Q9NVN8 (GNL3L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein-like 3-like protein

Gene names

Name:

GNL3L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus 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 process	Ribosome biogenesis
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ribosome biogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA
Molecular_function	GTP 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
MDM2	Q00987	8	EBI-746682,EBI-389668

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 582	582	Guanine nucleotide-binding protein-like 3-like protein		PRO_0000284381
Regions
	Domain	264 – 320	57	G
	Nucleotide binding	173 – 176	4	GTP Potential
	Nucleotide binding	259 – 266	8	GTP Potential
	Nucleotide binding	303 – 306	4	GTP Potential
	Region	9 – 35	27	Required for nucleolar localization
	Coiled coil	58 – 88	31	Potential
Natural variations
	Natural variant	320	1	R → H. Corresponds to variant rs2298284 [ dbSNP | Ensembl ].		VAR_049495
Experimental info
	Mutagenesis	9 – 10	2	KK → AA: Loss of nucleolar localization; when associated with 34-A-A-35. Loss of nuclear location; when associated with 19-A-A-20.
	Mutagenesis	19 – 20	2	KK → AA: Loss of nuclear location; when associated with 9-A-A-10. Loss of nuclear location; when associated with 34-A-A-35.
	Mutagenesis	34 – 35	2	KK → AA: Loss of nucleolar localization; when associated with 9-A-A-10. Loss of nuclear location; when associated with 19-A-A-20.
	Mutagenesis	145 – 147	3	RDP → AAA: Loss of GTP binding. Loss of nucleolar localization. No effect on nuclear localization. Ref.5
	Mutagenesis	309 – 310	2	PG → AA: Loss of nucleolar localization. No effect on nuclear localization.

Sequences

	Sequence		Length	Mass (Da)
	Q9NVN8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B65EE072424F54BC	FASTA	582	65,573
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.
IPI	IPI00005132.
RefSeq	NP_001171748.1. NM_001184819.1. NP_061940.1. NM_019067.5.
UniGene	Hs.654677.
3D structure databases
ProteinModelPortal	Q9NVN8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NVN8. 3 interactions.
MINT	MINT-1440315.
STRING	9606.ENSP00000338573.
PTM databases
PhosphoSite	Q9NVN8.
Polymorphism databases
DMDM	74752999.
Proteomic databases
PaxDb	Q9NVN8.
PeptideAtlas	Q9NVN8.
PRIDE	Q9NVN8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336470; ENSP00000338573; ENSG00000130119. ENST00000360845; ENSP00000354091; ENSG00000130119.
GeneID	54552.
KEGG	hsa:54552.
UCSC	uc004dth.2. human.
Organism-specific databases
CTD	54552.
GeneCards	GC0XP054573.
HGNC	HGNC:25553. GNL3L.
HPA	HPA036314.
MIM	300873. gene.
neXtProt	NX_Q9NVN8.
PharmGKB	PA134922876.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1161.
HOGENOM	HOG000207716.
HOVERGEN	HBG051747.
InParanoid	Q9NVN8.
KO	K14538.
OMA	QTTEHFL.
OrthoDB	EOG46MBJD.
PhylomeDB	Q9NVN8.
Gene expression databases
Bgee	Q9NVN8.
CleanEx	HS_GNL3L.
Genevestigator	Q9NVN8.
Family and domain databases
InterPro	IPR006073. GTP_binding_domain. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF01926. MMR_HSR1. 1 hit. [Graphical view]
PRINTS	PR00326. GTP1OBG.
SUPFAM	SSF52540. SSF52540. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	54552.
NextBio	57019.
SOURCE	Search...

Entry information

Entry name

GNL3L_HUMAN

Accession

Primary (citable) accession number: Q9NVN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.