ID GTPB1_HUMAN Reviewed; 669 AA. AC O00178; Q6IC67; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 3. DT 28-JAN-2026, entry version 201. DE RecName: Full=GTP-binding protein 1 {ECO:0000303|PubMed:38118446}; DE Short=G-protein 1; DE Short=GP-1 {ECO:0000303|PubMed:9070279}; DE Short=GP1 {ECO:0000312|EMBL:AAH14075.3}; DE EC=3.6.5.3 {ECO:0000269|PubMed:30108131}; GN Name=GTPBP1 {ECO:0000312|HGNC:HGNC:4669}; 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 GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-669. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-669. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-669. RX PubMed=9070279; DOI=10.1006/bbrc.1997.6103; RA Senju S., Nishimura Y.; RT "Identification of human and mouse GP-1, a putative member of a novel G- RT protein family."; RL Biochem. Biophys. Res. Commun. 231:360-364(1997). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-44; SER-47 AND RP SER-580, AND 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 [6] RP IDENTIFICATION BY MASS 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY RP 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-44; SER-47; SER-69 RP AND SER-580, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] 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 [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30108131; DOI=10.1101/gad.314724.118; RA Zinoviev A., Goyal A., Jindal S., LaCava J., Komar A.A., Rodnina M.V., RA Hellen C.U.T., Pestova T.V.; RT "Functions of unconventional mammalian translational GTPases GTPBP1 and RT GTPBP2."; RL Genes Dev. 32:1226-1241(2018). RN [14] RP VARIANTS NEDFET1 ALA-208; 509-TYR--CYS-669 DEL AND 555-GLN--CYS-669 DEL, RP AND INVOLVEMENT IN NEDFET1. RX PubMed=38118446; DOI=10.1016/j.ajhg.2023.11.012; RG SYNAPS Study Group; RA Salpietro V., Maroofian R., Zaki M.S., Wangen J., Ciolfi A., Barresi S., RA Efthymiou S., Lamaze A., Aughey G.N., Al Mutairi F., Rad A., Rocca C., RA Cali E., Accogli A., Zara F., Striano P., Mojarrad M., Tariq H., RA Giacopuzzi E., Taylor J.C., Oprea G., Skrahina V., Rehman K.U., RA Abd Elmaksoud M., Bassiony M., El Said H.G., Abdel-Hamid M.S., RA Al Shalan M., Seo G., Kim S., Lee H., Khang R., Issa M.Y., Elbendary H.M., RA Rafat K., Marinakis N.M., Traeger-Synodinos J., Ververi A., Sourmpi M., RA Eslahi A., Khadivi Zand F., Beiraghi Toosi M., Babaei M., Jackson A., RA Bertoli-Avella A., Pagnamenta A.T., Niceta M., Battini R., Corsello A., RA Leoni C., Chiarelli F., Dallapiccola B., Faqeih E.A., Tallur K.K., RA Alfadhel M., Alobeid E., Maddirevula S., Mankad K., Banka S., RA Ghayoor-Karimiani E., Tartaglia M., Chung W.K., Green R., Alkuraya F.S., RA Jepson J.E.C., Houlden H.; RT "Bi-allelic genetic variants in the translational GTPases GTPBP1 and GTPBP2 RT cause a distinct identical neurodevelopmental syndrome."; RL Am. J. Hum. Genet. 111:200-210(2024). CC -!- FUNCTION: GTPase that plays a role in the elongation phase of protein CC synthesis by forming ternary complexes with GTP and aminoacyl-transfer CC RNAs (aa-tRNAs), and delivering aa-tRNAs to the ribosomal A site in a CC GTP-dependent manner (PubMed:30108131). Is also able to deliver CC deacylated tRNA to the A site (PubMed:30108131). Additionally, it is CC involved in RNA quality control; after GTP hydrolysis, which is not CC immediately followed by rapid peptide bond formation, GTPBP1 likely CC retains aa-tRNA in the A site and promotes exosomal degradation of CC faulty mRNAs engaged in 80S elongation complexes (PubMed:30108131). CC Plays a role in the regulation of circadian mRNA stability (By CC similarity). {ECO:0000250|UniProtKB:D2XV59, CC ECO:0000269|PubMed:30108131}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; CC Evidence={ECO:0000269|PubMed:30108131}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000269|PubMed:30108131}; CC -!- SUBUNIT: Form complexes with GTP and aa-tRNAs; aa-tRNA binding CC stabilizes GTP binding and stimulates GTP hydrolysis (PubMed:30108131). CC Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46, HNRNPD, HNRNPR CC and SYNCRIP. Identified in a complex with AANAT mRNA, but does not bind CC mRNA by itself (By similarity). {ECO:0000250|UniProtKB:D2XV59, CC ECO:0000269|PubMed:30108131}. CC -!- INTERACTION: CC O00178; Q9BPX7: C7orf25; NbExp=3; IntAct=EBI-4403245, EBI-718586; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D2XV59}. CC -!- DISEASE: Neurodevelopmental disorder with characteristic facial and CC ectodermal features and tetraparesis 1 (NEDFET1) [MIM:620888]: An CC autosomal recessive disorder characterized by microcephaly, profound CC neurodevelopmental impairment, distinctive craniofacial features, CC ectodermal defects, and tetraparesis. {ECO:0000269|PubMed:38118446}. CC Note=The disease may be caused by variants affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. GTPBP1 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB51273.