Nucleoporin NUP1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P20676 (NUP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nucleoporin NUP1

Alternative name(s):
Nuclear pore protein NUP1

Gene names

Name:	NUP1
Ordered Locus Names:	YOR098C
ORF Names:	YOR3182C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1076 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nuclear 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 Ref.19 Ref.20 Ref.21
Miscellaneous	Present with 468 molecules/cell in log phase SD medium. Ref.14

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	NLS-bearing substrate import into nucleus Inferred from mutant phenotype Ref.7. Source: SGD poly(A)+ mRNA export from nucleus Inferred from mutant phenotype. Source: SGD ribosomal large subunit export from nucleus Inferred from mutant phenotype. Source: SGD transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Inferred from mutant phenotype. Source: SGD
Cellular component	nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from direct assay Ref.6 Ref.7 Ref.1. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KAP95	Q06142	6	EBI-12392,EBI-9145

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1076

1076

Nucleoporin NUP1

PRO_0000204902

Regions

Repeat

336 – 338

FXF 1

Repeat

384 – 386

FXF 2

Repeat

406 – 409

FXFG 1

Repeat

422 – 425

FXFG 2

Repeat

448 – 451

FXFG 3

Repeat

484 – 487

FXFG 4

Repeat

510 – 513

FXFG 5

Repeat

525 – 528

FXFG 6

Repeat

543 – 546

FXFG 7

Repeat

571 – 574

FXFG 8

Repeat

591 – 593

FXF 3

Repeat

614 – 616

FXF 4

Repeat

636 – 638

FXF 5

Repeat

657 – 659

FXF 6

Repeat

671 – 674

FXFG 9

Repeat

689 – 691

FXF 7

Repeat

708 – 711

FXFG 10

Repeat

727 – 730

FXFG 11

Repeat

753 – 755

FXF 8

Repeat

800 – 803

FXFG 12

Repeat

819 – 821

FXF 9

Repeat

866 – 868

FXF 10

Repeat

885 – 888

FXFG 13

Repeat

929 – 931

FXF 11

Repeat

1008 – 1009

FG 1

Repeat

1027 – 1028

FG 2

Repeat

1038 – 1039

FG 3

Region

1040 – 1076

Interaction with KAP95

Compositional bias

81 – 84

Poly-Asn

Compositional bias

718 – 723

Poly-Thr

Compositional bias

830 – 833

Poly-Thr

Compositional bias

881 – 1022

142

Asn-rich

Amino acid modifications

Modified residue

Phosphoserine Ref.20

Modified residue

Phosphoserine Ref.21

Modified residue

157

Phosphoserine Ref.21

Modified residue

158

Phosphoserine Ref.21

Modified residue

159

Phosphothreonine Ref.21

Modified residue

161

Phosphoserine Ref.19

Modified residue

249

Phosphoserine Ref.21

Modified residue

252

Phosphoserine Ref.20 Ref.21

Modified residue

313

Phosphothreonine Ref.20

Modified residue

356

Phosphoserine Ref.20

Modified residue

381

Phosphothreonine Ref.21

Modified residue

383

Phosphoserine; by CHEK2 Ref.20 Ref.21

Modified residue

387

Phosphoserine Ref.20

Modified residue

419

Phosphoserine Ref.20

Modified residue

437

Phosphoserine Ref.20

Modified residue

449

Phosphoserine; by CHEK2 Ref.20

Modified residue

509

Phosphoserine Ref.20 Ref.21

Modified residue

572

Phosphothreonine Ref.20

Modified residue

592

Phosphoserine; by CHEK2 Ref.20 Ref.21

Modified residue

594

Phosphoserine Ref.21

Modified residue

615

Phosphoserine; by CHEK2 Ref.20

Modified residue

635

Phosphothreonine Ref.20

Modified residue

637

Phosphoserine; by CHEK2 Ref.20 Ref.21

Modified residue

639

Phosphothreonine Ref.21

Modified residue

647

Phosphoserine Ref.20

Modified residue

656

Phosphoserine; by CHEK2 Ref.20 Ref.21

Modified residue

672

Phosphoserine; by CHEK2 Ref.20

Modified residue

754

Phosphoserine; by CHEK2 Ref.20 Ref.21

Modified residue

765

Phosphoserine Ref.20 Ref.21

Modified residue

767

Phosphoserine Ref.21

Modified residue

769

Phosphothreonine Ref.21

Secondary structure

1076

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P20676 [UniParc].

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

FASTA

1,076

113,581

        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' referencesShow '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: 2190694] [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: 9200815] [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. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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: 10525531] [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: 10684247] [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: 11046143] [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: 11387327] [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: 11535617] [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: 12372823] [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: 12543930] [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: 11867631] [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: 12917401] [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: 14562106] [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: 12604785] [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: 15039779] [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: 12791264] [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: 14574415] [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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY. Strain: ADR376.
[20]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-252; THR-313; SER-356; SER-383; SER-387; SER-419; SER-437; SER-449; SER-509; THR-572; SER-592; SER-615; SER-656; THR-635; SER-637; SER-647; SER-672; SER-754 AND SER-765, MASS SPECTROMETRY.
[21]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-157; SER-158; THR-159; SER-249; SER-252; THR-381; SER-383; SER-509; SER-592; SER-594; SER-637; THR-639; SER-656; SER-754; SER-765; SER-767 AND THR-769, MASS SPECTROMETRY.
+	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.

PIR

A35622.

RefSeq

NP_014741.1. NM_001183517.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BPT	X-ray	1.99	B	974-1012	[»]

ProteinModelPortal

P20676.

SMR

P20676. Positions 974-1012.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-81N.

IntAct

P20676. 47 interactions.

MINT

MINT-1759946.

STRING

P20676.

Protein family/group databases

TCDB

9.A.14.1.1. nuclear pore complex (NPC) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR098C; YOR098C; YOR098C.

GeneID

854265.

KEGG

sce:YOR098C.

NMPDR

fig|4932.3.peg.5843.

Organism-specific databases

CYGD

YOR098c.

SGD

S000005624. NUP1.

Phylogenomic databases

eggNOG

fuNOG11989.

GeneTree

EFGT00050000000035.

OMA

HGRSAIY.

OrthoDB

EOG4J40SX.

Gene expression databases

ArrayExpress

P20676.

Genevestigator

P20676.

GermOnline

YOR098C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR018892. Retro-transposon_transp_CS.
[Graphical view]

Pfam

PF10599. Nup_retrotrp_bd. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976209.

Entry information

Entry name

NUP1_YEAST

Accession

Primary (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:	December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents