IKZF1_HUMAN
ID IKZF1_HUMAN Reviewed; 519 AA.
AC Q13422; A4D260; B4E0Z1; D3DVM5; O00598; Q53XL2; Q69BM4; Q8WVA3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 206.
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=IK1, IKAROS, LYF1, ZNFN1A1;
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], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=8964602; DOI=10.1016/0165-2478(95)02479-4;
RA Nietfeld W., Meyerhans A.;
RT "Cloning and sequencing of hIk-1, a cDNA encoding a human homologue of
RT mouse Ikaros/LyF-1.";
RL Immunol. Lett. 49:139-141(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=8543809;
RA Molnar A., Wu P., Largespada D.A., Vortkamp A., Scherer S., Copeland N.G.,
RA Jenkins N.A., Bruns G., Georgopoulos K.;
RT "The Ikaros gene encodes a family of lymphocyte-restricted zinc finger DNA
RT binding proteins, highly conserved in human and mouse.";
RL J. Immunol. 156:585-592(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IKX).
RA Sanchez-Tapia E.M., Rodriguez R.E., Gonzalez-Sarmiento R.;
RT "Molecular misreading is involved in generation of Ikaros diversity.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
RC TISSUE=Lymph;
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 [10]
RP IDENTIFICATION IN THE NURD COMPLEX, INTERACTION WITH SMARCA4 AND CHD4, AND
RP FUNCTION.
RX PubMed=10204490; DOI=10.1016/s1074-7613(00)80034-5;
RA Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S.,
RA Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.;
RT "Ikaros DNA-binding proteins direct formation of chromatin remodeling
RT complexes in lymphocytes.";
RL Immunity 10:345-355(1999).
RN [11]
RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION
RP WITH BCL6.
RX PubMed=10753856;
RA Hosokawa Y., Maeda Y., Ichinohasama R., Miura I., Taniwaki M., Seto M.;
RT "The Ikaros gene, a central regulator of lymphoid differentiation, fuses to
RT the BCL6 gene as a result of t(3;7)(q27;p12) translocation in a patient
RT with diffuse large B-cell lymphoma.";
RL Blood 95:2719-2721(2000).
RN [12]
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 [13]
RP FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17135265; DOI=10.1074/jbc.m605627200;
RA Ronni T., Payne K.J., Ho S., Bradley M.N., Dorsam G., Dovat S.;
RT "Human Ikaros function in activated T cells is regulated by coordinated
RT expression of its largest isoforms.";
RL J. Biol. Chem. 282:2538-2547(2007).
RN [14]
RP FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=17934067; DOI=10.1182/blood-2007-07-098202;
RA Dijon M., Bardin F., Murati A., Batoz M., Chabannon C., Tonnelle C.;
RT "The role of Ikaros in human erythroid differentiation.";
RL Blood 111:1138-1146(2008).
RN [15]
RP FUNCTION IN GAMMA SATELLITE DNA-BINDING.
RX PubMed=19141594; DOI=10.1101/gr.086496.108;
RA Kim J.-H., Ebersole T., Kouprina N., Noskov V.N., Ohzeki J.-I.,
RA Masumoto H., Mravinac B., Sullivan B.A., Pavlicek A., Dovat S., Pack S.D.,
RA Kwon Y.-W., Flanagan P.T., Loukinov D., Lobanenkov V., Larionov V.;
RT "Human gamma-satellite DNA maintains open chromatin structure and protects
RT a transgene from epigenetic silencing.";
RL Genome Res. 19:533-544(2009).
RN [16]
RP INVOLVEMENT IN ACUTE LYMPHOBLASIC LEUKEMIA.
RX PubMed=19129520; DOI=10.1056/nejmoa0808253;
RA Mullighan C.G., Su X., Zhang J., Radtke I., Phillips L.A., Miller C.B.,
RA Ma J., Liu W., Cheng C., Schulman B.A., Harvey R.C., Chen I.-M.,
RA Clifford R.J., Carroll W.L., Reaman G., Bowman W.P., Devidas M.,
RA Gerhard D.S., Yang W., Relling M.V., Shurtleff S.A., Campana D.,
RA Borowitz M.J., Pui C.H., Smith M., Hunger S.P., Willman C.L., Downing J.R.;
RT "Deletion of IKZF1 and prognosis in acute lymphoblastic leukemia.";
RL N. Engl. J. Med. 360:470-480(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-258; SER-361 AND
RP SER-364, AND 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP FUNCTION IN DNA-BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP ALTERNATIVE SPLICING.
