CNOT9_HUMAN
ID CNOT9_HUMAN Reviewed; 299 AA.
AC Q92600; B2RPI0; B5MDQ4; B7Z1E5; Q96IX4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=CCR4-NOT transcription complex subunit 9 {ECO:0000312|HGNC:HGNC:10445};
DE AltName: Full=Cell differentiation protein RQCD1 homolog;
DE Short=Rcd-1;
GN Name=CNOT9 {ECO:0000312|HGNC:HGNC:10445}; Synonyms=RCD1, RQCD1;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Foreskin;
RX PubMed=9447985; DOI=10.1128/mcb.18.2.887;
RA Okazaki N., Okazaki K., Watanabe Y., Kato-Hayashi M., Yamamoto M.,
RA Okayama H.;
RT "Novel factor highly conserved among eukaryotes controls sexual development
RT in fission yeast.";
RL Mol. Cell. Biol. 18:887-895(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP THR-143.
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 [6]
RP PROTEIN SEQUENCE OF 1-21; 36-44; 180-188 AND 275-292, ACETYLATION AT MET-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [7]
RP FUNCTION, AND INTERACTION WITH ZNF335.
RX PubMed=18180299; DOI=10.1074/jbc.m706986200;
RA Garapaty S., Mahajan M.A., Samuels H.H.;
RT "Components of the CCR4-NOT complex function as nuclear hormone receptor
RT coactivators via association with the NRC-interacting Factor NIF-1.";
RL J. Biol. Chem. 283:6806-6816(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION IN THE CCR4-NOT COMPLEX.
RX PubMed=23232451; DOI=10.4161/rna.23065;
RA Mauxion F., Preve B., Seraphin B.;
RT "C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex.";
RL RNA Biol. 10:267-276(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-285, DOMAIN, SUBUNIT, FUNCTION,
RP AND MUTAGENESIS OF ARG-227.
RX PubMed=17189474; DOI=10.1110/ps.062600507;
RA Garces R.G., Gillon W., Pai E.F.;
RT "Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with
RT in vitro nucleic acid binding properties.";
RL Protein Sci. 16:176-188(2007).
CC -!- FUNCTION: Component of the CCR4-NOT complex which is one of the major
CC cellular mRNA deadenylases and is linked to various cellular processes
CC including bulk mRNA degradation, miRNA-mediated repression,
CC translational repression during translational initiation and general
CC transcription regulation. Additional complex functions may be a
CC consequence of its influence on mRNA expression. Involved in down-
CC regulation of MYB- and JUN-dependent transcription. May play a role in
CC cell differentiation (By similarity). Can bind oligonucleotides, such
CC as poly-G, poly-C or poly-T (in vitro), but the physiological relevance
CC of this is not certain. Does not bind poly-A. Enhances ligand-dependent
CC transcriptional activity of nuclear hormone receptors, including RARA,
CC expect ESR1-mediated transcription that is not only slightly increased,
CC if at all. {ECO:0000250, ECO:0000269|PubMed:17189474,
CC ECO:0000269|PubMed:18180299}.
CC -!- SUBUNIT: Homodimer. Component of the CCR4-NOT complex; distinct
CC complexes seem to exist that differ in the participation of probably
CC mutually exclusive catalytic subunits. Interacts with MYB, ATF2, RARA,
CC RARB, RARG, RXRA, RXRB and RXRG. Identified in a complex with ATF2
CC bound to target DNA (By similarity). Interacts with NANOS2 (By
CC similarity). Directly interacts with ZNF335. {ECO:0000250,
CC ECO:0000269|PubMed:17189474, ECO:0000269|PubMed:18180299,
CC ECO:0000269|PubMed:23232451}.
