ID IKZF1_MOUSE Reviewed; 517 AA. AC Q03267; Q64044; Q64045; Q64051; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 24-JAN-2024, entry version 186. DE RecName: Full=DNA-binding protein Ikaros; DE AltName: Full=Ikaros family zinc finger protein 1; DE AltName: Full=Lymphoid transcription factor LyF-1; GN Name=Ikzf1; Synonyms=Ikaros, Lyf1, Zfpn1a1, Znfn1a1; 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] (ISOFORM V), FUNCTION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=1439790; DOI=10.1126/science.1439790; RA Georgopoulos K., Moore D.D., Derfler B.; RT "Ikaros, an early lymphoid-specific transcription factor and a putative RT mediator for T cell commitment."; RL Science 258:808-812(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, RP AND TISSUE SPECIFICITY. RX PubMed=7935426; DOI=10.1128/mcb.14.11.7111-7123.1994; RA Hahm K., Ernst P., Lo K., Kim G.S., Turck C., Smale S.T.; RT "The lymphoid transcription factor LyF-1 is encoded by specific, RT alternatively spliced mRNAs derived from the Ikaros gene."; RL Mol. Cell. Biol. 14:7111-7123(1994). RN [3] RP INTERACTION WITH IKZF3. RX PubMed=9155026; DOI=10.1093/emboj/16.8.2004; RA Morgan B., Sun L., Avitahl N., Andrikopoulos K., Ikeda T., Gonzales E., RA Wu P., Neben S., Georgopoulos K.; RT "Aiolos, a lymphoid restricted transcription factor that interacts with RT Ikaros to regulate lymphocyte differentiation."; RL EMBO J. 16:2004-2013(1997). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=10544193; DOI=10.1084/jem.190.9.1201; RA Nichogiannopoulou A., Trevisan M., Neben S., Friedrich C., Georgopoulos K.; RT "Defects in hemopoietic stem cell activity in Ikaros mutant mice."; RL J. Exp. Med. 190:1201-1214(1999). RN [5] RP DNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-152; PHE-153; RP THR-154; GLN-155; LYS-156; GLY-157; ASN-158; LEU-159; LEU-160; ARG-161; RP LYS-173; ASN-178; TYR-179; ALA-180; CYS-181; ARG-182; ARG-183; ARG-184; RP ASP-185; ALA-186; LEU-187; THR-188; GLY-189; LEU-191; ARG-192 AND THR-193. RX PubMed=10970879; DOI=10.1101/gad.816400; RA Cobb B.S., Morales-Alcelay S., Kleiger G., Brown K.E., Fisher A.G., RA Smale S.T.; RT "Targeting of Ikaros to pericentromeric heterochromatin by direct DNA RT binding."; RL Genes Dev. 14:2146-2160(2000). RN [6] RP IDENTIFICATION IN THE NURD COMPLEX, IDENTIFICATION IN THE BAF COMPLEX, RP INTERACTION WITH CHD4, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11003653; DOI=10.1128/mcb.20.20.7572-7582.2000; RA O'Neill D.W., Schoetz S.S., Lopez R.A., Castle M., Rabinowitz L., Shor E., RA Krawchuk D., Goll M.G., Renz M., Seelig H.P., Han S., Seong R.H., RA Park S.D., Agalioti T., Munshi N., Thanos D., Erdjument-Bromage H., RA Tempst P., Bank A.; RT "An ikaros-containing chromatin-remodeling complex in adult-type erythroid RT cells."; RL Mol. Cell. Biol. 20:7572-7582(2000). RN [7] RP PHOSPHORYLATION AT THR-140; SER-167 AND SER-195, SUBCELLULAR LOCATION, RP DNA-BINDING, AND MUTAGENESIS OF THR-140; SER-167 AND SER-195. RX PubMed=12464629; DOI=10.1101/gad.1040502; RA Dovat S., Ronni T., Russell D., Ferrini R., Cobb B.S., Smale S.T.; RT "A common mechanism for mitotic inactivation of C2H2 zinc finger DNA- RT binding domains."; RL Genes Dev. 16:2985-2990(2002). RN [8] RP PHOSPHORYLATION AT SER-63; SER-384; SER-386; SER-388; SER-392 AND THR-393, RP DNA-BINDING, FUNCTION, AND MUTAGENESIS OF SER-63; SER-384; SER-386; RP SER-388; SER-392 AND THR-393. RX PubMed=15024069; DOI=10.1128/mcb.24.7.2797-2807.2004; RA Gomez-del Arco P., Maki K., Georgopoulos K.; RT "Phosphorylation controls Ikaros's ability to negatively regulate the G(1)- RT S transition."; RL Mol. Cell. Biol. 24:2797-2807(2004). RN [9] RP SUMOYLATION AT LYS-58 AND LYS-239, INTERACTION WITH SUMO1; PIAS2; PIAS3 AND RP SMARCA4, FUNCTION, AND MUTAGENESIS OF LYS-58; LYS-239; LYS-424 AND LYS-458. RX PubMed=15767674; DOI=10.1128/mcb.25.7.2688-2697.2005; RA Gomez-del Arco P., Koipally J., Georgopoulos K.; RT "Ikaros SUMOylation: switching out of repression."; RL Mol. Cell. Biol. 25:2688-2697(2005). RN [10] RP FUNCTION. RX PubMed=16369973; DOI=10.1002/ajh.20507; RA Pulte D., Lopez R.A., Baker S.T., Ward M., Ritchie E., Richardson C.A., RA O'Neill D.W., Bank A.; RT "Ikaros increases normal apoptosis in adult erythroid cells."; RL Am. J. Hematol. 