RX PubMed=22106042; DOI=10.1002/pbc.23406;
RA Li Z., Song C., Ouyang H., Lai L., Payne K.J., Dovat S.;
RT "Cell cycle-specific function of Ikaros in human leukemia.";
RL Pediatr. Blood Cancer 59:69-76(2012).
RN [20]
RP PHOSPHORYLATION AT SER-361 AND SER-364 BY SYK, AND SUBCELLULAR LOCATION.
RX PubMed=23071339; DOI=10.1073/pnas.1209828109;
RA Uckun F.M., Ma H., Zhang J., Ozer Z., Dovat S., Mao C., Ishkhanian R.,
RA Goodman P., Qazi S.;
RT "Serine phosphorylation by SYK is critical for nuclear localization and
RT transcription factor function of Ikaros.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18072-18077(2012).
RN [21]
RP INVOLVEMENT IN CVID13, VARIANT CVID13 CYS-210, CHARACTERIZATION OF VARIANT
RP CVID13 CYS-210, AND SUBCELLULAR LOCATION.
RX PubMed=21548011; DOI=10.1002/pbc.23160;
RA Goldman F.D., Gurel Z., Al-Zubeidi D., Fried A.J., Icardi M., Song C.,
RA Dovat S.;
RT "Congenital pancytopenia and absence of B lymphocytes in a neonate with a
RT mutation in the Ikaros gene.";
RL Pediatr. Blood Cancer 58:591-597(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-261; SER-289;
RP SER-298; SER-364; SER-368; SER-427 AND SER-445, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP VARIANTS CVID13 GLN-162; LEU-162; ARG-167 AND GLN-184, CHARACTERIZATION OF
RP VARIANTS CVID13 GLN-162; LEU-162; ARG-167; GLN-184 AND CYS-210, AND
RP MUTAGENESIS OF ASN-159 AND HIS-191.
RX PubMed=26981933; DOI=10.1056/nejmoa1512234;
RA Kuehn H.S., Boisson B., Cunningham-Rundles C., Reichenbach J.,
RA Stray-Pedersen A., Gelfand E.W., Maffucci P., Pierce K.R., Abbott J.K.,
RA Voelkerding K.V., South S.T., Augustine N.H., Bush J.S., Dolen W.K.,
RA Wray B.B., Itan Y., Cobat A., Sorte H.S., Ganesan S., Prader S.,
RA Martins T.B., Lawrence M.G., Orange J.S., Calvo K.R., Niemela J.E.,
RA Casanova J.L., Fleisher T.A., Hill H.R., Kumanovics A., Conley M.E.,
RA Rosenzweig S.D.;
RT "Loss of B Cells in Patients with Heterozygous Mutations in IKAROS.";
RL N. Engl. J. Med. 374:1032-1043(2016).
CC -!- FUNCTION: Transcription regulator of hematopoietic cell differentiation
CC (PubMed:17934067). Binds gamma-satellite DNA (PubMed:17135265,
CC PubMed:19141594). 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 (fikzfterminal
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. Confers early temporal competence
CC to retinal progenitor cells (RPCs) (By similarity). Function is
CC isoform-specific and is modulated by dominant-negative inactive
CC isoforms (PubMed:17135265, PubMed:17934067).
CC {ECO:0000250|UniProtKB:Q03267, ECO:0000269|PubMed:10204490,
CC ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:17934067,
CC ECO:0000269|PubMed:19141594}.
CC -!- SUBUNIT: Heterodimer formed by the various isoforms; this modulates
CC transcription regulator activity (PubMed:17135265, PubMed:17934067).
CC Heterodimer with other IKAROS family members. Interacts with IKZF4 AND
CC IKZF5 (PubMed:10978333). Component of the chromatin-remodeling NuRD
CC repressor complex which includes at least HDAC1, HDAC2, RBBP4, RBBP7,
CC IKZF1, MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4. Interacts directly with
CC the CHD4 component of the NuRD complex. Interacts directly with
CC SMARCA4; the interaction associates IKFZ1 with the BAF complex
CC (PubMed:10204490). Interacts with SUMO1; the interaction sumoylates
CC IKAROS, promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform
CC alpha); the interaction promotes sumoylation and reduces transcription
CC repression. Interacts, to a lesser extent, with PIAS3. Interacts with
CC PPP1CC; the interaction targets PPP1CC to pericentromeric
CC heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it
CC from degradation. Interacts with IKZF3 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10204490, ECO:0000269|PubMed:10978333,
CC ECO:0000305|PubMed:17135265, ECO:0000305|PubMed:17934067}.
