HINFP_HUMAN
ID HINFP_HUMAN Reviewed; 517 AA.
AC Q9BQA5; B3KPH6; B4DWB4; E9PQF4; Q96E65; Q9Y4M7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Histone H4 transcription factor;
DE AltName: Full=Histone nuclear factor P;
DE Short=HiNF-P;
DE AltName: Full=MBD2-interacting zinc finger protein;
DE AltName: Full=Methyl-CpG-binding protein 2-interacting zinc finger protein;
GN Name=HINFP; Synonyms=MIZF, ZNF743;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Synovium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-4;
RP CYS-78 AND VAL-493.
RC TISSUE=Eye, and Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 356-517 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP MBD2.
RX PubMed=11553631; DOI=10.1074/jbc.m107048200;
RA Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.;
RT "Involvement of a novel zinc finger protein, MIZF, in transcriptional
RT repression by interacting with a methyl-CpG-binding protein, MBD2.";
RL J. Biol. Chem. 276:42632-42638(2001).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=14585971; DOI=10.1128/mcb.23.22.8110-8123.2003;
RA Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y.,
RA Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.;
RT "Identification of HiNF-P, a key activator of cell cycle-controlled histone
RT H4 genes at the onset of S phase.";
RL Mol. Cell. Biol. 23:8110-8123(2003).
RN [8]
RP FUNCTION.
RX PubMed=14752047; DOI=10.1093/nar/gkh249;
RA Sekimata M., Homma Y.;
RT "Sequence-specific transcriptional repression by an MBD2-interacting zinc
RT finger protein MIZF.";
RL Nucleic Acids Res. 32:590-597(2004).
RN [9]
RP FUNCTION, INTERACTION WITH NPAT, AND SUBCELLULAR LOCATION.
RX PubMed=15988025; DOI=10.1128/mcb.25.14.6140-6153.2005;
RA Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L.,
RA Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L.,
RA Stein G.S.;
RT "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4
RT gene regulation at the G1/S phase cell cycle transition.";
RL Mol. Cell. Biol. 25:6140-6153(2005).
RN [10]
RP UBIQUITINATION.
RX PubMed=17176114; DOI=10.1021/bi061425m;
RA Medina R., van Wijnen A.J., Stein G.S., Stein J.L.;
RT "The histone gene transcription factor HiNF-P stabilizes its cell cycle
RT regulatory co-activator p220NPAT.";
RL Biochemistry 45:15915-15920(2006).
RN [11]
RP FUNCTION.
RX PubMed=17974976; DOI=10.1158/0008-5472.can-07-1560;
RA Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L.,
RA van Wijnen A.J., Stein J.L., Stein G.S.;
RT "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone
RT target genes.";
RL Cancer Res. 67:10334-10342(2007).
RN [12]
RP FUNCTION.
RX PubMed=17163457; DOI=10.1002/jcb.21157;
RA Mitra P., Xie R.-L., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.;
RT "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4
RT gene transcription.";
RL J. Cell. Biochem. 101:181-191(2007).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, REGION, AND MUTAGENESIS OF TYR-381.
RX PubMed=18850719; DOI=10.1021/bi800961d;
RA Medina R., Buck T., Zaidi S.K., Miele-Chamberland A., Lian J.B.,
RA Stein J.L., van Wijnen A.J., Stein G.S.;
RT "The histone gene cell cycle regulator HiNF-P is a unique zinc finger
RT transcription factor with a novel conserved auxiliary DNA-binding motif.";
RL Biochemistry 47:11415-11423(2008).
CC -!- FUNCTION: Transcriptional repressor that binds to the consensus
CC sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional
CC activator that promotes histone H4 gene transcription at the G1/S phase
CC transition in conjunction with NPAT. Also activates transcription of
CC the ATM and PRKDC genes. Autoregulates its expression by associating
CC with its own promoter. {ECO:0000269|PubMed:11553631,
CC ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:14752047,
CC ECO:0000269|PubMed:15988025, ECO:0000269|PubMed:17163457,
CC ECO:0000269|PubMed:17974976, ECO:0000269|PubMed:18850719}.
