ID GTPB4_HUMAN Reviewed; 634 AA. AC Q9BZE4; B3KMC5; B4DY13; B7Z7A3; O95446; Q5T3R8; Q9NVJ8; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=GTP-binding protein 4; DE AltName: Full=Chronic renal failure gene protein; DE AltName: Full=GTP-binding protein NGB; DE AltName: Full=Nucleolar GTP-binding protein 1; GN Name=GTPBP4 {ECO:0000312|HGNC:HGNC:21535}; Synonyms=CRFG, NOG1; 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). RA Cheng J.Q., Cao C.H., Testa J.R., Golemis E.A., Jiang C., Yuan W., RA Nicosia S.V.; RT "Cloning and characterization of a novel GTP-binding protein, NGB."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RC TISSUE=Kidney; RX PubMed=11316846; DOI=10.1681/asn.v125883; RA Laping N.J., Olson B.A., Zhu Y.; RT "Identification of a novel nuclear guanosine triphosphate-binding protein RT differentially expressed in renal disease."; RL J. Am. Soc. Nephrol. 12:883-890(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP HIS-525. RC TISSUE=Testis; 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]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [8] RP PROTEIN SEQUENCE OF 2-7; 9-25; 37-42; 53-71; 94-111; 119-125; 146-155; RP 161-169; 191-213; 217-248; 267-276; 296-330; 353-359; 372-384; 398-425; RP 429-448; 450-460 AND 526-544, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION RP AT ALA-2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470; SER-472 AND RP SER-558, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470 AND SER-472, 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-522, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP FUNCTION. RX PubMed=20308539; DOI=10.1073/pnas.1002447107; RA Lunardi A., Di Minin G., Provero P., Dal Ferro M., Carotti M., Del Sal G., RA Collavin L.; RT "A genome-scale protein interaction profile of Drosophila p53 uncovers RT additional nodes of the human p53 network."; RL Proc. Natl. Acad. Sci. U.S.A. 107:6322-6327(2010). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470 AND SER-472, AND 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-332 AND LYS-534, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [20] RP INTERACTION WITH MINAS-60. RX PubMed=35393574; DOI=10.1038/s41589-022-01003-9; RA Cao X., Khitun A., Harold C.M., Bryant C.J., Zheng S.J., Baserga S.J., RA Slavoff S.A.; RT "Nascent alt-protein chemoproteomics reveals a pre-60S assembly checkpoint RT inhibitor."; RL Nat. Chem. Biol. 0:0-0(2022). RN [21] {ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8} RP STRUCTURE BY ELECTRON MICROSCOPY (3.13 ANGSTROMS), FUNCTION, AND RP INTERACTION WITH PRE-60S RIBOSOMAL PARTICLES. RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x; RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.; RT "Structural snapshots of human pre-60S ribosomal particles before and after RT nuclear export."; RL Nat. Commun. 11:3542-3542(2020). CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit CC (PubMed:32669547). Acts as a TP53 repressor, preventing TP53 CC stabilization and cell cycle arrest (PubMed:20308539). CC {ECO:0000269|PubMed:20308539, ECO:0000269|PubMed:32669547}. CC -!- SUBUNIT: Associates with pre-60S ribosomal particles (PubMed:32669547). CC Interacts with MINAS-60 (product of an alternative open reading frame CC of RBM10) (PubMed:35393574). {ECO:0000269|PubMed:32669547, CC ECO:0000269|PubMed:35393574}. CC -!