CC -!- INTERACTION:
CC Q13422; Q8WTP8: AEN; NbExp=3; IntAct=EBI-745305, EBI-8637627;
CC Q13422; Q96Q83: ALKBH3; NbExp=5; IntAct=EBI-745305, EBI-6658697;
CC Q13422; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-745305, EBI-541426;
CC Q13422; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-745305, EBI-742909;
CC Q13422; Q13895: BYSL; NbExp=5; IntAct=EBI-745305, EBI-358049;
CC Q13422; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-745305, EBI-8643161;
CC Q13422; Q8IYL3: C1orf174; NbExp=4; IntAct=EBI-745305, EBI-715898;
CC Q13422; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-745305, EBI-715389;
CC Q13422; Q9HC52: CBX8; NbExp=3; IntAct=EBI-745305, EBI-712912;
CC Q13422; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-745305, EBI-10181988;
CC Q13422; P61024: CKS1B; NbExp=3; IntAct=EBI-745305, EBI-456371;
CC Q13422; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-745305, EBI-10171858;
CC Q13422; P56545: CTBP2; NbExp=5; IntAct=EBI-745305, EBI-741533;
CC Q13422; P56545-3: CTBP2; NbExp=3; IntAct=EBI-745305, EBI-10171902;
CC Q13422; O43602: DCX; NbExp=4; IntAct=EBI-745305, EBI-8646694;
CC Q13422; P26196: DDX6; NbExp=3; IntAct=EBI-745305, EBI-351257;
CC Q13422; Q92630: DYRK2; NbExp=3; IntAct=EBI-745305, EBI-749432;
CC Q13422; Q3B820: FAM161A; NbExp=3; IntAct=EBI-745305, EBI-719941;
CC Q13422; Q7L5A3: FAM214B; NbExp=6; IntAct=EBI-745305, EBI-745689;
CC Q13422; Q9Y247: FAM50B; NbExp=4; IntAct=EBI-745305, EBI-742802;
CC Q13422; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-745305, EBI-10247271;
CC Q13422; P61328: FGF12; NbExp=3; IntAct=EBI-745305, EBI-6657662;
CC Q13422; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-745305, EBI-741729;
CC Q13422; O76003: GLRX3; NbExp=3; IntAct=EBI-745305, EBI-374781;
CC Q13422; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-745305, EBI-745707;
CC Q13422; Q9H1K1: ISCU; NbExp=3; IntAct=EBI-745305, EBI-1047335;
CC Q13422; Q8TAP4: LMO3; NbExp=3; IntAct=EBI-745305, EBI-742259;
CC Q13422; Q9Y4Z0: LSM4; NbExp=3; IntAct=EBI-745305, EBI-372521;
CC Q13422; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-745305, EBI-77889;
CC Q13422; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-745305, EBI-348259;
CC Q13422; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-745305, EBI-399246;
CC Q13422; Q15014: MORF4L2; NbExp=3; IntAct=EBI-745305, EBI-399257;
CC Q13422; Q13330: MTA1; NbExp=3; IntAct=EBI-745305, EBI-714236;
CC Q13422; Q9HC98: NEK6; NbExp=3; IntAct=EBI-745305, EBI-740364;
CC Q13422; Q9BVI4: NOC4L; NbExp=3; IntAct=EBI-745305, EBI-395927;
CC Q13422; Q13526: PIN1; NbExp=3; IntAct=EBI-745305, EBI-714158;
CC Q13422; Q96T60: PNKP; NbExp=3; IntAct=EBI-745305, EBI-1045072;
CC Q13422; O43741: PRKAB2; NbExp=3; IntAct=EBI-745305, EBI-1053424;
CC Q13422; P25786: PSMA1; NbExp=3; IntAct=EBI-745305, EBI-359352;
CC Q13422; P25789: PSMA4; NbExp=3; IntAct=EBI-745305, EBI-359310;
CC Q13422; O75771: RAD51D; NbExp=5; IntAct=EBI-745305, EBI-1055693;
CC Q13422; P57060: RWDD2B; NbExp=4; IntAct=EBI-745305, EBI-724442;
CC Q13422; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-745305, EBI-748391;
CC Q13422; O00560: SDCBP; NbExp=3; IntAct=EBI-745305, EBI-727004;
CC Q13422; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-745305, EBI-747035;
CC Q13422; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-745305, EBI-10313866;
CC Q13422; P62306: SNRPF; NbExp=3; IntAct=EBI-745305, EBI-356900;
CC Q13422; Q13573: SNW1; NbExp=3; IntAct=EBI-745305, EBI-632715;
CC Q13422; Q9H0A9: SPATC1L; NbExp=3; IntAct=EBI-745305, EBI-372911;
