DHX34_HUMAN
ID DHX34_HUMAN Reviewed; 1143 AA.
AC Q14147; B4DMY8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Probable ATP-dependent RNA helicase DHX34 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 34 {ECO:0000312|HGNC:HGNC:16719};
DE AltName: Full=DExH-box helicase 34 {ECO:0000312|HGNC:HGNC:16719};
GN Name=DHX34 {ECO:0000312|HGNC:HGNC:16719};
GN Synonyms=DDX34 {ECO:0000312|HGNC:HGNC:16719}, KIAA0134;
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].
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-1143.
RC TISSUE=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-749 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-749 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-749 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP FUNCTION, INTERACTION WITH UPF1; MOV10; EIF4A3; XRN2; SMG1; SMG6; SMG7;
RP SMG9; UPF3A; UPF3B; CASC3; XRN1; DIS3; DCP1A AND NCBP1, AND MUTAGENESIS OF
RP LYS-191 AND ASP-279.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-749 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH UPF1 AND SMG1, INTERACTION WITH UPF1 AND
RP SMG1, AND MUTAGENESIS OF ASP-279.
RX PubMed=26841701; DOI=10.1038/ncomms10585;
RA Melero R., Hug N., Lopez-Perrote A., Yamashita A., Caceres J.F., Llorca O.;
RT "The RNA helicase DHX34 functions as a scaffold for SMG1-mediated UPF1
RT phosphorylation.";
RL Nat. Commun. 7:10585-10585(2016).
RN [11]
RP FUNCTION, INTERACTION WITH RUVBL1 AND RUVBL2, AND MUTAGENESIS OF ASP-279.
RX PubMed=33205750; DOI=10.7554/elife.63042;
RA Lopez-Perrote A., Hug N., Gonzalez-Corpas A., Rodriguez C.F., Serna M.,
RA Garcia-Martin C., Boskovic J., Fernandez-Leiro R., Caceres J.F., Llorca O.;
RT "Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA
RT decay factor DHX34, as evidenced by Cryo-EM.";
RL Elife 9:0-0(2020).
RN [12]
RP VARIANTS 156-GLN--VAL-1143 DEL; SER-441 AND PRO-776, AND TISSUE
RP SPECIFICITY.
RX PubMed=31256877; DOI=10.1016/j.ajhg.2019.06.001;
RG University of Washington Center for Mendelian Genomics, Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed Diseases Program;
RA Paine I., Posey J.E., Grochowski C.M., Jhangiani S.N., Rosenheck S.,
RA Kleyner R., Marmorale T., Yoon M., Wang K., Robison R., Cappuccio G.,
RA Pinelli M., Magli A., Coban Akdemir Z., Hui J., Yeung W.L., Wong B.K.Y.,
RA Ortega L., Bekheirnia M.R., Bierhals T., Hempel M., Johannsen J.,
RA Santer R., Aktas D., Alikasifoglu M., Bozdogan S., Aydin H., Karaca E.,
RA Bayram Y., Ityel H., Dorschner M., White J.J., Wilichowski E.,
RA Wortmann S.B., Casella E.B., Kitajima J.P., Kok F., Monteiro F.,
RA Muzny D.M., Bamshad M., Gibbs R.A., Sutton V.R., Van Esch H.,
RA Brunetti-Pierri N., Hildebrandt F., Brautbar A., Van den Veyver I.B.,
RA Glass I., Lessel D., Lyon G.J., Lupski J.R.;
RT "Paralog studies augment gene discovery: DDX and DHX genes.";
RL Am. J. Hum. Genet. 105:302-316(2019).
CC -!- FUNCTION: Probable ATP-binding RNA helicase required for nonsense-
CC mediated decay (NMD) degradation of mRNA transcripts containing
CC premature stop codons (PubMed:25220460, PubMed:33205750). Promotes the
CC phosphorylation of UPF1 along with its interaction with key NMD pathway
CC proteins UPF2 and EIF4A3 (PubMed:25220460). Interaction with the
CC RUVBL1-RUVBL2 complex results in loss of nucleotide binding ability and
CC ATP hydrolysis of the complex (PubMed:33205750). Negatively regulates
CC the nucleotide binding ability and ATP hydrolysis of the RUVBL1-RUVBL2
CC complex via induction of N-terminus conformation changes of the RUVBL2
CC subunits (PubMed:33205750). {ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:33205750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Forms a complex with RUVBL1 and RUVBL2 (PubMed:33205750). Part
CC of a complex composed of SMG1, DHX34 and UPF1; within the complex DHX34
CC acts as a scaffolding protein to facilitate SMG1 phosphorylation of
CC UPF1 (PubMed:26841701). Interacts with UPF1, MOV10, EIF4A3, XRN2, SMG6,
CC SMG7, SMG9, UPF3A, UPF3B, CASC3/MLN51, XRN1, DIS3 and DCP1A; the
CC interactions are RNA-independent (PubMed:25220460). Interacts with
CC NCBP1/CPB80; the interaction is RNA-dependent (PubMed:25220460).
