GFI1_HUMAN
ID GFI1_HUMAN Reviewed; 422 AA.
AC Q99684; Q8N564;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Zinc finger protein Gfi-1;
DE AltName: Full=Growth factor independent protein 1;
DE AltName: Full=Zinc finger protein 163;
GN Name=GFI1; Synonyms=ZNF163;
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].
RC TISSUE=Bone marrow;
RX PubMed=9051000; DOI=10.1038/sj.onc.1200910;
RA Roberts T., Cowell J.K.;
RT "Cloning of the human Gfi-1 gene and its mapping to chromosome region
RT 1p22.";
RL Oncogene 14:1003-1005(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
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 [3]
RP DNA-BINDING, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=8754800; DOI=10.1128/mcb.16.8.4024;
RA Zweidler-Mckay P.A., Grimes H.L., Flubacher M.M., Tsichlis P.N.;
RT "Gfi-1 encodes a nuclear zinc finger protein that binds DNA and functions
RT as a transcriptional repressor.";
RL Mol. Cell. Biol. 16:4024-4034(1996).
RN [4]
RP INTERACTION WITH PIAS3, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11060035; DOI=10.1093/emboj/19.21.5845;
RA Roedel B., Tavassoli K., Karsunky H., Schmidt T., Bachmann M., Schaper F.,
RA Heinrich P., Shuai K., Elsaesser H.-P., Moeroey T.;
RT "The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting
RT with the STAT3 inhibitor PIAS3.";
RL EMBO J. 19:5845-5855(2000).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH RUNX1T1; HDAC1; HDAC2 AND HDAC3,
RP INTERACTION WITH RUNX1T1, AND SUBCELLULAR LOCATION.
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH EHMT2 AND HDAC1, INTERACTION WITH EHMT2
RP AND HDAC1, AND FUNCTION.
RX PubMed=16287849; DOI=10.1128/mcb.25.23.10338-10351.2005;
RA Duan Z., Zarebski A., Montoya-Durango D., Grimes H.L., Horwitz M.;
RT "Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of
RT histone lysine methyltransferase G9a and histone deacetylase 1.";
RL Mol. Cell. Biol. 25:10338-10351(2005).
RN [7]
RP FUNCTION, INTERACTION WITH ARIH2, AND UBIQUITINATION.
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 [8]
RP INTERACTION WITH SPI1, DOMAIN ZINC-FINGER, FUNCTION, AND MUTAGENESIS OF
RP PRO-2.
RX PubMed=17197705; DOI=10.1074/jbc.m607613200;
RA Dahl R., Iyer S.R., Owens K.S., Cuylear D.D., Simon M.C.;
RT "The transcriptional repressor GFI-1 antagonizes PU.1 activity through
RT protein-protein interaction.";
RL J. Biol. Chem. 282:6473-6483(2007).
RN [9]
RP INTERACTION WITH AJUBA IN THE GFI1-AJUBA-HDAC COMPLEX, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=18805794; DOI=10.1074/jbc.m802320200;
RA Montoya-Durango D.E., Velu C.S., Kazanjian A., Rojas M.E., Jay C.M.,
RA Longmore G.D., Grimes H.L.;
RT "Ajuba functions as a histone deacetylase-dependent co-repressor for
RT autoregulation of the growth factor-independent-1 transcription factor.";
RL J. Biol. Chem. 283:32056-32065(2008).
RN [10]
RP FUNCTION.
RX PubMed=19026687; DOI=10.1016/j.jneumeth.2008.10.031;
RA Ossovskaya V.S., Dolganov G., Basbaum A.I.;
RT "Loss of function genetic screens reveal MTGR1 as an intracellular
RT repressor of beta1 integrin-dependent neurite outgrowth.";
RL J. Neurosci. Methods 177:322-333(2009).
RN [11]
RP FUNCTION, AND INTERACTION WITH ZBTB17.
RX PubMed=19164764; DOI=10.1073/pnas.0804863106;
RA Basu S., Liu Q., Qiu Y., Dong F.;
RT "Gfi-1 represses CDKN2B encoding p15INK4B through interaction with Miz-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1433-1438(2009).
RN [12]
RP INTERACTION WITH RELA, SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX PubMed=20547752; DOI=10.1128/mcb.00087-10;
RA Sharif-Askari E., Vassen L., Kosan C., Khandanpour C., Gaudreau M.C.,
RA Heyd F., Okayama T., Jin J., Rojas M.E., Grimes H.L., Zeng H., Moroy T.;
RT "Zinc finger protein Gfi1 controls the endotoxin-mediated Toll-like
RT receptor inflammatory response by antagonizing NF-kappaB p65.";
RL Mol. Cell. Biol. 30:3929-3942(2010).
