RPB7_HUMAN
ID RPB7_HUMAN Reviewed; 172 AA.
AC P62487; B2R5C0; P52433; Q2M1Z4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB7;
DE Short=RNA polymerase II subunit B7;
DE AltName: Full=DNA-directed RNA polymerase II subunit G;
DE AltName: Full=RNA polymerase II 19 kDa subunit;
DE Short=RPB19;
GN Name=POLR2G; Synonyms=RPB7;
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].
RX PubMed=7579693; DOI=10.1091/mbc.6.7.759;
RA Khazak V., Sadhale P.P., Woychik N.A., Brent R., Golemis E.A.;
RT "Human RNA polymerase II subunit hsRPB7 functions in yeast and influences
RT stress survival and cell morphology.";
RL Mol. Biol. Cell 6:759-775(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9256063; DOI=10.1016/s0167-4781(97)00041-9;
RA Schoen T.J., Chandrasekharappa S.C., Guru S.C., Mazuruk K., Chader G.J.,
RA Rodriguez I.R.;
RT "Human gene for the RNA polymerase II seventh subunit (hsRPB7): structure,
RT expression and chromosomal localization.";
RL Biochim. Biophys. Acta 1353:39-49(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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].
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].
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 FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines that
RT conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF THE POL II RPB4-RPB7 SUBCOMPLEX,
RP RNA-BINDING, AND MUTAGENESIS OF HIS-14; GLU-33; LYS-41; THR-90; ASN-93;
RP LYS-94; PHE-107; SER-109; HIS-111; ARG-151; ASP-153 AND PHE-158.
RX PubMed=16282592; DOI=10.1093/nar/gki945;
RA Meka H., Werner F., Cordell S.C., Onesti S., Brick P.;
RT "Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA
RT polymerase II.";
RL Nucleic Acids Res. 33:6435-6444(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB7 is part of a
CC subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and
CC RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems
CC to lock the clamp via RPB7 in the closed conformation thus preventing
CC double-stranded DNA to enter the active site cleft. The RPB4-RPB7
CC subcomplex binds single-stranded DNA and RNA (By similarity). Binds
CC RNA. {ECO:0000250, ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the
CC 10-subunit Pol II core complex. {ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC P62487; Q5TBC7: BCL2L15; NbExp=3; IntAct=EBI-347928, EBI-10247136;
CC P62487; Q8WYQ4-2: C22orf15; NbExp=3; IntAct=EBI-347928, EBI-12030460;
CC P62487; Q96Q77: CIB3; NbExp=3; IntAct=EBI-347928, EBI-10292696;
CC P62487; Q9UHC6: CNTNAP2; NbExp=3; IntAct=EBI-347928, EBI-310892;
CC P62487; P17661: DES; NbExp=3; IntAct=EBI-347928, EBI-1055572;
CC P62487; Q68J44: DUSP29; NbExp=3; IntAct=EBI-347928, EBI-1054321;
CC P62487; O15371: EIF3D; NbExp=3; IntAct=EBI-347928, EBI-353818;
CC P62487; P38919: EIF4A3; NbExp=3; IntAct=EBI-347928, EBI-299104;
CC P62487; P15408: FOSL2; NbExp=3; IntAct=EBI-347928, EBI-3893419;
CC P62487; Q92917: GPKOW; NbExp=3; IntAct=EBI-347928, EBI-746309;
CC P62487; Q00444: HOXC5; NbExp=4; IntAct=EBI-347928, EBI-11955357;
CC P62487; P33176: KIF5B; NbExp=3; IntAct=EBI-347928, EBI-355878;
CC P62487; P25791-3: LMO2; NbExp=4; IntAct=EBI-347928, EBI-11959475;
CC P62487; P28482: MAPK1; NbExp=3; IntAct=EBI-347928, EBI-959949;
CC P62487; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-347928, EBI-9057006;
CC P62487; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-347928, EBI-3921217;
CC P62487; O15160: POLR1C; NbExp=3; IntAct=EBI-347928, EBI-1055079;
CC P62487; P28062-2: PSMB8; NbExp=3; IntAct=EBI-347928, EBI-372312;
CC P62487; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-347928, EBI-11119202;
CC P62487; Q6AZZ1: TRIM68; NbExp=3; IntAct=EBI-347928, EBI-2130449;
CC P62487; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-347928, EBI-372432;
CC P62487; Q96BW1: UPRT; NbExp=3; IntAct=EBI-347928, EBI-742943;
CC P62487; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-347928, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; U20659; AAA86500.1; -; mRNA.
DR EMBL; U52427; AAB96827.1; -; Genomic_DNA.
DR EMBL; AK312131; BAG35067.1; -; mRNA.
DR EMBL; CH471076; EAW74092.1; -; Genomic_DNA.
DR EMBL; BC112162; AAI12163.1; -; mRNA.
DR EMBL; BC112164; AAI12165.1; -; mRNA.
DR CCDS; CCDS31585.1; -.
DR RefSeq; NP_002687.1; NM_002696.2.
DR PDB; 2C35; X-ray; 2.70 A; B/D/F/H=1-172.
