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Protein

Nucleolar GTP-binding protein 1

Gene

NOG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the biogenesis of the 60S ribosomal subunit.1 Publication

Miscellaneous

Present with 28000 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi174 – 181GTPPROSITE-ProRule annotation8
Nucleotide bindingi220 – 224GTPPROSITE-ProRule annotation5
Nucleotide bindingi288 – 291GTPPROSITE-ProRule annotation4

GO - Molecular functioni

  • GTP binding Source: SGD

GO - Biological processi

  • assembly of large subunit precursor of preribosome Source: SGD
  • ribosomal large subunit biogenesis Source: SGD
  • ribosomal subunit export from nucleus Source: SGD
  • rRNA processing Source: SGD

Keywordsi

Biological processRibosome biogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33997-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar GTP-binding protein 1
Gene namesi
Name:NOG1
Ordered Locus Names:YPL093W
ORF Names:LPG15W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL093W
SGDiS000006014 NOG1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001950351 – 647Nucleolar GTP-binding protein 1Add BLAST647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei563PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02892
PaxDbiQ02892
PRIDEiQ02892

PTM databases

iPTMnetiQ02892

Interactioni

Subunit structurei

Associated with nucleolar and cytoplasmic pre-60S particles. Directly interacts with RLP24.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi36088, 336 interactors
DIPiDIP-2785N
IntActiQ02892, 102 interactors
MINTiQ02892
STRINGi4932.YPL093W

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCTelectron microscopy3.08b1-647[»]
4V7Felectron microscopy8.70o1-647[»]
5FL8electron microscopy9.50o1-647[»]
5JCSelectron microscopy9.50o1-647[»]
6C0Felectron microscopy3.70W1-647[»]
6ELZelectron microscopy3.30b1-647[»]
6EM1electron microscopy3.60b1-647[»]
6EM5electron microscopy4.30b1-647[»]
ProteinModelPortaliQ02892
SMRiQ02892
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini168 – 340OBG-type GPROSITE-ProRule annotationAdd BLAST173

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000018475
HOGENOMiHOG000164071
InParanoidiQ02892
KOiK06943
OMAiSLYQCKQ
OrthoDBiEOG092C1W1B

Family and domain databases

InterProiView protein in InterPro
IPR031167 G_OBG
IPR006073 GTP_binding_domain
IPR024926 NOG1
IPR010674 NOG1_Rossman_fold_dom
IPR012973 NOG_C
IPR027417 P-loop_NTPase
PANTHERiPTHR11702:SF4 PTHR11702:SF4, 1 hit
PfamiView protein in Pfam
PF06858 NOG1, 1 hit
PF08155 NOGCT, 1 hit
PIRSFiPIRSF038919 NOG1, 1 hit
PRINTSiPR00326 GTP1OBG
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51710 G_OBG, 1 hit

Sequencei

Sequence statusi: Complete.

Q02892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLSWKDIPT VAPANDLLDI VLNRTQRKTP TVIRPGFKIT RIRAFYMRKV
60 70 80 90 100
KYTGEGFVEK FEDILKGFPN INDVHPFHRD LMDTLYEKNH YKISLAAISR
110 120 130 140 150
AKSLVEQVAR DYVRLLKFGQ SLFQCKQLKR AALGRMATIV KKLRDPLAYL
160 170 180 190 200
EQVRQHIGRL PSIDPNTRTL LICGYPNVGK SSFLRCITKS DVDVQPYAFT
210 220 230 240 250
TKSLYVGHFD YKYLRFQAID TPGILDRPTE EMNNIEMQSI YAIAHLRSCV
260 270 280 290 300
LYFMDLSEQC GFTIEAQVKL FHSIKPLFAN KSVMVVINKT DIIRPEDLDE
310 320 330 340 350
ERAQLLESVK EVPGVEIMTS SCQLEENVME VRNKACEKLL ASRIENKLKS
360 370 380 390 400
QSRINNVLNK IHVAQPQARD DVKRTPFIPE SVKNLKKYDP EDPNRRKLAR
410 420 430 440 450
DIEAENGGAG VFNVNLKDKY LLEDDEWKND IMPEILDGKN VYDFLDPEIA
460 470 480 490 500
AKLQALEEEE EKLENEGFYN SDDEEEIYDG FEASEVDDIK EKAAWIRNRQ
510 520 530 540 550
KTMIAEARNR KSLKNKAIMP RSKLTKSFGK MEEHMSTLGH DMSALQDKQN
560 570 580 590 600
RAARKNRYVE RGSDVVFGDQ DALTASTENG VKLRQTDRLL DGVADGSMRS
610 620 630 640
KADRMAKMER RERNRHAKQG ESDRHNAVSL SKHLFSGKRG VGKTDFR
Length:647
Mass (Da):74,410
Last modified:November 1, 1996 - v1
Checksum:i640324779AE4D716
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA Translation: AAB68206.1
BK006949 Genomic DNA Translation: DAA11340.1
PIRiS61973
RefSeqiNP_015232.1, NM_001183907.1

Genome annotation databases

EnsemblFungiiYPL093W; YPL093W; YPL093W
GeneIDi856012
KEGGisce:YPL093W

Similar proteinsi

Entry informationi

Entry nameiNOG1_YEAST
AccessioniPrimary (citable) accession number: Q02892
Secondary accession number(s): D6W3S4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 159 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health