CC Q13422; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-745305, EBI-745392;
CC Q13422; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-745305, EBI-10180829;
CC Q13422; Q15007: WTAP; NbExp=3; IntAct=EBI-745305, EBI-751647;
CC Q13422; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-745305, EBI-2682299;
CC Q13422; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-745305, EBI-740727;
CC Q13422; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-745305, EBI-745520;
CC Q13422; A8K932; NbExp=3; IntAct=EBI-745305, EBI-10174671;
CC Q13422-7; A1A5B0: ANKRD36; NbExp=3; IntAct=EBI-11522367, EBI-14100900;
CC Q13422-7; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-11522367, EBI-541426;
CC Q13422-7; Q99728: BARD1; NbExp=3; IntAct=EBI-11522367, EBI-473181;
CC Q13422-7; Q13895: BYSL; NbExp=3; IntAct=EBI-11522367, EBI-358049;
CC Q13422-7; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-11522367, EBI-8643161;
CC Q13422-7; Q8IYL3: C1orf174; NbExp=3; IntAct=EBI-11522367, EBI-715898;
CC Q13422-7; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-11522367, EBI-715389;
CC Q13422-7; Q9HC52: CBX8; NbExp=3; IntAct=EBI-11522367, EBI-712912;
CC Q13422-7; Q8N715: CCDC185; NbExp=3; IntAct=EBI-11522367, EBI-740814;
CC Q13422-7; O00311: CDC7; NbExp=3; IntAct=EBI-11522367, EBI-374980;
CC Q13422-7; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-11522367, EBI-3919850;
CC Q13422-7; P61024: CKS1B; NbExp=3; IntAct=EBI-11522367, EBI-456371;
CC Q13422-7; Q96SW2-2: CRBN; NbExp=2; IntAct=EBI-11522367, EBI-10693561;
CC Q13422-7; Q13363-2: CTBP1; NbExp=5; IntAct=EBI-11522367, EBI-10171858;
CC Q13422-7; P56545-3: CTBP2; NbExp=3; IntAct=EBI-11522367, EBI-10171902;
CC Q13422-7; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-11522367, EBI-5453285;
CC Q13422-7; O43602-2: DCX; NbExp=3; IntAct=EBI-11522367, EBI-14148644;
CC Q13422-7; P26196: DDX6; NbExp=3; IntAct=EBI-11522367, EBI-351257;
CC Q13422-7; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-11522367, EBI-745689;
CC Q13422-7; Q14192: FHL2; NbExp=3; IntAct=EBI-11522367, EBI-701903;
CC Q13422-7; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-11522367, EBI-13213391;
CC Q13422-7; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-11522367, EBI-11522367;
CC Q13422-7; A0A0S2Z5S9: LHX4; NbExp=3; IntAct=EBI-11522367, EBI-16429099;
CC Q13422-7; P25800: LMO1; NbExp=3; IntAct=EBI-11522367, EBI-8639312;
CC Q13422-7; P25791-3: LMO2; NbExp=3; IntAct=EBI-11522367, EBI-11959475;
CC Q13422-7; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11522367, EBI-11742507;
CC Q13422-7; P61968: LMO4; NbExp=3; IntAct=EBI-11522367, EBI-2798728;
CC Q13422-7; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-11522367, EBI-746778;
CC Q13422-7; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-11522367, EBI-726739;
CC Q13422-7; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-11522367, EBI-348259;
CC Q13422-7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11522367, EBI-16439278;
CC Q13422-7; P00540: MOS; NbExp=3; IntAct=EBI-11522367, EBI-1757866;
CC Q13422-7; Q9Y5B8: NME7; NbExp=6; IntAct=EBI-11522367, EBI-744782;
CC Q13422-7; O43809: NUDT21; NbExp=3; IntAct=EBI-11522367, EBI-355720;
CC Q13422-7; O75928-2: PIAS2; NbExp=3; IntAct=EBI-11522367, EBI-348567;
CC Q13422-7; Q13526: PIN1; NbExp=3; IntAct=EBI-11522367, EBI-714158;
CC Q13422-7; Q96T60: PNKP; NbExp=3; IntAct=EBI-11522367, EBI-1045072;
CC Q13422-7; O60437: PPL; NbExp=3; IntAct=EBI-11522367, EBI-368321;
CC Q13422-7; P54646: PRKAA2; NbExp=3; IntAct=EBI-11522367, EBI-1383852;
CC Q13422-7; Q99633: PRPF18; NbExp=3; IntAct=EBI-11522367, EBI-2798416;
