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Q9BVP2 (GNL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein-like 3
Alternative name(s):
E2-induced gene 3 protein
Novel nucleolar protein 47
Short name=NNP47
Nucleolar GTP-binding protein 3
Nucleostemin
Gene names
Name:GNL3
Synonyms:E2IG3, NS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation By similarity. Ref.2 Ref.8

Subunit structure

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. Indirectly interacts with TP53, via MDM2-binding By similarity. Ref.8

Subcellular location

Nucleus By similarity. Nucleusnucleolus By similarity. Note: Shuttles between the nucleus and nucleolus By similarity. Ref.6 Ref.7 Ref.8

Tissue specificity

Increased levels in lung tissue in cancer patients. Ref.2

Domain

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 By similarity.

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.

Sequence similarities

Belongs to the MMR1/HSR1 GTP-binding protein family.

Contains 1 G (guanine nucleotide-binding) domain.

Sequence caution

The sequence AAF09482.1 differs from that shown. Reason: Frameshift at position 516.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BVP2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BVP2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 549549Guanine nucleotide-binding protein-like 3
PRO_0000122444

Regions

Domain266 – 34782G
Nucleotide binding178 – 1814GTP Potential
Nucleotide binding261 – 2688GTP Potential
Nucleotide binding305 – 3084GTP Potential
Region2 – 4645Basic By similarity
Region282 – 456175Intermediate By similarity
Region465 – 54379Acidic By similarity
Coiled coil56 – 9540 Potential

Amino acid modifications

Modified residue791N6-acetyllysine Ref.10
Modified residue5291Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 1212Missing in isoform 2.
VSP_013411
Natural variant391R → Q. Ref.1 Ref.2 Ref.5
Corresponds to variant rs11177 [ dbSNP | Ensembl ].
VAR_022160
Natural variant3671V → M. Ref.1 Ref.2 Ref.5 Ref.11
Corresponds to variant rs2289247 [ dbSNP | Ensembl ].
VAR_022161

Experimental info

Sequence conflict31R → K in AAV74413. Ref.2
Sequence conflict861L → Q in AAV74413. Ref.2
Sequence conflict4361N → D in AAV74413. Ref.2
Sequence conflict4631I → M in BAB55169. Ref.3
Sequence conflict4951V → A in AAV74413. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: F3928FE1C77C77F4

FASTA54961,993
        10         20         30         40         50         60 
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV PNSAPFKEAL 

        70         80         90        100        110        120 
LREAELRKQR LEELKQQQKL DRQKELEKKR KLETNPDIKP SNVEPMEKEF GLCKTENKAK 

       130        140        150        160        170        180 
SGKQNSKKLY CQELKKVIEA SDVVLEVLDA RDPLGCRCPQ VEEAIVQSGQ KKLVLILNKS 

       190        200        210        220        230        240 
DLVPKENLES WLNYLKKELP TVVFRASTKP KDKGKITKRV KAKKNAAPFR SEVCFGKEGL 

       250        260        270        280        290        300 
WKLLGGFQET CSKAIRVGVI GFPNVGKSSI INSLKQEQMC NVGVSMGLTR SMQVVPLDKQ 

       310        320        330        340        350        360 
ITIIDSPSFI VSPLNSSSAL ALRSPASIEV VKPMEAASAI LSQADARQVV LKYTVPGYRN 

       370        380        390        400        410        420 
SLEFFTVLAQ RRGMHQKGGI PNVEGAAKLL WSEWTGASLA YYCHPPTSWT PPPYFNESIV 

       430        440        450        460        470        480 
VDMKSGFNLE ELEKNNAQSI RAIKGPHLAN SILFQSSGLT NGIIEEKDIH EELPKRKERK 

       490        500        510        520        530        540 
QEEREDDKDS DQETVDEEVD ENSSGMFAAE ETGEALSEET TAGEQSTRSF ILDKIIEEDD 


AYDFSTDYV 

« Hide

Isoform 2 [UniParc].

