ID GTPB2_HUMAN Reviewed; 602 AA. AC Q9BX10; Q5T7E8; Q8ND84; Q8TAH7; Q8WUA5; Q9HCS9; Q9NRU4; Q9NX60; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 28-JAN-2026, entry version 175. DE RecName: Full=GTP-binding protein 2; GN Name=GTPBP2 {ECO:0000312|EMBL:CAC36269.1}; 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] {ECO:0000305, ECO:0000312|EMBL:BAB12431.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=11054535; DOI=10.1016/s0378-1119(00)00346-2; RA Watanabe M., Yoshida K., Hida M., Kato H., Uchida K., Yamaguchi R., RA Tateyama S., Sugano S.; RT "Cloning, expression analysis, and chromosomal mapping of GTPBP2, a novel RT member of the G protein family."; RL Gene 256:51-58(2000). RN [2] {ECO:0000312|EMBL:CAC36269.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA91160.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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] {ECO:0000305, ECO:0000312|EMBL:AAH64968.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon {ECO:0000312|EMBL:AAH20980.2}, Ovary RC {ECO:0000312|EMBL:AAH28347.2}, and Skin {ECO:0000312|EMBL:AAH64968.1}; 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] {ECO:0000305, ECO:0000312|EMBL:AAF78884.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-602 (ISOFORM 1), AND INDUCTION. RX PubMed=10833435; DOI=10.1006/bbrc.2000.2763; RA Kudo H., Senju S., Mitsuya H., Nishimura Y.; RT "Mouse and human GTPBP2, newly identified members of the GP-1 family of RT GTPase."; RL Biochem. Biophys. Res. Commun. 272:456-465(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-602 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP INVOLVEMENT IN JABELS. RX PubMed=26675814; DOI=10.1016/j.neurobiolaging.2015.10.034; RA Jaberi E., Rohani M., Shahidi G.A., Nafissi S., Arefian E., Soleimani M., RA Rasooli P., Ahmadieh H., Daftarian N., KaramiNejadRanjbar M., Klotzle B., RA Fan J.B., Turk C., Steemers F., Elahi E.; RT "Identification of mutation in GTPBP2 in patients of a family with RT neurodegeneration accompanied by iron deposition in the brain."; RL Neurobiol. Aging 38:216.E11-216.E18(2016). RN [8] RP FUNCTION. 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 [9] RP INVOLVEMENT IN JABELS, AND VARIANTS JABELS 144-ARG--PHE-602 DEL; RP 407-GLN--PHE-602 DEL AND 470-ARG--PHE-602 DEL. RX PubMed=29449720; DOI=10.1038/s41431-018-0097-3; RA Bertoli-Avella A.M., Garcia-Aznar J.M., Brandau O., Al-Hakami F., RA Yueksel Z., Marais A., Gruening N.M., Abbasi Moheb L., Paknia O., RA Alshaikh N., Alameer S., Marafi M.J., Al-Mulla F., Al-Sannaa N., Rolfs A., RA Bauer P.; RT "Biallelic inactivating variants in the GTPBP2 gene cause a RT neurodevelopmental disorder with severe intellectual disability."; RL Eur. J. Hum. Genet. 26:592-598(2018). RN [10] RP VARIANTS JABELS 3-SER--PHE-602 DEL; PRO-93; 121-ARG--PHE-602 DEL; ARG-125; RP ASN-319; 332-GLN--PHE-602 DEL; 470-ARG--PHE-602 DEL AND 521-ARG--PHE-602 RP DEL, AND INVOLVEMENT IN JABELS. 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). RN [11] RP VARIANTS JABELS 219-ARG--PHE-602 DEL; 470-ARG--PHE-602 DEL AND RP 520-ARG--PHE-602 DEL. RX PubMed=30790272; DOI=10.1111/cge.13523; RG Care4Rare Canada Consortium; RA Carter M.T., Venkateswaran S., Shapira-Zaltsberg G., Davila J., RA Humphreys P., Kernohan K.D., Boycott K.M.; RT "Clinical delineation of GTPBP2-associated neuro-ectodermal syndrome: RT Report of two new families and review of the literature."; RL Clin. Genet. 