GFI1B_HUMAN
ID GFI1B_HUMAN Reviewed; 330 AA.
AC Q5VTD9; O95270; Q5VTD8; Q6FHZ2; Q6T888;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Zinc finger protein Gfi-1b;
DE AltName: Full=Growth factor independent protein 1B;
DE AltName: Full=Potential regulator of CDKN1A translocated in CML;
GN Name=GFI1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Umbilical cord blood;
RX PubMed=9878267; DOI=10.1006/geno.1998.5601;
RA Roedel B., Wagner T., Zoernig M., Niessing J., Moeroey T.;
RT "The human homologue (GFI1B) of the chicken GFI gene maps to chromosome
RT 9q34.13-A locus frequently altered in hematopoietic diseases.";
RL Genomics 54:580-582(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION BY GATA1.
RX PubMed=15280509; DOI=10.1093/nar/gkh719;
RA Huang D.Y., Kuo Y.Y., Lai J.S., Suzuki Y., Sugano S., Chang Z.F.;
RT "GATA-1 and NF-Y cooperate to mediate erythroid-specific transcription of
RT Gfi-1B gene.";
RL Nucleic Acids Res. 32:3935-3946(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12351384; DOI=10.1182/blood-2002-01-0182;
RA Osawa M., Yamaguchi T., Nakamura Y., Kaneko S., Onodera M., Sawada K.,
RA Jegalian A., Wu H., Nakauchi H., Iwama A.;
RT "Erythroid expansion mediated by the Gfi-1B zinc finger protein: role in
RT normal hematopoiesis.";
RL Blood 100:2769-2777(2002).
RN [8]
RP INTERACTION WITH RUNX1T1.
RX PubMed=12874834; DOI=10.1002/jcb.10548;
RA McGhee L., Bryan J., Elliott L., Grimes H.L., Kazanjian A., Davis J.N.,
RA Meyers S.;
RT "Gfi-1 attaches to the nuclear matrix, associates with ETO (MTG8) and
RT histone deacetylase proteins, and represses transcription using a TSA-
RT sensitive mechanism.";
RL J. Cell. Biochem. 89:1005-1018(2003).
RN [9]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH GATA1.
RX PubMed=16177182; DOI=10.1093/nar/gki838;
RA Huang D.-Y., Kuo Y.-Y., Chang Z.-F.;
RT "GATA-1 mediates auto-regulation of Gfi-1B transcription in K562 cells.";
RL Nucleic Acids Res. 33:5331-5342(2005).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EHMT2 AND SUV39H1.
RX PubMed=16688220; DOI=10.1038/sj.emboj.7601124;
RA Vassen L., Fiolka K., Moeroey T.;
RT "Gfi1b alters histone methylation at target gene promoters and sites of
RT gamma-satellite containing heterochromatin.";
RL EMBO J. 25:2409-2419(2006).
RN [11]
RP FUNCTION.
RX PubMed=16782810; DOI=10.1073/pnas.0603728103;
RA Schwartz R., Engel I., Fallahi-Sichani M., Petrie H.T., Murre C.;
RT "Gene expression patterns define novel roles for E47 in cell cycle
RT progression, cytokine-mediated signaling, and T lineage development.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9976-9981(2006).
RN [12]
RP INTERACTION WITH ARIH2.
RX PubMed=17646546; DOI=10.1182/blood-2006-11-058602;
RA Marteijn J.A., van der Meer L.T., van Emst L., van Reijmersdal S.,
RA Wissink W., de Witte T., Jansen J.H., Van der Reijden B.A.;
RT "Gfi1 ubiquitination and proteasomal degradation is inhibited by the
RT ubiquitin ligase Triad1.";
RL Blood 110:3128-3135(2007).
RN [13]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF ASN-290.
RX PubMed=17272506; DOI=10.1182/blood-2006-08-043331;
RA Wei X., Kee B.L.;
RT "Growth factor independent 1B (Gfi1b) is an E2A target gene that modulates
RT Gata3 in T-cell lymphomas.";
RL Blood 109:4406-4414(2007).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17156408; DOI=10.1111/j.1365-2141.2006.06407.x;
RA Elmaagacli A.H., Koldehoff M., Zakrzewski J.L., Steckel N.K., Ottinger H.,
RA Beelen D.W.;
RT "Growth factor-independent 1B gene (GFI1B) is overexpressed in
RT erythropoietic and megakaryocytic malignancies and increases their
RT proliferation rate.";
RL Br. J. Haematol. 136:212-219(2007).