RN [13]
RP INTERACTION WITH ZBTB17, FUNCTION, INDUCTION, AND CHARACTERIZATION OF
RP VARIANT SER-382.
RX PubMed=20190815; DOI=10.1038/onc.2010.48;
RA Liu Q., Basu S., Qiu Y., Tang F., Dong F.;
RT "A role of Miz-1 in Gfi-1-mediated transcriptional repression of CDKN1A.";
RL Oncogene 29:2843-2852(2010).
RN [14]
RP VARIANT NI-CINA ARG-403, VARIANT SCN2 SER-382, CHARACTERIZATION OF VARIANTS
RP NI-CINA ARG-403 AND SCN2 SER-382, AND FUNCTION.
RX PubMed=12778173; DOI=10.1038/ng1170;
RA Person R.E., Li F.-Q., Duan Z., Benson K.F., Wechsler J., Papadaki H.A.,
RA Eliopoulos G., Kaufman C., Bertolone S.J., Nakamoto B., Papayannopoulou T.,
RA Grimes H.L., Horwitz M.;
RT "Mutations in proto-oncogene GFI1 cause human neutropenia and target
RT ELA2.";
RL Nat. Genet. 34:308-312(2003).
CC -!- FUNCTION: Transcription repressor essential for hematopoiesis.
CC Functions in a cell-context and development-specific manner. Binds to
CC 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of
CC genes. Component of several complexes, including the EHMT2-GFI1-HDAC1,
CC AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via
CC histone deacetylase (HDAC) recruitment, a number of genes implicated in
CC multilineage blood cell development. Regulates neutrophil
CC differentiation, promotes proliferation of lymphoid cells, and is
CC required for granulocyte development. Mediates, together with U2AF1L4,
CC the alternative splicing of CD45 and controls T-cell receptor
CC signaling. Regulates the endotoxin-mediated Toll-like receptor (TLR)
CC inflammatory response by antagonizing RELA. Cooperates with CBFA2T2 to
CC regulate ITGB1-dependent neurite growth. Controls cell-cycle
CC progression by repressing CDKNIA/p21 transcription in response to TGFB1
CC via recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB
CC promoters. Required for the maintenance of inner ear hair cells.
CC {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:12778173,
CC ECO:0000269|PubMed:16287849, ECO:0000269|PubMed:17197705,
CC ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:18805794,
CC ECO:0000269|PubMed:19026687, ECO:0000269|PubMed:19164764,
CC ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:20547752,
CC ECO:0000269|PubMed:8754800}.
CC -!- SUBUNIT: Interacts with U2AF1L4. Component of RCOR-GFI-KDM1A-HDAC
CC complexes. Interacts directly with RCOR1, KDM1A and HDAC2 (By
CC similarity). Also interacts with HDAC1. Interacts (via the zinc-finger
CC domain) with ARIH2; the interaction prevents GFI1 ubiquitination and
CC proteasomal degradation. Interacts with PIAS3; the interaction relieves
CC the inhibitory effect of PIAS3 on STAT3-mediated transcriptional
CC activity. Forms a complex with EHMT2 and HDAC1 to promote 'Lys-9'
CC dimethylation of H3 (H3K9Me2) and repress expression of target genes.
CC Interacts directly with EHMT2. Component of the GFI1-AJUBA-HDAC1
CC repressor complex. Interacts directly with AJUBA (via ITS LIM domains);
CC the interaction results in the HDAC-dependent corepression of a subset
CC of GFI1 target genes and, occurs independently of the SNAG domain.
CC Interacts with SPI1; the interaction inhibits SPI1 transcriptional
CC activity and represses SPI1-regulated macrophage-specific genes
CC required for proper granulocyte development. Interacts with RUNX1T1;
CC the interaction represses HDAC-mediated transcriptional activity.
CC Interacts with RELA; the interaction occurs on liposaccharide (LPS)
CC stimulation and controls RELA DNA binding activity and regulates
CC endotoxin-mediated TOLL-like receptor inflammatory response. Interacts
CC (via the C-terminal zinc fingers) with ZBTB17; the interaction results
CC in the recruitment of GFI1 to the CDKN1A/p21 and CDKN1B promoters and
CC repression of transcription. {ECO:0000250, ECO:0000269|PubMed:11060035,
CC ECO:0000269|PubMed:12874834, ECO:0000269|PubMed:16287849,
CC ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:17646546,
CC ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:19164764,
CC ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:20547752}.