95:601-606(2019). CC -!- FUNCTION: Involved in the rescue of ribosome stalling due to the CC presence of non-functional tRNA (By similarity). Has very low GTP- CC binding activity (PubMed:30108131). {ECO:0000250|UniProtKB:Q3UJK4, CC ECO:0000269|PubMed:30108131}. CC -!- SUBUNIT: Interacts with PELO. {ECO:0000250|UniProtKB:Q3UJK4}. CC -!- INTERACTION: CC Q9BX10; P49760: CLK2; NbExp=3; IntAct=EBI-6115579, EBI-750020; CC Q9BX10; Q9UHW5: GPN3; NbExp=3; IntAct=EBI-6115579, EBI-395491; CC Q9BX10; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-6115579, EBI-6115579; CC Q9BX10; O60341: KDM1A; NbExp=2; IntAct=EBI-6115579, EBI-710124; CC Q9BX10; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-6115579, EBI-398874; CC Q9BX10; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-6115579, EBI-79165; CC Q9BX10; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6115579, EBI-742388; CC Q9BX10; O14744: PRMT5; NbExp=2; IntAct=EBI-6115579, EBI-351098; CC Q9BX10; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-6115579, EBI-912440; CC Q9BX10; P20618: PSMB1; NbExp=3; IntAct=EBI-6115579, EBI-372273; CC Q9BX10; P08621: SNRNP70; NbExp=3; IntAct=EBI-6115579, EBI-1049228; CC Q9BX10; O43463: SUV39H1; NbExp=2; IntAct=EBI-6115579, EBI-349968; CC Q9BX10; Q99757: TXN2; NbExp=5; IntAct=EBI-6115579, EBI-2932492; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1 {ECO:0000269|PubMed:10833435}; CC IsoId=Q9BX10-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:11054535}; CC IsoId=Q9BX10-2; Sequence=VSP_052154; CC Name=3 {ECO:0000269|PubMed:14702039}; CC IsoId=Q9BX10-3; Sequence=VSP_052154, VSP_052156; CC Name=4 {ECO:0000269|PubMed:14574404}; CC IsoId=Q9BX10-4; Sequence=VSP_052155; CC -!- TISSUE SPECIFICITY: Predominantly expressed in thymus, spleen, and CC testis. Expressed at lower levels in brain, lung, kidney, and ovary. CC {ECO:0000269|PubMed:11054535}. CC -!- INDUCTION: Up-regulated by IFNG/IFN-gamma in human monocytic cell line CC THP-1. {ECO:0000269|PubMed:10833435}. CC -!- DISEASE: Jaberi-Elahi syndrome (JABELS) [MIM:617988]: An autosomal CC recessive disorder characterized by developmental delay and CC intellectual disability. Additional variable features include ataxic CC gait and abnormal movements, visual impairment, microcephaly, abnormal CC foot or hand posturing, kyphoscoliosis, dysmorphic facial features or CC seizures. Brain imaging typically shows cerebellar atrophy and CC hypoplasia of the corpus callosum. {ECO:0000269|PubMed:26675814, CC ECO:0000269|PubMed:29449720, ECO:0000269|PubMed:30790272, CC ECO:0000269|PubMed:38118446}. Note=The disease is caused by variants CC affecting the gene 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=CAD38999.1; 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; AB024574; BAB12431.1; -; mRNA. DR EMBL; AL353602; CAC36269.1; -; Genomic_DNA. DR EMBL; AL353602; CAI12785.1; -; Genomic_DNA. DR EMBL; AK000430; BAA91160.1; -; mRNA. DR EMBL; BC020980; AAH20980.2; -; mRNA. DR EMBL; BC028347; AAH28347.2; -; mRNA. DR