- INTERACTION: CC Q9BZE4; P53618: COPB1; NbExp=3; IntAct=EBI-1056249, EBI-359063; CC Q9BZE4; P42858: HTT; NbExp=3; IntAct=EBI-1056249, EBI-466029; CC Q9BZE4; P35240: NF2; NbExp=9; IntAct=EBI-1056249, EBI-1014472; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11316846, CC ECO:0000269|PubMed:12429849, ECO:0000269|Ref.8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9BZE4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZE4-2; Sequence=VSP_056147; CC Name=3; CC IsoId=Q9BZE4-3; Sequence=VSP_056146; CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. NOG subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU01047}. 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; AF120334; AAD09830.1; -; mRNA. DR EMBL; AF325353; AAK13444.1; -; mRNA. DR EMBL; AK001548; BAG50937.1; -; mRNA. DR EMBL; AK001552; BAA91752.1; -; mRNA. DR EMBL; AK301721; BAH13539.1; -; mRNA. DR EMBL; AK302219; BAG63575.1; -; mRNA. DR EMBL; AC022536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359878; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86526.1; -; Genomic_DNA. DR EMBL; BC038975; AAH38975.1; -; mRNA. DR CCDS; CCDS31132.1; -. [Q9BZE4-1] DR RefSeq; NP_036473.2; NM_012341.2. [Q9BZE4-1] DR PDB; 6LSS; EM; 3.23 A; 4=1-634. DR PDB; 6LU8; EM; 3.13 A; 4=1-634. DR PDB; 8FKP; EM; 2.85 A; SR=1-634. DR PDB; 8FKQ; EM; 2.76 A; SR=1-634. DR PDB; 8FKR; EM; 2.89 A; SR=1-634. DR PDB; 8FKS; EM; 2.88 A; SR=1-634. DR PDB; 8FKT; EM; 2.81 A; SR=1-634. DR PDB; 8FKU; EM; 2.82 A; SR=1-634. DR PDB; 8FKV; EM; 2.47 A; SR=1-634. DR PDB; 8FKW; EM; 2.50 A; SR=1-634. DR PDB; 8FKX; EM; 2.59 A; SR=1-634. DR PDB; 8FKY; EM; 2.67 A; SR=1-634. DR PDB; 8FKZ; EM; 3.04 A; SR=1-634. DR PDB; 8FL0; EM; 2.91 A; SR=1-634. DR PDB; 8FL2; EM; 2.67 A; SR=1-634. DR PDB; 8FL3; EM; 2.53 A; SR=1-634. DR PDB; 8FL4; EM; 2.89 A; SR=1-634. DR PDB; 8FL6; EM; 2.62 A; SR=1-634. DR PDB; 8FL7; EM; 2.55 A; SR=1-634. DR PDB; 8FL9; EM; 2.75 A; SR=1-634. DR PDB; 8FLA; EM; 2.63 A; SR=1-634. DR PDB; 8FLB; EM; 2.55 A; SR=1-634. DR PDB; 8FLC; EM; 2.76 A; SR=1-634. DR PDB; 8FLD; EM; 2.58 A; SR=1-634. DR PDB; 8FLE; EM; 2.48 A; SR=1-634. DR PDB; 8FLF; EM; 2.65 A; SR=1-634. DR PDB; 8IDT; EM; 2.80 A; 4=1-634. DR PDB; 8IDY; EM; 3.00 A; 4=1-634. DR PDB; 8IE3; EM; 3.30 A; 4=1-634. DR PDB; 8INE; EM; 3.20 A; 4=1-634. DR PDB; 8INF; EM; 3.00 A; 4=1-634. DR PDB; 8INK; EM; 3.20 A; 4=1-634. DR PDB; 8IPD; EM; 3.20 A; 4=1-634. DR PDB; 8IPX; EM; 4.30 A; 4=1-634. DR PDB; 8IPY; EM; 3.20 A; 4=1-634. DR PDB; 8IR1; EM; 3.30 A; 4=1-634. DR PDB; 8IR3; EM; 3.50 A; 4=1-634. DR PDBsum; 6LSS; -. DR PDBsum; 6LU8; -. DR PDBsum; 8FKP; -. DR PDBsum; 8FKQ; -. DR PDBsum; 8FKR; -. DR PDBsum; 8FKS; -. DR PDBsum; 8FKT; -. DR PDBsum; 8FKU; -. DR PDBsum; 8FKV; -. DR PDBsum; 8FKW; -. DR PDBsum; 8FKX; -. DR PDBsum; 8FKY; -. DR PDBsum; 8FKZ; -. DR PDBsum; 8FL0; -. DR PDBsum; 8FL2; -. DR PDBsum; 8FL3; -. DR PDBsum; 8FL4; -. DR PDBsum; 8FL6; -. DR PDBsum; 8FL7; -. DR PDBsum; 8FL9; -. DR PDBsum; 8FLA; -. DR PDBsum; 8FLB; -. DR PDBsum; 8FLC; -. DR PDBsum; 8FLD; -. DR PDBsum; 8FLE; -. DR PDBsum; 8FLF; -. DR PDBsum; 8IDT; -. DR PDBsum; 8IDY; -. DR PDBsum; 8IE3; -. DR PDBsum; 8INE; -. DR PDBsum; 8INF; -. DR PDBsum; 8INK; -. DR PDBsum; 8IPD; -. DR PDBsum; 8IPX; -. DR PDBsum; 8IPY; -. DR PDBsum; 8IR1; -. DR PDBsum; 8IR3; -. DR