CC Interacts (via C-terminus) with SMG1; the interaction is RNA-
CC independent (PubMed:25220460, PubMed:26841701).
CC {ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:26841701,
CC ECO:0000269|PubMed:33205750}.
CC -!- TISSUE SPECIFICITY: Expressed in whole blood, testis and spleen. Also
CC expressed in the brain. {ECO:0000269|PubMed:31256877}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09483.2; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAG60050.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50924; BAA09483.2; ALT_SEQ; mRNA.
DR EMBL; AC008754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK297692; BAG60050.1; ALT_INIT; mRNA.
DR CCDS; CCDS12700.1; -.
DR RefSeq; NP_055496.2; NM_014681.5.
DR RefSeq; XP_005259500.1; XM_005259443.3.
DR RefSeq; XP_011525852.1; XM_011527550.2.
DR RefSeq; XP_011525853.1; XM_011527551.2.
DR RefSeq; XP_016883013.1; XM_017027524.1.
DR AlphaFoldDB; Q14147; -.
DR SMR; Q14147; -.
DR BioGRID; 115056; 28.
DR IntAct; Q14147; 15.
DR MINT; Q14147; -.
DR STRING; 9606.ENSP00000331907; -.
DR iPTMnet; Q14147; -.
DR PhosphoSitePlus; Q14147; -.
DR BioMuta; DHX34; -.
DR DMDM; 311033371; -.
DR EPD; Q14147; -.
DR jPOST; Q14147; -.
DR MassIVE; Q14147; -.
DR MaxQB; Q14147; -.
DR PaxDb; Q14147; -.
DR PeptideAtlas; Q14147; -.
DR PRIDE; Q14147; -.
DR ProteomicsDB; 59851; -.
DR Antibodypedia; 31552; 82 antibodies from 16 providers.
DR DNASU; 9704; -.
DR Ensembl; ENST00000328771.9; ENSP00000331907.4; ENSG00000134815.19.
DR GeneID; 9704; -.
DR KEGG; hsa:9704; -.
DR MANE-Select; ENST00000328771.9; ENSP00000331907.4; NM_014681.6; NP_055496.2.
DR UCSC; uc010xyn.2; human.
DR CTD; 9704; -.
DR DisGeNET; 9704; -.
DR GeneCards; DHX34; -.
DR HGNC; HGNC:16719; DHX34.
DR HPA; ENSG00000134815; Low tissue specificity.
DR MIM; 615475; gene.
DR neXtProt; NX_Q14147; -.
DR OpenTargets; ENSG00000134815; -.
DR PharmGKB; PA27221; -.
DR VEuPathDB; HostDB:ENSG00000134815; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000158721; -.
DR HOGENOM; CLU_001832_5_2_1; -.
DR InParanoid; Q14147; -.
DR OMA; IVCDGWL; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q14147; -.
DR TreeFam; TF313217; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q14147; -.
DR SignaLink; Q14147; -.
DR BioGRID-ORCS; 9704; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; DHX34; human.
DR GenomeRNAi; 9704; -.
DR Pharos; Q14147; Tbio.
DR PRO; PR:Q14147; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q14147; protein.
DR Bgee; ENSG00000134815; Expressed in right testis and 146 other tissues.
DR ExpressionAtlas; Q14147; baseline and differential.
