NELFD_HUMAN
ID NELFD_HUMAN Reviewed; 590 AA.
AC Q8IXH7; B4DE06; Q9BYL2; Q9H405; Q9H888; Q9H8T3; Q9NVX5; Q9P029; Q9UGN1;
AC Q9UGN2; Q9UGN3;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Negative elongation factor C/D;
DE Short=NELF-C/D;
DE AltName: Full=TH1-like protein;
GN Name=NELFCD; Synonyms=NELFD, TH1, TH1L; ORFNames=HSPC130;
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 (ISOFORM NELF-C), AND TISSUE SPECIFICITY.
RX PubMed=11030415; DOI=10.1007/s004390000344;
RA Bonthron D.T., Hayward B.E., Moran V., Strain L.;
RT "Characterization of TH1 and CTSZ, two non-imprinted genes downstream of
RT GNAS1 in chromosome 20q13.";
RL Hum. Genet. 107:165-175(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NELF-C).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS NELF-C AND 3).
RC TISSUE=Ovarian carcinoma, Teratocarcinoma, and Thyroid;
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NELF-C).
RC TISSUE=Skin;
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 126-139; 223-230; 303-315 AND 476-491, IDENTIFICATION
RP IN A NELF COMPLEX, ALTERNATIVE INITIATION, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12612062; DOI=10.1128/mcb.23.6.1863-1873.2003;
RA Narita T., Yamaguchi Y., Yano K., Sugimoto S., Chanarat S., Wada T.,
RA Kim D.-K., Hasegawa J., Omori M., Inukai N., Endoh M., Yamada T., Handa H.;
RT "Human transcription elongation factor NELF: identification of novel
RT subunits and reconstitution of the functionally active complex.";
RL Mol. Cell. Biol. 23:1863-1873(2003).
RN [7]
RP INTERACTION WITH ARAF.
RX PubMed=11952167; DOI=10.1023/a:1014437024129;
RA Yin X.L., Chen S., Gu J.X.;
RT "Identification of TH1 as an interaction partner of A-Raf kinase.";
RL Mol. Cell. Biochem. 231:69-74(2002).
RN [8]
RP FUNCTION OF THE NELF COMPLEX.
RX PubMed=10199401; DOI=10.1016/s0092-8674(00)80713-8;
RA Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S.,
RA Hasegawa J., Handa H.;
RT "NELF, a multisubunit complex containing RD, cooperates with DSIF to
RT repress RNA polymerase II elongation.";
RL Cell 97:41-51(1999).
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 FUNCTION OF THE NELF COMPLEX IN HIV-1 LATENCY (MICROBIAL INFECTION), AND
RP INTERACTION WITH PCF11.
RX PubMed=23884411; DOI=10.1074/jbc.m113.496489;
RA Natarajan M., Schiralli Lester G.M., Lee C., Missra A., Wasserman G.A.,
RA Steffen M., Gilmour D.S., Henderson A.J.;
RT "Negative elongation factor (NELF) coordinates RNA polymerase II pausing,
RT premature termination, and chromatin remodeling to regulate HIV
RT transcription.";
RL J. Biol. Chem. 288:25995-26003(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 186-590 IN COMPLEX WITH NELFA,
RP RECONSTITUTION OF THE NELF COMPLEX, RNA BINDING, AND MUTAGENESIS OF
RP ARG-291; LYS-315; LYS-371; LYS-372; LYS-374; LYS-384; ARG-419 AND ARG-506.
RX PubMed=27282391; DOI=10.7554/elife.14981;
RA Vos S.M., Pollmann D., Caizzi L., Hofmann K.B., Rombaut P., Zimniak T.,
RA Herzog F., Cramer P.;
RT "Architecture and RNA binding of the human negative elongation factor.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Essential component of the NELF complex, a complex that
CC negatively regulates the elongation of transcription by RNA polymerase
CC II (PubMed:12612062). The NELF complex, which acts via an association
CC with the DSIF complex and causes transcriptional pausing, is
CC counteracted by the P-TEFb kinase complex (PubMed:10199401).
CC {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12612062}.
CC -!- FUNCTION: (Microbial infection) The NELF complex is involved in HIV-1
CC latency possibly involving recruitment of PCF11 to paused RNA
CC polymerase II. {ECO:0000269|PubMed:23884411}.
CC -!- SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD (isoform
CC NELF-C or isoform NELF-D) and NELFE; NELFA and NELFCD form a stable
CC subcomplex that binds primarily through NELFCD to the N-terminus of
CC NELFB (PubMed:27282391, PubMed:12612062). Binds RNA which may help to
CC stabilize the NELF complex on nucleic acid (PubMed:27282391). In vitro,
CC the NELFA:NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and
CC structure-dependent manner (PubMed:27282391). Interacts with ARAF
CC (PubMed:11952167). Interacts with PCF11 (PubMed:23884411). Interacts
CC with KAT8 (By similarity). {ECO:0000250|UniProtKB:Q922L6,
CC ECO:0000269|PubMed:11952167, ECO:0000269|PubMed:12612062,
CC ECO:0000269|PubMed:23884411, ECO:0000269|PubMed:27282391}.
