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Q9NVN8

- GNL3L_HUMAN

UniProt

Q9NVN8 - GNL3L_HUMAN

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
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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 – 1764GTPSequence Analysis
    Nucleotide bindingi259 – 2668GTPSequence Analysis
    Nucleotide bindingi303 – 3064GTPSequence Analysis

    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

    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. membrane Source: UniProtKB
    3. mitochondrion Source: HPA
    4. nucleolus Source: HPA
    5. nucleus Source: HPA

    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. 1 Publication
    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. 1 Publication
    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. 1 Publication
    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. 1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 310186CP-type GPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili58 – 8831Sequence AnalysisAdd
    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

    Belongs to the TRAFAC class YlqF/YawG GTPase family.PROSITE-ProRule annotation
    Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 111 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