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Q9NVN8 (GNL3L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 105. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein-like 3-like protein
Gene names
Name:GNL3L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP. Ref.4 Ref.5 Ref.6 Ref.7

Subunit structure

Interacts with MDM2; this interaction, which occurs in the nucleoplasm, stabilizes MDM2. Indirectly interacts with TP53, via MDM2-binding. Interacts with TERF1; this interaction probably occurs in the nucleoplasm and is increased during mitosis, when the nucleolus is disassembled. This binding may promote TERF1 homodimerization. Interacts with TERT. Ref.6 Ref.7

Subcellular location

Nucleusnucleolus Ref.5.

Developmental stage

Up-regulated during mitosis and down-regulated in the G1 phase. Ref.6

Domain

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.

Ontologies

Keywords
   Biological processRibosome biogenesis
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandGTP-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processribosome biogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentmitochondrion

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDM2Q009878EBI-746682,EBI-389668

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 582582Guanine nucleotide-binding protein-like 3-like protein
PRO_0000284381

Regions

Domain264 – 32057G
Nucleotide binding173 – 1764GTP Potential
Nucleotide binding259 – 2668GTP Potential
Nucleotide binding303 – 3064GTP Potential
Region9 – 3527Required for nucleolar localization
Coiled coil58 – 8831 Potential

Natural variations

Natural variant3201R → H.
Corresponds to variant rs2298284 [ dbSNP | Ensembl ].
VAR_049495

Experimental info

Mutagenesis9 – 102KK → AA: Loss of nucleolar localization; when associated with 34-A-A-35. Loss of nuclear location; when associated with 19-A-A-20.
Mutagenesis19 – 202KK → AA: Loss of nuclear location; when associated with 9-A-A-10. Loss of nuclear location; when associated with 34-A-A-35.
Mutagenesis34 – 352KK → AA: Loss of nucleolar localization; when associated with 9-A-A-10. Loss of nuclear location; when associated with 19-A-A-20.
Mutagenesis145 – 1473RDP → AAA: Loss of GTP binding. Loss of nucleolar localization. No effect on nuclear localization. Ref.5
Mutagenesis309 – 3102PG → AA: Loss of nucleolar localization. No effect on nuclear localization.

Sequences

Sequence LengthMass (Da)Tools
Q9NVN8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B65EE072424F54BC

FASTA58265,573
        10         20         30         40         50         60 
MMKLRHKNKK PGEGSKGHKK ISWPYPQPAK QNGKKATSKV PSAPHFVHPN DHANREAELK 

        70         80         90        100        110        120 
KKWVEEMREK QQAAREQERQ KRRTIESYCQ DVLRRQEEFE HKEEVLQELN MFPQLDDEAT 

       130        140        150        160        170        180 
RKAYYKEFRK VVEYSDVILE VLDARDPLGC RCFQMEEAVL RAQGNKKLVL VLNKIDLVPK 

       190        200        210        220        230        240 
EVVEKWLDYL RNELPTVAFK ASTQHQVKNL NRCSVPVDQA SESLLKSKAC FGAENLMRVL 

       250        260        270        280        290        300 
GNYCRLGEVR THIRVGVVGL PNVGKSSLIN SLKRSRACSV GAVPGITKFM QEVYLDKFIR 

       310        320        330        340        350        360 
LLDAPGIVPG PNSEVGTILR NCVHVQKLAD PVTPVETILQ RCNLEEISNY YGVSGFQTTE 

       370        380        390        400        410        420 
HFLTAVAHRL GKKKKGGLYS QEQAAKAVLA DWVSGKISFY IPPPATHTLP THLSAEIVKE 

       430        440        450        460        470        480 
MTEVFDIEDT EQANEDTMEC LATGESDELL GDTDPLEMEI KLLHSPMTKI ADAIENKTTV 

       490        500        510        520        530        540 
YKIGDLTGYC TNPNRHQMGW AKRNVDHRPK SNSMVDVCSV DRRSVLQRIM ETDPLQQGQA 

       550        560        570        580 
LASALKNKKK MQKRADKIAS KLSDSMMSAL DLSGNADDGV GD 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: Lung.
[4]"The homologous putative GTPases Grn1p from fission yeast and the human GNL3L are required for growth and play a role in processing of nucleolar pre-rRNA."
Du X., Rao M.R.K.S., Chen X.Q., Wu W., Mahalingam S., Balasundaram D.
Mol. Biol. Cell 17:460-474(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"A novel lysine-rich domain and GTP binding motifs regulate the nucleolar retention of human guanine nucleotide binding protein, GNL3L."
Rao M.R.K.S., Kumari G., Balasundaram D., Sankaranarayanan R., Mahalingam S.
J. Mol. Biol. 364:637-654(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 9-LYS-LYS-10; 19-LYS-LYS-20; 34-LYS-LYS-35; 145-ARG--PRO-147 AND 309-PRO-GLY-310.
[6]"GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TERF1, DEVELOPMENTAL STAGE.
[7]"GNL3L depletion destabilizes MDM2 and induces p53-dependent G2/M arrest."
Meng L., Hsu J.K., Tsai R.Y.
Oncogene 30:1716-1726(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001475 mRNA. Translation: BAA91712.1.
AL391139 Genomic DNA. Translation: CAI40396.1.
BC011720 mRNA. Translation: AAH11720.1.
RefSeqNP_001171748.1. NM_001184819.1.
NP_061940.1. NM_019067.5.
XP_005262077.1. XM_005262020.1.
UniGeneHs.654677.

3D structure databases

ProteinModelPortalQ9NVN8.
SMRQ9NVN8. Positions 122-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120037. 9 interactions.
IntActQ9NVN8. 4 interactions.
MINTMINT-1440315.
STRING9606.ENSP00000338573.

PTM databases

PhosphoSiteQ9NVN8.

Polymorphism databases

DMDM74752999.

Proteomic databases

PaxDbQ9NVN8.
PeptideAtlasQ9NVN8.
PRIDEQ9NVN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336470; ENSP00000338573; ENSG00000130119.
ENST00000360845; ENSP00000354091; ENSG00000130119.
GeneID54552.
KEGGhsa:54552.
UCSCuc004dth.2. human.

Organism-specific databases

CTD54552.
GeneCardsGC0XP054573.
HGNCHGNC:25553. GNL3L.
HPAHPA036314.
HPA036315.
MIM300873. gene.
neXtProtNX_Q9NVN8.
PharmGKBPA134922876.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1161.
HOGENOMHOG000207716.
HOVERGENHBG051747.
InParanoidQ9NVN8.
KOK14538.
OMAGFQTTEH.
OrthoDBEOG7SXW2W.
PhylomeDBQ9NVN8.
TreeFamTF313085.

Gene expression databases

BgeeQ9NVN8.
CleanExHS_GNL3L.
GenevestigatorQ9NVN8.

Family and domain databases

InterProIPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSPR00326. GTP1OBG.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi54552.
NextBio57019.
PROQ9NVN8.
SOURCESearch...

Entry information

Entry nameGNL3L_HUMAN
AccessionPrimary (citable) accession number: Q9NVN8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 105 of the entry and version 1 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 X

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