CC Q13422-7; P25789: PSMA4; NbExp=3; IntAct=EBI-11522367, EBI-359310;
CC Q13422-7; P47897: QARS1; NbExp=3; IntAct=EBI-11522367, EBI-347462;
CC Q13422-7; O75771: RAD51D; NbExp=3; IntAct=EBI-11522367, EBI-1055693;
CC Q13422-7; Q6ZSC3: RBM43; NbExp=3; IntAct=EBI-11522367, EBI-2880658;
CC Q13422-7; P78317: RNF4; NbExp=3; IntAct=EBI-11522367, EBI-2340927;
CC Q13422-7; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-11522367, EBI-16428950;
CC Q13422-7; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-11522367, EBI-748391;
CC Q13422-7; P09661: SNRPA1; NbExp=3; IntAct=EBI-11522367, EBI-876439;
CC Q13422-7; P62306: SNRPF; NbExp=3; IntAct=EBI-11522367, EBI-356900;
CC Q13422-7; Q15560: TCEA2; NbExp=3; IntAct=EBI-11522367, EBI-710310;
CC Q13422-7; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-11522367, EBI-8994397;
CC Q13422-7; P42681: TXK; NbExp=3; IntAct=EBI-11522367, EBI-7877438;
CC Q13422-7; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-11522367, EBI-10180829;
CC Q13422-7; Q15007: WTAP; NbExp=7; IntAct=EBI-11522367, EBI-751647;
CC Q13422-7; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-11522367, EBI-740727;
CC Q13422-7; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-11522367, EBI-746277;
CC Q13422-7; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-11522367, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17135265,
CC ECO:0000269|PubMed:21548011, ECO:0000269|PubMed:22106042,
CC ECO:0000269|PubMed:23071339}. 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. {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:22106042}.
CC -!- SUBCELLULAR LOCATION: [Isoform Ik2]: 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Ik6]: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=Ik1;
CC IsoId=Q13422-1; Sequence=Displayed;
CC Name=Ik2;
CC IsoId=Q13422-2; Sequence=VSP_006848;
CC Name=Ik3;
CC IsoId=Q13422-3; Sequence=VSP_006850;
CC Name=Ik4;
CC IsoId=Q13422-4; Sequence=VSP_006847, VSP_006850;
CC Name=Ik5;
CC IsoId=Q13422-5; Sequence=VSP_006852;
CC Name=Ik6;
CC IsoId=Q13422-6; Sequence=VSP_006849;
CC Name=Ik7;
CC IsoId=Q13422-7; Sequence=VSP_006851;
CC Name=Ikx;
CC IsoId=Q13422-8; Sequence=VSP_006851, VSP_053404, VSP_053405;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in thymus, spleen and
CC peripheral blood Leukocytes and lymph nodes. Lower expression in bone
CC marrow and small intestine. {ECO:0000269|PubMed:8543809,
CC ECO:0000269|PubMed:8964602}.
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. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal zinc-finger domain is required for dimerization.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation controls cell-cycle progression from late G(1)
CC stage to S stage. Hyperphosphorylated during G2/M phase.
CC Dephosphorylated state during late G(1) phase. Phosphorylation on Thr-
CC 140 is required for DNA and pericentromeric location during mitosis.
CC CK2 is the main kinase, in vitro. GSK3 and CDK may also contribute to
CC phosphorylation of the C-terminal serine and threonine residues.
CC Phosphorylation on these C-terminal residues reduces the DNA-binding
CC ability. Phosphorylation/dephosphorylation events on Ser-13 and Ser-295
CC regulate TDT expression during thymocyte differentiation.
CC Dephosphorylation by protein phosphatase 1 regulates stability and
CC pericentromeric heterochromatin location. Phosphorylated in both
CC lymphoid and non-lymphoid tissues (By similarity). Phosphorylation at
CC Ser-361 and Ser-364 downstream of SYK induces nuclear translocation.