81:12-18(2006). RN [11] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=18940586; DOI=10.1016/j.neuron.2008.08.008; RA Elliott J., Jolicoeur C., Ramamurthy V., Cayouette M.; RT "Ikaros confers early temporal competence to mouse retinal progenitor RT cells."; RL Neuron 60:26-39(2008). RN [12] RP PHOSPHORYLATION AT SER-13; THR-23; SER-63; SER-101 AND SER-293, FUNCTION, RP SUBCELLULAR LOCATION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, AND RP MUTAGENESIS OF SER-13; THR-23; SER-63; SER-101 AND SER-293. RX PubMed=18223295; DOI=10.1074/jbc.m707906200; RA Gurel Z., Ronni T., Ho S., Kuchar J., Payne K.J., Turk C.W., Dovat S.; RT "Recruitment of ikaros to pericentromeric heterochromatin is regulated by RT phosphorylation."; RL J. Biol. Chem. 283:8291-8300(2008). RN [13] RP INTERACTION WITH PPP1CC, PHOSPHORYLATION, SUBCELLULAR LOCATION, RP UBIQUITINATION, AND MUTAGENESIS OF 465-LEU--LEU-467. RX PubMed=19282287; DOI=10.1074/jbc.m900209200; RA Popescu M., Gurel Z., Ronni T., Song C., Hung K.Y., Payne K.J., Dovat S.; RT "Ikaros stability and pericentromeric localization are regulated by protein RT phosphatase 1."; RL J. Biol. Chem. 284:13869-13880(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-397 AND SER-440, AND RP IDENTIFICATION BY 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: Transcription regulator of hematopoietic cell CC differentiation. Binds gamma-satellite DNA. Binds with higher affinity CC to gamma satellite A. Plays a role in the development of lymphocytes, CC B- and T-cells. Binds and activates the enhancer (delta-A element) of CC the CD3-delta gene. Repressor of the TDT (terminal CC deoxynucleotidyltransferase) gene during thymocyte differentiation. CC Regulates transcription through association with both HDAC-dependent CC and HDAC-independent complexes. Targets the 2 chromatin-remodeling CC complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), CC to the beta-globin locus in adult erythrocytes. Increases normal CC apoptosis in adult erythroid cells (By similarity). Confers early CC temporal competence to retinal progenitor cells (RPCs). Function is CC isoform-specific and is modulated by dominant-negative inactive CC isoforms (By similarity). {ECO:0000250|UniProtKB:Q13422, CC ECO:0000269|PubMed:11003653, ECO:0000269|PubMed:1439790, CC ECO:0000269|PubMed:15024069, ECO:0000269|PubMed:15767674, CC ECO:0000269|PubMed:16369973, ECO:0000269|PubMed:18223295, CC ECO:0000269|PubMed:18940586}. CC -!- SUBUNIT: Heterodimer with other IKAROS family members. Interacts with CC IKZF4 and IKZF5 (By similarity). Component of the chromatin-remodeling CC NuRD repressor complex which includes at least HDAC1, HDAC2, RBBP4, CC RBBP7, IKZF1, MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4. Interacts CC directly with the CHD4 component of the NuRD complex. Interacts CC directly with SMARCA4; the interaction associates IKFZ1 with the BAF CC complex. Interacts with SUMO1; the interaction sumoylates IKAROS, CC promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform alpha); the CC interaction promotes sumoylation and reduces transcription repression. CC Interacts, to a lesser extent, with PIAS3. Interacts with PPP1CC; the CC interaction targets PPP1CC to pericentromeric heterochromatin, CC dephosphorylates IKAROS, stabilizes it and prevents it from CC degradation. Interacts with IKZF3. {ECO:0000250|UniProtKB:Q13422, CC ECO:0000269|PubMed:11003653, ECO:0000269|PubMed:15767674, CC ECO:0000269|PubMed:19282287, ECO:0000269|PubMed:9155026}. CC -!