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Q9NVN8

- GNL3L_HUMAN

UniProt

Q9NVN8 - GNL3L_HUMAN

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Protein

Guanine nucleotide-binding protein-like 3-like protein

Gene
GNL3L
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1764GTP Reviewed prediction
Nucleotide bindingi259 – 2668GTP Reviewed prediction
Nucleotide bindingi303 – 3064GTP Reviewed prediction

GO - Molecular functioni

  1. GTPase activity Source: RefGenome
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. ribosome biogenesis Source: RefGenome
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein-like 3-like protein
Gene namesi
Name:GNL3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:25553. GNL3L.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. mitochondrion Source: HPA
  3. nucleolus Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 102KK → AA: Loss of nucleolar localization; when associated with 34-A-A-35. Loss of nuclear location; when associated with 19-A-A-20.
Mutagenesisi19 – 202KK → AA: Loss of nuclear location; when associated with 9-A-A-10. Loss of nuclear location; when associated with 34-A-A-35.
Mutagenesisi34 – 352KK → AA: Loss of nucleolar localization; when associated with 9-A-A-10. Loss of nuclear location; when associated with 19-A-A-20.
Mutagenesisi145 – 1473RDP → AAA: Loss of GTP binding. Loss of nucleolar localization. No effect on nuclear localization. 1 Publication
Mutagenesisi309 – 3102PG → AA: Loss of nucleolar localization. No effect on nuclear localization.

Organism-specific databases

PharmGKBiPA134922876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582Guanine nucleotide-binding protein-like 3-like proteinPRO_0000284381Add
BLAST

Proteomic databases

MaxQBiQ9NVN8.
PaxDbiQ9NVN8.
PeptideAtlasiQ9NVN8.
PRIDEiQ9NVN8.

PTM databases

PhosphoSiteiQ9NVN8.

Expressioni

Developmental stagei

Up-regulated during mitosis and down-regulated in the G1 phase.1 Publication

Gene expression databases

BgeeiQ9NVN8.
CleanExiHS_GNL3L.
GenevestigatoriQ9NVN8.

Organism-specific databases

HPAiHPA036314.
HPA036315.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q009878EBI-746682,EBI-389668

Protein-protein interaction databases

BioGridi120037. 10 interactions.
IntActiQ9NVN8. 4 interactions.
MINTiMINT-1440315.
STRINGi9606.ENSP00000338573.

Structurei

3D structure databases

ProteinModelPortaliQ9NVN8.
SMRiQ9NVN8. Positions 126-402.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 310186CP-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 3527Required for nucleolar localizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili58 – 8831 Reviewed predictionAdd
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1161.
HOGENOMiHOG000207716.
HOVERGENiHBG051747.
InParanoidiQ9NVN8.
KOiK14538.
OMAiGFQTTEH.
OrthoDBiEOG7SXW2W.
PhylomeDBiQ9NVN8.
TreeFamiTF313085.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NVN8-1 [UniParc]FASTAAdd to Basket

« Hide

MMKLRHKNKK PGEGSKGHKK ISWPYPQPAK QNGKKATSKV PSAPHFVHPN    50
DHANREAELK KKWVEEMREK QQAAREQERQ KRRTIESYCQ DVLRRQEEFE 100
HKEEVLQELN MFPQLDDEAT RKAYYKEFRK VVEYSDVILE VLDARDPLGC 150
RCFQMEEAVL RAQGNKKLVL VLNKIDLVPK EVVEKWLDYL RNELPTVAFK 200
ASTQHQVKNL NRCSVPVDQA SESLLKSKAC FGAENLMRVL GNYCRLGEVR 250
THIRVGVVGL PNVGKSSLIN SLKRSRACSV GAVPGITKFM QEVYLDKFIR 300
LLDAPGIVPG PNSEVGTILR NCVHVQKLAD PVTPVETILQ RCNLEEISNY 350
YGVSGFQTTE HFLTAVAHRL GKKKKGGLYS QEQAAKAVLA DWVSGKISFY 400
IPPPATHTLP THLSAEIVKE MTEVFDIEDT EQANEDTMEC LATGESDELL 450
GDTDPLEMEI KLLHSPMTKI ADAIENKTTV YKIGDLTGYC TNPNRHQMGW 500
AKRNVDHRPK SNSMVDVCSV DRRSVLQRIM ETDPLQQGQA LASALKNKKK 550
MQKRADKIAS KLSDSMMSAL DLSGNADDGV GD 582
Length:582
Mass (Da):65,573
Last modified:October 1, 2000 - v1
Checksum:iB65EE072424F54BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201R → H.
Corresponds to variant rs2298284 [ dbSNP | Ensembl ].
VAR_049495

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK001475 mRNA. Translation: BAA91712.1.
AL391139 Genomic DNA. Translation: CAI40396.1.
BC011720 mRNA. Translation: AAH11720.1.
CCDSiCCDS14360.1.
RefSeqiNP_001171748.1. NM_001184819.1.
NP_061940.1. NM_019067.5.
UniGeneiHs.654677.

Genome annotation databases

EnsembliENST00000336470; ENSP00000338573; ENSG00000130119.
ENST00000360845; ENSP00000354091; ENSG00000130119.
GeneIDi54552.
KEGGihsa:54552.
UCSCiuc004dth.2. human.

Polymorphism databases

DMDMi74752999.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK001475 mRNA. Translation: BAA91712.1 .
AL391139 Genomic DNA. Translation: CAI40396.1 .
BC011720 mRNA. Translation: AAH11720.1 .
CCDSi CCDS14360.1.
RefSeqi NP_001171748.1. NM_001184819.1.
NP_061940.1. NM_019067.5.
UniGenei Hs.654677.

3D structure databases

ProteinModelPortali Q9NVN8.
SMRi Q9NVN8. Positions 126-402.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120037. 10 interactions.
IntActi Q9NVN8. 4 interactions.
MINTi MINT-1440315.
STRINGi 9606.ENSP00000338573.

PTM databases

PhosphoSitei Q9NVN8.

Polymorphism databases

DMDMi 74752999.

Proteomic databases

MaxQBi Q9NVN8.
PaxDbi Q9NVN8.
PeptideAtlasi Q9NVN8.
PRIDEi Q9NVN8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336470 ; ENSP00000338573 ; ENSG00000130119 .
ENST00000360845 ; ENSP00000354091 ; ENSG00000130119 .
GeneIDi 54552.
KEGGi hsa:54552.
UCSCi uc004dth.2. human.

Organism-specific databases

CTDi 54552.
GeneCardsi GC0XP054573.
HGNCi HGNC:25553. GNL3L.
HPAi HPA036314.
HPA036315.
MIMi 300873. gene.
neXtProti NX_Q9NVN8.
PharmGKBi PA134922876.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1161.
HOGENOMi HOG000207716.
HOVERGENi HBG051747.
InParanoidi Q9NVN8.
KOi K14538.
OMAi GFQTTEH.
OrthoDBi EOG7SXW2W.
PhylomeDBi Q9NVN8.
TreeFami TF313085.

Miscellaneous databases

GenomeRNAii 54552.
NextBioi 57019.
PROi Q9NVN8.
SOURCEi Search...

Gene expression databases

Bgeei Q9NVN8.
CleanExi HS_GNL3L.
Genevestigatori Q9NVN8.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF01926. MMR_HSR1. 1 hit.
[Graphical view ]
PRINTSi PR00326. GTP1OBG.
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51721. G_CP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiGNL3L_HUMAN
AccessioniPrimary (citable) accession number: Q9NVN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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