CC -!- INTERACTION:
CC Q92600-3; P24522: GADD45A; NbExp=5; IntAct=EBI-12907584, EBI-448167;
CC Q92600-3; O75293: GADD45B; NbExp=3; IntAct=EBI-12907584, EBI-448187;
CC Q92600-3; O95257: GADD45G; NbExp=3; IntAct=EBI-12907584, EBI-448202;
CC Q92600-3; Q14696: MESD; NbExp=3; IntAct=EBI-12907584, EBI-6165891;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JKY0}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9JKY0}. Note=NANOS2 promotes
CC its localization to P-body. {ECO:0000250|UniProtKB:Q9JKY0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92600-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92600-2; Sequence=VSP_054371;
CC Name=3;
CC IsoId=Q92600-3; Sequence=VSP_055744, VSP_055745;
CC -!- TISSUE SPECIFICITY: Detected in spleen, thymus, prostate, testis, ovary
CC and intestine. {ECO:0000269|PubMed:9447985}.
CC -!- SIMILARITY: Belongs to the CNOT9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07102.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D87957; BAA13508.1; -; Genomic_DNA.
DR EMBL; AK293281; BAH11481.1; -; mRNA.
DR EMBL; AC012510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70625.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70624.1; -; Genomic_DNA.
DR EMBL; BC007102; AAH07102.2; ALT_INIT; mRNA.
DR EMBL; BC137455; AAI37456.1; -; mRNA.
DR EMBL; BC137456; AAI37457.1; -; mRNA.
DR CCDS; CCDS33379.1; -. [Q92600-1]
DR CCDS; CCDS63122.1; -. [Q92600-2]
DR CCDS; CCDS63123.1; -. [Q92600-3]
DR RefSeq; NP_001258563.1; NM_001271634.1. [Q92600-2]
DR RefSeq; NP_001258564.1; NM_001271635.1. [Q92600-3]
DR RefSeq; NP_005435.1; NM_005444.2. [Q92600-1]
DR PDB; 2FV2; X-ray; 2.20 A; A/B/C/D=18-285.
DR PDB; 4CRU; X-ray; 1.65 A; B=19-285.
DR PDB; 4CRV; X-ray; 2.05 A; B=19-285.
DR PDB; 4CT6; X-ray; 2.10 A; B=18-285.
DR PDB; 4CT7; X-ray; 1.90 A; B=16-285.
DR PDB; 5LSW; X-ray; 2.15 A; A/C=19-285.
DR PDB; 5ONA; X-ray; 2.70 A; B/E=19-285.
DR PDB; 5ONB; X-ray; 3.00 A; A/C/E/G=19-285.
DR PDB; 6HOM; X-ray; 2.10 A; A/C=19-285.
DR PDB; 6HON; X-ray; 2.20 A; A/C=19-285.
DR PDBsum; 2FV2; -.
DR PDBsum; 4CRU; -.
DR PDBsum; 4CRV; -.
DR PDBsum; 4CT6; -.
DR PDBsum; 4CT7; -.
DR PDBsum; 5LSW; -.
DR PDBsum; 5ONA; -.
DR PDBsum; 5ONB; -.
DR PDBsum; 6HOM; -.
DR PDBsum; 6HON; -.
DR AlphaFoldDB; Q92600; -.
DR SMR; Q92600; -.
DR BioGRID; 114573; 228.
DR ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant.
DR ComplexPortal; CPX-2535; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant.
DR ComplexPortal; CPX-2849; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT8 variant.
DR ComplexPortal; CPX-707; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant.
DR CORUM; Q92600; -.
DR DIP; DIP-46840N; -.
DR IntAct; Q92600; 47.
DR STRING; 9606.ENSP00000273064; -.
DR ChEMBL; CHEMBL4105961; -.
DR iPTMnet; Q92600; -.
DR PhosphoSitePlus; Q92600; -.
DR BioMuta; CNOT9; -.
DR DMDM; 74716599; -.
DR EPD; Q92600; -.
DR jPOST; Q92600; -.
DR MassIVE; Q92600; -.
DR MaxQB; Q92600; -.
DR PaxDb; Q92600; -.
DR PeptideAtlas; Q92600; -.
DR PRIDE; Q92600; -.
DR ProteomicsDB; 6190; -.
DR ProteomicsDB; 6324; -.
