Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BZE4 (NOG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar GTP-binding protein 1
Alternative name(s):
Chronic renal failure gene protein
GTP-binding protein NGB
Gene names
Name:GTPBP4
Synonyms:CRFG, NOG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biogenesis of the 60S ribosomal subunit By similarity.

Subcellular location

Nucleusnucleolus Ref.2 Ref.7 Ref.8.

Sequence similarities

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

Contains 1 OBG-type G (guanine nucleotide-binding) domain.

Ontologies

Keywords
   Biological processRibosome biogenesis
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay PubMed 17210637. Source: GOC

negative regulation of DNA replication

Inferred from mutant phenotype PubMed 17210637. Source: HGNC

negative regulation of cell migration

Inferred from direct assay PubMed 17210637. Source: HGNC

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 17210637. Source: HGNC

negative regulation of cell-cell adhesion

Inferred from direct assay PubMed 17210637. Source: HGNC

negative regulation of collagen binding

Inferred from mutant phenotype PubMed 17210637. Source: HGNC

negative regulation of protein ubiquitination

Inferred from direct assay PubMed 17210637. Source: HGNC

protein stabilization

Inferred from direct assay PubMed 17210637. Source: HGNC

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 17210637. Source: HGNC

ribosome biogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay PubMed 17210637. Source: HGNC

nuclear membrane

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 17210637. Source: HGNC

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17210637. Source: HGNC

   Molecular_functionGTP binding

Inferred from direct assay PubMed 17210637. Source: HGNC

GTPase activity

Inferred from direct assay PubMed 17210637. Source: HGNC

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NF2P352409EBI-1056249,EBI-1014472

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 634633Nucleolar GTP-binding protein 1
PRO_0000195023

Regions

Domain169 – 340172OBG-type G
Nucleotide binding175 – 1828GTP Potential
Nucleotide binding221 – 2255GTP Potential
Nucleotide binding289 – 2924GTP Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue1031N6-acetyllysine Ref.13
Modified residue4681Phosphoserine Ref.11 Ref.12 Ref.14 Ref.16
Modified residue4701Phosphoserine Ref.11 Ref.12 Ref.14 Ref.16
Modified residue4721Phosphoserine Ref.11 Ref.12 Ref.14
Modified residue5221N6-acetyllysine Ref.13
Modified residue5581Phosphoserine Ref.11

Natural variations

Natural variant5251R → H. Ref.3
Corresponds to variant rs3207775 [ dbSNP | Ensembl ].
VAR_068801

Experimental info

Sequence conflict5931Missing in AAD09830. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9BZE4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0A05E65E65D6DB62

FASTA63473,964
        10         20         30         40         50         60 
MAHYNFKKIT VVPSAKDFID LTLSKTQRKT PTVIHKHYQI HRIRHFYMRK VKFTQQNYHD 

        70         80         90        100        110        120 
RLSQILTDFP KLDDIHPFYA DLMNILYDKD HYKLALGQIN IAKNLVDNVA KDYVRLMKYG 

       130        140        150        160        170        180 
DSLYRCKQLK RAALGRMCTV IKRQKQSLEY LEQVRQHLSR LPTIDPNTRT LLLCGYPNVG 

       190        200        210        220        230        240 
KSSFINKVTR ADVDVQPYAF TTKSLFVGHM DYKYLRWQVV DTPGILDHPL EDRNTIEMQA 

       250        260        270        280        290        300 
ITALAHLRAA VLYVMDLSEQ CGHGLREQLE LFQNIRPLFI NKPLIVVANK CDVKRIAELS 

       310        320        330        340        350        360 
EDDQKIFTDL QSEGFPVIET STLTEEGVIK VKTEACDRLL AHRVETKMKG NKVNEVLNRL 

       370        380        390        400        410        420 
HLAIPTRRDD KERPPFIPEG VVARRKRMET EESRKKRERD LELEMGDDYI LDLQKYWDLM 

