MANE-Select; ENST00000434687.6; ENSP00000412869.1; NM_001387220.1; NP_001374149.1.
DR UCSC; uc002ven.5; human. [Q9UKS7-1]
DR CTD; 22807; -.
DR DisGeNET; 22807; -.
DR GeneCards; IKZF2; -.
DR HGNC; HGNC:13177; IKZF2.
DR HPA; ENSG00000030419; Tissue enhanced (lymphoid).
DR MIM; 606234; gene.
DR neXtProt; NX_Q9UKS7; -.
DR OpenTargets; ENSG00000030419; -.
DR PharmGKB; PA162391927; -.
DR VEuPathDB; HostDB:ENSG00000030419; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157137; -.
DR HOGENOM; CLU_3086568_0_0_1; -.
DR InParanoid; Q9UKS7; -.
DR OMA; MEYWEHM; -.
DR OrthoDB; 385551at2759; -.
DR PhylomeDB; Q9UKS7; -.
DR TreeFam; TF331189; -.
DR PathwayCommons; Q9UKS7; -.
DR SignaLink; Q9UKS7; -.
DR SIGNOR; Q9UKS7; -.
DR BioGRID-ORCS; 22807; 22 hits in 1097 CRISPR screens.
DR ChiTaRS; IKZF2; human.
DR GeneWiki; IKZF2; -.
DR GenomeRNAi; 22807; -.
DR Pharos; Q9UKS7; Tbio.
DR PRO; PR:Q9UKS7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UKS7; protein.
DR Bgee; ENSG00000030419; Expressed in thymus and 165 other tissues.
DR ExpressionAtlas; Q9UKS7; baseline and differential.
DR Genevisible; Q9UKS7; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..526
FT /note="Zinc finger protein Helios"
FT /id="PRO_0000047092"
FT ZN_FING 112..134
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..190
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..219
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 471..493
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 499..523
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 28..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 46..341
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055344"
FT VAR_SEQ 47..52
FT /note="TNSVKL -> RSFSKI (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055345"
FT VAR_SEQ 53..526
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055346"
FT VAR_SEQ 111..136
FT /note="Missing (in isoform 2, isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_006845"
FT VAR_SEQ 137..148
FT /note="ERPFHCNQCGAS -> VAVVKTTFSEFC (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055347"
FT VAR_SEQ 149..526
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055348"
FT VAR_SEQ 192..237
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055349"
FT VAR_SEQ 238..285
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055350"
FT VAR_SEQ 238..239
FT /note="VP -> DS (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055351"
FT VAR_SEQ 240..526
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055352"
FT VARIANT 93
FT /note="N -> S (in dbSNP:rs16849611)"
FT /id="VAR_028227"
FT CONFLICT 4
FT /note="E -> D (in Ref. 1; AAF09441 and 2; AAS99855/
FT AAS99857/AAS99858/AAS99859/AAS99860/AAS99861/AAS99862/
FT AAS99863/AAS99864/AAS99865)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="D -> N (in Ref. 1; AAF09441 and 2; AAS99857/
FT AAS99859/AAS99861/AAS99862/AAS99863/AAS99864)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q9UKS7-2:95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9UKS7-4:95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9UKS7-7:95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 526 AA; 59574 MW; 949BE60E242BA8E8 CRC64;
METEAIDGYI TCDNELSPER EHSNMAIDLT SSTPNGQHAS PSHMTSTNSV KLEMQSDEEC
DRKPLSREDE IRGHDEGSSL EEPLIESSEV ADNRKVQELQ GEGGIRLPNG KLKCDVCGMV
CIGPNVLMVH KRSHTGERPF HCNQCGASFT QKGNLLRHIK LHSGEKPFKC PFCSYACRRR
DALTGHLRTH SVGKPHKCNY CGRSYKQRSS LEEHKERCHN YLQNVSMEAA GQVMSHHVPP
MEDCKEQEPI MDNNISLVPF ERPAVIEKLT GNMGKRKSST PQKFVGEKLM RFSYPDIHFD
MNLTYEKEAE LMQSHMMDQA INNAITYLGA EALHPLMQHP PSTIAEVAPV ISSAYSQVYH
PNRIERPISR ETADSHENNM DGPISLIRPK SRPQEREASP SNSCLDSTDS ESSHDDHQSY
QGHPALNPKR KQSPAYMKED VKALDTTKAP KGSLKDIYKV FNGEGEQIRA FKCEHCRVLF
LDHVMYTIHM GCHGYRDPLE CNICGYRSQD RYEFSSHIVR GEHTFH
