NOG2_HUMAN
ID NOG2_HUMAN Reviewed; 731 AA.
AC Q13823; Q9BWN7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Nucleolar GTP-binding protein 2;
DE AltName: Full=Autoantigen NGP-1;
GN Name=GNL2; Synonyms=NGP1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Mammary carcinoma;
RX PubMed=8822211;
RA Racevskis J., Dill A., Stockert R., Fineberg S.A.;
RT "Cloning of a novel nucleolar guanosine 5'-triphosphate binding protein
RT autoantigen from a breast tumor.";
RL Cell Growth Differ. 7:271-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Muscle;
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 [3]
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 [4]
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 [5]
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 [6]
RP INTERACTION WITH IMPORTIN-ALPHA AND IMPORTIN-BETA, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 33-ARG--ARG-35; 39-ARG-ARG-40;
RP 49-ARG-ARG-50; 227-ARG--PRO-229; ASP-258; LYS-323; SER-324; SER-325;
RP 343-GLY--THR-345; 363-PRO-GLY-364; PRO-463; PRO-475; 682-ARG--ARG-684;
RP 711-LYS--LYS-713 AND 724-ARG--LYS-726.
RX PubMed=21495629; DOI=10.1021/bi200425b;
RA Chennupati V., Datta D., Rao M.R., Boddapati N., Kayasani M.,
RA Sankaranarayanan R., Mishra M., Seth P., Mani C., Mahalingam S.;
RT "Signals and pathways regulating nucleolar retention of novel putative
RT nucleolar GTPase NGP-1(GNL-2).";
RL Biochemistry 50:4521-4536(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION, AND INTERACTION WITH LYAR AND RPL23A.
RX PubMed=26203195; DOI=10.1074/jbc.m115.637280;
RA Datta D., Anbarasu K., Rajabather S., Priya R.S., Desai P., Mahalingam S.;
RT "Nucleolar GTP-binding protein-1 (NGP-1) promotes G1 to S phase transition
RT by activating cyclin-dependent kinase inhibitor p21 Cip1/Waf1.";
RL J. Biol. Chem. 290:21536-21552(2015).
RN [9] {ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS) IN COMPLEX WITH THE 60S
RP RIBOSOME, AND FUNCTION.
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: GTPase that associates with pre-60S ribosomal subunits in the
CC nucleolus and is required for their nuclear export and maturation
CC (PubMed:32669547). May promote cell proliferation possibly by
CC increasing p53/TP53 protein levels, and consequently those of its
CC downstream product CDKN1A/p21, and decreasing RPL23A protein levels
CC (PubMed:26203195). {ECO:0000269|PubMed:26203195,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Interacts with LYAR and RPL23A (PubMed:26203195). Interacts
CC with the nuclear importin-beta receptor and, at a lower extent, with
CC importin-alpha (PubMed:21495629). {ECO:0000269|PubMed:21495629,
CC ECO:0000269|PubMed:26203195}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:21495629}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression level
CC in testis. {ECO:0000269|PubMed:8822211}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in actively dividing cells, including
CC in peripheral blood mononuclear cells stimulated with Concanavalin-A.
CC Down-regulated in differentiating cells, including in neural precursor
CC cells induced to differentiate into astrocytes.
CC {ECO:0000269|PubMed:21495629}.
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; L05425; AAC37588.1; -; mRNA.
DR EMBL; BC000107; AAH00107.1; -; mRNA.
DR EMBL; BC009250; AAH09250.1; -; mRNA.
DR CCDS; CCDS421.1; -.
DR RefSeq; NP_037417.1; NM_013285.2.
DR PDB; 6LSS; EM; 3.23 A; 1=1-731.
DR PDB; 6LU8; EM; 3.13 A; 1=1-731.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR AlphaFoldDB; Q13823; -.
DR SMR; Q13823; -.
DR BioGRID; 118942; 331.
DR IntAct; Q13823; 80.
DR MINT; Q13823; -.
DR STRING; 9606.ENSP00000362153; -.
DR GlyGen; Q13823; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13823; -.
DR MetOSite; Q13823; -.
DR PhosphoSitePlus; Q13823; -.
DR SwissPalm; Q13823; -.
DR BioMuta; GNL2; -.
DR SWISS-2DPAGE; Q13823; -.
DR EPD; Q13823; -.
DR jPOST; Q13823; -.
DR MassIVE; Q13823; -.
DR PaxDb; Q13823; -.
DR PeptideAtlas; Q13823; -.
DR PRIDE; Q13823; -.
DR ProteomicsDB; 59695; -.
DR Antibodypedia; 31740; 181 antibodies from 29 providers.
DR DNASU; 29889; -.
DR Ensembl; ENST00000373062.8; ENSP00000362153.3; ENSG00000134697.13.
DR GeneID; 29889; -.
DR KEGG; hsa:29889; -.
DR MANE-Select; ENST00000373062.8; ENSP00000362153.3; NM_013285.3; NP_037417.1.
DR CTD; 29889; -.
DR DisGeNET; 29889; -.
DR GeneCards; GNL2; -.
DR HGNC; HGNC:29925; GNL2.
DR HPA; ENSG00000134697; Low tissue specificity.
DR MIM; 609365; gene.
DR neXtProt; NX_Q13823; -.
DR OpenTargets; ENSG00000134697; -.
DR PharmGKB; PA134944852; -.
DR VEuPathDB; HostDB:ENSG00000134697; -.
DR eggNOG; KOG2423; Eukaryota.
DR GeneTree; ENSGT00810000125524; -.