RN [15]
RP FUNCTION, AND INTERACTION WITH GATA1.
RX PubMed=17420275; DOI=10.1128/mcb.02212-06;
RA Kuo Y.-Y., Chang Z.-F.;
RT "GATA-1 and Gfi-1B interplay to regulate Bcl-xL transcription.";
RL Mol. Cell. Biol. 27:4261-4272(2007).
RN [16]
RP FUNCTION (ISOFORM 2), AND METHYLATION AT LYS-8.
RX PubMed=22399799; DOI=10.1242/jcs.095877;
RA Laurent B., Randrianarison-Huetz V., Frisan E., Andrieu-Soler C., Soler E.,
RA Fontenay M., Dusanter-Fourt I., Dumenil D.;
RT "A short Gfi-1B isoform controls erythroid differentiation by recruiting
RT the LSD1-CoREST complex through the dimethylation of its SNAG domain.";
RL J. Cell Sci. 125:993-1002(2012).
RN [17]
RP INVOLVEMENT IN BDPLT17.
RX PubMed=23927492; DOI=10.1111/jth.12368;
RA Stevenson W.S., Morel-Kopp M.C., Chen Q., Liang H.P., Bromhead C.J.,
RA Wright S., Turakulov R., Ng A.P., Roberts A.W., Bahlo M., Ward C.M.;
RT "GFI1B mutation causes a bleeding disorder with abnormal platelet
RT function.";
RL J. Thromb. Haemost. 11:2039-2047(2013).
RN [18]
RP INVOLVEMENT IN BDPLT17.
RX PubMed=24325358; DOI=10.1056/nejmoa1308130;
RA Monteferrario D., Bolar N.A., Marneth A.E., Hebeda K.M., Bergevoet S.M.,
RA Veenstra H., Laros-van Gorkom B.A., MacKenzie M.A., Khandanpour C.,
RA Botezatu L., Fransen E., Van Camp G., Duijnhouwer A.L., Salemink S.,
RA Willemsen B., Huls G., Preijers F., Van Heerde W., Jansen J.H.,
RA Kempers M.J., Loeys B.L., Van Laer L., Van der Reijden B.A.;
RT "A dominant-negative GFI1B mutation in the gray platelet syndrome.";
RL N. Engl. J. Med. 370:245-253(2014).
RN [19]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-231.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Essential proto-oncogenic transcriptional regulator necessary
CC for development and differentiation of erythroid and megakaryocytic
CC lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses,
CC via histone deacetylase (HDAC) recruitment, a number of genes
CC implicated in multilineage blood cell development and controls
CC hematopoietic differentiation. Transcriptional repressor or activator
CC depending on both promoter and cell type context; represses promoter
CC activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling
CC pathways. Cooperates with GATA1 to repress target gene transcription,
CC such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic
CC cell lines markedly increase apoptosis rate. Inhibits down-regulation
CC of MYC and MYB as well as the cyclin-dependent kinase inhibitor
CC CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses
CC expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated
CC transcription; as GATA1 also mediates erythroid GFI1B transcription,
CC both GATA1 and GFI1B participate in a feedback regulatory pathway
CC controlling the expression of GFI1B gene in erythroid cells. Suppresses
CC GATA1-mediated stimulation of GFI1B promoter through protein
CC interaction. Binds to gamma-satellite DNA and to its own promoter,
CC auto-repressing its own expression. Alters histone methylation by
CC recruiting histone methyltransferase to target genes promoters. Plays a
CC role in heterochromatin formation. {ECO:0000269|PubMed:12351384,
CC ECO:0000269|PubMed:16177182, ECO:0000269|PubMed:16688220,
CC ECO:0000269|PubMed:16782810, ECO:0000269|PubMed:17156408,
CC ECO:0000269|PubMed:17272506, ECO:0000269|PubMed:17420275}.
CC -!- SUBUNIT: Component of a RCOR-GFI-KDM1A-HDAC complex. Interacts directly
CC with RCOR1, KDM1A and HDAC2 (By similarity). Forms a complex with
CC GATA1. Interacts with histone methyltransferases EHMT2 and SUV39H1.
CC Interacts with ARIH2 (via RING-type 2). Interacts with RUNX1T1.
CC {ECO:0000250, ECO:0000269|PubMed:12874834, ECO:0000269|PubMed:16177182,
CC ECO:0000269|PubMed:16688220, ECO:0000269|PubMed:17420275,
CC ECO:0000269|PubMed:17646546}.
