NOG2_MOUSE
ID NOG2_MOUSE Reviewed; 728 AA.
AC Q99LH1; B1ASC3; Q8BIF8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Nucleolar GTP-binding protein 2;
GN Name=Gnl2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: GTPase that associates with pre-60S ribosomal subunits in the
CC nucleolus and is required for their nuclear export and maturation. May
CC promote cell proliferation possibly by increasing p53/TP53 protein
CC levels, and consequently those of its downstream product CDKN1A/p21,
CC and decreasing RPL23A protein levels. {ECO:0000250|UniProtKB:Q13823}.
CC -!- SUBUNIT: Interacts with LYAR and RPL23A. Interacts with the nuclear
CC importin-beta receptor and, at a lower extent, with importin-alpha.
CC {ECO:0000250|UniProtKB:Q13823}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q13823}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AK077532; BAC36850.1; -; mRNA.
DR EMBL; AL626775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003262; AAH03262.1; -; mRNA.
DR CCDS; CCDS18634.1; -.
DR RefSeq; NP_663527.2; NM_145552.2.
DR AlphaFoldDB; Q99LH1; -.
DR SMR; Q99LH1; -.
DR BioGRID; 231010; 34.
DR CORUM; Q99LH1; -.
DR IntAct; Q99LH1; 2.
DR MINT; Q99LH1; -.
DR STRING; 10090.ENSMUSP00000030684; -.
DR iPTMnet; Q99LH1; -.
DR PhosphoSitePlus; Q99LH1; -.
DR EPD; Q99LH1; -.
DR MaxQB; Q99LH1; -.
DR PaxDb; Q99LH1; -.
DR PRIDE; Q99LH1; -.
DR ProteomicsDB; 253093; -.
DR Antibodypedia; 31740; 181 antibodies from 29 providers.
DR DNASU; 230737; -.
DR Ensembl; ENSMUST00000030684; ENSMUSP00000030684; ENSMUSG00000028869.
DR GeneID; 230737; -.
DR KEGG; mmu:230737; -.
DR UCSC; uc008uro.2; mouse.
DR CTD; 29889; -.
DR MGI; MGI:2385207; Gnl2.
DR VEuPathDB; HostDB:ENSMUSG00000028869; -.
DR eggNOG; KOG2423; Eukaryota.
DR GeneTree; ENSGT00810000125524; -.
DR HOGENOM; CLU_011106_4_1_1; -.
DR InParanoid; Q99LH1; -.
DR OMA; HKHKKFR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q99LH1; -.
DR TreeFam; TF105668; -.
DR BioGRID-ORCS; 230737; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Gnl2; mouse.
DR PRO; PR:Q99LH1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99LH1; protein.
DR Bgee; ENSMUSG00000028869; Expressed in floor plate of midbrain and 269 other tissues.
DR ExpressionAtlas; Q99LH1; baseline and differential.
DR Genevisible; Q99LH1; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR024929; NOG2.
DR InterPro; IPR012971; NOG2_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11089:SF9; PTHR11089:SF9; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF08153; NGP1NT; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis.
FT CHAIN 1..728
FT /note="Nucleolar GTP-binding protein 2"
FT /id="PRO_0000215807"
FT DOMAIN 207..368
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..582
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 361..365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13823"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 176
FT /note="Q -> K (in Ref. 1; BAC36850)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="L -> I (in Ref. 3; AAH03262)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="R -> S (in Ref. 1; BAC36850)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="D -> V (in Ref. 3; AAH03262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 83345 MW; AB449483ABEFE956 CRC64;
MVKPKYKGRS TINRSAASTN PDRVQGAGGQ NMRDRGTIRR LNMYRQKERR NSRGKVIKPL
QYQSTVASGT VARVEPNIKW FGNTRVIKQA SLQKFQEEMD KVMKDPYKVV MKQSKLPMSL
LHDRIQPHNA KVHILDTESF ESTFGPKSQR KRPNLFASDM QSLLENAEMS TESYDQGKDR
DLVMEDTGVR NEAQEEIYKK GQSKRIWGEL YKVIDSSDVV VQVLDARDPM GTRSPHIEAY
LKKEKPWKHL IFVLNKCDLV PTWATKRWVA VLSQDYPTLA FHASLTNPFG KGAFIQLLRQ
FGKLHTDKKQ ISVGFIGYPN VGKSSVINTL RSKKVCNVAP IAGETKVWQY ITLMRRIFLI
DCPGVVYPSE DSETDIVLKG VVQVEKIKAP QDHIGAVLER AKPEYISKTY KIESWENAED
FLEKLALRTG KLLKGGEPDM LTVSKMVLND WQRGRIPFFV KPPNAELPTD SQLPPSSPLE
VPTETTQNNP EEETTETEVE RSDSITEKEP EGDCSQDRNS EMQQILARVR QNFGKINVGP
QFSADDLVPV EMSDLEDLES SGEEEEQEQE QPGEDAEEER SPDTQEEPVG NDTKAVLRAL
DEKIAKYQRF LNKAKAKKFS AVRISKDLSE KVFAKYKEEK KTSAEDSDAA PTKKARKWDA
QMEEEPSNKT QRMLTCKERR RAARQQQSKK VGVRYYETHN VKNRNRNKKK TSDSEGQKHR
RNKFRQKQ