DR HOGENOM; CLU_011106_4_1_1; -.
DR InParanoid; Q13823; -.
DR OMA; HKHKKFR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q13823; -.
DR TreeFam; TF105668; -.
DR PathwayCommons; Q13823; -.
DR SignaLink; Q13823; -.
DR BioGRID-ORCS; 29889; 732 hits in 1087 CRISPR screens.
DR ChiTaRS; GNL2; human.
DR GeneWiki; GNL2; -.
DR GenomeRNAi; 29889; -.
DR Pharos; Q13823; Tbio.
DR PRO; PR:Q13823; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13823; protein.
DR Bgee; ENSG00000134697; Expressed in tendon of biceps brachii and 202 other tissues.
DR ExpressionAtlas; Q13823; baseline and differential.
DR Genevisible; Q13823; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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 3D-structure; Acetylation; GTP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..731
FT /note="Nucleolar GTP-binding protein 2"
FT /id="PRO_0000215806"
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 481..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..731
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 555..586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..722
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:0007744|PubMed:22814378"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99LH1"
FT VARIANT 452
FT /note="Q -> H (in dbSNP:rs12025870)"
FT /id="VAR_050291"
FT MUTAGEN 33..35
FT /note="RDR->ADA: Diffused nuclear localization, loss of
FT nucleolar localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 39..40
FT /note="RR->AA: Diffused nuclear localization, loss of
FT nucleolar localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 39..40
FT /note="RR->AA: No effect on nucleolar localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 49..50
FT /note="RR->AA: Diffused nuclear localization, loss of
FT nucleolar localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 227..229
FT /note="RDP->AAA: Loss of GTP-binding. Efficient
FT localization to the nucleus, but excluded from nucleoli."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 258
FT /note="D->A: Loss of GTP-binding. Punctate pattern
FT throughout the nucleus, including nucleoli."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 323
FT /note="K->A: No effect on GTP-binding, nor on nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 324
FT /note="S->A: No effect on GTP-binding, nor on nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 325
FT /note="S->A: No effect on GTP-binding, nor on nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 343..345
FT /note="GET->AEA: No effect on GTP-binding, nor on nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 363..364
FT /note="PG->AA: No effect on GTP-binding, nor on nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 463
FT /note="P->A: No effect on nucleolar localization; when
FT associated with A-475."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 475
FT /note="P->A: No effect on nucleolar localization; when
FT associated with A-463."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 682..684
FT /note="RRR->AAA: No effect on nucleolar localization.
FT Predominantly cytoplasmic, with some nucleolar staining;
FT when associated with 711-AAA-713. Diffused localization to
FT both cytoplasm and nucleus; when associated with 711-AAA-
FT 713 and 724-AAA-726."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 711..713
FT /note="KKK->AAA: No effect on nucleolar localization
FT Predominantly cytoplasmic, with some nucleolar staining;
FT when associated with 682-AAA-684. Strong nucleolar
FT localization, with some cytoplasmic staining; when
FT associated with 724-AAA-726. Diffused localization to both
FT cytoplasm and nucleus; when associated with 682-AAA-684 and
FT 724-AAA-726."
FT /evidence="ECO:0000269|PubMed:21495629"
FT MUTAGEN 724..726
FT /note="RKK->AAA: No effect on nucleolar localization.
FT Strong nucleolar localization, with some cytoplasmic
FT staining; when associated with 711-AAA-713. Diffused
FT localization to both cytoplasm and nucleus; when associated
FT with 682-AAA-684 and 711-AAA-713."
FT /evidence="ECO:0000269|PubMed:21495629"
FT CONFLICT 284
FT /note="S -> I (in Ref. 2; AAH00107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 83655 MW; E90C638B58C0886E CRC64;
MVKPKYKGRS TINPSKASTN PDRVQGAGGQ NMRDRATIRR LNMYRQKERR NSRGKIIKPL
QYQSTVASGT VARVEPNIKW FGNTRVIKQS SLQKFQEEMD TVMKDPYKVV MKQSKLPMSL
LHDRIRPHNL KVHILDTESF ETTFGPKSQR KRPNLFASDM QSLIENAEMS TESYDQGKDR
DLVTEDTGVR NEAQEEIYKK GQSKRIWGEL YKVIDSSDVV VQVLDARDPM GTRSPHIETY
LKKEKPWKHL IFVLNKCDLV PTWATKRWVA VLSQDYPTLA FHASLTNPFG KGAFIQLLRQ
FGKLHTDKKQ ISVGFIGYPN VGKSSVINTL RSKKVCNVAP IAGETKVWQY ITLMRRIFLI
DCPGVVYPSE DSETDIVLKG VVQVEKIKSP EDHIGAVLER AKPEYISKTY KIDSWENAED
FLEKLAFRTG KLLKGGEPDL QTVGKMVLND WQRGRIPFFV KPPNAEPLVA PQLLPSSSLE
VVPEAAQNNP GEEVTETAGE GSESIIKEET EENSHCDANT EMQQILTRVR QNFGKINVVP
QFSGDDLVPV EVSDLEEELE SFSDEEEEEQ EQQRDDAEES SSEPEEENVG NDTKAVIKAL
DEKIAKYQKF LDKAKAKKFS AVRISKGLSE KIFAKPEEQR KTLEEDVDDR APSKKGKKRK
AQREEEQEHS NKAPRALTSK ERRRAVRQQR PKKVGVRYYE THNVKNRNRN KKKTNDSEGQ
KHKRKKFRQK Q