CC -!- INTERACTION:
CC Q5VTD9; Q9HC77: CENPJ; NbExp=2; IntAct=EBI-946212, EBI-946194;
CC Q5VTD9; Q9Y219: JAG2; NbExp=2; IntAct=EBI-946212, EBI-946223;
CC Q5VTD9; Q99435: NELL2; NbExp=2; IntAct=EBI-946212, EBI-946274;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16688220}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=p37;
CC IsoId=Q5VTD9-1; Sequence=Displayed;
CC Name=2; Synonyms=p32;
CC IsoId=Q5VTD9-2; Sequence=VSP_028459;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow and fetal liver, but also
CC detectable in fetal spleen, fetal thymus, and testes. Detected in
CC hematopoietic stem cells, erythroblasts, and megakaryocytes.
CC Overexpressed in bone marrow of patients with erythroleukemia and
CC megakaryocytic leukemia as well as in their corresponding leukemic cell
CC lines, and markedly repressed in severe aplastic anemia (SAA).
CC {ECO:0000269|PubMed:12351384, ECO:0000269|PubMed:17156408,
CC ECO:0000269|PubMed:9878267}.
CC -!- INDUCTION: By GATA1 which binds to GFI1B promoter in cooperation with
CC the transcription factor NFYA. Target gene of transcription factor E2-
CC alpha/TCF3 that promotes growth arrest and apoptosis in lymphomas.
CC {ECO:0000269|PubMed:15280509}.
CC -!- DOMAIN: The zinc finger domains are essential for erythroid expansion
CC and acts as an activation domain whereas non finger domain serves as
CC repression domain. {ECO:0000250}.
CC -!- DOMAIN: The SNAG domain of GFIs is required for nuclear location and
CC for interaction with some corepressors. {ECO:0000250}.
CC -!- PTM: Methylation at Lys-8 in the SNAG domain seems required for the
CC recruitment of the corepressor complex. {ECO:0000269|PubMed:22399799}.
CC -!- DISEASE: Bleeding disorder, platelet-type, 17 (BDPLT17) [MIM:187900]:
CC An autosomal dominant disorder characterized by increased bleeding
CC tendency due to platelet dysfunction, and associated with
CC macrothrombocytopenia and red cell anisopoikilocytosis. Platelets
CC appear abnormal on light microscopy, while electron microscopy shows a
CC heterogeneous decrease of alpha granules within platelets. Bone marrow
CC biopsy shows increased numbers of abnormal megakaryocytes, suggesting a
CC defect in megakaryopoiesis and platelet production. The severity of
CC bleeding is variable with some affected individuals experiencing
CC spontaneous bleeding while other exhibit only abnormal bleeding with
CC surgery. {ECO:0000269|PubMed:23927492, ECO:0000269|PubMed:24325358}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Essential for erythroid differentiation.
CC Binds to target gene promoters and associates with the LSD1-CoREST
CC repressor complex more efficiently than the major isoform 1.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GFI1BID40707ch9q34.html";
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; AF081946; AAD08672.1; -; mRNA.
DR EMBL; AY428733; AAR06639.1; -; mRNA.
DR EMBL; CR536546; CAG38783.1; -; mRNA.
DR EMBL; AL593851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88025.1; -; Genomic_DNA.
DR EMBL; BC043371; AAH43371.1; -; mRNA.
DR EMBL; BC035626; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS48049.1; -. [Q5VTD9-2]
DR CCDS; CCDS6957.1; -. [Q5VTD9-1]
DR RefSeq; NP_001128503.1; NM_001135031.1. [Q5VTD9-2]
DR RefSeq; NP_004179.3; NM_004188.6. [Q5VTD9-1]
DR RefSeq; XP_011517372.1; XM_011519070.2. [Q5VTD9-1]
DR RefSeq; XP_016870665.1; XM_017015176.1. [Q5VTD9-2]
DR AlphaFoldDB; Q5VTD9; -.
DR SMR; Q5VTD9; -.
DR BioGRID; 113924; 113.
DR IntAct; Q5VTD9; 72.
DR STRING; 9606.ENSP00000344782; -.
DR iPTMnet; Q5VTD9; -.
DR PhosphoSitePlus; Q5VTD9; -.
DR BioMuta; GFI1B; -.
DR DMDM; 74756792; -.
DR MassIVE; Q5VTD9; -.
DR PaxDb; Q5VTD9; -.
DR PeptideAtlas; Q5VTD9; -.
DR PRIDE; Q5VTD9; -.