EMBL; BC064968; AAH64968.1; -; mRNA. DR EMBL; AF168990; AAF78884.1; -; mRNA. DR EMBL; AL834331; CAD38999.1; ALT_INIT; mRNA. DR CCDS; CCDS4903.1; -. [Q9BX10-1] DR CCDS; CCDS69124.1; -. [Q9BX10-2] DR PIR; PC7084; PC7084. DR RefSeq; NP_001273145.1; NM_001286216.2. [Q9BX10-2] DR RefSeq; NP_061969.3; NM_019096.4. [Q9BX10-1] DR RefSeq; XP_024302245.1; XM_024446477.2. [Q9BX10-2] DR RefSeq; XP_024302246.1; XM_024446478.2. [Q9BX10-2] DR RefSeq; XP_054211706.1; XM_054355731.1. [Q9BX10-2] DR RefSeq; XP_054211707.1; XM_054355732.1. [Q9BX10-2] DR AlphaFoldDB; Q9BX10; -. DR SMR; Q9BX10; -. DR BioGRID; 120097; 66. DR FunCoup; Q9BX10; 776. DR IntAct; Q9BX10; 46. DR MINT; Q9BX10; -. DR STRING; 9606.ENSP00000303997; -. DR GlyGen; Q9BX10; 1 site. DR iPTMnet; Q9BX10; -. DR PhosphoSitePlus; Q9BX10; -. DR SwissPalm; Q9BX10; -. DR BioMuta; GTPBP2; -. DR DMDM; 74752415; -. DR jPOST; Q9BX10; -. DR MassIVE; Q9BX10; -. DR PaxDb; 9606-ENSP00000303997; -. DR PeptideAtlas; Q9BX10; -. DR ProteomicsDB; 79339; -. [Q9BX10-1] DR ProteomicsDB; 79340; -. [Q9BX10-2] DR ProteomicsDB; 79341; -. [Q9BX10-3] DR ProteomicsDB; 79342; -. [Q9BX10-4] DR Pumba; Q9BX10; -. DR Antibodypedia; 30525; 180 antibodies from 27 providers. DR DNASU; 54676; -. DR Ensembl; ENST00000307114.11; ENSP00000304893.7; ENSG00000172432.20. [Q9BX10-2] DR Ensembl; ENST00000307126.10; ENSP00000303997.5; ENSG00000172432.20. [Q9BX10-1] DR GeneID; 54676; -. DR KEGG; hsa:54676; -. DR MANE-Select; ENST00000307126.10; ENSP00000303997.5; NM_019096.5; NP_061969.3. DR UCSC; uc003ovs.5; human. [Q9BX10-1] DR AGR; HGNC:4670; -. DR ClinPGx; PA29058; -. DR CTD; 54676; -. DR DisGeNET; 54676; -. DR GeneCards; GTPBP2; -. DR HGNC; HGNC:4670; GTPBP2. DR HPA; ENSG00000172432; Low tissue specificity. DR MalaCards; GTPBP2; -. DR MIM; 607434; gene. DR MIM; 617988; phenotype. DR OpenTargets; ENSG00000172432; -. DR VEuPathDB; HostDB:ENSG00000172432; -. DR eggNOG; KOG1143; Eukaryota. DR GeneTree; ENSGT00940000155636; -. DR HOGENOM; CLU_012821_1_1_1; -. DR InParanoid; Q9BX10; -. DR OMA; WEDICEN; -. DR OrthoDB; 248233at2759; -. DR PAN-GO; Q9BX10; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9BX10; -. DR PathwayCommons; Q9BX10; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR SignaLink; Q9BX10; -. DR Agora; ENSG00000172432; -. DR BioGRID-ORCS; 54676; 32 hits in 1162 CRISPR screens. DR ChiTaRS; GTPBP2; human. DR GenomeRNAi; 54676; -. DR Pharos; Q9BX10; Tbio. DR PRO; PR:Q9BX10; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9BX10; protein. DR Bgee; ENSG00000172432; Expressed in lower esophagus mucosa and 171 other cell types or tissues. DR ExpressionAtlas; Q9BX10; baseline and differential. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:1904678; F:alpha-aminoacyl-tRNA binding; IDA:FlyBase. DR GO; GO:0005525; F:GTP binding; IDA:FlyBase. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:Ensembl. DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:Ensembl. 