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Protein

Nucleoporin GLE1

Gene

GLE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonuleoprotein (hnRNP) NAB2 from exported mRNA.5 Publications

GO - Molecular functioni

  • enzyme activator activity Source: SGD
  • inositol hexakisphosphate binding Source: SGD
  • phospholipid binding Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • mRNA export from nucleus Source: SGD
  • mRNA processing Source: UniProtKB-KW
  • poly(A)+ mRNA export from nucleus Source: SGD
  • positive regulation of catalytic activity Source: GOC
  • protein transport Source: UniProtKB-KW
  • regulation of translational initiation Source: SGD
  • regulation of translational termination Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29589-MONOMER.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin GLE1
Alternative name(s):
Nuclear pore protein GLE1
RNA export factor GLE1
Gene namesi
Name:GLE1
Synonyms:BRR3, RSS1
Ordered Locus Names:YDL207W
ORF Names:D1049
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL207W.
SGDiS000002366. GLE1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore cytoplasmic filaments Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi351 – 3511L → A: Partial loss of activity. 1 Publication
Mutagenesisi353 – 3531L → A: Partial loss of activity. 1 Publication
Mutagenesisi356 – 3561L → A: Temperature-sensitive. 1 Publication
Mutagenesisi358 – 3581L → A: Partial loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Nucleoporin GLE1PRO_0000204820Add
BLAST

Proteomic databases

MaxQBiQ12315.

PTM databases

iPTMnetiQ12315.

Interactioni

Subunit structurei

The nuclear pore complex (NPC) constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. The 55-60 MDa NPC is composed of at least 31 different subunits: ASM4, CDC31, GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120, NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42, NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34, SEH1 and SEC1. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. GLE1 interacts with the NUP82 subcomplex (NSP1, NUP82, NUP159) via NUP42. It also interacts with GFD1 and the ATP-dependent RNA helicase DBP5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SUP35P054532EBI-7635,EBI-6540

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi31839. 54 interactions.
DIPiDIP-2350N.
IntActiQ12315. 34 interactions.
MINTiMINT-4479947.

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi245 – 26622Combined sources
Helixi268 – 2736Combined sources
Helixi276 – 28914Combined sources
Helixi292 – 2954Combined sources
Helixi300 – 31516Combined sources
Turni316 – 3194Combined sources
Helixi321 – 34525Combined sources
Helixi347 – 3493Combined sources
Helixi350 – 36314Combined sources
Helixi367 – 37812Combined sources
Helixi380 – 3834Combined sources
Helixi392 – 3976Combined sources
Helixi411 – 43020Combined sources
Turni435 – 4406Combined sources
Helixi448 – 45811Combined sources
Helixi462 – 4643Combined sources
Helixi467 – 48822Combined sources
Helixi490 – 50011Combined sources
Helixi502 – 5065Combined sources
Helixi508 – 5103Combined sources
Helixi513 – 52614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PEUX-ray2.60B244-538[»]
3PEVX-ray2.50B244-538[»]
3RRMX-ray2.88B244-538[»]
3RRNX-ray4.00B244-538[»]
ProteinModelPortaliQ12315.
SMRiQ12315. Positions 244-538.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12315.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni257 – 538282Interactions with NUP42, DBP5 and GFD1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili131 – 244114Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi154 – 17017Bipartite nuclear localization signal 1Add
BLAST
Motifi272 – 28817Bipartite nuclear localization signal 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi157 – 22973Glu-richAdd
BLAST
Compositional biasi161 – 273113Lys-richAdd
BLAST
Compositional biasi164 – 1674Poly-Glu

Sequence similaritiesi

Belongs to the GLE1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000012903.
HOGENOMiHOG000248676.
InParanoidiQ12315.
KOiK18723.
OMAiYVELHQH.
OrthoDBiEOG7DJSWN.

Family and domain databases

InterProiIPR012476. GLE1.
[Graphical view]
PANTHERiPTHR12960. PTHR12960. 1 hit.
PfamiPF07817. GLE1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFVFDEVFN SDTDSPEFEE TCSTTSSTSS QCPTPEPSPA IKLPSFTKVG
60 70 80 90 100
TKKLVNESVV ILDPALENAL RDLNLQSKLI PINEPIVAAS SIIVPHSTNM
110 120 130 140 150
PLPRASHSSL LDNAKNSNAT APLLEAIEES FQRKMQNLVL ANQKEIQSIR
160 170 180 190 200
ENKRRVEEQR KRKEEEERKR KEAEEKAKRE QELLRQKKDE EERKRKEAEA
210 220 230 240 250
KLAQQKQEEE RKKIEEQNEK ERQLKKEHEA KLLQQKDKLG KAVTNFDKIS
260 270 280 290 300
KMFWHYKDKI AQIKQDIVLP IKKADVNVRN LLSRHKRKIN PKFGQLTNSN
310 320 330 340 350
QQLFKIQNEL TQLINDTKGD SLAYHWILNF IAKAVVHQAE TEVRVKPESA
360 370 380 390 400
LPLGKLTLYL LVQFPELQEL FMARLVKKCP FVIGFTCEID TEKGRQNMGW
410 420 430 440 450
KRNNENKWED NTSYDERMGG ILSLFAIITR LQLPQEFITT TSHPFPIALS
460 470 480 490 500
WHILARICNT PLNLITNTHF VILGSWWDAA AVQFLQAYGN QASKLLILIG
510 520 530
EELTSRMAEK KYVGAARLRI LLEAWQNNNM ESFPEMSP
Length:538
Mass (Da):62,073
Last modified:November 1, 1997 - v1
Checksum:iC9C6B1513AF95711
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68475 Genomic DNA. Translation: AAC49444.1.
X99000 Genomic DNA. Translation: CAA67484.1.
Z74255 Genomic DNA. Translation: CAA98785.1.
BK006938 Genomic DNA. Translation: DAA11657.1.
PIRiS67766.
RefSeqiNP_010074.1. NM_001180267.1.

Genome annotation databases

EnsemblFungiiYDL207W; YDL207W; YDL207W.
GeneIDi851320.
KEGGisce:YDL207W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68475 Genomic DNA. Translation: AAC49444.1.
X99000 Genomic DNA. Translation: CAA67484.1.
Z74255 Genomic DNA. Translation: CAA98785.1.
BK006938 Genomic DNA. Translation: DAA11657.1.
PIRiS67766.
RefSeqiNP_010074.1. NM_001180267.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PEUX-ray2.60B244-538[»]
3PEVX-ray2.50B244-538[»]
3RRMX-ray2.88B244-538[»]
3RRNX-ray4.00B244-538[»]
ProteinModelPortaliQ12315.
SMRiQ12315. Positions 244-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31839. 54 interactions.
DIPiDIP-2350N.
IntActiQ12315. 34 interactions.
MINTiMINT-4479947.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiQ12315.

Proteomic databases

MaxQBiQ12315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL207W; YDL207W; YDL207W.
GeneIDi851320.
KEGGisce:YDL207W.

Organism-specific databases

EuPathDBiFungiDB:YDL207W.
SGDiS000002366. GLE1.

Phylogenomic databases

GeneTreeiENSGT00390000012903.
HOGENOMiHOG000248676.
InParanoidiQ12315.
KOiK18723.
OMAiYVELHQH.
OrthoDBiEOG7DJSWN.

Enzyme and pathway databases

BioCyciYEAST:G3O-29589-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12315.
PROiQ12315.

Family and domain databases

InterProiIPR012476. GLE1.
[Graphical view]
PANTHERiPTHR12960. PTHR12960. 1 hit.
PfamiPF07817. GLE1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An RNA-export mediator with an essential nuclear export signal."
    Murphy R., Wente S.R.
    Nature 383:357-360(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
  2. "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new open reading frames, nine known genes and one gene for Gly-tRNA."
    Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U., Schmidt E.R.
    Yeast 13:163-169(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr255p."
    Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., Stutz F.
    EMBO J. 18:5761-5777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP42; DBP5 AND GFD1.
  6. "Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells."
    Hodge C.A., Colot H.V., Stafford P., Cole C.N.
    EMBO J. 18:5778-5788(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "The yeast nuclear pore complex: composition, architecture, and transport mechanism."
    Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.
    J. Cell Biol. 148:635-651(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NPC SUBUNIT LOCATION.
  8. "A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription."
    Jensen T.H., Patricio K., McCarthy T., Rosbash M.
    Mol. Cell 7:887-898(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA TRANSPORT.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a direct interaction with Gfd1 and to Gle1 function."
    Suntharalingam M., Alcazar-Roman A.R., Wente S.R.
    J. Biol. Chem. 279:35384-35391(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NAB2.
  11. "Peering through the pore: nuclear pore complex structure, assembly, and function."
    Suntharalingam M., Wente S.R.
    Dev. Cell 4:775-789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiGLE1_YEAST
AccessioniPrimary (citable) accession number: Q12315
Secondary accession number(s): D6VRE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1040 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.