Nucleoporin NSP1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P14907 (NSP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 126. History...

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

Documents (4) |

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 NSP1

Alternative name(s):
Nuclear pore protein NSP1
Nucleoskeletal-like protein
p110

Gene names

Name:	NSP1
Ordered Locus Names:	YJL041W
ORF Names:	J1207

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	823 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). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19
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. NSP1 interacts alternatively with NUP82 or NUP57 through its C-terminal coiled coil in two distinct NPC subcomplexes, the NUP82 subcomplex (NUP82, NSP1, NUP159) and the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57). The NUP82 subcomplex is the base for interactions with NUP116 and GLE2 and with NUP42 and GLE1. Interacts through its FG repeats with karyopherins, such as KAP95, KAP123, PSE1, LOS1, NTF2, the heterodimeric mRNA transport factor MEX67/MTR2, and GSP1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.16 Ref.23
Subcellular location	Nucleus › nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Symmetric distribution.
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. Ref.4
Miscellaneous	Present with 2400 molecules/cell in log phase SD medium. Ref.17
Sequence similarities	Belongs to the nucleoporin NSP1/NUP62 family.

Ontologies

Keywords
Biological process	Cell cycle Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW ncRNA export from nucleus Inferred from mutant phenotype Ref.15. Source: SGD poly(A)+ mRNA export from nucleus Inferred from genetic interaction Ref.12. Source: SGD protein import into nucleus Inferred from mutant phenotype Ref.4. Source: SGD ribosomal large subunit export from nucleus Inferred from mutant phenotype Ref.14. Source: SGD ribosomal small subunit export from nucleus Inferred from mutant phenotype Ref.14. Source: SGD tRNA export from nucleus Inferred from mutant phenotype. Source: SGD
Cellular component	Nic96 complex Inferred from direct assay Ref.5. Source: SGD Nup82 complex Inferred from direct assay. Source: SGD nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phospholipid binding Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct structural constituent of nuclear pore Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
KAP95	Q06142	3	EBI-12265,EBI-9145
NUP57	P48837	4	EBI-12265,EBI-12324
NUP82	P40368	9	EBI-12265,EBI-12331

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 823

823

Nucleoporin NSP1

PRO_0000204865

Regions

Repeat

13 – 16

FSFG 1

Repeat

36 – 37

FG 1

Repeat

43 – 44

FG 2

Repeat

64 – 65

FG 3

Repeat

74 – 75

FG 4

Repeat

84 – 85

FG 5

Repeat

94 – 95

FG 6

Repeat

104 – 105

FG 7

Repeat

123 – 124

FG 8

Repeat

142 – 143

FG 9

Repeat

147 – 148

FG 10

Repeat

168 – 169

FG 11

Repeat

179 – 182

FSFG 2

Repeat

217 – 220

FSFG 3

Repeat

239 – 240

FG 12

Repeat

268 – 269

FG 13

Repeat

284 – 287

FSFG 4

Repeat

303 – 306

FSFG 5

Repeat

322 – 325

FSFG 6

Repeat

341 – 344

FSFG 7

Repeat

360 – 363

FSFG 8

Repeat

379 – 382

FSFG 9

Repeat

398 – 401

FSFG 10

Repeat

417 – 420

FSFG 11

Repeat

436 – 439

FSFG 12

Repeat

455 – 458

FSFG 13

Repeat

474 – 477

FSFG 14

Repeat

493 – 496

FSFG 15

Repeat

512 – 515

FSFG 16

Repeat

531 – 534

FSFG 17

Repeat

550 – 553

FSFG 18

Repeat

571 – 572

FG 14

Repeat

588 – 591

FSFG 19; approximate

Region

673 – 738

Competitive binding site of NUP57 and NUP82

Region

740 – 823

Required for association with NUP57 subcomplex

Coiled coil

630 – 823

194

Potential

Compositional bias

2 – 175

174

Asn-rich

Compositional bias

308 – 628

321

Lys-rich

Amino acid modifications

Modified residue

221

Phosphoserine Ref.22

Modified residue

238

Phosphoserine Ref.22

Modified residue

281

Phosphothreonine Ref.22

Modified residue

283

Phosphoserine Ref.22

Modified residue

285

Phosphoserine Ref.22

Modified residue

375

Phosphoserine Ref.22

Modified residue

456

Phosphoserine Ref.21 Ref.22

Modified residue

570

Phosphoserine Ref.22

Modified residue

622

Phosphoserine Ref.22

Modified residue

728

Phosphothreonine Ref.22

Modified residue

729

Phosphoserine Ref.22

Modified residue

730

Phosphoserine Ref.22

Sequences

Sequence

Length

Mass (Da)