CC {ECO:0000250, ECO:0000269|PubMed:22106042,
CC ECO:0000269|PubMed:23071339}.
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 (By similarity). {ECO:0000250}.
CC -!- PTM: Polyubiquitinated. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in IKZF1 are frequent occurrences (28.6%) in
CC acute lymphoblasic leukemia (ALL). Such alterations or deletions lead
CC to poor prognosis for ALL.
CC -!- DISEASE: Note=Chromosomal aberrations involving IKZF1 are a cause of B-
CC cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;7)(q27;p12),
CC with BCL6.
CC -!- DISEASE: Immunodeficiency, common variable, 13 (CVID13) [MIM:616873]: A
CC primary immunodeficiency characterized by antibody deficiency,
CC hypogammaglobulinemia, recurrent bacterial infections and an inability
CC to mount an antibody response to antigen. CVID13 is an autosomal
CC dominant disease associated with a striking decrease in B-cell numbers.
CC {ECO:0000269|PubMed:21548011, ECO:0000269|PubMed:26981933}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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/IkarosID258.html";
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DR EMBL; U40462; AAC50459.1; -; mRNA.
DR EMBL; S80876; AAB50683.1; -; mRNA.
DR EMBL; AY377974; AAR84585.1; -; mRNA.
DR EMBL; AK303586; BAG64603.1; -; mRNA.
DR EMBL; BT009836; AAP88838.1; -; mRNA.
DR EMBL; AC124014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC233268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471128; EAW60977.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW60978.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW60981.1; -; Genomic_DNA.
DR EMBL; CH236955; EAL23900.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW60979.1; -; Genomic_DNA.
DR EMBL; BC018349; AAH18349.1; -; mRNA.
DR CCDS; CCDS59055.1; -. [Q13422-7]
DR CCDS; CCDS69299.1; -. [Q13422-5]
DR CCDS; CCDS75596.1; -. [Q13422-1]
DR CCDS; CCDS75597.1; -. [Q13422-3]
DR CCDS; CCDS78233.1; -. [Q13422-2]
DR RefSeq; NP_001207694.1; NM_001220765.2. [Q13422-7]
DR RefSeq; NP_001207696.1; NM_001220767.2.
DR RefSeq; NP_001207697.1; NM_001220768.2. [Q13422-3]
DR RefSeq; NP_001207699.1; NM_001220770.2.
DR RefSeq; NP_001207700.1; NM_001220771.2. [Q13422-5]
DR RefSeq; NP_001278766.1; NM_001291837.1. [Q13422-7]
DR RefSeq; NP_001278767.1; NM_001291838.1. [Q13422-2]
DR RefSeq; NP_001278768.1; NM_001291839.1.
DR RefSeq; NP_001278769.1; NM_001291840.1. [Q13422-6]
DR RefSeq; NP_001278770.1; NM_001291841.1.
DR RefSeq; NP_001278771.1; NM_001291842.1.
DR RefSeq; NP_001278772.1; NM_001291843.1.
DR RefSeq; NP_001278773.1; NM_001291844.1.
DR RefSeq; NP_006051.1; NM_006060.5. [Q13422-1]
DR RefSeq; XP_011513370.1; XM_011515068.2. [Q13422-1]
DR RefSeq; XP_011513371.1; XM_011515069.2. [Q13422-1]
DR RefSeq; XP_011513377.1; XM_011515075.2. [Q13422-2]
DR RefSeq; XP_011513378.1; XM_011515076.2. [Q13422-2]
DR RefSeq; XP_016867157.1; XM_017011668.1. [Q13422-2]
DR PDB; 6H0F; X-ray; 3.25 A; C/F/I/L=141-174.
DR PDBsum; 6H0F; -.
DR AlphaFoldDB; Q13422; -.
DR SMR; Q13422; -.
DR BioGRID; 115604; 194.
DR DIP; DIP-41110N; -.
DR ELM; Q13422; -.
DR IntAct; Q13422; 135.
DR MINT; Q13422; -.
DR STRING; 9606.ENSP00000331614; -.
DR BindingDB; Q13422; -.
DR ChEMBL; CHEMBL4739685; -.
DR GlyGen; Q13422; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q13422; -.
DR MetOSite; Q13422; -.
DR PhosphoSitePlus; Q13422; -.
DR BioMuta; IKZF1; -.
DR DMDM; 3913926; -.