CC -!- INTERACTION:
CC Q99684; Q13111: CHAF1A; NbExp=4; IntAct=EBI-949368, EBI-1020839;
CC Q99684; Q96KQ7: EHMT2; NbExp=2; IntAct=EBI-949368, EBI-744366;
CC Q99684; Q13547: HDAC1; NbExp=4; IntAct=EBI-949368, EBI-301834;
CC Q99684; Q9NQX1: PRDM5; NbExp=2; IntAct=EBI-949368, EBI-4292031;
CC Q99684; Q04206: RELA; NbExp=2; IntAct=EBI-949368, EBI-73886;
CC Q99684; Q91XC0: Ajuba; Xeno; NbExp=4; IntAct=EBI-949368, EBI-1565930;
CC Q99684; P17433: Spi1; Xeno; NbExp=2; IntAct=EBI-949368, EBI-607588;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060035,
CC ECO:0000269|PubMed:12874834, ECO:0000269|PubMed:18805794,
CC ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:8754800}.
CC Note=Colocalizes with PIAS3 and RUNX1T1 in nuclear dots.
CC -!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:20190815,
CC ECO:0000269|PubMed:20547752}.
CC -!- DOMAIN: Zinc fingers 3, 4 and 5 are required for DNA-binding and for
CC interaction with SPI1. {ECO:0000269|PubMed:17197705}.
CC -!- DOMAIN: The SNAG domain of GFIs is required for nuclear location and
CC for interaction with some corepressors. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination and degradation by the proteasome is
CC inhibited by the ubiquitin ligase, ARIH2.
CC {ECO:0000269|PubMed:17646546}.
CC -!- DISEASE: Neutropenia, severe congenital 2, autosomal dominant (SCN2)
CC [MIM:613107]: A disorder of hematopoiesis characterized by maturation
CC arrest of granulopoiesis at the level of promyelocytes with peripheral
CC blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of
CC severe bacterial infections. {ECO:0000269|PubMed:12778173}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Dominant nonimmune chronic idiopathic neutropenia of adults
CC (NI-CINA) [MIM:607847]: Relatively mild form of neutropenia diagnosed
CC in adults, but predisposing to leukemia in a subset of patients.
CC {ECO:0000269|PubMed:12778173}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=GFI1base; Note=GFI1 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/GFI1base/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GFI1ID40706ch1p22.html";
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DR EMBL; U67369; AAB37272.1; -; mRNA.
DR EMBL; BC032751; AAH32751.1; -; mRNA.
DR EMBL; BC074866; AAH74866.1; -; mRNA.
DR EMBL; BC074867; AAH74867.1; -; mRNA.
DR CCDS; CCDS30773.1; -.
DR RefSeq; NP_001120687.1; NM_001127215.1.
DR RefSeq; NP_001120688.1; NM_001127216.1.
DR RefSeq; NP_005254.2; NM_005263.3.
DR RefSeq; XP_005270806.1; XM_005270749.3.
DR RefSeq; XP_011539547.1; XM_011541245.2.
DR RefSeq; XP_011539548.1; XM_011541246.2.
DR AlphaFoldDB; Q99684; -.
DR SMR; Q99684; -.
DR BioGRID; 108940; 20.
DR CORUM; Q99684; -.
DR DIP; DIP-38452N; -.
DR IntAct; Q99684; 17.
DR STRING; 9606.ENSP00000359357; -.
DR iPTMnet; Q99684; -.
DR PhosphoSitePlus; Q99684; -.
DR BioMuta; GFI1; -.
DR DMDM; 33860154; -.
DR EPD; Q99684; -.
DR jPOST; Q99684; -.
DR MassIVE; Q99684; -.
DR PaxDb; Q99684; -.
DR PeptideAtlas; Q99684; -.
DR PRIDE; Q99684; -.
DR ProteomicsDB; 78396; -.
DR Antibodypedia; 4402; 299 antibodies from 33 providers.
DR DNASU; 2672; -.
DR Ensembl; ENST00000294702.6; ENSP00000294702.5; ENSG00000162676.12.
DR Ensembl; ENST00000370332.5; ENSP00000359357.1; ENSG00000162676.12.
DR Ensembl; ENST00000427103.5; ENSP00000399719.1; ENSG00000162676.12.
DR GeneID; 2672; -.
DR KEGG; hsa:2672; -.
DR MANE-Select; ENST00000294702.6; ENSP00000294702.5; NM_005263.5; NP_005254.2.
DR UCSC; uc001dou.5; human.
DR CTD; 2672; -.
DR DisGeNET; 2672; -.
DR GeneCards; GFI1; -.
DR HGNC; HGNC:4237; GFI1.
DR HPA; ENSG00000162676; Group enriched (bone marrow, lymphoid tissue).
