ID ERF3A_HUMAN Reviewed; 499 AA.
AC P15170; J3KQG6; Q96GF2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 27-MAR-2024, entry version 211.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit ERF3A;
DE Short=Eukaryotic peptide chain release factor subunit 3a;
DE Short=eRF3a;
DE EC=3.6.5.- {ECO:0000269|PubMed:16777602, ECO:0000305|PubMed:15987998};
DE AltName: Full=G1 to S phase transition protein 1 homolog;
GN Name=GSPT1; Synonyms=ERF3A;
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).
RX PubMed=2511002; DOI=10.1002/j.1460-2075.1989.tb08558.x;
RA Hoshino S., Miyazawa H., Enomoto T., Hanaoka F., Kikuchi Y., Kikuchi A.,
RA Ui M.;
RT "A human homologue of the yeast GST1 gene codes for a GTP-binding protein
RT and is expressed in a proliferation-dependent manner in mammalian cells.";
RL EMBO J. 8:3807-3814(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15987998; DOI=10.1128/mcb.25.14.5801-5811.2005;
RA Chauvin C., Salhi S., Le Goff C., Viranaicken W., Diop D., Jean-Jean O.;
RT "Involvement of human release factors eRF3a and eRF3b in translation
RT termination and regulation of the termination complex formation.";
RL Mol. Cell. Biol. 25:5801-5811(2005).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16777602; DOI=10.1016/j.cell.2006.04.035;
RA Alkalaeva E.Z., Pisarev A.V., Frolova L.Y., Kisselev L.L., Pestova T.V.;
RT "In vitro reconstitution of eukaryotic translation reveals cooperativity
RT between release factors eRF1 and eRF3.";
RL Cell 125:1125-1136(2006).
RN [7]
RP IDENTIFICATION IN THE SURF COMPLEX, AND FUNCTION.
RX PubMed=19417104; DOI=10.1101/gad.1767209;
RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y.,
RA Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H.,
RA Anderson P., Ohno S.;
RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
RT remodeling of the mRNA surveillance complex during nonsense-mediated mRNA
RT decay.";
RL Genes Dev. 23:1091-1105(2009).
RN [8]
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 [9]
RP INTERACTION WITH JMJD4.
RX PubMed=24486019; DOI=10.1016/j.molcel.2013.12.028;
RA Feng T., Yamamoto A., Wilkins S.E., Sokolova E., Yates L.A., Muenzel M.,
RA Singh P., Hopkinson R.J., Fischer R., Cockman M.E., Shelley J.,
RA Trudgian D.C., Schoedel J., McCullagh J.S., Ge W., Kessler B.M.,
RA Gilbert R.J., Frolova L.Y., Alkalaeva E., Ratcliffe P.J., Schofield C.J.,
RA Coleman M.L.;
RT "Optimal translational termination requires C4 lysyl hydroxylation of
RT eRF1.";
RL Mol. Cell 53:645-654(2014).
RN [10]
RP FUNCTION, AND INTERACTION WITH SHFL.
RX PubMed=30682371; DOI=10.1016/j.cell.2018.12.030;
RA Wang X., Xuan Y., Han Y., Ding X., Ye K., Yang F., Gao P., Goff S.P.,
RA Gao G.;
RT "Regulation of HIV-1 Gag-Pol Expression by Shiftless, an Inhibitor of
RT Programmed -1 Ribosomal Frameshifting.";
RL Cell 176:625.E14-635.E14(2019).
RN [11] {ECO:0007744|PDB:3E1Y}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 301-499 IN CCOMPLEX WITH ETF1,
RP FUNCTION, AND IDENTIFICATION IN THE ERF1-ERF3-GTP TERNARY COMPLEX.
RX PubMed=19417105; DOI=10.1101/gad.1770109;
RA Cheng Z., Saito K., Pisarev A.V., Wada M., Pisareva V.P., Pestova T.V.,
RA Gajda M., Round A., Kong C., Lim M., Nakamura Y., Svergun D.I., Ito K.,
RA Song H.;
RT "Structural insights into eRF3 and stop codon recognition by eRF1.";
RL Genes Dev. 23:1106-1118(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 73-87 (ISOFORM 2).
RX PubMed=20418951; DOI=10.1371/journal.pone.0010169;
RA Kozlov G., Gehring K.;
RT "Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding
RT protein.";
RL PLoS ONE 5:E10169-E10169(2010).
RN [13] {ECO:0007744|PDB:5LZT}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.65 ANGSTROMS) IN COMPLEX WITH ETF1/ERF1
RP AND RIBOSOME, FUNCTION, AND IDENTIFICATION IN THE ERF1-ERF3-GTP TERNARY
RP COMPLEX.
RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046;
RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.;
RT "Decoding mammalian ribosome-mRNA states by translational GTPase
RT complexes.";
RL Cell 167:1229-1240(2016).
