Skip Header

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

UniProtKB - P20676 (NUP1_YEAST)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Nucleoporin NUP1

Gene

NUP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 NUP1 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 NUP2 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, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex.9 Publications

Miscellaneous

Present with 468 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • nuclear localization sequence binding Source: GO_Central
  • structural constituent of nuclear pore Source: SGD
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • NLS-bearing protein import into nucleus Source: SGD
  • poly(A)+ mRNA export from nucleus Source: SGD
  • protein import into nucleus Source: SGD
  • ribosomal large subunit export from nucleus Source: SGD
  • transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processmRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33631-MONOMER

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP1
Alternative name(s):
Nuclear pore protein NUP1
Gene namesi
Name:NUP1
Ordered Locus Names:YOR098C
ORF Names:YOR3182C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR098C
SGDiS000005624 NUP1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002049022 – 1076Nucleoporin NUP1Add BLAST1075

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei54PhosphoserineCombined sources1
Modified residuei161PhosphoserineCombined sources1
Modified residuei381PhosphothreonineCombined sources1
Modified residuei383PhosphoserineCombined sources1
Modified residuei637PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by CDC28.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20676
PaxDbiP20676
PRIDEiP20676

PTM databases

iPTMnetiP20676

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, SEC13 and SEH1. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Interacts through its FG repeats with nuclear transport receptors. Binds to the nuclear basket of the NPC through NUP60. Interacts with KAP122.4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi34496, 93 interactors
ComplexPortaliCPX-824 Nuclear pore complex
DIPiDIP-81N
IntActiP20676, 56 interactors
MINTiP20676
STRINGi4932.YOR098C

Structurei

Secondary structure

11076
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1004 – 1007Combined sources4
Turni1008 – 1010Combined sources3

3D structure databases

DisProtiDP01075
ProteinModelPortaliP20676
SMRiP20676
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20676

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati336 – 338FXF 13
Repeati384 – 386FXF 23
Repeati406 – 409FXFG 14
Repeati422 – 425FXFG 24
Repeati448 – 451FXFG 34
Repeati484 – 487FXFG 44
Repeati510 – 513FXFG 54
Repeati525 – 528FXFG 64
Repeati543 – 546FXFG 74
Repeati571 – 574FXFG 84
Repeati591 – 593FXF 33
Repeati614 – 616FXF 43
Repeati636 – 638FXF 53
Repeati657 – 659FXF 63
Repeati671 – 674FXFG 94
Repeati689 – 691FXF 73
Repeati708 – 711FXFG 104
Repeati727 – 730FXFG 114
Repeati753 – 755FXF 83
Repeati800 – 803FXFG 124
Repeati819 – 821FXF 93
Repeati866 – 868FXF 103
Repeati885 – 888FXFG 134
Repeati929 – 931FXF 113
Repeati1008 – 1009FG 12
Repeati1027 – 1028FG 22
Repeati1038 – 1039FG 32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1040 – 1076Interaction with KAP95Add BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi81 – 84Poly-Asn4
Compositional biasi718 – 723Poly-Thr6
Compositional biasi830 – 833Poly-Thr4
Compositional biasi881 – 1022Asn-richAdd BLAST142

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).

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00730000111010
InParanoidiP20676
KOiK18721
OMAiKPANANT
OrthoDBiEOG092C4QBH

Family and domain databases

InterProiView protein in InterPro
IPR026054 Nucleoporin
PANTHERiPTHR23193 PTHR23193, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNTSSVMS SPRVEKRSFS STLKSFFTNP NKKRPSSKKV FSSNLSYANH 
        60         70         80         90        100
LEESDVEDTL HVNKRKRVSG TSQHSDSLTQ NNNNAPIIIY GTENTERPPL 
       110        120        130        140        150
LPILPIQRLR LLREKQRVRN MRELGLIQST EFPSITSSVI LGSQSKSDEG 
       160        170        180        190        200
GSYLCTSSTP SPIKNGSCTR QLAGKSGEDT NVGLPILKSL KNRSNRKRFH 
       210        220        230        240        250
SQSKGTVWSA NFEYDLSEYD AIQKKDNKDK EGNAGGDQKT SENRNNIKSS 
       260        270        280        290        300
ISNGNLATGP NLTSEIEDLR ADINSNRLSN PQKNLLLKGP ASTVAKTAPI 
       310        320        330        340        350
QESFVPNSER SGTPTLKKNI EPKKDKESIV LPTVGFDFIK DNETPSKKTS 
       360        370        380        390        400
PKATSSAGAV FKSSVEMGKT DKSTKTAEAP TLSFNFSQKA NKTKAVDNTV 
       410        420        430        440        450
PSTTLFNFGG KSDTVTSASQ PFKFGKTSEK SENHTESDAP PKSTAPIFSF 
       460        470        480        490        500
GKQEENGDEG DDENEPKRKR RLPVSEDTNT KPLFDFGKTG DQKETKKGES 
       510        520        530        540        550
EKDASGKPSF VFGASDKQAE GTPLFTFGKK ADVTSNIDSS AQFTFGKAAT 
       560        570        580        590        600
AKETHTKPSE TPATIVKKPT FTFGQSTSEN KISEGSAKPT FSFSKSEEER 
       610        620        630        640        650
KSSPISNEAA KPSFSFPGKP VDVQAPTDDK TLKPTFSFTE PAQKDSSVVS 
       660        670        680        690        700
EPKKPSFTFA SSKTSQPKPL FSFGKSDAAK EPPGSNTSFS FTKPPANETD 
       710        720        730        740        750
KRPTPPSFTF GGSTTNNTTT TSTKPSFSFG APESMKSTAS TAAANTEKLS 
       760        770        780        790        800
NGFSFTKFNH NKEKSNSPTS FFDGSASSTP IPVLGKPTDA TGNTTSKSAF 
       810        820        830        840        850
SFGTANTNGT NASANSTSFS FNAPATGNGT TTTSNTSGTN IAGTFNVGKP 
       860        870        880        890        900
DQSIASGNTN GAGSAFGFSS SGTAATGAAS NQSSFNFGNN GAGGLNPFTS 
       910        920        930        940        950
ATSSTNANAG LFNKPPSTNA QNVNVPSAFN FTGNNSTPGG GSVFNMNGNT 
       960        970        980        990       1000
NANTVFAGSN NQPHQSQTPS FNTNSSFTPS TVPNINFSGL NGGITNTATN 
      1010       1020       1030       1040       1050
ALRPSDIFGA NAASGSNSNV TNPSSIFGGA GGVPTTSFGQ PQSAPNQMGM 
      1060       1070 
GTNNGMSMGG GVMANRKIAR MRHSKR
Length:1,076
Mass (Da):113,581
Last modified:February 1, 1991 - v1
Checksum:i4AC23567D2FB53CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33632 Genomic DNA Translation: AAA34822.1
X94335 Genomic DNA Translation: CAA64020.1
Z75006 Genomic DNA Translation: CAA99295.1
BK006948 Genomic DNA Translation: DAA10875.1
PIRiA35622
RefSeqiNP_014741.1, NM_001183517.1

Genome annotation databases

EnsemblFungiiYOR098C; YOR098C; YOR098C
GeneIDi854265
KEGGisce:YOR098C

Similar proteinsi

Entry informationi

Entry nameiNUP1_YEAST
AccessioniPrimary (citable) accession number: P20676
Secondary accession number(s): D6W2F9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 18, 2018
This is version 176 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health