GNL3_MOUSE
ID GNL3_MOUSE Reviewed; 538 AA.
AC Q8CI11; Q811R9; Q811S8; Q8BK21;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Guanine nucleotide-binding protein-like 3;
DE AltName: Full=Nucleolar GTP-binding protein 3;
DE AltName: Full=Nucleostemin;
GN Name=Gnl3; Synonyms=Ns;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=12464630; DOI=10.1101/gad.55671;
RA Tsai R.Y.L., McKay R.D.G.;
RT "A nucleolar mechanism controlling cell proliferation in stem and cancer
RT cells.";
RL Genes Dev. 16:2991-3003(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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-505, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-493 AND SER-505, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Spleen;
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).
RN [6]
RP FUNCTION, INTERACTION WITH MDM2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-256.
RX PubMed=21132010; DOI=10.1038/onc.2010.550;
RA Meng L., Hsu J.K., Tsai R.Y.;
RT "GNL3L depletion destabilizes MDM2 and induces p53-dependent G2/M arrest.";
RL Oncogene 30:1716-1726(2011).
CC -!- FUNCTION: May be required to maintain the proliferative capacity of
CC stem cells (By similarity). Stabilizes MDM2 by preventing its
CC ubiquitination, and hence proteasomal degradation. {ECO:0000250,
CC ECO:0000269|PubMed:21132010}.
CC -!- SUBUNIT: Interacts with MDM2; this interaction stabilizes MDM2.
CC Interaction with MDM2 occurs in the nucleoplasm and is triggered by a
CC nucleolar release mechanism, such as mitosis-induced nucleolar
CC disassembly. Indirectly interacts with TP53, via MDM2-binding (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21132010}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12464630}. Note=Shuttles between the
CC nucleus and nucleolus. {ECO:0000250|UniProtKB:Q811S9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q8CI11-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q8CI11-2; Sequence=VSP_013412;
CC -!- TISSUE SPECIFICITY: Expressed in the adult bone marrow population that
CC is enriched in hematopoietic stem cells. {ECO:0000269|PubMed:12464630}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 8.5 dpc and 10.5 dpc in the cerebral
CC cortex; expression declines rapidly from this point.
CC {ECO:0000269|PubMed:12464630}.
CC -!- DOMAIN: The basic domain (B) allows nucleolar localization in the
CC absence of GTP. The intermediate domain (I) inhibits nucleolar
CC localization by the B domain and is required for exit from the
CC nucleolus. Exit from the nucleolus to the nucleoplasm requires both the
CC I and the acidic (A) domains, and may be triggered by GTP hydrolysis
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AY181025; AAO19472.1; -; mRNA.
DR EMBL; AY185498; AAO19473.1; -; mRNA.
DR EMBL; AK077523; BAC36844.1; -; mRNA.
DR EMBL; BC037996; AAH37996.2; -; mRNA.
DR CCDS; CCDS26905.1; -. [Q8CI11-1]
DR RefSeq; NP_705775.2; NM_153547.6. [Q8CI11-1]
DR AlphaFoldDB; Q8CI11; -.
DR SMR; Q8CI11; -.
DR BioGRID; 205989; 42.
DR STRING; 10090.ENSMUSP00000047119; -.
DR iPTMnet; Q8CI11; -.
DR PhosphoSitePlus; Q8CI11; -.
DR SwissPalm; Q8CI11; -.
DR EPD; Q8CI11; -.
DR jPOST; Q8CI11; -.
DR MaxQB; Q8CI11; -.
DR PaxDb; Q8CI11; -.
DR PeptideAtlas; Q8CI11; -.
DR PRIDE; Q8CI11; -.
DR ProteomicsDB; 263382; -. [Q8CI11-1]
DR ProteomicsDB; 263383; -. [Q8CI11-2]
DR Antibodypedia; 31298; 544 antibodies from 40 providers.
DR DNASU; 30877; -.
DR Ensembl; ENSMUST00000037739; ENSMUSP00000047119; ENSMUSG00000042354. [Q8CI11-1]
DR GeneID; 30877; -.
DR KEGG; mmu:30877; -.
DR UCSC; uc007swi.3; mouse. [Q8CI11-1]
DR CTD; 26354; -.
DR MGI; MGI:1353651; Gnl3.
DR VEuPathDB; HostDB:ENSMUSG00000042354; -.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000158320; -.
DR HOGENOM; CLU_011106_5_3_1; -.
DR InParanoid; Q8CI11; -.
DR OMA; FKLDGLW; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q8CI11; -.
DR TreeFam; TF313085; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 30877; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Gnl3; mouse.
DR PRO; PR:Q8CI11; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CI11; protein.
DR Bgee; ENSMUSG00000042354; Expressed in embryonic post-anal tail and 92 other tissues.
DR ExpressionAtlas; Q8CI11; baseline and differential.
DR Genevisible; Q8CI11; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0017145; P:stem cell division; ISO:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:MGI.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; GTP-binding;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..538
FT /note="Guanine nucleotide-binding protein-like 3"
FT /id="PRO_0000122445"
FT DOMAIN 129..307
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..46
FT /note="Basic"
FT /evidence="ECO:0000250"
FT REGION 69..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..451
FT /note="Intermediate"
FT /evidence="ECO:0000250"
FT REGION 460..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..532
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT COILED 54..95
FT /evidence="ECO:0000255"
FT COMPBIAS 1..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 256..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 300..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811S9"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT VAR_SEQ 465..497
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12464630"
FT /id="VSP_013412"
FT MUTAGEN 256
FT /note="G->V: Mislocalized to the nucleoplasm. No effect on
FT MDM2-binding."
FT /evidence="ECO:0000269|PubMed:21132010"
FT CONFLICT 470
FT /note="R -> S (in Ref. 1; AAO19472)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="K -> Q (in Ref. 1; AAO19472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60786 MW; C092AD5305E5D69F CRC64;
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV PNSAPFKEAL
LREAELRKQQ LEELKQQQKL DRQKEQERKR KLEVSPGDEQ SNVETREESD EPKRKKAKAG
KQNPKKLHCQ ELKKVIEASD IVLEVLDARD PLGCRCPQIE EAVIQSGSKK LILVLNKSDL
VPKENLENWL NYLNKELPTV VFKASTNLKN RKTFKIKKKK VVPFQSKICC GKEALWKLLG
DFQQSCGKDI QVGVIGFPNV GKSSVINSLK QEWICNVGIS MGLTRSMQIV PLDKQITIID
SPCLIISPCN SPTALALRSP ASIEELRPLE AASAILSQAD NEQVVLKYTV PEYKDSLHFF
TKLAQRRGLH QKGGSPNVES AAKLVWSEWT GASLGYYCHP PASWNHSLHF NENIAAVMKK
GFNLEELEKN NAHSIQVLKG PHLTNRILFR SSGLTNGILD EKDIVEESPR QTEDKQDADD
QENGSGERNA EISDVAPVEE TRELSPEQST AGKPSDGSSA LDRASQEDET YDFTTDYI
