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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
 
 
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