AlphaFoldDB; Q9BZE4; -. DR EMDB; EMD-29252; -. DR EMDB; EMD-29253; -. DR EMDB; EMD-29254; -. DR EMDB; EMD-29255; -. DR EMDB; EMD-29256; -. DR EMDB; EMD-29257; -. DR EMDB; EMD-29258; -. DR EMDB; EMD-29259; -. DR EMDB; EMD-29260; -. DR EMDB; EMD-29261; -. DR EMDB; EMD-29262; -. DR EMDB; EMD-29263; -. DR EMDB; EMD-29265; -. DR EMDB; EMD-29266; -. DR EMDB; EMD-29267; -. DR EMDB; EMD-29268; -. DR EMDB; EMD-29269; -. DR EMDB; EMD-29271; -. DR EMDB; EMD-29272; -. DR EMDB; EMD-29273; -. DR EMDB; EMD-29274; -. DR EMDB; EMD-29275; -. DR EMDB; EMD-29276; -. DR EMDB; EMD-29277; -. DR EMDB; EMD-35370; -. DR EMDB; EMD-35371; -. DR EMDB; EMD-35375; -. DR EMDB; EMD-35596; -. DR EMDB; EMD-35597; -. DR EMDB; EMD-35599; -. DR EMDB; EMD-35639; -. DR EMDB; EMD-35649; -. DR EMDB; EMD-35651; -. DR EMDB; EMD-35672; -. DR EMDB; EMD-35673; -. DR SMR; Q9BZE4; -. DR BioGRID; 117104; 418. DR IntAct; Q9BZE4; 143. DR MINT; Q9BZE4; -. DR STRING; 9606.ENSP00000354040; -. DR ChEMBL; CHEMBL4105780; -. DR GlyGen; Q9BZE4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BZE4; -. DR PhosphoSitePlus; Q9BZE4; -. DR SwissPalm; Q9BZE4; -. DR BioMuta; GTPBP4; -. DR DMDM; 17368711; -. DR EPD; Q9BZE4; -. DR jPOST; Q9BZE4; -. DR MassIVE; Q9BZE4; -. DR MaxQB; Q9BZE4; -. DR PaxDb; 9606-ENSP00000354040; -. DR PeptideAtlas; Q9BZE4; -. DR ProteomicsDB; 5488; -. DR ProteomicsDB; 6843; -. DR ProteomicsDB; 79822; -. [Q9BZE4-1] DR Pumba; Q9BZE4; -. DR Antibodypedia; 23768; 213 antibodies from 33 providers. DR DNASU; 23560; -. DR Ensembl; ENST00000360803.9; ENSP00000354040.4; ENSG00000107937.19. [Q9BZE4-1] DR GeneID; 23560; -. DR KEGG; hsa:23560; -. DR MANE-Select; ENST00000360803.9; ENSP00000354040.4; NM_012341.3; NP_036473.2. DR UCSC; uc001ift.4; human. [Q9BZE4-1] DR AGR; HGNC:21535; -. DR CTD; 23560; -. DR DisGeNET; 23560; -. DR GeneCards; GTPBP4; -. DR HGNC; HGNC:21535; GTPBP4. DR HPA; ENSG00000107937; Low tissue specificity. DR MIM; 619169; gene. DR neXtProt; NX_Q9BZE4; -. DR OpenTargets; ENSG00000107937; -. DR PharmGKB; PA134922009; -. DR VEuPathDB; HostDB:ENSG00000107937; -. DR eggNOG; KOG1490; Eukaryota. DR GeneTree; ENSGT00390000018475; -. DR HOGENOM; CLU_011784_4_1_1; -. DR InParanoid; Q9BZE4; -. DR OMA; EWKNDVM; -. DR OrthoDB; 5476718at2759; -. DR PhylomeDB; Q9BZE4; -. DR TreeFam; TF300430; -. DR PathwayCommons; Q9BZE4; -. DR SignaLink; Q9BZE4; -. DR BioGRID-ORCS; 23560; 853 hits in 1166 CRISPR screens. DR ChiTaRS; GTPBP4; human. DR GeneWiki; GTPBP4; -. DR GenomeRNAi; 23560; -. DR Pharos; Q9BZE4; Tchem. DR PRO; PR:Q9BZE4; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9BZE4; Protein. DR Bgee; ENSG00000107937; Expressed in sperm and 204 other cell types or tissues. DR ExpressionAtlas; Q9BZE4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL. DR GO; GO:0005525; F:GTP binding; IDA:HGNC-UCL. DR GO; GO:0003924; F:GTPase activity; IDA:HGNC-UCL. DR GO; GO:1990275; F:preribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:Ensembl. DR GO; GO:0030336; P:negative regulation of cell migration; IDA:HGNC-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:HGNC-UCL. DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:HGNC-UCL. DR GO; GO:0033342; P:negative regulation of collagen binding; IMP:HGNC-UCL. DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:HGNC-UCL. