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P20676 (NUP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 NUP1
Alternative name(s):
Nuclear pore protein NUP1
Gene names
Name:NUP1
Ordered Locus Names:YOR098C
ORF Names:YOR3182C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1076 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16

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. Interacts through its FG repeats with nuclear transport receptors. Binds to the nuclear basket of the NPC through NUP60. Interacts with KAP122. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

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).

Post-translational modification

Phosphorylated by CDC28 Probable. Ref.18

Miscellaneous

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KAP95Q061426EBI-12392,EBI-9145

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.22
Chain2 – 10761075Nucleoporin NUP1
PRO_0000204902

Regions

Repeat336 – 3383FXF 1
Repeat384 – 3863FXF 2
Repeat406 – 4094FXFG 1
Repeat422 – 4254FXFG 2
Repeat448 – 4514FXFG 3
Repeat484 – 4874FXFG 4
Repeat510 – 5134FXFG 5
Repeat525 – 5284FXFG 6
Repeat543 – 5464FXFG 7
Repeat571 – 5744FXFG 8
Repeat591 – 5933FXF 3
Repeat614 – 6163FXF 4
Repeat636 – 6383FXF 5
Repeat657 – 6593FXF 6
Repeat671 – 6744FXFG 9
Repeat689 – 6913FXF 7
Repeat708 – 7114FXFG 10
Repeat727 – 7304FXFG 11
Repeat753 – 7553FXF 8
Repeat800 – 8034FXFG 12
Repeat819 – 8213FXF 9
Repeat866 – 8683FXF 10
Repeat885 – 8884FXFG 13
Repeat929 – 9313FXF 11
Repeat1008 – 10092FG 1
Repeat1027 – 10282FG 2
Repeat1038 – 10392FG 3
Region1040 – 107637Interaction with KAP95
Compositional bias81 – 844Poly-Asn
Compositional bias718 – 7236Poly-Thr
Compositional bias830 – 8334Poly-Thr
Compositional bias881 – 1022142Asn-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.22
Modified residue541Phosphoserine Ref.20
Modified residue1611Phosphoserine Ref.19
Modified residue3811Phosphothreonine Ref.20
Modified residue3831Phosphoserine Ref.20
Modified residue6371Phosphoserine Ref.20

Secondary structure

.... 1076
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20676 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 4AC23567D2FB53CC

FASTA1,076113,581
        10         20         30         40         50         60 
MSSNTSSVMS SPRVEKRSFS STLKSFFTNP NKKRPSSKKV FSSNLSYANH LEESDVEDTL 

        70         80         90        100        110        120 
HVNKRKRVSG TSQHSDSLTQ NNNNAPIIIY GTENTERPPL LPILPIQRLR LLREKQRVRN 

       130        140        150        160        170        180 
MRELGLIQST EFPSITSSVI LGSQSKSDEG GSYLCTSSTP SPIKNGSCTR QLAGKSGEDT 

       190        200        210        220        230        240 
NVGLPILKSL KNRSNRKRFH SQSKGTVWSA NFEYDLSEYD AIQKKDNKDK EGNAGGDQKT 

       250        260        270        280        290        300 
SENRNNIKSS ISNGNLATGP NLTSEIEDLR ADINSNRLSN PQKNLLLKGP ASTVAKTAPI 

       310        320        330        340        350        360 
QESFVPNSER SGTPTLKKNI EPKKDKESIV LPTVGFDFIK DNETPSKKTS PKATSSAGAV 

       370        380        390        400        410        420 
FKSSVEMGKT DKSTKTAEAP TLSFNFSQKA NKTKAVDNTV PSTTLFNFGG KSDTVTSASQ 

       430        440        450        460        470        480 
PFKFGKTSEK SENHTESDAP PKSTAPIFSF GKQEENGDEG DDENEPKRKR RLPVSEDTNT 

       490        500        510        520        530        540 
KPLFDFGKTG DQKETKKGES EKDASGKPSF VFGASDKQAE GTPLFTFGKK ADVTSNIDSS 

       550        560        570        580        590        600 
AQFTFGKAAT AKETHTKPSE TPATIVKKPT FTFGQSTSEN KISEGSAKPT FSFSKSEEER 

       610        620        630        640        650        660 
KSSPISNEAA KPSFSFPGKP VDVQAPTDDK TLKPTFSFTE PAQKDSSVVS EPKKPSFTFA 

       670        680        690        700        710        720 
SSKTSQPKPL FSFGKSDAAK EPPGSNTSFS FTKPPANETD KRPTPPSFTF GGSTTNNTTT 

       730        740        750        760        770        780 
TSTKPSFSFG APESMKSTAS TAAANTEKLS NGFSFTKFNH NKEKSNSPTS FFDGSASSTP 

       790        800        810        820        830        840 
IPVLGKPTDA TGNTTSKSAF SFGTANTNGT NASANSTSFS FNAPATGNGT TTTSNTSGTN 

       850        860        870        880        890        900 
IAGTFNVGKP DQSIASGNTN GAGSAFGFSS SGTAATGAAS NQSSFNFGNN GAGGLNPFTS 

       910        920        930        940        950        960 
ATSSTNANAG LFNKPPSTNA QNVNVPSAFN FTGNNSTPGG GSVFNMNGNT NANTVFAGSN 

       970        980        990       1000       1010       1020 
NQPHQSQTPS FNTNSSFTPS TVPNINFSGL NGGITNTATN ALRPSDIFGA NAASGSNSNV 

      1030       1040       1050       1060       1070 
TNPSSIFGGA GGVPTTSFGQ PQSAPNQMGM GTNNGMSMGG GVMANRKIAR MRHSKR 

« Hide

References

« Hide 'large scale' references
[1]"The NUP1 gene encodes an essential component of the yeast nuclear pore complex."
Davis L.I., Fink G.R.
Cell 61:965-978(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequencing and analysis of 130 kb from yeast chromosome XV."
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.
Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[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 THROUGH FG REPEATS.
[12]"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, IMPORT COMPLEX DISASSEMBLY.
[13]"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, AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
[14]"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].
[15]"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.
[16]"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.
[17]"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.
[18]"Targets of the cyclin-dependent kinase Cdk1."
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O.
Nature 425:859-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CDC28.
[19]"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-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[20]"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-54; THR-381; SER-383 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33632 Genomic DNA. Translation: AAA34822.1.
X94335 Genomic DNA. Translation: CAA64020.1.
Z75006 Genomic DNA. Translation: CAA99295.1.
BK006948 Genomic DNA. Translation: DAA10875.1.
PIRA35622.
RefSeqNP_014741.1. NM_001183517.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BPTX-ray1.99B974-1012[»]
ProteinModelPortalP20676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34496. 68 interactions.
DIPDIP-81N.
IntActP20676. 47 interactions.
MINTMINT-1759946.
STRING4932.YOR098C.

Protein family/group databases

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

Proteomic databases

PaxDbP20676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR098C; YOR098C; YOR098C.
GeneID854265.
KEGGsce:YOR098C.

Organism-specific databases

CYGDYOR098c.
SGDS000005624. NUP1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00730000111010.
OMAENTERPP.
OrthoDBEOG7BW0ST.

Enzyme and pathway databases

BioCycYEAST:G3O-33631-MONOMER.

Gene expression databases

GenevestigatorP20676.

Family and domain databases

InterProIPR026054. Nucleoporin.
IPR018892. Retro-transposon_transp_CS.
[Graphical view]
PANTHERPTHR23193. PTHR23193. 1 hit.
PfamPF10599. Nup_retrotrp_bd. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20676.
NextBio976209.

Entry information

Entry nameNUP1_YEAST
AccessionPrimary (citable) accession number: P20676
Secondary accession number(s): D6W2F9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

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

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references