DR PDB; 5IY6; EM; 7.20 A; G=1-172.
DR PDB; 5IY7; EM; 8.60 A; G=1-172.
DR PDB; 5IY8; EM; 7.90 A; G=1-172.
DR PDB; 5IY9; EM; 6.30 A; G=1-172.
DR PDB; 5IYA; EM; 5.40 A; G=1-172.
DR PDB; 5IYB; EM; 3.90 A; G=1-172.
DR PDB; 5IYC; EM; 3.90 A; G=1-172.
DR PDB; 5IYD; EM; 3.90 A; G=1-172.
DR PDB; 6DRD; EM; 3.90 A; G=1-172.
DR PDB; 6O9L; EM; 7.20 A; G=1-172.
DR PDB; 6XRE; EM; 4.60 A; G=1-172.
DR PDB; 7LBM; EM; 4.80 A; G=1-172.
DR PDBsum; 2C35; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 6DRD; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6XRE; -.
DR PDBsum; 7LBM; -.
DR AlphaFoldDB; P62487; -.
DR SMR; P62487; -.
DR BioGRID; 111432; 169.
DR CORUM; P62487; -.
DR DIP; DIP-32663N; -.
DR IntAct; P62487; 106.
DR MINT; P62487; -.
DR STRING; 9606.ENSP00000301788; -.
DR iPTMnet; P62487; -.
DR MetOSite; P62487; -.
DR PhosphoSitePlus; P62487; -.
DR BioMuta; POLR2G; -.
DR DMDM; 50403601; -.
DR EPD; P62487; -.
DR jPOST; P62487; -.
DR MassIVE; P62487; -.
DR MaxQB; P62487; -.
DR PaxDb; P62487; -.
DR PeptideAtlas; P62487; -.
DR PRIDE; P62487; -.
DR ProteomicsDB; 57401; -.
DR Antibodypedia; 14963; 226 antibodies from 32 providers.
DR DNASU; 5436; -.
DR Ensembl; ENST00000301788.12; ENSP00000301788.7; ENSG00000168002.12.
DR GeneID; 5436; -.
DR KEGG; hsa:5436; -.
DR MANE-Select; ENST00000301788.12; ENSP00000301788.7; NM_002696.3; NP_002687.1.
DR UCSC; uc001nva.4; human.
DR CTD; 5436; -.
DR DisGeNET; 5436; -.
DR GeneCards; POLR2G; -.
DR HGNC; HGNC:9194; POLR2G.
DR HPA; ENSG00000168002; Low tissue specificity.
DR MIM; 602013; gene.
DR neXtProt; NX_P62487; -.
DR OpenTargets; ENSG00000168002; -.
DR PharmGKB; PA33514; -.
DR VEuPathDB; HostDB:ENSG00000168002; -.
DR eggNOG; KOG3298; Eukaryota.
DR GeneTree; ENSGT00390000008975; -.
DR HOGENOM; CLU_085878_2_0_1; -.
DR InParanoid; P62487; -.
DR OMA; MRQPGLG; -.
DR OrthoDB; 1140388at2759; -.
DR PhylomeDB; P62487; -.
DR TreeFam; TF103042; -.
DR PathwayCommons; P62487; -.
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-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
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-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR SignaLink; P62487; -.
DR SIGNOR; P62487; -.
DR BioGRID-ORCS; 5436; 772 hits in 1086 CRISPR screens.
DR ChiTaRS; POLR2G; human.
DR EvolutionaryTrace; P62487; -.
DR GeneWiki; POLR2G; -.
DR GenomeRNAi; 5436; -.
DR Pharos; P62487; Tbio.
DR PRO; PR:P62487; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P62487; protein.
DR Bgee; ENSG00000168002; Expressed in ventricular zone and 203 other tissues.
DR ExpressionAtlas; P62487; baseline and differential.
DR Genevisible; P62487; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; IBA:GO_Central.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW RNA-binding; Transcription.
FT CHAIN 1..172
FT /note="DNA-directed RNA polymerase II subunit RPB7"
FT /id="PRO_0000073986"
FT MUTAGEN 14
FT /note="H->E: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 33
FT /note="E->K: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 41
FT /note="K->E: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 90
FT /note="T->A: Reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 93
FT /note="N->A: Reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 94
FT /note="K->E: Reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 107
FT /note="F->E: Reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 109
FT /note="S->A: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 111
FT /note="H->E: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 151
FT /note="R->E: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 153
FT /note="D->E: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT MUTAGEN 158
FT /note="F->A: Strongly reduces RNA-binding."
FT /evidence="ECO:0000269|PubMed:16282592"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:2C35"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2C35"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:2C35"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 64..77
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2C35"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:2C35"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2C35"
SQ SEQUENCE 172 AA; 19294 MW; AF3CE655F658CD5C CRC64;
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ
PGRGFVLYPV KYKAIVFRPF KGEVVDAVVT QVNKVGLFTE IGPMSCFISR HSIPSEMEFD
PNSNPPCYKT MDEDIVIQQD DEIRLKIVGT RVDKNDIFAI GSLMDDYLGL VS
