GRHL1_HUMAN
ID GRHL1_HUMAN Reviewed; 618 AA.
AC Q9NZI5; A6NLA4; B2R7E4; B5MEC2; Q53T93; Q6NWN7; Q6NWN8; Q6NWN9; Q8NI33;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Grainyhead-like protein 1 homolog {ECO:0000312|HGNC:HGNC:17923};
DE AltName: Full=Mammalian grainyhead;
DE AltName: Full=NH32;
DE AltName: Full=Transcription factor CP2-like 2;
DE AltName: Full=Transcription factor LBP-32;
GN Name=GRHL1 {ECO:0000312|HGNC:HGNC:17923};
GN Synonyms=LBP32, MGR, TFCP2L2 {ECO:0000312|HGNC:HGNC:17923};
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=Placenta;
RX PubMed=10644752; DOI=10.1074/jbc.275.4.2852;
RA Huang N., Miller W.L.;
RT "Cloning of factors related to HIV-inducible LBP proteins that regulate
RT steroidogenic factor-1-independent human placental transcription of the
RT cholesterol side-chain cleavage enzyme, P450scc.";
RL J. Biol. Chem. 275:2852-2858(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, AND INTERACTION WITH GRHL2.
RC TISSUE=Fetal brain;
RX PubMed=12175488; DOI=10.1016/s0925-4773(02)00046-1;
RA Wilanowski T., Tuckfield A., Cerruti L., O'Connell S., Saint R., Parekh V.,
RA Tao J., Cunningham J.M., Jane S.M.;
RT "A highly conserved novel family of mammalian developmental transcription
RT factors related to Drosophila grainyhead.";
RL Mech. Dev. 114:37-50(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP SER-191 AND ILE-397.
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 INTERACTION WITH GRHL3.
RX PubMed=12549979; DOI=10.1042/bj20021476;
RA Ting S.B., Wilanowski T., Cerruti L., Zhao L.L., Cunningham J.M.,
RA Jane S.M.;
RT "The identification and characterization of human sister-of-mammalian
RT grainyhead (SOM) expands the grainyhead-like family of developmental
RT transcription factors.";
RL Biochem. J. 370:953-962(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18288204; DOI=10.1038/emboj.2008.24;
RA Wilanowski T., Caddy J., Ting S.B., Hislop N.R., Cerruti L., Auden A.,
RA Zhao L.L., Asquith S., Ellis S., Sinclair R., Cunningham J.M., Jane S.M.;
RT "Perturbed desmosomal cadherin expression in grainy head-like 1-null
RT mice.";
RL EMBO J. 27:886-897(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 248-485 IN COMPLEX WITH DNA,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-378; THR-380; GLN-385; CYS-421;
RP ARG-427; LYS-428 AND ARG-430.
RX PubMed=29309642; DOI=10.1093/nar/gkx1299;
RA Ming Q., Roske Y., Schuetz A., Walentin K., Ibraimi I., Schmidt-Ott K.M.,
RA Heinemann U.;
RT "Structural basis of gene regulation by the Grainyhead/CP2 transcription
RT factor family.";
RL Nucleic Acids Res. 46:2082-2095(2018).
CC -!- FUNCTION: Transcription factor involved in epithelial development.
CC Binds directly to the consensus DNA sequence 5'-AACCGGTT-3'
CC (PubMed:12175488, PubMed:18288204, PubMed:29309642). Important
CC regulator of DSG1 in the context of hair anchorage and epidermal
CC differentiation, participates in the maintenance of the skin barrier.
CC There is no genetic interaction with GRHL3, no functional cooperativity
CC due to diverse target gene selectivity during epithelia development (By
CC similarity). {ECO:0000250|UniProtKB:Q921D9,
CC ECO:0000269|PubMed:12175488, ECO:0000269|PubMed:18288204,
CC ECO:0000269|PubMed:29309642}.
CC -!- FUNCTION: [Isoform 1]: Functions as transcription activator.
CC {ECO:0000269|PubMed:12175488, ECO:0000269|PubMed:29309642}.
CC -!- FUNCTION: [Isoform 2]: May function as a repressor in tissues where
CC both isoform 1 and isoform 2 are expressed.
CC {ECO:0000269|PubMed:12175488}.
CC -!- SUBUNIT: Binds DNA as homodimer (PubMed:29309642). Homodimer, also
CC forms heterodimers with GRHL2 or GRHL3 (PubMed:12175488,
CC PubMed:12549979, PubMed:29309642). {ECO:0000269|PubMed:12175488,
CC ECO:0000269|PubMed:12549979, ECO:0000269|PubMed:29309642}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18288204}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=p70 MGR;
CC IsoId=Q9NZI5-1; Sequence=Displayed;
CC Name=2; Synonyms=p49 MGR;
CC IsoId=Q9NZI5-2; Sequence=VSP_017636, VSP_017637;
CC Name=3;
CC IsoId=Q9NZI5-3; Sequence=VSP_017638, VSP_017639;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in brain, pancreas,
CC tonsil, placenta and kidney. Isoform 2 is highly expressed in brain and
CC liver. Expressed at very low levels in non-steroidogenic cells.