CC -!- SUBUNIT: Binds MBD2 and a histone deacetylase complex. Interacts with
CC NPAT. {ECO:0000269|PubMed:11553631, ECO:0000269|PubMed:15988025}.
CC -!- INTERACTION:
CC Q9BQA5; Q6PF18: MORN3; NbExp=3; IntAct=EBI-749065, EBI-9675802;
CC Q9BQA5; O14561: NDUFAB1; NbExp=3; IntAct=EBI-749065, EBI-1246261;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11553631,
CC ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15988025,
CC ECO:0000269|PubMed:18850719}. Note=Associated with discrete nuclear
CC foci.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQA5-2; Sequence=VSP_044719, VSP_044720;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart,
CC skeletal muscle, spleen, kidney, small intestine, placenta and liver.
CC {ECO:0000269|PubMed:11553631}.
CC -!- PTM: Ubiquitinated. Ubiquitination may lead to proteasome-mediated
CC degradation. {ECO:0000269|PubMed:17176114}.
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DR EMBL; AK056362; BAG51688.1; -; mRNA.
DR EMBL; AK301452; BAG62976.1; -; mRNA.
DR EMBL; AP002956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67461.1; -; Genomic_DNA.
DR EMBL; BC001073; AAH01073.1; -; mRNA.
DR EMBL; BC001945; AAH01945.1; -; mRNA.
DR EMBL; BC012856; AAH12856.1; -; mRNA.
DR EMBL; BC017234; AAH17234.1; -; mRNA.
DR EMBL; AL080201; CAB45773.1; -; mRNA.
DR CCDS; CCDS58188.1; -. [Q9BQA5-2]
DR CCDS; CCDS8414.1; -. [Q9BQA5-1]
DR PIR; T12509; T12509.
DR RefSeq; NP_001230188.1; NM_001243259.1. [Q9BQA5-2]
DR RefSeq; NP_056332.2; NM_015517.4. [Q9BQA5-1]
DR RefSeq; NP_945322.1; NM_198971.2. [Q9BQA5-1]
DR RefSeq; XP_011541047.1; XM_011542745.2.
DR AlphaFoldDB; Q9BQA5; -.
DR BioGRID; 117469; 40.
DR IntAct; Q9BQA5; 7.
DR MINT; Q9BQA5; -.
DR STRING; 9606.ENSP00000318085; -.
DR iPTMnet; Q9BQA5; -.
DR PhosphoSitePlus; Q9BQA5; -.
DR BioMuta; HINFP; -.
DR DMDM; 322510032; -.
DR EPD; Q9BQA5; -.
DR MassIVE; Q9BQA5; -.
DR PaxDb; Q9BQA5; -.
DR PeptideAtlas; Q9BQA5; -.
DR PRIDE; Q9BQA5; -.
DR ProteomicsDB; 23003; -.
DR ProteomicsDB; 78648; -. [Q9BQA5-1]
DR Antibodypedia; 32617; 196 antibodies from 25 providers.
DR DNASU; 25988; -.
DR Ensembl; ENST00000350777.7; ENSP00000318085.3; ENSG00000172273.13. [Q9BQA5-1]
DR Ensembl; ENST00000527410.3; ENSP00000436815.1; ENSG00000172273.13. [Q9BQA5-2]
DR GeneID; 25988; -.
DR KEGG; hsa:25988; -.
DR MANE-Select; ENST00000350777.7; ENSP00000318085.3; NM_198971.3; NP_945322.1.
DR UCSC; uc001pvq.4; human. [Q9BQA5-1]
DR CTD; 25988; -.
DR DisGeNET; 25988; -.
DR GeneCards; HINFP; -.
DR HGNC; HGNC:17850; HINFP.
DR HPA; ENSG00000172273; Low tissue specificity.
DR MIM; 607099; gene.