- INTERACTION: CC Q03267; P63166: Sumo1; NbExp=2; IntAct=EBI-908572, EBI-80152; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10970879, CC ECO:0000269|PubMed:12464629, ECO:0000269|PubMed:18223295, CC ECO:0000269|PubMed:19282287}. Note=In resting lymphocytes, distributed CC diffusely throughout the nucleus. Localizes to pericentromeric CC heterochromatin in proliferating cells. This localization requires DNA CC binding which is regulated by phosphorylation / dephosphorylation CC events. CC -!- SUBCELLULAR LOCATION: [Isoform V]: Nucleus. Note=In resting CC lymphocytes, distributed diffusely throughout the nucleus. Localizes to CC pericentromeric heterochromatin in proliferating cells. This CC localization requires DNA binding which is regulated by phosphorylation CC / dephosphorylation events. CC -!- SUBCELLULAR LOCATION: [Isoform I]: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=VI; CC IsoId=Q03267-1; Sequence=Displayed; CC Name=I; CC IsoId=Q03267-2; Sequence=VSP_006855; CC Name=II; CC IsoId=Q03267-3; Sequence=VSP_006853, VSP_006855; CC Name=III; CC IsoId=Q03267-4; Sequence=VSP_006856; CC Name=IV; CC IsoId=Q03267-5; Sequence=VSP_006853, VSP_006856; CC Name=V; CC IsoId=Q03267-6; Sequence=VSP_006854; CC -!- TISSUE SPECIFICITY: Strongly expressed in T-cells and their CC progenitors,in B-cells, and in all early embryonic retinal progenitor CC cells (RPCs). Isoforms V and VI are the predominant isoforms in CC lymphocytes. {ECO:0000269|PubMed:1439790, ECO:0000269|PubMed:18940586, CC ECO:0000269|PubMed:7935426}. CC -!- DEVELOPMENTAL STAGE: First detected in fetal liver and embryonic CC thymus. {ECO:0000269|PubMed:1439790}. CC -!- DOMAIN: The N-terminal zinc-fingers 2 and 3 are required for DNA CC binding as well as for targeting IKFZ1 to pericentromeric CC heterochromatin. CC -!- DOMAIN: The C-terminal zinc-finger domain is required for dimerization. CC -!- PTM: Phosphorylation at Ser-357 and Ser-360 downstream of SYK induces CC nuclear translocation (By similarity). Phosphorylation controls cell- CC cycle progression from late G(1) stage to S stage. Hyperphosphorylated CC during G2/M phase. Dephosphorylated state during late G(1) phase. CC Phosphorylation on Thr-140 is required for DNA and pericentromeric CC location during mitosis. CK2 is the main kinase, in vitro. GSK3 and CDK CC may also contribute to phosphorylation of the C-terminal serine and CC threonine residues. Phosphorylation on these C-terminal residues CC reduces the DNA-binding ability. Phosphorylation/dephosphorylation CC events on Ser-13 and Ser-293 regulate TDT expression during thymocyte CC differentiation. Dephosphorylation by protein phosphatase 1 regulates CC stability and pericentromeric heterochromatin location. Phosphorylated CC in both lymphoid and non-lymphoid tissues. {ECO:0000250, CC ECO:0000269|PubMed:12464629, ECO:0000269|PubMed:15024069, CC ECO:0000269|PubMed:18223295, ECO:0000269|PubMed:19282287}. CC -!- PTM: Sumoylated. Simultaneous sumoylation on the 2 sites results in a CC loss of both HDAC-dependent and HDAC-independent repression. Has no CC effect on pericentromeric heterochromatin location. Desumoylated by CC SENP1. {ECO:0000269|PubMed:15767674}. CC -!- PTM: Polyubiquitinated. {ECO:0000269|PubMed:19282287}. CC -!- DISRUPTION PHENOTYPE: Defects in hemopoietic stem cell activity. CC Progressive reduction in multipotent CFU-S(14) (colony-forming unit- CC spleen) progenitors and the earliest erythroid-restricted precursors CC (BFU-E). {ECO:0000269|PubMed:10544193}. CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L03547; AAA66193.1; -; mRNA. DR EMBL; S74517; AAB32248.2; ALT_SEQ; mRNA. DR EMBL; S74518; AAB32249.2; -; mRNA. DR EMBL; S74708; AAB32250.2; -; mRNA. DR PIR; A56355; A56355. DR PIR; I59572; I59572. DR AlphaFoldDB; Q03267; -. DR SMR; Q03267; -. DR CORUM; Q03267; -. DR IntAct; Q03267; 11. DR STRING; 10090.ENSMUSP00000075992; -. DR iPTMnet; Q03267; -. DR PhosphoSitePlus; Q03267; -. DR SwissPalm; Q03267; -. DR EPD; Q03267; -. DR jPOST; Q03267; -. DR MaxQB; Q03267; -. DR PeptideAtlas; Q03267; -. DR ProteomicsDB; 267308; -. [Q03267-1] DR ProteomicsDB; 267309; -. [Q03267-2] DR ProteomicsDB; 267310; -. [Q03267-3] DR ProteomicsDB; 267311; -. [Q03267-4] DR ProteomicsDB; 267312; -. [Q03267-5] DR ProteomicsDB; 267313; -. [Q03267-6] DR AGR; MGI:1342540; -. DR MGI; MGI:1342540; Ikzf1. DR eggNOG; KOG1721; Eukaryota. DR InParanoid; Q03267; -. DR ChiTaRS; Ikzf1; mouse. DR PRO; PR:Q03267; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q03267; Protein. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0032993; C:protein-DNA complex; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0035881; P:amacrine cell differentiation; IDA:MGI. DR GO; GO:0030183; P:B cell differentiation; IMP:MGI. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IMP:MGI. DR GO; GO:0048732; P:gland development; IMP:MGI. DR GO; GO:0030097; P:hemopoiesis; IMP:MGI. DR GO; GO:0048535; P:lymph node development; IMP:MGI. DR GO; GO:0030098; P:lymphocyte differentiation; ISS:UniProtKB. DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0048541; P:Peyer's patch development; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0045660; P:positive regulation of neutrophil differentiation; IMP:MGI. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IMP:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0060040; P:retinal bipolar neuron differentiation; IDA:MGI. DR GO; GO:0030217; P:T cell differentiation; IMP:MGI. DR GO; GO:0048538; P:thymus development; IMP:MGI. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24404:SF36; DNA-BINDING PROTEIN IKAROS; 1. DR PANTHER; PTHR24404; ZINC FINGER PROTEIN; 1. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 6. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Cell cycle; Chromatin regulator; KW Cytoplasm; Developmental protein; Direct protein sequencing; DNA-binding; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..517 FT /note="DNA-binding protein Ikaros" FT /id="PRO_0000047095" FT ZN_FING 117..139 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 144..166 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 172..194 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 200..223 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 457..479 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 488..512 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 153..162 FT /note="Required for both high-affinity DNA binding and FT pericentromeric heterochromatin localization" FT REGION 179..194 FT /note="Required for both high-affinity DNA binding and FT pericentromeric heterochromatin localization" FT REGION 376..400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 463..466 FT /note="Required for binding PP1CC" FT COMPBIAS 37..61 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 158 FT /note="Required for both pericentromeric heterochromatin FT localization and complete DNA binding" FT SITE 161 FT /note="Required for both pericentromeric heterochromatin FT localization and complete DNA binding" FT SITE 187 FT /note="Required for both pericentromeric heterochromatin FT localization and DNA binding" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18223295" FT MOD_RES 23 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18223295" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15024069, FT ECO:0000269|PubMed:18223295, ECO:0007744|PubMed:21183079" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18223295" FT MOD_RES 140 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:12464629" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12464629" FT