CC {ECO:0000269|PubMed:10644752, ECO:0000269|PubMed:12175488}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver and brain.
CC {ECO:0000269|PubMed:12175488}.
CC -!- MISCELLANEOUS: GRHL genes (GRHL1, GRHL2 and GRHL3) show a paradoxal
CC lack of redundancy despite their extensive sequence identity in the
CC DNA-binding and protein dimerization domains and the fact that the core
CC consensus DNA binding sites are identical. They have related but
CC remarkably different functions during embryogenesis because of their
CC differential spatiotemporal expression patterns during development.
CC {ECO:0000250|UniProtKB:Q921D9}.
CC -!- SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily.
CC {ECO:0000305}.
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DR EMBL; AF198489; AAF32276.1; -; mRNA.
DR EMBL; AF411210; AAM22616.1; -; mRNA.
DR EMBL; AK312950; BAG35791.1; -; mRNA.
DR EMBL; AC010969; AAX93273.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00973.1; -; Genomic_DNA.
DR EMBL; BC067519; AAH67519.1; -; mRNA.
DR EMBL; BC067520; AAH67520.1; -; mRNA.
DR EMBL; BC067521; AAH67521.1; -; mRNA.
DR CCDS; CCDS33144.2; -. [Q9NZI5-1]
DR RefSeq; NP_937825.2; NM_198182.2. [Q9NZI5-1]
DR RefSeq; XP_005246216.1; XM_005246159.3. [Q9NZI5-2]
DR PDB; 5MPF; X-ray; 2.92 A; A/B=248-485.
DR PDB; 5MPH; X-ray; 2.34 A; A=248-485.
DR PDB; 5MPI; X-ray; 2.35 A; A=248-485.
DR PDBsum; 5MPF; -.
DR PDBsum; 5MPH; -.
DR PDBsum; 5MPI; -.
DR AlphaFoldDB; Q9NZI5; -.
DR SMR; Q9NZI5; -.
DR BioGRID; 118928; 9.
DR IntAct; Q9NZI5; 6.
DR MINT; Q9NZI5; -.
DR STRING; 9606.ENSP00000324693; -.
DR iPTMnet; Q9NZI5; -.
DR PhosphoSitePlus; Q9NZI5; -.
DR BioMuta; GRHL1; -.
DR DMDM; 90101332; -.
DR EPD; Q9NZI5; -.
DR jPOST; Q9NZI5; -.
DR MassIVE; Q9NZI5; -.
DR MaxQB; Q9NZI5; -.
DR PaxDb; Q9NZI5; -.
DR PeptideAtlas; Q9NZI5; -.
DR PRIDE; Q9NZI5; -.
DR ProteomicsDB; 83404; -. [Q9NZI5-1]
DR ProteomicsDB; 83405; -. [Q9NZI5-2]
DR ProteomicsDB; 83406; -. [Q9NZI5-3]
DR Antibodypedia; 1788; 127 antibodies from 24 providers.
DR DNASU; 29841; -.
DR Ensembl; ENST00000324907.14; ENSP00000324693.9; ENSG00000134317.18. [Q9NZI5-1]
DR Ensembl; ENST00000405379.6; ENSP00000384209.3; ENSG00000134317.18. [Q9NZI5-2]
DR Ensembl; ENST00000472167.5; ENSP00000418275.1; ENSG00000134317.18. [Q9NZI5-3]
DR GeneID; 29841; -.
DR KEGG; hsa:29841; -.
DR MANE-Select; ENST00000324907.14; ENSP00000324693.9; NM_198182.3; NP_937825.2.
DR UCSC; uc002raa.4; human. [Q9NZI5-1]
DR CTD; 29841; -.
DR DisGeNET; 29841; -.
DR GeneCards; GRHL1; -.
DR HGNC; HGNC:17923; GRHL1.
DR HPA; ENSG00000134317; Tissue enhanced (esophagus, skin, vagina).
DR MIM; 609786; gene.
DR neXtProt; NX_Q9NZI5; -.
DR OpenTargets; ENSG00000134317; -.
DR PharmGKB; PA134971477; -.
DR VEuPathDB; HostDB:ENSG00000134317; -.
DR eggNOG; KOG4091; Eukaryota.
DR GeneTree; ENSGT00940000157612; -.
DR HOGENOM; CLU_021156_1_1_1; -.
DR InParanoid; Q9NZI5; -.
DR OMA; VHHPISK; -.
DR OrthoDB; 286319at2759; -.
DR PhylomeDB; Q9NZI5; -.
DR TreeFam; TF314132; -.
DR PathwayCommons; Q9NZI5; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR SignaLink; Q9NZI5; -.
DR BioGRID-ORCS; 29841; 15 hits in 1103 CRISPR screens.
DR ChiTaRS; GRHL1; human.
