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P32499 (NUP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Nucleoporin NUP2
Alternative name(s):
Nuclear pore protein NUP2
p95
Gene names
Name:NUP2
Ordered Locus Names:YLR335W
ORF Names:L8300.9
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18

Subunit structure

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. Binds to the nuclear basket of the NPC through NUP60 in a (GSP1, GSP2) GTPase-GTP-dependent manner. Interacts through its FG repeats with nuclear transport factors. Interacts with KAP122. Ref.4 Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.17

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.

Domain

Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: FXFG repeats are especially abundant in NUPs on the nucleoplasmic side (in a highly charged environment and enriched in Ser and Thr).

Miscellaneous

Present with 2960 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 RanBD1 domain.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentMembrane
Nuclear pore complex
Nucleus
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Inferred from mutant phenotype Ref.6. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 21818277. Source: SGD

mRNA export from nucleus in response to heat stress

Inferred from mutant phenotype PubMed 18258809. Source: SGD

maintenance of chromatin silencing at telomere

Inferred from mutant phenotype PubMed 16365162. Source: SGD

poly(A)+ mRNA export from nucleus

Inferred from mutant phenotype PubMed 21036941. Source: SGD

posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 20932479. Source: SGD

protein export from nucleus

Inferred from mutant phenotype PubMed 10542277PubMed 10725229Ref.6. Source: SGD

protein import into nucleus, substrate release

Inferred from direct assay Ref.6Ref.13. Source: SGD

protein targeting to nuclear inner membrane

Inferred from mutant phenotype PubMed 16929305. Source: SGD

transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 20932479. Source: SGD

   Cellular_componentnuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore cytoplasmic filaments

Inferred from direct assay Ref.8. Source: SGD

nuclear pore nuclear basket

Inferred from direct assay PubMed 10725229Ref.8. Source: SGD

   Molecular_functionRan GTPase binding

Inferred from physical interaction PubMed 7638224. Source: SGD

nucleocytoplasmic transporter activity

Inferred from genetic interaction Ref.6Ref.7. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Nucleoporin NUP2
PRO_0000204903

Regions

Repeat67 – 693FXF 1
Repeat189 – 1924FXFG 1
Repeat216 – 2183FXF 2
Repeat247 – 2493FXF 3
Repeat285 – 2884FXFG 2
Repeat302 – 3054FXFG 3
Repeat318 – 3214FXFG 4
Repeat352 – 3543FXF 4
Repeat369 – 3724FXFG 5
Repeat386 – 3894FXFG 6
Repeat438 – 4414FXFG 7
Repeat474 – 4774FXFG 8
Repeat493 – 4964FXFG 9
Repeat511 – 5144FXFG 10
Repeat524 – 5274FXFG 11
Repeat550 – 5523FXF 5
Domain583 – 720138RanBD1
Region35 – 5016Interaction with SRP1 NLS binding site 1
Compositional bias333 – 37745Ser-rich

Amino acid modifications

Modified residue171Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23
Modified residue201Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23
Modified residue1371Phosphoserine Ref.22
Modified residue1651Phosphoserine Ref.20
Modified residue2031Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23
Modified residue2051Phosphoserine Ref.20 Ref.21 Ref.22
Modified residue3481Phosphoserine Ref.23
Modified residue3511Phosphoserine Ref.22
Modified residue3611Phosphothreonine Ref.23
Modified residue5811Phosphoserine Ref.23
Modified residue5901Phosphothreonine Ref.23

Experimental info

Sequence conflict1371S → F in CAA49587. Ref.1
Sequence conflict3701S → N in CAA49587. Ref.1
Sequence conflict4181L → F in CAA49587. Ref.1

Secondary structure

....... 720
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32499 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: 467210F14FA73311

FASTA72077,881
        10         20         30         40         50         60 
MAKRVADAQI QRETYDSNES DDDVTPSTKV ASSAVMNRRK IAMPKRRMAF KPFGSAKSDE 

        70         80         90        100        110        120 
TKQASSFSFL NRADGTGEAQ VDNSPTTESN SRLKALNLQF KAKVDDLVLG KPLADLRPLF 

       130        140        150        160        170        180 
TRYELYIKNI LEAPVKSIEN PTQTKGNDAK PAKVEDVQKS SDSSSEDEVK VEGPKFTIDA 

       190        200        210        220        230        240 
KPPISDSVFS FGPKKENRKK DESDSENDIE IKGPEFKFSG TVSSDVFKLN PSTDKNEKKT 

       250        260        270        280        290        300 
ETNAKPFSFS SATSTTEQTK SKNPLSLTEA TKTNVDNNSK AEASFTFGTK HAADSQNNKP 

       310        320        330        340        350        360 
SFVFGQAAAK PSLEKSSFTF GSTTIEKKND ENSTSNSKPE KSSDSNDSNP SFSFSIPSKN 

       370        380        390        400        410        420 
TPDASKPSFS FGVPNSSKNE TSKPVFSFGA ATPSAKEASQ EDDNNNVEKP SSKPAFNLIS 