MOD_RES 195 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12464629" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13422" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13422" FT MOD_RES 293 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18223295" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13422" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13422" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15024069" FT MOD_RES 386 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15024069" FT MOD_RES 388 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15024069" FT MOD_RES 392 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15024069" FT MOD_RES 393 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15024069" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 58 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15767674" FT CROSSLNK 239 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15767674" FT VAR_SEQ 53 FT /note="M -> VAYGADGFRDFHAIISDRGM (in isoform II and isoform FT IV)" FT /evidence="ECO:0000305" FT /id="VSP_006853" FT VAR_SEQ 54..282 FT /note="Missing (in isoform I and isoform II)" FT /evidence="ECO:0000305" FT /id="VSP_006855" FT VAR_SEQ 54..140 FT /note="Missing (in isoform V)" FT /evidence="ECO:0000303|PubMed:1439790" FT /id="VSP_006854" FT VAR_SEQ 141..282 FT /note="Missing (in isoform III and isoform IV)" FT /evidence="ECO:0000305" FT /id="VSP_006856" FT MUTAGEN 13 FT /note="S->A: Abolishes phosphorylation. No change in FT binding to gamma satellites A and B. No change in FT pericentromeric location. Increased DNA binding affinity FT toward TDT." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 13 FT /note="S->D: Decreased binding to gamma satellite A by FT 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear FT location." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 23 FT /note="T->A: Abolishes phosphorylation. No change in FT binding to gamma satellites A and B. No change in FT pericentromeric location." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 23 FT /note="T->D: Decreased binding to gamma satellites A and B FT by 3-fold. Little change in pericentromeric location." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 58 FT /note="K->R: Some loss of sumoylation. Complete loss of FT sumoylation, increased repressor activity but no change in FT pericentromeric heterochromatin location; when associated FT with R-240 and R-459." FT /evidence="ECO:0000269|PubMed:15767674" FT MUTAGEN 63 FT /note="S->A: No change in pericentromeric location. Greatly FT reduced phosphorylation; when associated with A-384; A-386; FT A-388; A392 and A-393. No effect on DNA-binding activity. FT Increased DNA-binding activity; when associated with A-384; FT A-386; A-388; A-392 and A-393." FT /evidence="ECO:0000269|PubMed:15024069, FT ECO:0000269|PubMed:18223295" FT MUTAGEN 63 FT /note="S->D: No change in binding to gamma satellites A and FT B. No change in pericentromeric location." FT /evidence="ECO:0000269|PubMed:15024069, FT ECO:0000269|PubMed:18223295" FT MUTAGEN 101 FT /note="S->A: Abolishes phosphorylation. No change in FT pericentromeric location." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 101 FT /note="S->D: No change in binding to gamma satellites A and FT B. No change in pericentromeric location." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 140 FT /note="T->A: Abolishes phosphorylation, DNA binding and FT pericentromeric location. Loss of DNA binding and FT pericentromeric location; when associated with A-167 and FT A-195." FT /evidence="ECO:0000269|PubMed:12464629" FT MUTAGEN 140 FT /note="T->E: Abolishes phosphorylation, DNA binding and FT pericentromeric location. Loss of DNA binding and FT pericentromeric location; when associated with E-167 and FT D-195." FT /evidence="ECO:0000269|PubMed:12464629" FT MUTAGEN 152 FT /note="S->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 153 FT /note="F->A: Disrupts pericentromeric heterochromatin FT location. Partial cytoplasmic location. Abolishes DNA FT binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 154 FT /note="T->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 155 FT /note="Q->A: Loss of pericentromeric heterochromatin FT location. Disrupted DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 156 FT /note="K->A: Disrupts pericentromeric heterochromatin FT location. Partial cytoplasmic location." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 157 FT /note="G->A: Loss of pericentromeric heterochromatin FT location. Disrupted DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 158 FT /note="N->A: Loss of pericentromeric heterochromatin FT location. Abolishes DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 159 FT /note="L->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 160 FT /note="L->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 161 FT /note="R->A: Disrupts pericentromeric heterochromatin FT location. Partial cytoplasmic location. Abolishes DNA FT binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 167 FT /note="S->A: Abolishes phosphorylation, no effect on DNA FT binding nor on pericentromeric location. Loss of DNA FT binding and pericentromeric location; when associated with FT A-140 and A-195." FT /evidence="ECO:0000269|PubMed:12464629" FT MUTAGEN 167 FT /note="S->E: Abolishes phosphorylation, no effect on DNA FT binding nor on pericentromeric location. Loss of DNA FT binding and pericentromeric location; when associated with FT E-140 and D-195." FT /evidence="ECO:0000269|PubMed:12464629" FT MUTAGEN 173 FT /note="K->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 178 FT /note="N->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 179 FT /note="Y->A: Loss of pericentromeric heterochromatin FT location. Abolishes DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 180 FT /note="A->L: Loss of pericentromeric heterochromatin FT location. Disrupted DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 181 FT /note="C->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 182 FT /note="R->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 183 FT /note="R->A: Disrupts pericentromeric heterochromatin FT location. Partial cytoplasmic location. Abolishes DNA FT binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 184 FT /note="R->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 185 FT /note="D->A: No effect on pericentromeric heterochromatin FT location. Disrupted DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 186 FT /note="A->L: No effect on pericentromeric heterochromatin FT location. Disrupted DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 187 FT /note="L->A: Loss of pericentromeric heterochromatin FT location. Abolishes DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 188 FT /note="T->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 189 FT /note="G->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 191 FT /note="L->A: No effect on pericentromeric heterochromatin FT location. Disrupted DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 192 FT /note="R->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 193 FT /note="T->A: No effect on pericentromeric heterochromatin FT location. No change in DNA binding." FT /evidence="ECO:0000269|PubMed:10970879" FT MUTAGEN 195 FT /note="S->A: Abolishes phosphorylation, no effect on DNA FT binding nor on pericentromeric location. Loss of DNA FT binding and pericentromeric location; when associated with FT A-140 and A-167." FT /evidence="ECO:0000269|PubMed:12464629" FT MUTAGEN 195 FT /note="S->D: