IKZF1_MOUSE
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 25-MAY-2022, entry version 181.
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}.
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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 iPTMnet; Q03267; -.
DR PhosphoSitePlus; Q03267; -.
DR EPD; Q03267; -.
DR jPOST; Q03267; -.
DR MaxQB; Q03267; -.
DR PaxDb; Q03267; -.
DR PeptideAtlas; Q03267; -.
DR PRIDE; 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 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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048541; P:Peyer's patch development; IMP: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 from RNA polymerase II promoter; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 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; 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 5-
FT 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 A-
FT 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 D-
FT 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 5-
FT fold and to gamma satellite B by 3-fold. Diffuse nuclear
FT location. Decreased DNA binding affinity toward TdT by 3-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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