DR ProteomicsDB; 65320; -. [Q5VTD9-1]
DR ProteomicsDB; 65321; -. [Q5VTD9-2]
DR Antibodypedia; 1815; 120 antibodies from 24 providers.
DR DNASU; 8328; -.
DR Ensembl; ENST00000339463.7; ENSP00000344782.3; ENSG00000165702.15. [Q5VTD9-1]
DR Ensembl; ENST00000372122.4; ENSP00000361195.1; ENSG00000165702.15. [Q5VTD9-1]
DR Ensembl; ENST00000372123.5; ENSP00000361196.1; ENSG00000165702.15. [Q5VTD9-2]
DR GeneID; 8328; -.
DR KEGG; hsa:8328; -.
DR MANE-Select; ENST00000372122.4; ENSP00000361195.1; NM_001377304.1; NP_001364233.1.
DR UCSC; uc004ccg.4; human. [Q5VTD9-1]
DR CTD; 8328; -.
DR DisGeNET; 8328; -.
DR GeneCards; GFI1B; -.
DR HGNC; HGNC:4238; GFI1B.
DR HPA; ENSG00000165702; Tissue enriched (bone).
DR MalaCards; GFI1B; -.
DR MIM; 187900; phenotype.
DR MIM; 604383; gene.
DR neXtProt; NX_Q5VTD9; -.
DR OpenTargets; ENSG00000165702; -.
DR Orphanet; 734; Alpha delta granule deficiency.
DR Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
DR PharmGKB; PA28649; -.
DR VEuPathDB; HostDB:ENSG00000165702; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160010; -.
DR HOGENOM; CLU_002678_94_9_1; -.
DR InParanoid; Q5VTD9; -.
DR PhylomeDB; Q5VTD9; -.
DR TreeFam; TF350784; -.
DR PathwayCommons; Q5VTD9; -.
DR SignaLink; Q5VTD9; -.
DR SIGNOR; Q5VTD9; -.
DR BioGRID-ORCS; 8328; 23 hits in 1087 CRISPR screens.
DR ChiTaRS; GFI1B; human.
DR GeneWiki; GFI1B; -.
DR GenomeRNAi; 8328; -.
DR Pharos; Q5VTD9; Tbio.
DR PRO; PR:Q5VTD9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VTD9; protein.
DR Bgee; ENSG00000165702; Expressed in sperm and 98 other tissues.
DR ExpressionAtlas; Q5VTD9; baseline and differential.
DR Genevisible; Q5VTD9; HS.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; NAS:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; TAS:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:1903706; P:regulation of hemopoiesis; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator;
KW Developmental protein; DNA-binding; Metal-binding; Methylation; Nucleus;
KW Proto-oncogene; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..330
FT /note="Zinc finger protein Gfi-1b"
FT /id="PRO_0000306327"
FT ZN_FING 163..186
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..214
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..242
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..270
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..298
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..327
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..20
FT /note="SNAG domain"
FT REGION 91..330
FT /note="Interaction with ARIH2"
FT /evidence="ECO:0000269|PubMed:17646546"
FT REGION 164..330
FT /note="Mediates interaction with GATA1"
FT MOD_RES 8
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:22399799"
FT VAR_SEQ 171..216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028459"
FT VARIANT 231
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs761044764)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035556"
FT MUTAGEN 290
FT /note="N->S: Prevents DNA-binding."
FT /evidence="ECO:0000269|PubMed:17272506"
FT CONFLICT 11
FT /note="K -> M (in Ref. 2; AAR06639)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="W -> R (in Ref. 3; CAG38783)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="P -> H (in Ref. 1; AAD08672)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="R -> W (in Ref. 2; AAR06639)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="S -> N (in Ref. 1; AAD08672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 37492 MW; 947DD9C34B5BD962 CRC64;
MPRSFLVKSK KAHTYHQPRV QEDEPLWPPA LTPVPRDQAP SNSPVLSTLF PNQCLDWTNL
KREPELEQDQ NLARMAPAPE GPIVLSRPQD GDSPLSDSPP FYKPSFSWDT LATTYGHSYR
QAPSTMQSAF LEHSVSLYGS PLVPSTEPAL DFSLRYSPGM DAYHCVKCNK VFSTPHGLEV
HVRRSHSGTR PFACDICGKT FGHAVSLEQH THVHSQERSF ECRMCGKAFK RSSTLSTHLL
IHSDTRPYPC QFCGKRFHQK SDMKKHTYIH TGEKPHKCQV CGKAFSQSSN LITHSRKHTG
FKPFSCELCT KGFQRKVDLR RHRESQHNLK