GTPB4_HUMAN
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 03-AUG-2022, entry version 196.
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; 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 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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20] {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 {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}.
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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 PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR AlphaFoldDB; Q9BZE4; -.
DR SMR; Q9BZE4; -.
DR BioGRID; 117104; 364.
DR IntAct; Q9BZE4; 135.
DR MINT; Q9BZE4; -.
DR STRING; 9606.ENSP00000354040; -.
DR ChEMBL; CHEMBL4105780; -.
DR iPTMnet; Q9BZE4; -.
DR PhosphoSitePlus; Q9BZE4; -.
DR SwissPalm; Q9BZE4; -.
DR BioMuta; GTPBP4; -.
DR DMDM; 17368711; -.
DR SWISS-2DPAGE; Q9BZE4; -.
DR EPD; Q9BZE4; -.
DR jPOST; Q9BZE4; -.
DR MassIVE; Q9BZE4; -.
DR MaxQB; Q9BZE4; -.
DR PaxDb; Q9BZE4; -.
DR PeptideAtlas; Q9BZE4; -.
DR PRIDE; Q9BZE4; -.
DR ProteomicsDB; 5488; -.
DR ProteomicsDB; 6843; -.
DR ProteomicsDB; 79822; -. [Q9BZE4-1]
DR Antibodypedia; 23768; 192 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 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 PhylomeDB; Q9BZE4; -.
DR TreeFam; TF300430; -.
DR PathwayCommons; Q9BZE4; -.
DR SignaLink; Q9BZE4; -.
DR BioGRID-ORCS; 23560; 819 hits in 1086 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 202 other tissues.
DR ExpressionAtlas; Q9BZE4; baseline and differential.
DR Genevisible; Q9BZE4; HS.
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: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; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
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