DR EPD; Q13422; -.
DR jPOST; Q13422; -.
DR MassIVE; Q13422; -.
DR MaxQB; Q13422; -.
DR PaxDb; Q13422; -.
DR PeptideAtlas; Q13422; -.
DR PRIDE; Q13422; -.
DR ProteomicsDB; 59401; -. [Q13422-1]
DR ProteomicsDB; 59402; -. [Q13422-2]
DR ProteomicsDB; 59403; -. [Q13422-3]
DR ProteomicsDB; 59404; -. [Q13422-4]
DR ProteomicsDB; 59405; -. [Q13422-5]
DR ProteomicsDB; 59406; -. [Q13422-6]
DR ProteomicsDB; 59407; -. [Q13422-7]
DR ProteomicsDB; 66152; -.
DR Antibodypedia; 3980; 580 antibodies from 47 providers.
DR DNASU; 10320; -.
DR Ensembl; ENST00000331340.8; ENSP00000331614.3; ENSG00000185811.20. [Q13422-1]
DR Ensembl; ENST00000343574.9; ENSP00000342750.5; ENSG00000185811.20. [Q13422-2]
DR Ensembl; ENST00000349824.8; ENSP00000342485.4; ENSG00000185811.20. [Q13422-5]
DR Ensembl; ENST00000357364.8; ENSP00000349928.4; ENSG00000185811.20. [Q13422-3]
DR Ensembl; ENST00000359197.9; ENSP00000352123.5; ENSG00000185811.20. [Q13422-7]
DR Ensembl; ENST00000438033.5; ENSP00000396554.1; ENSG00000185811.20. [Q13422-2]
DR Ensembl; ENST00000439701.2; ENSP00000413025.1; ENSG00000185811.20. [Q13422-7]
DR GeneID; 10320; -.
DR KEGG; hsa:10320; -.
DR MANE-Select; ENST00000331340.8; ENSP00000331614.3; NM_006060.6; NP_006051.1.
DR UCSC; uc003tow.5; human. [Q13422-1]
DR CTD; 10320; -.
DR DisGeNET; 10320; -.
DR GeneCards; IKZF1; -.
DR HGNC; HGNC:13176; IKZF1.
DR HPA; ENSG00000185811; Group enriched (bone marrow, lymphoid tissue).
DR MalaCards; IKZF1; -.
DR MIM; 603023; gene.
DR MIM; 616873; phenotype.
DR neXtProt; NX_Q13422; -.
DR OpenTargets; ENSG00000185811; -.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR Orphanet; 317473; Pancytopenia due to IKZF1 mutations.
DR Orphanet; 36426; Stevens-Johnson syndrome.
DR PharmGKB; PA37748; -.
DR VEuPathDB; HostDB:ENSG00000185811; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156782; -.
DR HOGENOM; CLU_025502_2_0_1; -.
DR InParanoid; Q13422; -.
DR OMA; LASDMNG; -.
DR OrthoDB; 385551at2759; -.
DR PhylomeDB; Q13422; -.
DR TreeFam; TF331189; -.
DR PathwayCommons; Q13422; -.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription. [Q13422-1]
DR SignaLink; Q13422; -.
DR SIGNOR; Q13422; -.
DR BioGRID-ORCS; 10320; 32 hits in 1098 CRISPR screens.
DR ChiTaRS; IKZF1; human.
DR GeneWiki; IKZF1; -.
DR GenomeRNAi; 10320; -.
DR Pharos; Q13422; Tbio.
DR PRO; PR:Q13422; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q13422; protein.
DR Bgee; ENSG00000185811; Expressed in leukocyte and 161 other tissues.
DR ExpressionAtlas; Q13422; baseline and differential.
DR Genevisible; Q13422; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; IMP:UniProtKB.