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:000058; GTP binding protein 2; 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; 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:SF3; GTP-BINDING PROTEIN 2; 1. DR Pfam; PF00009; GTP_EFTU; 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 Alternative splicing; Disease variant; GTP-binding; KW Intellectual disability; Nucleotide-binding; Proteomics identification; KW Reference proteome. FT CHAIN 1..602 FT /note="GTP-binding protein 2" FT /id="PRO_0000248500" FT DOMAIN 170..398 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 16..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..50 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 179..186 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O00178" FT BINDING 260..264 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O00178" FT BINDING 316..319 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O00178" FT VAR_SEQ 1..88 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:11054535, FT ECO:0000303|PubMed:14702039" FT /id="VSP_052154" FT VAR_SEQ 72..79 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14574404" FT /id="VSP_052155" FT VAR_SEQ 101..370 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_052156" FT VARIANT 3..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089984" FT VARIANT 93 FT /note="L -> P (in JABELS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089985" FT VARIANT 121..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089986" FT VARIANT 125 FT /note="K -> R (in JABELS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089987" FT VARIANT 144..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:29449720" FT /id="VAR_080975" FT VARIANT 219..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:30790272" FT /id="VAR_089988" FT VARIANT 319 FT /note="D -> N (in JABELS; uncertain significance; FT dbSNP:rs1399993191)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089989" FT VARIANT 332..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089990" FT VARIANT 407..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:29449720" FT /id="VAR_080976" FT VARIANT 470..602 FT /note="Missing (in JABELS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:29449720, FT ECO:0000269|PubMed:30790272, ECO:0000269|PubMed:38118446" FT /id="VAR_080977" FT VARIANT 520..602 FT /note="Missing (in JABELS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30790272" FT /id="VAR_089991" FT VARIANT 521..602 FT /note="Missing (in JABELS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38118446" FT /id="VAR_089992" FT CONFLICT 42..43 FT /note="KK -> TR (in Ref. 5; AAF78884)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="G -> E (in Ref. 1; BAB12431)" FT /evidence="ECO:0000305" SQ SEQUENCE 602 AA; 65768 MW; BA9CA08F3797A7B1 CRC64; MDSRVSELFG GCCRPGGGPA VGGTLKARGA GSSSGCGGPK GKKKNGRNRG GKANNPPYLP PEAEDGNIEY KLKLVNPSQY RFEHLVTQMK WRLQEGRGEA VYQIGVEDNG LLVGLAEEEM RASLKTLHRM AEKVGADITV LREREVDYDS DMPRKITEVL VRKVPDNQQF LDLRVAVLGN VDSGKSTLLG VLTQGELDNG RGRARLNLFR HLHEIQSGRT SSISFEILGF NSKGEVVNYS DSRTAEEICE SSSKMITFID LAGHHKYLHT TIFGLTSYCP DCALLLVSAN TGIAGTTREH LGLALALKVP FFIVVSKIDL CAKTTVERTV RQLERVLKQP GCHKVPMLVT SEDDAVTAAQ QFAQSPNVTP IFTLSSVSGE SLDLLKVFLN ILPPLTNSKE QEELMQQLTE FQVDEIYTVP EVGTVVGGTL SSGICREGDQ LVVGPTDDGC FLELRVCSIQ RNRSACRVLR AGQAATLALG DFDRALLRKG MVMVSPEMNP TICSVFEAEI VLLFHATTFR RGFQVTVHVG NVRQTAVVEK IHAKDKLRTG EKAVVRFRFL KHPEYLKVGA KLLFREGVTK GIGHVTDVQA ITAGEAQANM GF //