Tools

P14907 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: A258003CB1917810
Show »

FASTA

823

86,516

        10         20         30         40         50         60 
MNFNTPQQNK TPFSFGTANN NSNTTNQNSS TGAGAFGTGQ STFGFNNSAP NNTNNANSSI 

        70         80         90        100        110        120 
TPAFGSNNTG NTAFGNSNPT SNVFGSNNST TNTFGSNSAG TSLFGSSSAQ QTKSNGTAGG 

       130        140        150        160        170        180 
NTFGSSSLFN NSTNSNTTKP AFGGLNFGGG NNTTPSSTGN ANTSNNLFGA TANANKPAFS 

       190        200        210        220        230        240 
FGATTNDDKK TEPDKPAFSF NSSVGNKTDA QAPTTGFSFG SQLGGNKTVN EAAKPSLSFG 

       250        260        270        280        290        300 
SGSAGANPAG ASQPEPTTNE PAKPALSFGT ATSDNKTTNT TPSFSFGAKS DENKAGATSK 

       310        320        330        340        350        360 
PAFSFGAKPE EKKDDNSSKP AFSFGAKSNE DKQDGTAKPA FSFGAKPAEK NNNETSKPAF 

       370        380        390        400        410        420 
SFGAKSDEKK DGDASKPAFS FGAKPDENKA SATSKPAFSF GAKPEEKKDD NSSKPAFSFG 

       430        440        450        460        470        480 
AKSNEDKQDG TAKPAFSFGA KPAEKNNNET SKPAFSFGAK SDEKKDGDAS KPAFSFGAKS 

       490        500        510        520        530        540 
DEKKDSDSSK PAFSFGTKSN EKKDSGSSKP AFSFGAKPDE KKNDEVSKPA FSFGAKANEK 

       550        560        570        580        590        600 
KESDESKSAF SFGSKPTGKE EGDGAKAAIS FGAKPEEQKS SDTSKPAFTF GAQKDNEKKT 

       610        620        630        640        650        660 
EESSTGKSTA DVKSSDSLKL NSKPVELKPV SLDNKTLDDL VTKWTNQLTE SASHFEQYTK 

       670        680        690        700        710        720 
KINSWDQVLV KGGEQISQLY SDAVMAEHSQ NKIDQSLQYI ERQQDELENF LDNFETKTEA 

       730        740        750        760        770        780 
LLSDVVSTSS GAAANNNDQK RQQAYKTAQT LDENLNSLSS NLSSLIVEIN NVSNTFNKTT 