DR ProteomicsDB; 75350; -. [Q92600-1]
DR Antibodypedia; 51420; 127 antibodies from 24 providers.
DR DNASU; 9125; -.
DR Ensembl; ENST00000273064.11; ENSP00000273064.6; ENSG00000144580.14. [Q92600-1]
DR Ensembl; ENST00000295701.9; ENSP00000295701.5; ENSG00000144580.14. [Q92600-3]
DR Ensembl; ENST00000542068.5; ENSP00000443687.1; ENSG00000144580.14. [Q92600-1]
DR Ensembl; ENST00000627282.2; ENSP00000486540.1; ENSG00000144580.14. [Q92600-2]
DR GeneID; 9125; -.
DR KEGG; hsa:9125; -.
DR MANE-Select; ENST00000273064.11; ENSP00000273064.6; NM_005444.3; NP_005435.1.
DR UCSC; uc002vih.3; human. [Q92600-1]
DR CTD; 9125; -.
DR DisGeNET; 9125; -.
DR GeneCards; CNOT9; -.
DR HGNC; HGNC:10445; CNOT9.
DR HPA; ENSG00000144580; Low tissue specificity.
DR MIM; 612054; gene.
DR neXtProt; NX_Q92600; -.
DR OpenTargets; ENSG00000144580; -.
DR PharmGKB; PA34859; -.
DR VEuPathDB; HostDB:ENSG00000144580; -.
DR eggNOG; KOG3036; Eukaryota.
DR GeneTree; ENSGT00390000001225; -.
DR HOGENOM; CLU_039962_2_0_1; -.
DR InParanoid; Q92600; -.
DR OMA; SAWMHQQ; -.
DR OrthoDB; 1129961at2759; -.
DR PhylomeDB; Q92600; -.
DR TreeFam; TF105734; -.
DR PathwayCommons; Q92600; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR SignaLink; Q92600; -.
DR SIGNOR; Q92600; -.
DR BioGRID-ORCS; 9125; 399 hits in 1082 CRISPR screens.
DR ChiTaRS; CNOT9; human.
DR EvolutionaryTrace; Q92600; -.
DR GenomeRNAi; 9125; -.
DR Pharos; Q92600; Tbio.
DR PRO; PR:Q92600; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q92600; protein.
DR Bgee; ENSG00000144580; Expressed in adrenal tissue and 196 other tissues.
DR ExpressionAtlas; Q92600; baseline and differential.
DR Genevisible; Q92600; HS.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IC:ComplexPortal.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0007548; P:sex differentiation; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007216; CNOT9.
DR PANTHER; PTHR12262:SF0; PTHR12262:SF0; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Nucleus; Reference proteome; Repressor;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..299
FT /note="CCR4-NOT transcription complex subunit 9"
FT /id="PRO_0000327224"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT VAR_SEQ 143
FT /note="I -> IVETGFHHVGQADLELPTSSDLPASASQSAGIT (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054371"
FT VAR_SEQ 245..258
FT /note="AREALRQCLPDQLK -> FSDLTFCWSSFQRK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055744"
FT VAR_SEQ 259..299
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055745"
FT VARIANT 143
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042429"
FT MUTAGEN 227
FT /note="R->E: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:17189474"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:4CRU"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4CT7"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:4CRU"
FT TURN 44..48
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4CRU"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:4CRU"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:4CRU"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 130..147
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 203..222
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4CRU"
FT TURN 261..268
FT /evidence="ECO:0007829|PDB:4CRU"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:4CRU"
SQ SEQUENCE 299 AA; 33631 MW; CFA0E108F5E9D8F2 CRC64;
MHSLATAAPV PTTLAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP DLAPMLWHSF
GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV ASHPETRSAF LAAHIPLFLY
PFLHTVSKTR PFEYLRLTSL GVIGALVKTD EQEVINFLLT TEIIPLCLRI MESGSELSKT
VATFILQKIL LDDTGLAYIC QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS
DNPRAREALR QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ
