IKZF2_MOUSE
ID IKZF2_MOUSE Reviewed; 526 AA.
AC P81183; Q8C8A3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein Helios;
DE AltName: Full=Ikaros family zinc finger protein 2;
GN Name=Ikzf2; Synonyms=Helios, Zfpn1a2, Znfn1a2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 246-267 AND 289-306.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=9512513; DOI=10.1101/gad.12.6.782;
RA Hahm K., Cobb B.S., McCarty A.S., Brown K.E., Klug C.A., Lee R., Akashi K.,
RA Weissman I.L., Fisher A.G., Smale S.T.;
RT "Helios, a T cell-restricted Ikaros family member that quantitatively
RT associates with Ikaros at centromeric heterochromatin.";
RL Genes Dev. 12:782-796(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Associates with Ikaros at centromeric heterochromatin.
CC -!- SUBUNIT: Interacts with IKZF4 AND IKZF5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P81183-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P81183-2; Sequence=VSP_006846;
CC -!- TISSUE SPECIFICITY: Restricted to the T-cell lineage. Abundant in
CC thymus, low expression in bone marrow and brain and no detectable
CC expression in spleen, liver, kidney or muscle.
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF044257; AAC00513.1; -; mRNA.
DR EMBL; AK047925; BAC33191.1; -; mRNA.
DR EMBL; CH466548; EDL00252.1; -; Genomic_DNA.
DR EMBL; BC138606; AAI38607.1; -; mRNA.
DR EMBL; BC138608; AAI38609.1; -; mRNA.
DR CCDS; CCDS15026.1; -. [P81183-1]
DR RefSeq; NP_035900.2; NM_011770.4. [P81183-1]
DR RefSeq; XP_006496029.1; XM_006495966.3. [P81183-1]
DR RefSeq; XP_006496030.1; XM_006495967.3. [P81183-1]
DR RefSeq; XP_017175888.1; XM_017320399.1. [P81183-1]
DR AlphaFoldDB; P81183; -.
DR BMRB; P81183; -.
DR SMR; P81183; -.
DR BioGRID; 204701; 1.
DR CORUM; P81183; -.
DR IntAct; P81183; 1.
DR STRING; 10090.ENSMUSP00000027146; -.
DR iPTMnet; P81183; -.
DR PhosphoSitePlus; P81183; -.
DR jPOST; P81183; -.
DR MaxQB; P81183; -.
DR PaxDb; P81183; -.
DR PRIDE; P81183; -.
DR ProteomicsDB; 266964; -. [P81183-1]
DR ProteomicsDB; 266965; -. [P81183-2]
DR Antibodypedia; 34212; 369 antibodies from 39 providers.
DR DNASU; 22779; -.
DR Ensembl; ENSMUST00000027146; ENSMUSP00000027146; ENSMUSG00000025997. [P81183-1]
DR Ensembl; ENSMUST00000187184; ENSMUSP00000141075; ENSMUSG00000025997. [P81183-2]
DR GeneID; 22779; -.
DR KEGG; mmu:22779; -.
DR UCSC; uc007bjd.2; mouse. [P81183-1]
DR CTD; 22807; -.
DR MGI; MGI:1342541; Ikzf2.
DR VEuPathDB; HostDB:ENSMUSG00000025997; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157137; -.
DR HOGENOM; CLU_025502_0_1_1; -.
DR InParanoid; P81183; -.
DR OrthoDB; 385551at2759; -.
DR TreeFam; TF331189; -.
DR BioGRID-ORCS; 22779; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ikzf2; mouse.
DR PRO; PR:P81183; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P81183; protein.
DR Bgee; ENSMUSG00000025997; Expressed in conjunctival fornix and 186 other tissues.
DR ExpressionAtlas; P81183; baseline and differential.
DR Genevisible; P81183; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
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 Acetylation; Activator; Alternative splicing; Direct protein sequencing;
KW DNA-binding; 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_0000047093"
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..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..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..94
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:21183079"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT VAR_SEQ 111..136
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_006846"
FT CONFLICT 384
FT /note="I -> T (in Ref. 1; AAC00513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59401 MW; D70217FE9CCC2F7D CRC64;
METDAIDGYI TCDNELSPEG EHANMAIDLT SSTPNGQHAS PSHMTSTNSV KLEMQSDEEC
DRQPLSREDE IRGHDEGSSL EEPLIESSEV ADNRKVQDLQ GEGGIRLPNG KLKCDVCGMV
CIGPNVLMVH KRSHTGERPF HCNQCGASFT QKGNLLRHIK LHSGEKPFKC PFCSYACRRR
DALTGHLRTH SVGKPHKCNY CGRSYKQRSS LEEHKERCHN YLQNVSMEAA GQVMSHHVPP
MEDCKEQEPI MDNNISLVPF ERPAVIEKLT ANMGKRKSST PQKFVGEKLM RFSYPDIHFD
MNLTYEKEAE LMQSHMMDQA INNAITYLGA EALHPLMQHA PSTIAEVAPV ISSAYSQVYH
PNRIERPISR ETSDSHENNM DGPISLIRPK SRPQEREASP SNSCLDSTDS ESSHDDRQSY
QGNPALNPKR KQSPAYMKED VKALDATKAP KGSLKDIYKV FNGEGEQIRA FKCEHCRVLF
LDHVMYTIHM GCHGYRDPLE CNICGYRSQD RYEFSSHIVR GEHTFH