       430        440        450        460        470        480 
NAGTEKEKES KKDSKPAFSF GISNGSESKD SDKPSLPSAV DGENDKKEAT KPAFSFGINT 

       490        500        510        520        530        540 
NTTKTADTKA PTFTFGSSAL ADNKEDVKKP FSFGTSQPNN TPSFSFGKTT ANLPANSSTS 

       550        560        570        580        590        600 
PAPSIPSTGF KFSLPFEQKG SQTTTNDSKE ESTTEATGNE SQDATKVDAT PEESKPINLQ 

       610        620        630        640        650        660 
NGEEDEVALF SQKAKLMTFN AETKSYDSRG VGEMKLLKKK DDPSKVRLLC RSDGMGNVLL 

       670        680        690        700        710        720 
NATVVDSFKY EPLAPGNDNL IKAPTVAADG KLVTYIVKFK QKEEGRSFTK AIEDAKKEMK 

« Hide

References

« Hide 'large scale' references
[1]"NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex."
Loeb J.D.J., Davis L.I., Fink G.R.
Mol. Biol. Cell 4:209-222(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus."
Titov A.A., Blobel G.
J. Cell Biol. 147:235-246(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAP122.
[5]"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: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[6]"Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha."
Solsbacher J., Maurer P., Vogel F., Schlenstedt G.
Mol. Cell. Biol. 20:8468-8479(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SRP1 RECYCLING.
[7]"Proteomic analysis of nucleoporin interacting proteins."
Allen N.P., Huang L., Burlingame A., Rexach M.
J. Biol. Chem. 276:29268-29274(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION THROUGH FG REPEATS.
[8]"Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex."
Dilworth D.J., Suprapto A., Padovan J.C., Chait B.T., Wozniak R.W., Rout M.P., Aitchison J.D.
J. Cell Biol. 153:1465-1478(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH NPC.
[9]"The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex."
Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.
J. Cell Biol. 154:937-950(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NUP60.
[10]"GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta."
Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.
J. Biol. Chem. 277:50597-50606(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION.
[11]"Deciphering networks of protein interactions at the nuclear pore complex."
Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A., Lutzmann M., Hurt E.C., Rexach M.
Mol. Cell. Proteomics 1:930-946(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KARYOPHERINS THROUH FG REPEATS.
[12]"Chromatin boundaries in budding yeast: the nuclear pore connection."
Ishii K., Arib G., Lin C., Van Houwe G., Laemmli U.K.
Cell 109:551-562(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHROMATIN BOUNDARY ACTIVITY.
[13]"Accelerating the rate of disassembly of karyopherin-cargo complexes."
Gilchrist D., Mykytka B., Rexach M.
J. Biol. Chem. 277:18161-18172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SRP1-KAP95 NUCLEAR IMPORT COMPLEX DISASSEMBLY.
[14]"A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex."
Pyhtila B., Rexach M.
J. Biol. Chem. 278:42699-42709(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FG REPEAT AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
[15]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded."
Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.
Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FG REPEAT STRUCTURE.
[17]"Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm."
Gilchrist D., Rexach M.
J. Biol. Chem. 278:51937-51949(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SRP1.
[18]"Minimal nuclear pore complexes define FG repeat domains essential for transport."
Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.
Nat. Cell Biol. 6:197-206(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
[19]"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.
[20]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-165; SER-203 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[21]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-137; SER-203; SER-205 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203; SER-348; THR-361; SER-581 AND THR-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import."
Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.
EMBO J. 22:5358-5369(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 36-50 IN COMPLEX WITH SRP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69964 Genomic DNA. Translation: CAA49587.1.
U19028 Genomic DNA. Translation: AAB67259.1.
BK006945 Genomic DNA. Translation: DAA09641.1.
PIRS51340.
RefSeqNP_013439.1. NM_001182224.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UN0X-ray2.60C/D1-51[»]
2C1TX-ray2.60C/D1-51[»]
DisProtDP00222.
ProteinModelPortalP32499.
SMRP32499. Positions 2-46, 606-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31599. 88 interactions.
DIPDIP-859N.
IntActP32499. 30 interactions.
MINTMINT-395606.
STRING4932.YLR335W.

Protein family/group databases

TCDB1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

PaxDbP32499.
PeptideAtlasP32499.

Protocols and materials databases

DNASU851048.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR335W; YLR335W; YLR335W.
GeneID851048.
KEGGsce:YLR335W.

Organism-specific databases

CYGDYLR335w.
SGDS000004327. NUP2.

Phylogenomic databases

eggNOGCOG5171.
GeneTreeENSGT00730000113442.
HOGENOMHOG000248337.
OMAENEDTVI.
OrthoDBEOG7TF7N6.

Enzyme and pathway databases

BioCycYEAST:G3O-32414-MONOMER.

Gene expression databases

GenevestigatorP32499.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR015007. NUP2/50/61.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamPF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32499.
NextBio967658.

Entry information

Entry nameNUP2_YEAST
AccessionPrimary (citable) accession number: P32499
Secondary accession number(s): D6VYX5, Q06130
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 16, 2003
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references