Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleoporin NUP2

Gene

NUP2

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. 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.12 Publications

GO - Molecular functioni

  • nucleocytoplasmic transporter activity Source: SGD
  • Ran GTPase binding Source: SGD

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • maintenance of chromatin silencing at telomere Source: SGD
  • mRNA export from nucleus in response to heat stress Source: SGD
  • NLS-bearing protein import into nucleus Source: SGD
  • poly(A)+ mRNA export from nucleus Source: SGD
  • posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  • protein export from nucleus Source: SGD
  • protein import into nucleus, substrate release Source: SGD
  • protein targeting to nuclear inner membrane Source: SGD
  • transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32414-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP2
Alternative name(s):
Nuclear pore protein NUP2
p95
Gene namesi
Name:NUP2
Ordered Locus Names:YLR335W
ORF Names:L8300.9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR335W.
SGDiS000004327. NUP2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore cytoplasmic filaments Source: SGD
  • nuclear pore nuclear basket Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002049031 – 720Nucleoporin NUP2Add BLAST720

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Modified residuei165PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei205PhosphoserineCombined sources1
Modified residuei348PhosphoserineCombined sources1
Modified residuei351PhosphoserineCombined sources1
Modified residuei361PhosphothreonineCombined sources1
Modified residuei581PhosphoserineCombined sources1
Modified residuei590PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32499.
PRIDEiP32499.

PTM databases

iPTMnetiP32499.

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. 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 KAP122.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KAP95Q061425EBI-12401,EBI-9145
NUP60P397052EBI-12401,EBI-20731
SRP1Q028213EBI-12401,EBI-1797

GO - Molecular functioni

  • Ran GTPase binding Source: SGD

Protein-protein interaction databases

BioGridi31599. 92 interactors.
DIPiDIP-859N.
IntActiP32499. 31 interactors.
MINTiMINT-395606.

Structurei

Secondary structure

1720
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni12 – 14Combined sources3
Helixi34 – 37Combined sources4
Turni47 – 49Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UN0X-ray2.60C/D1-51[»]
2C1TX-ray2.60C/D1-51[»]
DisProtiDP00222.
ProteinModelPortaliP32499.
SMRiP32499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32499.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati67 – 69FXF 13
Repeati189 – 192FXFG 14
Repeati216 – 218FXF 23
Repeati247 – 249FXF 33
Repeati285 – 288FXFG 24
Repeati302 – 305FXFG 34
Repeati318 – 321FXFG 44
Repeati352 – 354FXF 43
Repeati369 – 372FXFG 54
Repeati386 – 389FXFG 64
Repeati438 – 441FXFG 74
Repeati474 – 477FXFG 84
Repeati493 – 496FXFG 94
Repeati511 – 514FXFG 104
Repeati524 – 527FXFG 114
Repeati550 – 552FXF 53
Domaini583 – 720RanBD1PROSITE-ProRule annotationAdd BLAST138

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 50Interaction with SRP1 NLS binding site 1Add BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi333 – 377Ser-richAdd BLAST45

Domaini

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).