Checksum: 342BCB22B4234056
Show »

FASTA53760,540

References

« Hide 'large scale' references
[1]"Effects of estrogen on global gene expression: identification of novel targets of estrogen action."
Charpentier A.H., Bednarek A.K., Daniel R.L., Hawkins K.A., Laflin K.J., Gaddis S., MacLeod M.C., Aldaz C.M.
Cancer Res. 60:5977-5983(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-39 AND MET-367.
[2]"Cloning of the nucleostemin gene and its function in transforming human embryonic bone marrow mesenchymal stem cells into F6 tumor cells."
Han C., Zhang X., Xu W., Wang W., Qian H., Chen Y.
Int. J. Mol. Med. 16:205-213(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANTS GLN-39 AND MET-367.
[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] (ISOFORMS 1 AND 2).
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1), VARIANTS GLN-39 AND MET-367.
Tissue: Eye.
[6]"Directed proteomic analysis of the human nucleolus."
Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I.
Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[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]"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: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
[9]"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-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: VARIANT [LARGE SCALE ANALYSIS] MET-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF191018 mRNA. Translation: AAF09482.1. Frameshift.
AY825265 mRNA. Translation: AAV74413.1.
AK027514 mRNA. Translation: BAB55168.1.
AK027516 mRNA. Translation: BAB55169.1.
AK315484 mRNA. Translation: BAG37868.1.
AC104446 Genomic DNA. No translation available.
BC001024 mRNA. Translation: AAH01024.1.
RefSeqNP_055181.3. NM_014366.4.
NP_996561.1. NM_206825.1.
NP_996562.1. NM_206826.1.
UniGeneHs.313544.

3D structure databases

ProteinModelPortalQ9BVP2.
SMRQ9BVP2. Positions 132-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117690. 60 interactions.
IntActQ9BVP2. 18 interactions.
MINTMINT-1405256.
STRING9606.ENSP00000395772.

PTM databases

PhosphoSiteQ9BVP2.

Polymorphism databases

DMDM229462872.

2D gel databases

SWISS-2DPAGEQ9BVP2.

Proteomic databases

PaxDbQ9BVP2.
PRIDEQ9BVP2.

Protocols and materials databases

DNASU26354.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394799; ENSP00000378278; ENSG00000163938. [Q9BVP2-2]
ENST00000418458; ENSP00000395772; ENSG00000163938. [Q9BVP2-1]
GeneID26354.
KEGGhsa:26354.
UCSCuc003dfd.3. human. [Q9BVP2-1]

Organism-specific databases

CTD26354.
GeneCardsGC03P052718.
H-InvDBHIX0003367.
HGNCHGNC:29931. GNL3.
HPACAB020770.
MIM608011. gene.
neXtProtNX_Q9BVP2.
PharmGKBPA134952132.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1161.
HOGENOMHOG000207716.
HOVERGENHBG051747.
InParanoidQ9BVP2.
KOK14538.
OMAKLYCQEL.
OrthoDBEOG7J9VPR.
PhylomeDBQ9BVP2.
TreeFamTF313085.

Gene expression databases

ArrayExpressQ9BVP2.
BgeeQ9BVP2.
CleanExHS_GNL3.
GenevestigatorQ9BVP2.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR014813. Gnl3_N_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF08701. GN3L_Grn1. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGNL3. human.
GeneWikiGNL3.
GenomeRNAi26354.
NextBio48693.
PROQ9BVP2.
SOURCESearch...

Entry information

Entry nameGNL3_HUMAN
AccessionPrimary (citable) accession number: Q9BVP2
Secondary accession number(s): B2RDC1 expand/collapse secondary AC list , Q5PU80, Q96SV6, Q96SV7, Q9UJY0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 117 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 3

Human chromosome 3: entries, gene names and cross-references to MIM