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAG30387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL021707; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014075; AAH14075.3; -; mRNA. DR EMBL; CR456501; CAG30387.1; ALT_INIT; mRNA. DR EMBL; U87964; AAB51273.1; ALT_INIT; mRNA. DR CCDS; CCDS13977.2; -. DR PIR; JC5291; JC5291. DR RefSeq; NP_004277.2; NM_004286.5. DR AlphaFoldDB; O00178; -. DR SMR; O00178; -. DR BioGRID; 114937; 141. DR FunCoup; O00178; 1859. DR IntAct; O00178; 59. DR MINT; O00178; -. DR STRING; 9606.ENSP00000216044; -. DR GlyCosmos; O00178; 2 sites, 1 glycan. DR GlyGen; O00178; 5 sites, 2 O-linked glycans (4 sites). DR iPTMnet; O00178; -. DR PhosphoSitePlus; O00178; -. DR BioMuta; GTPBP1; -. DR CPTAC; CPTAC-1610; -. DR jPOST; O00178; -. DR MassIVE; O00178; -. DR PaxDb; 9606-ENSP00000216044; -. DR PeptideAtlas; O00178; -. DR ProteomicsDB; 47762; -. DR Pumba; O00178; -. DR Antibodypedia; 26419; 196 antibodies from 27 providers. DR DNASU; 9567; -. DR Ensembl; ENST00000216044.10; ENSP00000216044.5; ENSG00000100226.17. DR GeneID; 9567; -. DR KEGG; hsa:9567; -. DR MANE-Select; ENST00000216044.10; ENSP00000216044.5; NM_004286.5; NP_004277.2. DR UCSC; uc003awg.4; human. DR AGR; HGNC:4669; -. DR ClinPGx; PA29057; -. DR CTD; 9567; -. DR DisGeNET; 9567; -. DR GeneCards; GTPBP1; -. DR HGNC; HGNC:4669; GTPBP1. DR HPA; ENSG00000100226; Tissue enhanced (bone). DR MalaCards; GTPBP1; -. DR MIM; 602245; gene. DR MIM; 620888; phenotype. DR OpenTargets; ENSG00000100226; -. DR VEuPathDB; HostDB:ENSG00000100226; -. DR eggNOG; KOG0463; Eukaryota. DR GeneTree; ENSGT00940000156054; -. DR HOGENOM; CLU_012821_2_0_1; -. DR InParanoid; O00178; -. DR OMA; FRFIQRP; -. DR OrthoDB; 248233at2759; -. DR PAN-GO; O00178; 2 GO annotations based on evolutionary models. DR PhylomeDB; O00178; -. DR PathwayCommons; O00178; -. DR SignaLink; O00178; -. DR Agora; ENSG00000100226; -. DR BioGRID-ORCS; 9567; 22 hits in 1156 CRISPR screens. DR ChiTaRS; GTPBP1; human. DR GeneWiki; GTPBP1; -. DR GenomeRNAi; 9567; -. DR Pharos; O00178; Tbio. DR PRO; PR:O00178; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; O00178; protein. DR Bgee; ENSG00000100226; Expressed in sural nerve and 182 other cell types or tissues. DR ExpressionAtlas; O00178; baseline and differential. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:1904678; F:alpha-aminoacyl-tRNA binding; IDA:FlyBase. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003746; F:translation elongation factor activity; IDA:FlyBase. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; IDA:FlyBase. DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB. DR GO; GO:0071025; P:RNA surveillance; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR CDD; cd04165; GTPBP1_like; 1. DR CDD; cd03694; GTPBP_II; 1. DR CDD; cd03708; GTPBP_III; 1. DR FunFam; 2.40.30.10:FF:000028; GTP-binding protein 1,-like; 1. DR FunFam; 2.40.30.10:FF:000014; Probable GTP-binding protein 1; 1. DR FunFam; 3.40.50.300:FF:000091; Probable GTP-binding protein 1; 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; IPR050055; EF-Tu_GTPase. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR035531; GTPBP1-like. 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 PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. DR PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. 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; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW Cytoplasm; GTP-binding; Hydrolase; Intellectual disability; KW Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; RNA-binding. FT CHAIN 1..669 FT /note="GTP-binding protein 1" FT /id="PRO_0000122469" FT DOMAIN 158..389 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 167..174 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 206..210 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 252..255 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 308..311 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 366..368 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 573..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 573..595 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 646..657 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 167..174 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 252..256 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 308..311 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08582" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08582" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08582" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 44 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 580 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VARIANT 91 FT /note="G -> R (in dbSNP:rs11547402)" FT /id="VAR_049496" FT VARIANT 208 FT /note="T -> A (in NEDFET1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089981" FT VARIANT 509..669 FT /note="Missing (in NEDFET1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089982" FT VARIANT 555..669 FT /note="Missing (in NEDFET1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089983" SQ SEQUENCE 669 AA; 72454 MW; 0814F4DC03740ABE CRC64; MATERSRSAM DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI CEKSTKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLT KRDEGGPSGG PAVGAPPPGD EASSVGAGQP AASSNLQPQP KPSSGGRRRG GQRHKVKSQG ACVTPASGC //