DR MalaCards; GFI1; -.
DR MIM; 600871; gene.
DR MIM; 607847; phenotype.
DR MIM; 613107; phenotype.
DR neXtProt; NX_Q99684; -.
DR OpenTargets; ENSG00000162676; -.
DR Orphanet; 486; Autosomal dominant severe congenital neutropenia.
DR PharmGKB; PA24344; -.
DR VEuPathDB; HostDB:ENSG00000162676; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156166; -.
DR HOGENOM; CLU_002678_94_9_1; -.
DR InParanoid; Q99684; -.
DR OMA; KPYMWNS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q99684; -.
DR TreeFam; TF350784; -.
DR PathwayCommons; Q99684; -.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q99684; -.
DR SIGNOR; Q99684; -.
DR BioGRID-ORCS; 2672; 41 hits in 1096 CRISPR screens.
DR GeneWiki; GFI1; -.
DR GenomeRNAi; 2672; -.
DR Pharos; Q99684; Tbio.
DR PRO; PR:Q99684; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99684; protein.
DR Bgee; ENSG00000162676; Expressed in granulocyte and 107 other tissues.
DR Genevisible; Q99684; HS.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IEA:InterPro.
DR GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; IC:BHF-UCL.
DR GO; GO:0070105; P:positive regulation of interleukin-6-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:InterPro.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0016032; P:viral process; TAS:ProtInc.
DR InterPro; IPR029840; GFI1/1B.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24404:SF46; PTHR24404:SF46; 1.
DR Pfam; PF00096; zf-C2H2; 6.
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 Disease variant; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..422
FT /note="Zinc finger protein Gfi-1"
FT /id="PRO_0000047193"
FT ZN_FING 255..278
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..419
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 140..257
FT /note="Required for interaction with RELA"
FT /evidence="ECO:0000269|PubMed:20547752"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07120"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07120"
FT VARIANT 36
FT /note="S -> N (in dbSNP:rs34631763)"
FT /id="VAR_052722"
FT VARIANT 382
FT /note="N -> S (in SCN2; zero neutrophil count. marked
FT monocytosis and reduced T- and B-lymphocyte number leading
FT to recurrent infectious complications. Abolishes
FT recognition of DNA binding site of zinc finger. Diminished
FT repression activity and elevated ELA2 expression. No effect
FT on repression of CDKN1A/p21 transcription;
FT dbSNP:rs28936381)"
FT /evidence="ECO:0000269|PubMed:12778173,
FT ECO:0000269|PubMed:20190815"
FT /id="VAR_016212"
FT VARIANT 403
FT /note="K -> R (in NI-CINA; Neutropenic and elevated
FT monocytosis but no history of infectious complications. No
FT effect on DNA binding but diminished GFI1 repression
FT activity; dbSNP:rs28936382)"
FT /evidence="ECO:0000269|PubMed:12778173"
FT /id="VAR_016213"
FT MUTAGEN 2
FT /note="P->A: Abrogates transcriptional repression."
FT /evidence="ECO:0000269|PubMed:17197705"
FT CONFLICT 73..77
FT /note="DSCEG -> RQLRS (in Ref. 1; AAB37272)"
FT /evidence="ECO:0000305"
FT CONFLICT 184..186
FT /note="SCS -> NCI (in Ref. 1; AAB37272)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="R -> K (in Ref. 1; AAB37272)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="G -> R (in Ref. 1; AAB37272)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="D -> N (in Ref. 1; AAB37272)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="P -> L (in Ref. 1; AAB37272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 45297 MW; 740A466F72C5FC72 CRC64;
MPRSFLVKSK KAHSYHQPRS PGPDYSLRLE NVPAPSRADS TSNAGGAKAE PRDRLSPESQ
LTEAPDRASA SPDSCEGSVC ERSSEFEDFW RPPSPSASPA SEKSMCPSLD EAQPFPLPFK
PYSWSGLAGS DLRHLVQSYR PCGALERGAG LGLFCEPAPE PGHPAALYGP KRAAGGAGAG
APGSCSAGAG ATAGPGLGLY GDFGSAAAGL YERPTAAAGL LYPERGHGLH ADKGAGVKVE
SELLCTRLLL GGGSYKCIKC SKVFSTPHGL EVHVRRSHSG TRPFACEMCG KTFGHAVSLE
QHKAVHSQER SFDCKICGKS FKRSSTLSTH LLIHSDTRPY PCQYCGKRFH QKSDMKKHTF
IHTGEKPHKC QVCGKAFSQS SNLITHSRKH TGFKPFGCDL CGKGFQRKVD LRRHRETQHG
LK