GTPB4_MOUSE
ID GTPB4_MOUSE Reviewed; 634 AA.
AC Q99ME9; Q99K16; Q99P78; Q9CT02;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng J.Q.;
RT "Cloning and characterization of a mouse GTP-binding protein, NGB.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
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].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-347.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470 AND SER-472, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC {ECO:0000250|UniProtKB:Q9BZE4}.
CC -!- SUBUNIT: Associates with pre-60S ribosomal particles. Interacts with
CC MINAS-60 (product of an alternative open reading frame of RBM10).
CC {ECO:0000250|UniProtKB:Q9BZE4}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9BZE4}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11316846}.
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; AF348208; AAK19749.1; -; mRNA.
DR EMBL; AF325354; AAK13445.1; -; mRNA.
DR EMBL; BC005514; AAH05514.1; -; mRNA.
DR EMBL; BC025431; AAH25431.1; -; mRNA.
DR EMBL; AK011580; BAB27714.1; -; mRNA.
DR CCDS; CCDS26236.1; -.
DR RefSeq; NP_081276.2; NM_027000.4.
DR AlphaFoldDB; Q99ME9; -.
DR SMR; Q99ME9; -.
DR BioGRID; 213310; 42.
DR CORUM; Q99ME9; -.
DR IntAct; Q99ME9; 5.
DR MINT; Q99ME9; -.
DR STRING; 10090.ENSMUSP00000021574; -.
DR iPTMnet; Q99ME9; -.
DR PhosphoSitePlus; Q99ME9; -.
DR SwissPalm; Q99ME9; -.
DR EPD; Q99ME9; -.
DR MaxQB; Q99ME9; -.
DR PaxDb; Q99ME9; -.
DR PeptideAtlas; Q99ME9; -.
DR PRIDE; Q99ME9; -.
DR ProteomicsDB; 252983; -.
DR Antibodypedia; 23768; 192 antibodies from 33 providers.
DR Ensembl; ENSMUST00000222098; ENSMUSP00000152412; ENSMUSG00000021149.
DR GeneID; 69237; -.
DR KEGG; mmu:69237; -.
DR UCSC; uc007pkp.1; mouse.
DR CTD; 23560; -.
DR MGI; MGI:1916487; Gtpbp4.
DR VEuPathDB; HostDB:ENSMUSG00000021149; -.
DR eggNOG; KOG1490; Eukaryota.
DR GeneTree; ENSGT00390000018475; -.
DR HOGENOM; CLU_011784_4_1_1; -.
DR InParanoid; Q99ME9; -.
DR OMA; EWKNDVM; -.
DR OrthoDB; 678655at2759; -.
DR PhylomeDB; Q99ME9; -.
DR TreeFam; TF300430; -.
DR BioGRID-ORCS; 69237; 28 hits in 76 CRISPR screens.
DR ChiTaRS; Gtpbp4; mouse.
DR PRO; PR:Q99ME9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99ME9; protein.
DR Bgee; ENSMUSG00000021149; Expressed in otic placode and 264 other tissues.
DR ExpressionAtlas; Q99ME9; baseline and differential.
DR Genevisible; Q99ME9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005525; F:GTP binding; ISS:HGNC-UCL.
DR GO; GO:0003924; F:GTPase activity; ISS:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:HGNC-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:HGNC-UCL.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:HGNC-UCL.
DR GO; GO:0033342; P:negative regulation of collagen binding; ISS:HGNC-UCL.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISS:HGNC-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0050821; P:protein stabilization; ISS:HGNC-UCL.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS: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 Acetylation; GTP-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT CHAIN 2..634
FT /note="GTP-binding protein 4"
FT /id="PRO_0000195024"
FT DOMAIN 169..340
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT REGION 494..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..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:0000250|UniProtKB:Q9BZE4"
FT MOD_RES 103
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT CONFLICT 17
FT /note="D -> E (in Ref. 3; AAH05514)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..222
FT /note="DT -> TY (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> K (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> T (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="V -> A (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="E -> K (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..343
FT /note="AHR -> THG (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="D -> E (in Ref. 2; AAK13445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 74113 MW; 642F42BF8C717D6B CRC64;
MAHYNFKKIT VVPSAKDFID LTLSKTQRKT PTVIHKHYQI HRIRHFYMRK VKFTQQNYHD
RLSQILSDFP KLDDIHPFYA DLMNILYDKD HYKLALGQIN IAKNLVDNVA KDYVRLMKYG
DSLYRCKQLK RAALGRMCTI IKRQRQSLEY LEQVRQHLSR LPTIDPNTRT LLLCGYPNVG
KSSFINKVTR ADVDVQPYAF TTKSLFVGHM DYKYLRWQVV DTPGILDHPL EDRNTIEMQA
ITALAHLRAA VLYVMDLSEQ CGHGLKEQLE LFQNIRPLFI NKPLIVVANK CDVKRIAELS
EEDQKIFLDL QAEGFPVIET STLTEEGVIQ VKTEACDRLL AHRVETKMKG NKVNEVLNRL
HLAVPNKRDD KERPPFIPEG VIARRKRMEI EEPKKKRERD LELEMGDDYI LDLQKYWDLM
NSSEKYDKIP EIWEGHNVAD YIDPAIMKKL EELEKEEELR TAAGEYDSDS ESEDEEMMEI
RQLAKQIREK KKLKILQSKE KNKQGPRMPR TAKKVQRADL ENEMRSLGVD MDDKNNAHYA
VQARRSRSVT RKRKREESVP PSSTARSRSC SRTPRDVSGL RDVKMVKKAK TMMKKAQKKM
NRLGKKGEAD RHVFDMKPKH LLSGKRKAGK KDRR