Abolishes phosphorylation, no effect on DNA FT binding nor on pericentromeric location. Loss of DNA FT binding and pericentromeric location; when associated with FT E-140 and E-167." FT /evidence="ECO:0000269|PubMed:12464629" FT MUTAGEN 239 FT /note="K->R: Some loss of sumoylation. Complete loss of FT sumoylation, increased repressor activity but no change in FT pericentromeric heterochromatin location.; when associated FT with R-58 and R-459." FT /evidence="ECO:0000269|PubMed:15767674" FT MUTAGEN 293 FT /note="S->A: Abolishes phosphorylation. No change in FT binding to gamma satellites A and B. No change in FT pericentromeric location. Increased DNA binding affinity FT toward TDT." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 293 FT /note="S->D: Decreased binding to gamma satellite A by FT 5-fold and to gamma satellite B by 3-fold. Diffuse nuclear FT location. Decreased DNA binding affinity toward TdT by FT 3-fold." FT /evidence="ECO:0000269|PubMed:18223295" FT MUTAGEN 384 FT /note="S->A: Significantly reduced phosphorylation and FT 2- to 3-fold increase in ability to arrest in G(1); when FT associated with A-386; A-388; A-392 and A-393. and A-392. FT Further reduction in phosphorylation; when associated with FT A-63; A-386; A-388; A-392 and A-393." FT /evidence="ECO:0000269|PubMed:15024069" FT MUTAGEN 386 FT /note="S->A: Significantly reduced phosphorylation and FT 2- to 3-fold increase in ability to arrest in G(1); when FT associated with A-384; A-388; A-392 and A-393. Further FT reduction in phosphorylation; when associated with A-63; FT A-384; A-388; A-392 and A-393." FT /evidence="ECO:0000269|PubMed:15024069" FT MUTAGEN 388 FT /note="S->A: Significantly reduced phosphorylation and FT 2- to 3-fold increase in ability to arrest in G(1); when FT associated with A-384; A-386; A-392 and A-393. Further FT reduction in phosphorylation; when associated with A-63; FT A-384; A-386; A-392 and A-393." FT /evidence="ECO:0000269|PubMed:15024069" FT MUTAGEN 392 FT /note="S->A: Significantly reduced phosphorylation and FT 2- to 3-fold increase in ability to arrest in G(1); when FT associated with A-384; A-386; A-388 and A-392. Further FT reduction in phosphorylation; when associated with A-63; FT A-384; A-386; A-386 and A-388." FT /evidence="ECO:0000269|PubMed:15024069" FT MUTAGEN 393 FT /note="T->A: Significantly reduced phosphorylation and FT 2- to 3-fold increase in ability to arrest in G(1); when FT associated with A-384; A-386; A-388 and A-392. Further FT reduction in phosphorylation; when associated with A-63; FT A-384; A-386; A-388 and A-392." FT /evidence="ECO:0000269|PubMed:15024069" FT MUTAGEN 424 FT /note="K->R: No effect on sumoylation." FT /evidence="ECO:0000269|PubMed:15767674" FT MUTAGEN 458 FT /note="K->R: No effect on sumoylation." FT /evidence="ECO:0000269|PubMed:15767674" FT MUTAGEN 465..467 FT /note="LFL->AFA: Abolishes binding of PP1CC, decreases DNA FT binding, abolishes pericentromeric location, and results in FT IKAROS degradation." FT /evidence="ECO:0000269|PubMed:19282287" FT CONFLICT 234..235 FT /note="VC -> MY (in Ref. 2; AAB32250)" FT /evidence="ECO:0000305" FT CONFLICT 480..482 FT /note="Missing (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 517 AA; 57336 MW; 1052B8E76AF24287 CRC64; MDVDEGQDMS QVSGKESPPV SDTPDEGDEP MPVPEDLSTT SGAQQNSKSD RGMGSNVKVE TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD ICGIVCIGPN VLMVHKRSHT ERPFQCNQCG ASFTQKGNLL RHIKLHSGEK PFKCHLCNYA CRRRDALTGH LRTHSVGKPH KCGYCGRSYK QRSSLEEHKE RCHNYLESMG LPGVCPVIKE ETNHNEMAED LCKIGAERSL VLDRLASNVA KRKSSMPQKF LGDKCLSDMP YDSANYEKED MMTSHVMDQA INNAINYLGA ESLRPLVQTP PGSSEVVPVI SSMYQLHKPP SDGPPRSNHS AQDAVDNLLL LSKAKSVSSE REASPSNSCQ DSTDTESNAE EQRSGLIYLT NHINPHARNG LALKEEQRAY EVLRAASENS QDAFRVVSTS GEQLKVYKCE HCRVLFLDHV MYTIHMGCHG CHGFRDPFEC NMCGYHSQDR YEFSSHITRG EHRYHLS //