DR neXtProt; NX_Q9BQA5; -.
DR OpenTargets; ENSG00000172273; -.
DR PharmGKB; PA164720597; -.
DR VEuPathDB; HostDB:ENSG00000172273; -.
DR eggNOG; KOG3608; Eukaryota.
DR GeneTree; ENSGT00870000136508; -.
DR HOGENOM; CLU_026599_0_0_1; -.
DR InParanoid; Q9BQA5; -.
DR OMA; GERNCLW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9BQA5; -.
DR TreeFam; TF350923; -.
DR PathwayCommons; Q9BQA5; -.
DR SignaLink; Q9BQA5; -.
DR BioGRID-ORCS; 25988; 789 hits in 1109 CRISPR screens.
DR ChiTaRS; HINFP; human.
DR GeneWiki; MIZF; -.
DR GenomeRNAi; 25988; -.
DR Pharos; Q9BQA5; Tbio.
DR PRO; PR:Q9BQA5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BQA5; protein.
DR Bgee; ENSG00000172273; Expressed in cerebellar hemisphere and 133 other tissues.
DR ExpressionAtlas; Q9BQA5; baseline and differential.
DR Genevisible; Q9BQA5; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI: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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP: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; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..517
FT /note="Histone H4 transcription factor"
FT /id="PRO_0000047218"
FT ZN_FING 15..39
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 129..153
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 169..193
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..221
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 255..278
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..337
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..368
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 373..517
FT /note="Interaction with NPAT"
FT /evidence="ECO:0000269|PubMed:15988025"
FT REGION 374..407
FT /note="Required for activation of histone H4 transcription
FT and contributes to DNA-binding"
FT REGION 431..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 381..419
FT /note="YKEHEDGYMRLQLVRYESVELTQQLLRQPQEGSGLGTSL -> LGHFCIPLP
FT GFAALYAPTSPGTRNMKMAICGCSWFATRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044719"
FT VAR_SEQ 420..517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044720"
FT VARIANT 4
FT /note="P -> S (in dbSNP:rs17850972)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026547"
FT VARIANT 78
FT /note="S -> C (in dbSNP:rs17850974)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026548"
FT VARIANT 352
FT /note="K -> R (in dbSNP:rs34118252)"
FT /id="VAR_038793"
FT VARIANT 493
FT /note="A -> V (in dbSNP:rs100803)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019424"
FT MUTAGEN 381
FT /note="Y->A: Abolishes DNA-Binding."
FT /evidence="ECO:0000269|PubMed:18850719"
FT CONFLICT 62
FT /note="E -> G (in Ref. 1; BAG62976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 59678 MW; 2CE1910737B0B6EB CRC64;
MPPPGKVPRK ENLWLQCEWG SCSFVCSTME KFFEHVTQHL QQHLHGSGEE EEEEEEDDPL
EEEFSCLWQE CGFCSLDSSA DLIRHVYFHC YHTKLKQWGL QALQSQADLG PCILDFQSRN
VIPDIPDHFL CLWEHCENSF DNPEWFYRHV EAHSLCCEYE AVGKDNPVVL CGWKGCTCTF
KDRSKLREHL RSHTQEKVVA CPTCGGMFAN NTKFLDHIRR QTSLDQQHFQ CSHCSKRFAT
ERLLRDHMRN HVNHYKCPLC DMTCPLPSSL RNHMRFRHSE DRPFKCDCCD YSCKNLIDLQ
KHLDTHSEEP AYRCDFENCT FSARSLCSIK SHYRKVHEGD SEPRYKCHVC DKCFTRGNNL
TVHLRKKHQF KWPSGHPRFR YKEHEDGYMR LQLVRYESVE LTQQLLRQPQ EGSGLGTSLN
ESSLQGIILE TVPGEPGRKE EEEEGKGSEG TALSASQDNP SSVIHVVNQT NAQGQQEIVY
YVLSEAPGEP PPAPEPPSGG IMEKLQGIAE EPEIQMV