CC -!- FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a
CC ternary complex that mediates translation termination in response to
CC the termination codons UAA, UAG and UGA (PubMed:2511002,
CC PubMed:15987998, PubMed:19417105, PubMed:27863242). GSPT1/ERF3A
CC mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex
CC binds to a stop codon in the ribosomal A-site (PubMed:27863242). GTP
CC hydrolysis by GSPT1/ERF3A induces a conformational change that leads to
CC its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-
CC site (PubMed:16777602, PubMed:27863242). Component of the transient
CC SURF complex which recruits UPF1 to stalled ribosomes in the context of
CC nonsense-mediated decay (NMD) of mRNAs containing premature stop codons
CC (PubMed:24486019). Required for SHFL-mediated translation termination
CC which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from
CC viruses and cellular genes (PubMed:30682371).
CC {ECO:0000269|PubMed:15987998, ECO:0000269|PubMed:16777602,
CC ECO:0000269|PubMed:19417105, ECO:0000269|PubMed:24486019,
CC ECO:0000269|PubMed:2511002, ECO:0000269|PubMed:27863242,
CC ECO:0000269|PubMed:30682371}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:16777602, ECO:0000305|PubMed:15987998};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:15987998};
CC -!- SUBUNIT: Component of the eRF1-eRF3-GTP ternary complex, composed of
CC ETF1/ERF1 and ERF3 (GSPT1/ERF3A or GSPT2/ERF3B) and GTP
CC (PubMed:19417105, PubMed:27863242). Component of the transient SURF
CC (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). The ETF1-GSPT1 complex
CC interacts with JMJD4 (PubMed:24486019). Interacts with PABPC1 (By
CC similarity). Interacts with SHFL (PubMed:30682371).
CC {ECO:0000250|UniProtKB:Q8R050, ECO:0000269|PubMed:19417104,
CC ECO:0000269|PubMed:19417105, ECO:0000269|PubMed:24486019,
CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30682371}.
CC -!- INTERACTION:
CC P15170; P62495: ETF1; NbExp=4; IntAct=EBI-948993, EBI-750990;
CC P15170; Q92900: UPF1; NbExp=2; IntAct=EBI-948993, EBI-373471;
CC P15170-2; P11940: PABPC1; NbExp=2; IntAct=EBI-9094806, EBI-81531;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P15170-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15170-2; Sequence=VSP_042198, VSP_042199;
CC Name=3;
CC IsoId=P15170-3; Sequence=VSP_042198;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. ERF3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- CAUTION: eRF3 antibodies used in PubMed:19417104 do not differentiate
CC between GSPT1/ERF3A and GSPT2/ERF3B. {ECO:0000305}.
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DR EMBL; X17644; CAA35635.1; -; mRNA.
DR EMBL; U95742; AAB67250.1; -; Genomic_DNA.
DR EMBL; AC007216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009503; AAH09503.2; -; mRNA.
DR CCDS; CCDS45412.1; -. [P15170-3]
DR CCDS; CCDS45413.1; -. [P15170-2]
DR CCDS; CCDS45414.1; -. [P15170-1]
DR PIR; S06941; S06941.
DR RefSeq; NP_001123478.1; NM_001130006.1. [P15170-2]
DR RefSeq; NP_001123479.1; NM_001130007.1. [P15170-1]
DR PDB; 3E1Y; X-ray; 3.80 A; E/F/G/H=301-499.
DR PDB; 3J5Y; EM; 9.70 A; B=69-496.
DR PDB; 3KUI; X-ray; 2.30 A; B=64-78.
DR PDB; 4D61; EM; 9.00 A; i=72-497.
DR PDB; 5HXB; X-ray; 3.60 A; A/X=300-496.
DR PDB; 5LZT; EM; 3.65 A; jj=1-499.
DR PDB; 6XK9; X-ray; 3.64 A; A/X=300-496.
DR PDBsum; 3E1Y; -.
DR PDBsum; 3J5Y; -.
DR PDBsum; 3KUI; -.
DR PDBsum; 4D61; -.
DR PDBsum; 5HXB; -.
DR PDBsum; 5LZT; -.
DR PDBsum; 6XK9; -.
DR AlphaFoldDB; P15170; -.
DR EMDB; EMD-4131; -.
DR EMDB; EMD-5801; -.
DR SMR; P15170; -.
DR BioGRID; 109190; 298.
DR ComplexPortal; CPX-2721; Translation release factor ERF1-ERF3 complex.
DR CORUM; P15170; -.
DR IntAct; P15170; 27.
DR MINT; P15170; -.
DR STRING; 9606.ENSP00000398131; -.
DR BindingDB; P15170; -.
DR ChEMBL; CHEMBL4523593; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR GlyGen; P15170; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P15170; -.
DR MetOSite; P15170; -.
DR PhosphoSitePlus; P15170; -.
DR SwissPalm; P15170; -.
DR BioMuta; GSPT1; -.
DR DMDM; 121688; -.
DR EPD; P15170; -.
DR jPOST; P15170; -.
DR MassIVE; P15170; -.
DR MaxQB; P15170; -.
DR PaxDb; 9606-ENSP00000398131; -.
DR PeptideAtlas; P15170; -.
DR ProteomicsDB; 53116; -. [P15170-1]
DR ProteomicsDB; 53117; -. [P15170-2]
DR Pumba; P15170; -.
DR Antibodypedia; 24757; 200 antibodies from 30 providers.
DR DNASU; 2935; -.
DR Ensembl; ENST00000420576.6; ENSP00000399539.2; ENSG00000103342.13. [P15170-1]
DR Ensembl; ENST00000434724.7; ENSP00000398131.2; ENSG00000103342.13. [P15170-3]
DR Ensembl; ENST00000439887.6; ENSP00000408399.2; ENSG00000103342.13. [P15170-2]
DR Ensembl; ENST00000563468.5; ENSP00000454351.1; ENSG00000103342.13. [P15170-1]
DR GeneID; 2935; -.
DR KEGG; hsa:2935; -.
DR MANE-Select; ENST00000434724.7; ENSP00000398131.2; NM_002094.4; NP_002085.3. [P15170-3]
DR UCSC; uc002dbt.4; human. [P15170-1]
DR AGR; HGNC:4621; -.
DR CTD; 2935; -.
DR DisGeNET; 2935; -.
DR GeneCards; GSPT1; -.
DR HGNC; HGNC:4621; GSPT1.
DR HPA; ENSG00000103342; Low tissue specificity.
DR MIM; 139259; gene.
DR neXtProt; NX_P15170; -.
DR OpenTargets; ENSG00000103342; -.
DR PharmGKB; PA29012; -.
DR VEuPathDB; HostDB:ENSG00000103342; -.
DR eggNOG; KOG0459; Eukaryota.
DR GeneTree; ENSGT00940000155582; -.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; P15170; -.
DR OMA; GKMESGC; -.
DR OrthoDB; 5477300at2759; -.
DR PhylomeDB; P15170; -.
DR TreeFam; TF300566; -.
DR PathwayCommons; P15170; -.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P15170; -.
DR SIGNOR; P15170; -.
DR BioGRID-ORCS; 2935; 786 hits in 1166 CRISPR screens.
DR ChiTaRS; GSPT1; human.
DR EvolutionaryTrace; P15170; -.
DR GeneWiki; GSPT1; -.
DR GenomeRNAi; 2935; -.
DR Pharos; P15170; Tbio.
DR PRO; PR:P15170; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P15170; Protein.
DR Bgee; ENSG00000103342; Expressed in gingival epithelium and 209 other cell types or tissues.
DR ExpressionAtlas; P15170; baseline and differential.
DR Genevisible; P15170; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt.
DR GO; GO:0018444; C:translation release factor complex; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003747; F:translation release factor activity; IDA:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:MGI.
DR GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; IDA:UniProtKB.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03704; eRF3_C_III; 1.
DR CDD; cd04089; eRF3_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR23115:SF125; EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR GTP-BINDING SUBUNIT ERF3A; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTP-binding; Hydrolase;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..499
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit ERF3A"
FT /id="PRO_0000091480"
FT DOMAIN 72..298
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..88
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 137..141
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 158..161
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 220..223
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 262..264
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O74718"
FT BINDING 220..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O74718"
FT BINDING 262..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O74718"
FT VAR_SEQ 1
FT /note="M -> MDPGSGGGGGGGGGGGSSSGSSSSDSAPDCWDQADMEAPGPGPCGGG
FT GSLAAAAEAQRENLSAAFSRQLNVNAKPFVPNVHAAEFVPSFLRGPAAPPPPVGGAANN
FT HGAGSGAGGRAAPVESSQEEQSLCEGSNSAVSM (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042198"
FT VAR_SEQ 8
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042199"
FT CONFLICT P15170-2:6..9
FT /note="GGGG -> G (in Ref. 4; AAH09503)"
FT /evidence="ECO:0000305"
FT CONFLICT P15170-2:92
FT /note="G -> C (in Ref. 4; AAH09503)"
FT /evidence="ECO:0000305"
FT CONFLICT P15170-2:100
FT /note="V -> A (in Ref. 4; AAH09503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 55756 MW; DE20482CCABC3576 CRC64;
MELSEPIVEN GETEMSPEES WEHKEEISEA EPGGGSLGDG RPPEESAHEM MEEEEEIPKP
KSVVAPPGAP KKEHVNVVFI GHVDAGKSTI GGQIMYLTGM VDKRTLEKYE REAKEKNRET
WYLSWALDTN QEERDKGKTV EVGRAYFETE KKHFTILDAP GHKSFVPNMI GGASQADLAV
LVISARKGEF ETGFEKGGQT REHAMLAKTA GVKHLIVLIN KMDDPTVNWS NERYEECKEK
LVPFLKKVGF NPKKDIHFMP CSGLTGANLK EQSDFCPWYI GLPFIPYLDN LPNFNRSVDG
PIRLPIVDKY KDMGTVVLGK LESGSICKGQ QLVMMPNKHN VEVLGILSDD VETDTVAPGE
NLKIRLKGIE EEEILPGFIL CDPNNLCHSG RTFDAQIVII EHKSIICPGY NAVLHIHTCI
EEVEITALIC LVDKKSGEKS KTRPRFVKQD QVCIARLRTA GTICLETFKD FPQMGRFTLR
DEGKTIAIGK VLKLVPEKD
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