CC -!- INTERACTION:
CC Q8IXH7; P10398: ARAF; NbExp=5; IntAct=EBI-536725, EBI-365961;
CC Q8IXH7; O14901: KLF11; NbExp=3; IntAct=EBI-536725, EBI-948266;
CC Q8IXH7; Q9H3P2: NELFA; NbExp=12; IntAct=EBI-536725, EBI-5461341;
CC Q8IXH7; Q8WX92-2: NELFB; NbExp=3; IntAct=EBI-536725, EBI-22734860;
CC Q8IXH7; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-536725, EBI-2811583;
CC Q8IXH7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-536725, EBI-5235340;
CC Q8IXH7; A0A1U9X8X8; NbExp=3; IntAct=EBI-536725, EBI-17234977;
CC Q8IXH7-4; Q9H3P2: NELFA; NbExp=5; IntAct=EBI-6109710, EBI-5461341;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=NELF-C;
CC IsoId=Q8IXH7-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8IXH7-3; Sequence=VSP_008950, VSP_008951;
CC Name=NELF-D;
CC IsoId=Q8IXH7-4; Sequence=VSP_018769;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung,
CC placenta, liver, skeletal and cardiac muscle, adrenal, thyroid, kidney
CC and pancreas. {ECO:0000269|PubMed:11030415,
CC ECO:0000269|PubMed:12612062}.
CC -!- MISCELLANEOUS: [Isoform NELF-D]: Produced by alternative initiation at
CC Met-10 of isoform NELF-C. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NELF-D family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29094.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91618.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB64339.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ238374; CAB64337.1; -; mRNA.
DR EMBL; AJ238375; CAB64373.1; -; mRNA.
DR EMBL; AJ238379; CAB64339.1; ALT_INIT; mRNA.
DR EMBL; AF161479; AAF29094.1; ALT_FRAME; mRNA.
DR EMBL; AK001316; BAA91618.1; ALT_INIT; mRNA.
DR EMBL; AK023310; BAB14519.1; ALT_INIT; mRNA.
DR EMBL; AK023927; BAB14729.1; -; mRNA.
DR EMBL; AK293410; BAG56917.1; -; mRNA.
DR EMBL; AL109840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014952; AAH14952.1; -; mRNA.
DR CCDS; CCDS13473.2; -. [Q8IXH7-4]
DR RefSeq; NP_945327.2; NM_198976.2. [Q8IXH7-4]
DR PDB; 5L3X; X-ray; 2.75 A; B=186-590.
DR PDB; 6GML; EM; 3.20 A; W=10-590.
DR PDB; 7PKS; EM; 3.60 A; W=1-590.
DR PDBsum; 5L3X; -.
DR PDBsum; 6GML; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q8IXH7; -.
DR SMR; Q8IXH7; -.
DR BioGRID; 119572; 100.
DR ComplexPortal; CPX-6267; NELF negative elongation factor complex.
DR CORUM; Q8IXH7; -.
DR DIP; DIP-34061N; -.
DR IntAct; Q8IXH7; 44.
DR MINT; Q8IXH7; -.
DR STRING; 9606.ENSP00000473290; -.
DR GlyGen; Q8IXH7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IXH7; -.
DR MetOSite; Q8IXH7; -.
DR PhosphoSitePlus; Q8IXH7; -.
DR BioMuta; NELFCD; -.
DR DMDM; 38372376; -.
DR EPD; Q8IXH7; -.
DR jPOST; Q8IXH7; -.
DR MassIVE; Q8IXH7; -.
DR MaxQB; Q8IXH7; -.
DR PaxDb; Q8IXH7; -.
DR PeptideAtlas; Q8IXH7; -.
DR PRIDE; Q8IXH7; -.
DR ProteomicsDB; 70993; -. [Q8IXH7-1]
DR ProteomicsDB; 70994; -. [Q8IXH7-3]
DR ProteomicsDB; 70995; -. [Q8IXH7-4]
DR Antibodypedia; 29232; 182 antibodies from 29 providers.
DR DNASU; 51497; -.
DR Ensembl; ENST00000652272.2; ENSP00000499018.1; ENSG00000101158.15. [Q8IXH7-4]
DR GeneID; 51497; -.
DR KEGG; hsa:51497; -.
DR MANE-Select; ENST00000652272.2; ENSP00000499018.1; NM_198976.4; NP_945327.3. [Q8IXH7-4]
DR UCSC; uc061ydt.1; human. [Q8IXH7-1]
DR CTD; 51497; -.
DR DisGeNET; 51497; -.
DR GeneCards; NELFCD; -.
DR HGNC; HGNC:15934; NELFCD.
DR HPA; ENSG00000101158; Low tissue specificity.
DR MIM; 605297; gene.
DR neXtProt; NX_Q8IXH7; -.
DR OpenTargets; ENSG00000101158; -.
DR PharmGKB; PA38055; -.
DR VEuPathDB; HostDB:ENSG00000101158; -.
DR eggNOG; ENOG502QPUE; Eukaryota.
DR GeneTree; ENSGT00390000001799; -.
DR InParanoid; Q8IXH7; -.
DR OrthoDB; 1288184at2759; -.
DR PhylomeDB; Q8IXH7; -.
DR TreeFam; TF324118; -.
DR PathwayCommons; Q8IXH7; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q8IXH7; -.
DR BioGRID-ORCS; 51497; 530 hits in 1087 CRISPR screens.
DR ChiTaRS; NELFCD; human.
DR GeneWiki; TH1L; -.
DR GenomeRNAi; 51497; -.
DR Pharos; Q8IXH7; Tbio.
DR PRO; PR:Q8IXH7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8IXH7; protein.
DR Bgee; ENSG00000101158; Expressed in adenohypophysis and 198 other tissues.
DR ExpressionAtlas; Q8IXH7; baseline and differential.
DR Genevisible; Q8IXH7; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032021; C:NELF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR InterPro; IPR006942; TH1.
DR PANTHER; PTHR12144; PTHR12144; 1.
DR Pfam; PF04858; TH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing;
KW Direct protein sequencing; Nucleus; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..590
FT /note="Negative elongation factor C/D"
FT /id="PRO_0000019456"
FT REGION 16..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform NELF-D)"
FT /evidence="ECO:0000305"
FT /id="VSP_018769"
FT VAR_SEQ 178..201
FT /note="LISDAGYQGEITSVSTACQQLEVF -> VGRVLELRRKVFMNVYFWLLVCFL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008950"
FT VAR_SEQ 202..590
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008951"
FT MUTAGEN 291
FT /note="R->Q: Reduces RNA binding; when associated with M-
FT 315, M-371, M-372, M-374, M-384, M-388, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 315
FT /note="K->M: Reduces RNA binding; when associated with Q-
FT 291, M-371, M-372, M-374, M-384, M-388, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 371
FT /note="K->M: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-372, M-374, M-384, M-388, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 372
FT /note="K->M: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-371, M-374, M-384, M-388, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 374
FT /note="K->M: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-371, M-372, M-384, M-388, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 384
FT /note="K->M: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-371, M-372, M-374, M-388, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 388
FT /note="K->M: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-371, M-372, M-374, M-384, Q-419 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 419
FT /note="R->Q: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-371, M-372, M-374, M-384, M-388 and Q-506."
FT /evidence="ECO:0000269|PubMed:27282391"
FT MUTAGEN 506
FT /note="R->Q: Reduces RNA binding; when associated with Q-
FT 291, M-315, M-371, M-372, M-374, M-384, M-388 and Q-419."
FT /evidence="ECO:0000269|PubMed:27282391"
FT CONFLICT 117
FT /note="N -> D (in Ref. 3; BAA91618)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="N -> S (in Ref. 3; BAB14729)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="W -> R (in Ref. 3; BAA91618)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="L -> P (in Ref. 3; BAA91618)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="D -> V (in Ref. 3; BAA91618)"
FT /evidence="ECO:0000305"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:6GML"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:5L3X"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:5L3X"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:5L3X"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 353..365
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 383..399
FT /evidence="ECO:0007829|PDB:5L3X"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 421..436
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 466..477
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 486..504
FT /evidence="ECO:0007829|PDB:5L3X"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 527..538
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 547..557
FT /evidence="ECO:0007829|PDB:5L3X"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5L3X"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:6GML"
FT HELIX 574..585
FT /evidence="ECO:0007829|PDB:5L3X"
SQ SEQUENCE 590 AA; 66247 MW; 425437DC46DAF953 CRC64;
MAGAVPGAIM DEDYYGSAAE WGDEADGGQQ EDDSGEGEDD AEVQQECLHK FSTRDYIMEP
SIFNTLKRYF QAGGSPENVI QLLSENYTAV AQTVNLLAEW LIQTGVEPVQ VQETVENHLK
SLLIKHFDPR KADSIFTEEG ETPAWLEQMI AHTTWRDLFY KLAEAHPDCL MLNFTVKLIS
DAGYQGEITS VSTACQQLEV FSRVLRTSLA TILDGGEENL EKNLPEFAKM VCHGEHTYLF
AQAMMSVLAQ EEQGGSAVRR IAQEVQRFAQ EKGHDASQIT LALGTAASYP RACQALGAML
SKGALNPADI TVLFKMFTSM DPPPVELIRV PAFLDLFMQS LFKPGARINQ DHKHKYIHIL
AYAASVVETW KKNKRVSINK DELKSTSKAV ETVHNLCCNE NKGASELVAE LSTLYQCIRF
PVVAMGVLKW VDWTVSEPRY FQLQTDHTPV HLALLDEIST CHQLLHPQVL QLLVKLFETE
HSQLDVMEQL ELKKTLLDRM VHLLSRGYVL PVVSYIRKCL EKLDTDISLI RYFVTEVLDV
IAPPYTSDFV QLFLPILEND SIAGTIKTEG EHDPVTEFIA HCKSNFIMVN