DR Genevisible; Q14147; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1143
FT /note="Probable ATP-dependent RNA helicase DHX34"
FT /id="PRO_0000055166"
FT DOMAIN 172..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 368..536
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..955
FT /note="Negatively regulates interaction with UPF1"
FT /evidence="ECO:0000269|PubMed:26841701"
FT REGION 724..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..1143
FT /note="Required for phosphorylation of UPF1. Not required
FT for interaction with UPF1"
FT /evidence="ECO:0000269|PubMed:26841701"
FT REGION 957..1143
FT /note="Required for the interaction with SMG1 and
FT subsequent phosphorylation of UPF1"
FT /evidence="ECO:0000269|PubMed:26841701"
FT MOTIF 279..282
FT /note="DEAH box"
FT COMPBIAS 724..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 17
FT /note="R -> W (in dbSNP:rs12984558)"
FT /id="VAR_057241"
FT VARIANT 117
FT /note="G -> D (in dbSNP:rs8113564)"
FT /id="VAR_057242"
FT VARIANT 156..1143
FT /note="Missing (found in a patient with a
FT neurodevelopmental disorder; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083625"
FT VARIANT 441
FT /note="N -> S (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs549149043)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083626"
FT VARIANT 776
FT /note="R -> P (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs764483792)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083627"
FT MUTAGEN 191
FT /note="K->S: Results in interaction with ETF1/eRF1,
FT GSPT1/eRF3a and GSPT2/eRF3b. Reduces UPF1 phosphorylation.
FT No effect on mRNA binding or interaction with SMG1."
FT /evidence="ECO:0000269|PubMed:25220460"
FT MUTAGEN 279
FT /note="D->A: Results in interaction with ETF1/eRF1,
FT GSPT1/eRF3a and GSPT2/eRF3b. Increases mRNA binding.
FT Reduces UPF1 phosphorylation. Reduces ATPase activity. No
FT effect on interaction with SMG1."
FT /evidence="ECO:0000269|PubMed:25220460,
FT ECO:0000269|PubMed:26841701, ECO:0000269|PubMed:33205750"
SQ SEQUENCE 1143 AA; 128120 MW; 4081CAC2D9B4B840 CRC64;
MPPPRTREGR DRRDHHRAPS EEEALEKWDW NCPETRRLLE DAFFREEDYI RQGSEECQKF
WTFFERLQRF QNLKTSRKEE KDPGQPKHSI PALADLPRTY DPRYRINLSV LGPATRGSQG
LGRHLPAERV AEFRRALLHY LDFGQKQAFG RLAKLQRERA ALPIAQYGNR ILQTLKEHQV
VVVAGDTGCG KSTQVPQYLL AAGFSHVACT QPRRIACISL AKRVGFESLS QYGSQVGYQI
RFESTRSAAT KIVFLTVGLL LRQIQREPSL PQYEVLIVDE VHERHLHNDF LLGVLQRLLP
TRPDLKVILM SATINISLFS SYFSNAPVVQ VPGRLFPITV VYQPQEAEPT TSKSEKLDPR
PFLRVLESID HKYPPEERGD LLVFLSGMAE ISAVLEAAQT YASHTQRWVV LPLHSALSVA
DQDKVFDVAP PGVRKCILST NIAETSVTID GIRFVVDSGK VKEMSYDPQA KLQRLQEFWI
SQASAEQRKG RAGRTGPGVC FRLYAESDYD AFAPYPVPEI RRVALDSLVL QMKSMSVGDP
RTFPFIEPPP PASLETAILY LRDQGALDSS EALTPIGSLL AQLPVDVVIG KMLILGSMFS
LVEPVLTIAA ALSVQSPFTR SAQSSPECAA ARRPLESDQG DPFTLFNVFN AWVQVKSERS
RNSRKWCRRR GIEEHRLYEM ANLRRQFKEL LEDHGLLAGA QAAQVGDSYS RLQQRRERRA
LHQLKRQHEE GAGRRRKVLR LQEEQDGGSS DEDRAGPAPP GASDGVDIQD VKFKLRHDLA
QLQAAASSAQ DLSREQLALL KLVLGRGLYP QLAVPDAFNS SRKDSDQIFH TQAKQGAVLH
PTCVFAGSPE VLHAQELEAS NCDGSRDDKD KMSSKHQLLS FVSLLETNKP YLVNCVRIPA
LQSLLLFSRS LDTNGDCSRL VADGWLELQL ADSESAIRLL AASLRLRARW ESALDRQLAH
QAQQQLEEEE EDTPVSPKEV ATLSKELLQF TASKIPYSLR RLTGLEVQNM YVGPQTIPAT
PHLPGLFGSS TLSPHPTKGG YAVTDFLTYN CLTNDTDLYS DCLRTFWTCP HCGLHAPLTP
LERIAHENTC PQAPQDGPPG AEEAALETLQ KTSVLQRPYH CEACGKDFLF TPTEVLRHRK
QHV