DR GO; GO:0030098; P:lymphocyte differentiation; IMP:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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; Activator; Alternative splicing; Cell cycle;
KW Chromatin regulator; Chromosomal rearrangement; Cytoplasm;
KW Developmental protein; Disease variant; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..519
FT /note="DNA-binding protein Ikaros"
FT /id="PRO_0000047094"
FT ZN_FING 117..139
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 145..167
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 173..195
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 201..224
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..514
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..163
FT /note="Required for both high-affinity DNA binding and
FT pericentromeric heterochromatin localization"
FT /evidence="ECO:0000250"
FT REGION 180..195
FT /note="Required for both high-affinity DNA binding and
FT pericentromeric heterochromatin localization"
FT /evidence="ECO:0000250"
FT REGION 381..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..471
FT /note="Required for binding PP1CC"
FT /evidence="ECO:0000250"
FT COMPBIAS 37..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 159
FT /note="Required for both pericentromeric heterochromatin
FT localization and complete DNA binding"
FT /evidence="ECO:0000250"
FT SITE 162
FT /note="Required for both pericentromeric heterochromatin
FT localization and complete DNA binding"
FT /evidence="ECO:0000250"
FT SITE 188
FT /note="Required for both pericentromeric heterochromatin
FT localization and DNA binding"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23071339,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23071339,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03267"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 10..53
FT /note="Missing (in isoform Ik4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006847"
FT VAR_SEQ 54..283
FT /note="Missing (in isoform Ik6)"
FT /evidence="ECO:0000305"
FT /id="VSP_006849"
FT VAR_SEQ 54..140
FT /note="Missing (in isoform Ik2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006848"
FT VAR_SEQ 141..283
FT /note="Missing (in isoform Ik5)"
FT /evidence="ECO:0000305"
FT /id="VSP_006852"
FT VAR_SEQ 197..283
FT /note="Missing (in isoform Ik3 and isoform Ik4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006850"
FT VAR_SEQ 197..238
FT /note="Missing (in isoform Ik7 and isoform Ikx)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.5"
FT /id="VSP_006851"
FT VAR_SEQ 260..268
FT /note="RSLVLDRLA -> ISRAGQTSK (in isoform Ikx)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_053404"
FT VAR_SEQ 269..519
FT /note="Missing (in isoform Ikx)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_053405"
FT VARIANT 162
FT /note="R -> L (in CVID13; abolishes binding to DNA; has
FT diffuse nuclear localization; dbSNP:rs770551610)"
FT /evidence="ECO:0000269|PubMed:26981933"
FT /id="VAR_076401"
FT VARIANT 162
FT /note="R -> Q (in CVID13; abolishes binding to DNA; has
FT diffuse nuclear localization; dbSNP:rs770551610)"
FT /evidence="ECO:0000269|PubMed:26981933"
FT /id="VAR_076402"
FT VARIANT 167
FT /note="H -> R (in CVID13; abolishes binding to DNA; has
FT diffuse nuclear localization; dbSNP:rs869312884)"
FT /evidence="ECO:0000269|PubMed:26981933"
FT /id="VAR_076403"
FT VARIANT 184
FT /note="R -> Q (in CVID13; abolishes binding to DNA; has
FT diffuse nuclear localization; dbSNP:rs869312885)"
FT /evidence="ECO:0000269|PubMed:26981933"
FT /id="VAR_076404"
FT VARIANT 210
FT /note="Y -> C (in CVID13; decreases binding to
FT pericentromeric heterochromatin DNA; has diffuse nuclear
FT localization; dbSNP:rs869312883)"
FT /evidence="ECO:0000269|PubMed:21548011,
FT ECO:0000269|PubMed:26981933"
FT /id="VAR_076405"
FT MUTAGEN 159
FT /note="N->A: Abolishes binding to DNA and has diffuse
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:26981933"
FT MUTAGEN 191
FT /note="H->R: Abolishes binding to DNA and has diffuse
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:26981933"
FT CONFLICT 11..12
FT /note="QV -> FS (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> T (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="N -> K (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Missing (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="S -> T (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..355
FT /note="KPLA -> RRS (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="N -> Y (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..426
FT /note="PHARNGL -> RRAQRV (in Ref. 2; AAB50683)"
FT /evidence="ECO:0000305"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6H0F"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6H0F"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:6H0F"
SQ SEQUENCE 519 AA; 57528 MW; 7B0129C4E3FE41A8 CRC64;
MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE
TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD
ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY
ACRRRDALTG HLRTHSVGKP HKCGYCGRSY KQRSSLEEHK ERCHNYLESM GLPGTLYPVI
KEETNHSEMA EDLCKIGSER SLVLDRLASN VAKRKSSMPQ KFLGDKGLSD TPYDSSASYE
KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL HKPLAEGTPR
SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT ESNNEEQRSG LIYLTNHIAP
HARNGLSLKE EHRAYDLLRA ASENSQDALR VVSTSGEQMK VYKCEHCRVL FLDHVMYTIH
MGCHGFRDPF ECNMCGYHSQ DRYEFSSHIT RGEHRFHMS
