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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";
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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
 
 
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