Sequence similaritiesi

Contains 1 RanBD1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00730000113442.
HOGENOMiHOG000248337.
InParanoidiP32499.
KOiK18722.
OMAiMAVKSTF.
OrthoDBiEOG092C4THQ.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR015007. NUP2/50/61.
IPR011993. PH_dom-like.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32499-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKRVADAQI QRETYDSNES DDDVTPSTKV ASSAVMNRRK IAMPKRRMAF
60 70 80 90 100
KPFGSAKSDE TKQASSFSFL NRADGTGEAQ VDNSPTTESN SRLKALNLQF
110 120 130 140 150
KAKVDDLVLG KPLADLRPLF TRYELYIKNI LEAPVKSIEN PTQTKGNDAK
160 170 180 190 200
PAKVEDVQKS SDSSSEDEVK VEGPKFTIDA KPPISDSVFS FGPKKENRKK
210 220 230 240 250
DESDSENDIE IKGPEFKFSG TVSSDVFKLN PSTDKNEKKT ETNAKPFSFS
260 270 280 290 300
SATSTTEQTK SKNPLSLTEA TKTNVDNNSK AEASFTFGTK HAADSQNNKP
310 320 330 340 350
SFVFGQAAAK PSLEKSSFTF GSTTIEKKND ENSTSNSKPE KSSDSNDSNP
360 370 380 390 400
SFSFSIPSKN TPDASKPSFS FGVPNSSKNE TSKPVFSFGA ATPSAKEASQ
410 420 430 440 450
EDDNNNVEKP SSKPAFNLIS NAGTEKEKES KKDSKPAFSF GISNGSESKD
460 470 480 490 500
SDKPSLPSAV DGENDKKEAT KPAFSFGINT NTTKTADTKA PTFTFGSSAL
510 520 530 540 550
ADNKEDVKKP FSFGTSQPNN TPSFSFGKTT ANLPANSSTS PAPSIPSTGF
560 570 580 590 600
KFSLPFEQKG SQTTTNDSKE ESTTEATGNE SQDATKVDAT PEESKPINLQ
610 620 630 640 650
NGEEDEVALF SQKAKLMTFN AETKSYDSRG VGEMKLLKKK DDPSKVRLLC
660 670 680 690 700
RSDGMGNVLL NATVVDSFKY EPLAPGNDNL IKAPTVAADG KLVTYIVKFK
710 720
QKEEGRSFTK AIEDAKKEMK
Length:720
Mass (Da):77,881
Last modified:May 16, 2003 - v2
Checksum:i467210F14FA73311
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti137S → F in CAA49587 (PubMed:8443417).Curated1
Sequence conflicti370S → N in CAA49587 (PubMed:8443417).Curated1
Sequence conflicti418L → F in CAA49587 (PubMed:8443417).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69964 Genomic DNA. Translation: CAA49587.1.
U19028 Genomic DNA. Translation: AAB67259.1.
BK006945 Genomic DNA. Translation: DAA09641.1.
PIRiS51340.
RefSeqiNP_013439.1. NM_001182224.1.

Genome annotation databases

EnsemblFungiiYLR335W; YLR335W; YLR335W.
GeneIDi851048.
KEGGisce:YLR335W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69964 Genomic DNA. Translation: CAA49587.1.
U19028 Genomic DNA. Translation: AAB67259.1.
BK006945 Genomic DNA. Translation: DAA09641.1.
PIRiS51340.
RefSeqiNP_013439.1. NM_001182224.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UN0X-ray2.60C/D1-51[»]
2C1TX-ray2.60C/D1-51[»]
DisProtiDP00222.
ProteinModelPortaliP32499.
SMRiP32499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31599. 92 interactors.
DIPiDIP-859N.
IntActiP32499. 31 interactors.
MINTiMINT-395606.

Protein family/group databases

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

PTM databases

iPTMnetiP32499.

Proteomic databases

MaxQBiP32499.
PRIDEiP32499.

Protocols and materials databases

DNASUi851048.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR335W; YLR335W; YLR335W.
GeneIDi851048.
KEGGisce:YLR335W.

Organism-specific databases

EuPathDBiFungiDB:YLR335W.
SGDiS000004327. NUP2.

Phylogenomic databases

GeneTreeiENSGT00730000113442.
HOGENOMiHOG000248337.
InParanoidiP32499.
KOiK18722.
OMAiMAVKSTF.
OrthoDBiEOG092C4THQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-32414-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32499.
PROiP32499.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR015007. NUP2/50/61.
IPR011993. PH_dom-like.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNUP2_YEAST
AccessioniPrimary (citable) accession number: P32499
Secondary accession number(s): D6VYX5, Q06130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 16, 2003
Last modified: November 30, 2016
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2960 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.