       430        440        450        460        470        480 
NLSEKHDKIP EIWEGHNIAD YIDPAIMKKL EELEKEEELR TAAGEYDSVS ESEDEEMLEI 

       490        500        510        520        530        540 
RQLAKQIREK KKLKILESKE KNTQGPRMPR TAKKVQRTVL EKEMRSLGVD MDDKDDAHYA 

       550        560        570        580        590        600 
VQARRSRSIT RKRKREDSAP PSSVARSGSC SRTPRDVSGL RDVKMVKKAK TMMKNAQKKM 

       610        620        630 
NRLGKKGEAD RHVFDMKPKH LLSGKRKAGK KDRR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel GTP-binding protein, NGB."
Cheng J.Q., Cao C.H., Testa J.R., Golemis E.A., Jiang C., Yuan W., Nicosia S.V.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of a novel nuclear guanosine triphosphate-binding protein differentially expressed in renal disease."
Laping N.J., Olson B.A., Zhu Y.
J. Am. Soc. Nephrol. 12:883-890(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Kidney.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-525.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Uterus.
[7]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-7; 9-25; 37-42; 53-71; 94-111; 119-125; 146-155; 161-169; 191-213; 217-248; 267-276; 296-330; 353-359; 372-384; 398-425; 429-448; 450-460 AND 526-544, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470; SER-472 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470 AND SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470 AND SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF120334 mRNA. Translation: AAD09830.1.
AF325353 mRNA. Translation: AAK13444.1.
AK001548 mRNA. Translation: BAG50937.1.
AK001552 mRNA. Translation: BAA91752.1.
AL359878, AC022536 Genomic DNA. Translation: CAI13664.1.
CH471072 Genomic DNA. Translation: EAW86526.1.
BC038975 mRNA. Translation: AAH38975.1.
RefSeqNP_036473.2. NM_012341.2.
UniGeneHs.215766.

3D structure databases

ProteinModelPortalQ9BZE4.
SMRQ9BZE4. Positions 3-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117104. 19 interactions.
IntActQ9BZE4. 11 interactions.
MINTMINT-4728537.
STRING9606.ENSP00000354040.

PTM databases

PhosphoSiteQ9BZE4.

Polymorphism databases

DMDM17368711.

2D gel databases

SWISS-2DPAGEQ9BZE4.

Proteomic databases

PaxDbQ9BZE4.
PRIDEQ9BZE4.

Protocols and materials databases

DNASU23560.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360803; ENSP00000354040; ENSG00000107937.
GeneID23560.
KEGGhsa:23560.
UCSCuc001ift.3. human.

Organism-specific databases

CTD23560.
GeneCardsGC10P001034.
HGNCHGNC:21535. GTPBP4.
HPAHPA039618.
HPA056468.
neXtProtNX_Q9BZE4.
PharmGKBPA134922009.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1084.
HOGENOMHOG000164071.
HOVERGENHBG052642.
KOK06943.
OMAFMDIVLS.
OrthoDBEOG72G175.
PhylomeDBQ9BZE4.
TreeFamTF300430.

Gene expression databases

ArrayExpressQ9BZE4.
BgeeQ9BZE4.
CleanExHS_GTPBP4.
GenevestigatorQ9BZE4.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR006073. GTP_binding_domain.
IPR024926. NOG1.
IPR010674. NOG1_Rossman_fold_dom.
IPR012973. NOG_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamPF06858. NOG1. 1 hit.
PF08155. NOGCT. 1 hit.
[Graphical view]
PIRSFPIRSF038919. NOG1. 1 hit.
PRINTSPR00326. GTP1OBG.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51710. G_OBG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGTPBP4. human.
GeneWikiGTPBP4.
GenomeRNAi23560.
NextBio35468847.
PROQ9BZE4.

Entry information

Entry nameNOG1_HUMAN
AccessionPrimary (citable) accession number: Q9BZE4
Secondary accession number(s): B3KMC5 expand/collapse secondary AC list , O95446, Q5T3R8, Q9NVJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM