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Protein

Guanine nucleotide-binding protein-like 3

Gene

Gnl3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi176 – 1794GTPSequence analysis
Nucleotide bindingi256 – 2638GTPCurated
Nucleotide bindingi300 – 3034GTPSequence analysis

GO - Molecular functioni

  • GTP binding Source: UniProtKB
  • poly(A) RNA binding Source: Ensembl

GO - Biological processi

  • cell proliferation Source: RGD
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: Ensembl
  • regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein-like 3
Alternative name(s):
Nucleolar GTP-binding protein 3
Nucleostemin
Gene namesi
Name:Gnl3
Synonyms:Ns
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi631354. Gnl3.

Subcellular locationi

  • Nucleus 1 Publication
  • Nucleusnucleolus 2 Publications

  • Note: Shuttles between the nucleus and nucleolus (PubMed:15657390).1 Publication

GO - Cellular componenti

  • extracellular space Source: Ensembl
  • membrane Source: Ensembl
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561G → V: Abrogates GTP-binding and nucleolar localization. 1 Publication
Mutagenesisi261 – 2611G → V: Abrogates nucleolar localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Guanine nucleotide-binding protein-like 3PRO_0000122446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei95 – 951PhosphoserineBy similarity
Modified residuei101 – 1011PhosphoserineCombined sources
Modified residuei493 – 4931PhosphoserineBy similarity
Modified residuei505 – 5051PhosphoserineCombined sources
Modified residuei518 – 5181PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ811S9.
PRIDEiQ811S9.

PTM databases

iPTMnetiQ811S9.

Expressioni

Tissue specificityi

Expressed in testis.1 Publication

Developmental stagei

Expressed by developing CNS stem cells. When cortical stem cells differentiate into neurons, astrocytes, and oligodendrocytes, expression level is reduced in both dividing and postmitotic progeny.

Gene expression databases

GenevisibleiQ811S9. RN.

Interactioni

Subunit structurei

Interacts with MDM2; this interaction stabilizes MDM2. Interaction with MDM2 occurs in the nucleoplasm and is triggered by a nucleolar release mechanism, such as mitosis-induced nucleolar disassembly (By similarity). May interact with p53/TP53 via its basic domain. This interaction is most probably indirect and mediated by MDM2-binding (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035860.

Structurei

3D structure databases

ProteinModelPortaliQ811S9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 307179CP-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4645BasicAdd
BLAST
Regioni277 – 451175IntermediateAdd
BLAST
Regioni460 – 53273AcidicAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili54 – 9542Sequence analysisAdd
BLAST

Domaini

The basic domain (B) allows nucleolar localization in the absence of GTP. The intermediate domain (I) inhibits nucleolar localization by the B domain and is required for exit from the nucleolus. Exit from the nucleolus to the nucleoplasm requires both the I and the acidic (A) domains, and may be triggered by GTP hydrolysis.1 Publication
In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.1 Publication

Sequence similaritiesi

Belongs to the TRAFAC class YlqF/YawG GTPase family.PROSITE-ProRule annotation
Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2484. Eukaryota.
COG1161. LUCA.
GeneTreeiENSGT00810000125472.
HOGENOMiHOG000207716.
HOVERGENiHBG051747.
InParanoidiQ811S9.
KOiK14538.
OMAiEVCFGKE.
OrthoDBiEOG7J9VPR.
PhylomeDBiQ811S9.
TreeFamiTF313085.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030378. G_CP_dom.
IPR014813. Gnl3_N_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF08701. GN3L_Grn1. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q811S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPKKDPGV
60 70 80 90 100
PNSAPFKEAL LREAELRKQQ LEELKQQQKL DRQKEQERKR KLEISPDDEQ
110 120 130 140 150
SNVETQEESD EPKIKKAKSG KQNPKKLHCQ ELKKVIEASD IVLEVLDARD
160 170 180 190 200
PLGCRCPQVE EAVIQSGCKK LVLVLNKSDL VPKENLENWL TYLNKELPTV
210 220 230 240 250
VFKASTNLKN RKKTFKIKKK VVPFQSKLCC GKEALWKLLG GFQQSCGKGV
260 270 280 290 300
QVGVVGFPNV GKSSIINSLK QERICSVGVS MGLTRSMQIV PLDKQITIID
310 320 330 340 350
SPCFIISPCN SPAALALRSP ASIEVLRPLE AASAILSQAD SQQVVLKYTV
360 370 380 390 400
PGYKDSLDFF TKLAQRRGLH QKGGSPNVES AAKLLWSEWT GASLGYYCHP
410 420 430 440 450
PASWNHSPHF NENITAIMKR GFNLEELEKN NAHSIQVLKG PHLTNKILFR
460 470 480 490 500
SSGLTNGILE EKDIPEESPK QTEDQQDGDD QEHVTGEKNA EISDVTPVEE
510 520 530
TREMSPGQST ASKPSDRSFI LDKMSEEDDA YDFTTDYI
Length:538
Mass (Da):60,661
Last modified:June 1, 2003 - v1
Checksum:i936DF707F31A62CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY181024 mRNA. Translation: AAO19471.1.
BC093602 mRNA. Translation: AAH93602.1.
RefSeqiNP_783170.1. NM_175580.2.
UniGeneiRn.4110.

Genome annotation databases

EnsembliENSRNOT00000033677; ENSRNOP00000035860; ENSRNOG00000028461.
GeneIDi290556.
KEGGirno:290556.
UCSCiRGD:631354. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY181024 mRNA. Translation: AAO19471.1.
BC093602 mRNA. Translation: AAH93602.1.
RefSeqiNP_783170.1. NM_175580.2.
UniGeneiRn.4110.

3D structure databases

ProteinModelPortaliQ811S9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035860.

PTM databases

iPTMnetiQ811S9.

Proteomic databases

PaxDbiQ811S9.
PRIDEiQ811S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000033677; ENSRNOP00000035860; ENSRNOG00000028461.
GeneIDi290556.
KEGGirno:290556.
UCSCiRGD:631354. rat.

Organism-specific databases

CTDi26354.
RGDi631354. Gnl3.

Phylogenomic databases

eggNOGiKOG2484. Eukaryota.
COG1161. LUCA.
GeneTreeiENSGT00810000125472.
HOGENOMiHOG000207716.
HOVERGENiHBG051747.
InParanoidiQ811S9.
KOiK14538.
OMAiEVCFGKE.
OrthoDBiEOG7J9VPR.
PhylomeDBiQ811S9.
TreeFamiTF313085.

Miscellaneous databases

PROiQ811S9.

Gene expression databases

GenevisibleiQ811S9. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030378. G_CP_dom.
IPR014813. Gnl3_N_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF08701. GN3L_Grn1. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A nucleolar mechanism controlling cell proliferation in stem and cancer cells."
    Tsai R.Y.L., McKay R.D.G.
    Genes Dev. 16:2991-3003(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "A multistep, GTP-driven mechanism controlling the dynamic cycling of nucleostemin."
    Tsai R.Y.L., McKay R.D.G.
    J. Cell Biol. 168:179-184(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAINS, MUTAGENESIS OF GLY-256 AND GLY-261.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGNL3_RAT
AccessioniPrimary (citable) accession number: Q811S9
Secondary accession number(s): Q566E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.