       790        800        810        820 
NIDINNEDEN IQLIKILNSH FDALRSLDDN STSLEKQINS IKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae." Hurt E.C. EMBO J. 7:4323-4334(1988) [PubMed: 3072197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain." Nehrbass U., Kern H., Mutvei A., Horstmann H., Marshallsay B., Hurt E.C. Cell 61:979-989(1990) [PubMed: 2112428] [Abstract] Cited for: DOMAINS.
[5]	"In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p." Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C. Mol. Biol. Cell 8:33-46(1997) [PubMed: 9017593] [Abstract] Cited for: FUNCTION, NUP57 NPC SUBCOMPLEX.
[6]	"Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA." Hellmuth K., Lau D.M., Bischoff F.R., Kuenzler M., Hurt E.C., Simos G. Mol. Cell. Biol. 18:6374-6386(1998) [PubMed: 9774653] [Abstract] Cited for: FUNCTION, INTERACTION WITH LOS1.
[7]	"The small GTPase Gsp1p binds to the repeat domain of the nucleoporin Nsp1p." Stochaj U., Hejazi M., Belhumeur P. Biochem. J. 330:421-427(1998) [PubMed: 9461539] [Abstract] Cited for: FUNCTION, INTERACTION WITH GSP1.
[8]	"Functional characterization of a Nup159p-containing nuclear pore subcomplex." Belgareh N., Snay-Hodge C., Pasteau F., Dagher S., Cole C.N., Doye V. Mol. Biol. Cell 9:3475-3492(1998) [PubMed: 9843582] [Abstract] Cited for: FUNCTION, INTERACTION WITH NUP159.
[9]	"Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase." Seedorf M., Damelin M., Kahana J., Taura T., Silver P.A. Mol. Cell. Biol. 19:1547-1557(1999) [PubMed: 9891088] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSE1.
[10]	"The mechanism of ran import into the nucleus by nuclear transport factor 2." Quimby B.B., Lamitina T., L'Hernault S.W., Corbett A.H. J. Biol. Chem. 275:28575-28582(2000) [PubMed: 10889207] [Abstract] Cited for: FUNCTION, INTERACTION WITH NTF2.
[11]	"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.
[12]	"Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export." Straesser K., Bassler J., Hurt E.C. J. Cell Biol. 150:695-706(2000) [PubMed: 10952996] [Abstract] Cited for: FUNCTION, INTERACTION WITH MEX67/MTR2 HETERODIMER.
[13]	"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, NUCLEOPORIN INTERACTING PROTEINS.
[14]	"Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex." Gleizes P.-E., Noaillac-Depeyre J., Leger-Silvestre I., Teulieres F., Dauxois J.-Y., Pommet D., Azum-Gelade M.-C., Gas N. J. Cell Biol. 155:923-936(2001) [PubMed: 11739405] [Abstract] Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
[15]	"Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export." Grosshans H., Deinert K., Hurt E.C., Simos G. J. Cell Biol. 153:745-762(2001) [PubMed: 11352936] [Abstract] Cited for: FUNCTION, NUCLEAR SRP EXPORT.
[16]	"The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport." Bailer S.M., Balduf C., Hurt E.C. Mol. Cell. Biol. 21:7944-7955(2001) [PubMed: 11689687] [Abstract] Cited for: FUNCTION, SUBCOMPLEX ASSEMBLY, INTERACTION WITH NUP57 AND NUP82.
[17]	"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].
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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-456, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; SER-238; THR-281; SER-283; SER-285; SER-375; SER-456; SER-570; SER-622; THR-728; SER-729 AND SER-730, MASS SPECTROMETRY.
[23]	"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: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 511-516 IN COMPLEX WITH HUMAN IMPORTIN BETA-1 SUBUNIT, STRUCTURAL BASIS OF FG REPEAT INTERACTION, INTERACTION WITH KAP95.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M37160 Genomic DNA. Translation: AAA34821.1.
Z49316 Genomic DNA. Translation: CAA89332.1.
Z49314 Genomic DNA. Translation: CAA89331.1.
BK006943 Genomic DNA. Translation: DAA08759.1.

PIR

S14055.

RefSeq

NP_012494.1. NM_001181474.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O6O	X-ray	2.80	D/E/F	497-608	[»]

ProteinModelPortal

P14907.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1484N.

IntAct

P14907. 37 interactions.

MINT

MINT-405423.

STRING

P14907.

Protein family/group databases

TCDB

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

Proteomic databases

PeptideAtlas

P14907.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJL041W; YJL041W; YJL041W.

GeneID

853409.

KEGG

sce:YJL041W.

NMPDR

fig|4932.3.peg.3468.

Organism-specific databases

CYGD

YJL041w.

SGD

S000003577. NSP1.

Phylogenomic databases

eggNOG

fuNOG04689.

GeneTree

EFGT00050000000035.

HOGENOM

HBG591578.

OMA

LDEMGKD.

OrthoDB

EOG4578H2.

Gene expression databases

ArrayExpress

P14907.

Genevestigator

P14907.

GermOnline

YJL041W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007758. Nucleoporin_NSP1_C.
[Graphical view]

Pfam

PF05064. Nsp1_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

973915.

Entry information

Entry name

NSP1_YEAST

Accession

Primary (citable) accession number: P14907
Secondary accession number(s): D6VWE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	December 14, 2011
This is version 126 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

Yeast chromosome X

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic 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