DR GenomeRNAi; 29841; -.
DR Pharos; Q9NZI5; Tbio.
DR PRO; PR:Q9NZI5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NZI5; protein.
DR Bgee; ENSG00000134317; Expressed in upper arm skin and 148 other tissues.
DR ExpressionAtlas; Q9NZI5; baseline and differential.
DR Genevisible; Q9NZI5; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0002934; P:desmosome organization; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR007604; CP2.
DR Pfam; PF04516; CP2; 1.
DR PROSITE; PS51968; GRH_CP2_DB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Developmental protein;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..618
FT /note="Grainyhead-like protein 1 homolog"
FT /id="PRO_0000227990"
FT DOMAIN 248..474
FT /note="Grh/CP2 DB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT REGION 1..91
FT /note="Transcription activation"
FT /evidence="ECO:0000250|UniProtKB:Q8K5C0"
FT REGION 74..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..389
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:29309642"
FT REGION 427..430
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:29309642"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12175488"
FT /id="VSP_017636"
FT VAR_SEQ 190..249
FT /note="LNTDQFSSGAQAPNAQRRTPDSTFSETFKEGVQEVFFPSDLSLRMPGMNSED
FT YVFDSVSG -> MASLWESPQQCIILSPLSGWWFSIGISILTSSALVLKPQMLKGELQT
FT RPSQRPSRKAFRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12175488"
FT /id="VSP_017637"
FT VAR_SEQ 441..511
FT /note="VSDVKVPLLPSHKRMDITVFKPFIDLDTQPVLFIPDVHFANLQRGTHVLPIA
FT SEELEGEGSVLKRGPYGTE -> GKCPDPSSQFLMLKCHCFPLTSEWISQFSNPSLISI
FT LSLSSSFLTCTLPTCSGALMSFPLPLKNWRVKALS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017638"
FT VAR_SEQ 512..618
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017639"
FT VARIANT 191
FT /note="N -> S (in dbSNP:rs16867256)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025663"
FT VARIANT 397
FT /note="V -> I (in dbSNP:rs2303920)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025664"
FT MUTAGEN 378
FT /note="L->A: Decreases affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 380
FT /note="T->A: Decreases affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 385
FT /note="Q->A: Decreases affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 421
FT /note="C->A: No effect on affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 427
FT /note="R->A: Loss of activity as transcriptional activator.
FT Strongly decreases affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 427
FT /note="R->Q: Loss of activity as transcriptional activator.
FT Nearly abolishes affinity for target DNA. Causes steric
FT hindrance that impedes DNA-binding by neighboring
FT residues."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 428
FT /note="K->A: Decreases affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT MUTAGEN 430
FT /note="R->A: Decreases affinity for target DNA."
FT /evidence="ECO:0000269|PubMed:29309642"
FT CONFLICT 13
FT /note="V -> A (in Ref. 1; AAF32276)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="L -> F (in Ref. 6; AAH67521)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="I -> V (in Ref. 6; AAH67519)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="G -> A (in Ref. 6; AAH67521)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="I -> V (in Ref. 6; AAH67520)"
FT /evidence="ECO:0000305"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:5MPH"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:5MPH"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:5MPH"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 393..403
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:5MPH"
FT STRAND 410..421
FT /evidence="ECO:0007829|PDB:5MPH"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:5MPH"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:5MPF"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:5MPI"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:5MPI"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5MPF"
SQ SEQUENCE 618 AA; 70113 MW; 449587B17F4A8A44 CRC64;
MTQEYDNKRP VLVLQNEALY PQRRSYTSED EAWKSFLENP LTAATKAMMS INGDEDSAAA
LGLLYDYYKV PRERRSSTAK PEVEHPEPDH SKRNSIPIVT EQPLISAGEN RVQVLKNVPF
NIVLPHGNQL GIDKRGHLTA PDTTVTVSIA TMPTHSIKTE TQPHGFAVGI PPAVYHPEPT
ERVVVFDRNL NTDQFSSGAQ APNAQRRTPD STFSETFKEG VQEVFFPSDL SLRMPGMNSE
DYVFDSVSGN NFEYTLEASK SLRQKPGDST MTYLNKGQFY PITLKEVSSS EGIHHPISKV
RSVIMVVFAE DKSREDQLRH WKYWHSRQHT AKQRCIDIAD YKESFNTISN IEEIAYNAIS
FTWDINDEAK VFISVNCLST DFSSQKGVKG LPLNIQVDTY SYNNRSNKPV HRAYCQIKVF
CDKGAERKIR DEERKQSKRK VSDVKVPLLP SHKRMDITVF KPFIDLDTQP VLFIPDVHFA
NLQRGTHVLP IASEELEGEG SVLKRGPYGT EDDFAVPPST KLARIEEPKR VLLYVRKESE
EVFDALMLKT PSLKGLMEAI SDKYDVPHDK IGKIFKKCKK GILVNMDDNI VKHYSNEDTF
QLQIEEAGGS YKLTLTEI