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:HGNC-UCL. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IDA:HGNC-UCL. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:HGNC-UCL. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:UniProtKB. DR CDD; cd01897; NOG; 1. DR Gene3D; 1.20.120.1190; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR006073; GTP-bd. DR InterPro; IPR024926; NOG1. DR InterPro; IPR041623; NOG1_N. DR InterPro; IPR010674; NOG1_Rossman_fold_dom. DR InterPro; IPR012973; NOG_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR45759:SF1; GTP-BINDING PROTEIN 4; 1. DR PANTHER; PTHR45759; NUCLEOLAR GTP-BINDING PROTEIN 1; 1. DR Pfam; PF06858; NOG1; 1. DR Pfam; PF17835; NOG1_N; 1. DR Pfam; PF08155; NOGCT; 1. DR PIRSF; PIRSF038919; NOG1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51710; G_OBG; 1. DR SWISS-2DPAGE; Q9BZE4; -. DR Genevisible; Q9BZE4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW GTP-binding; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Ribosome biogenesis; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8" FT CHAIN 2..634 FT /note="GTP-binding protein 4" FT /id="PRO_0000195023" FT DOMAIN 169..340 FT /note="OBG-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" FT REGION 495..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 529..634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 601..622 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 175..182 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" FT BINDING 221..225 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" FT BINDING 289..292 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 103 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 122 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 468 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 470 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 472 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT MOD_RES 522 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 558 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 103 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 332 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 534 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..116 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_056146" FT VAR_SEQ 1..47 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056147" FT VARIANT 525 FT /note="R -> H (in dbSNP:rs3207775)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_068801" FT CONFLICT 593 FT /note="Missing (in Ref. 1; AAD09830)" FT /evidence="ECO:0000305" SQ SEQUENCE 634 AA; 73964 MW; 0A05E65E65D6DB62 CRC64; MAHYNFKKIT VVPSAKDFID LTLSKTQRKT PTVIHKHYQI HRIRHFYMRK VKFTQQNYHD RLSQILTDFP KLDDIHPFYA DLMNILYDKD HYKLALGQIN IAKNLVDNVA KDYVRLMKYG DSLYRCKQLK RAALGRMCTV IKRQKQSLEY LEQVRQHLSR LPTIDPNTRT LLLCGYPNVG KSSFINKVTR ADVDVQPYAF TTKSLFVGHM DYKYLRWQVV DTPGILDHPL EDRNTIEMQA ITALAHLRAA VLYVMDLSEQ CGHGLREQLE LFQNIRPLFI NKPLIVVANK CDVKRIAELS EDDQKIFTDL QSEGFPVIET STLTEEGVIK VKTEACDRLL AHRVETKMKG NKVNEVLNRL HLAIPTRRDD KERPPFIPEG VVARRKRMET EESRKKRERD LELEMGDDYI LDLQKYWDLM NLSEKHDKIP EIWEGHNIAD YIDPAIMKKL EELEKEEELR TAAGEYDSVS ESEDEEMLEI RQLAKQIREK KKLKILESKE KNTQGPRMPR TAKKVQRTVL EKEMRSLGVD MDDKDDAHYA VQARRSRSIT RKRKREDSAP PSSVARSGSC SRTPRDVSGL RDVKMVKKAK TMMKNAQKKM NRLGKKGEAD RHVFDMKPKH LLSGKRKAGK KDRR //