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P40477

- NU159_YEAST

UniProt

P40477 - NU159_YEAST

Protein

Nucleoporin NUP159

Gene

NUP159

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.13 Publications

    GO - Molecular functioni

    1. adenyl-nucleotide exchange factor activity Source: SGD
    2. nucleocytoplasmic transporter activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. ncRNA export from nucleus Source: SGD
    2. NLS-bearing protein import into nucleus Source: SGD
    3. nuclear pore distribution Source: SGD
    4. poly(A)+ mRNA export from nucleus Source: SGD
    5. protein export from nucleus Source: SGD
    6. regulation of catalytic activity Source: GOC
    7. ribosomal large subunit export from nucleus Source: SGD
    8. ribosomal small subunit export from nucleus Source: SGD

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31369-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoporin NUP159
    Alternative name(s):
    Nuclear pore protein NUP159
    Gene namesi
    Name:NUP159
    Synonyms:NUP158, RAT7
    Ordered Locus Names:YIL115C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIL115c.
    SGDiS000001377. NUP159.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear membrane Source: UniProtKB-SubCell
    2. nuclear pore Source: SGD
    3. nuclear pore central transport channel Source: SGD
    4. nuclear pore cytoplasmic filaments Source: SGD

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14601460Nucleoporin NUP159PRO_0000204849Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei404 – 4041Phosphoserine2 Publications
    Modified residuei657 – 6571Phosphoserine1 Publication
    Modified residuei724 – 7241Phosphoserine1 Publication
    Modified residuei735 – 7351Phosphoserine3 Publications
    Modified residuei745 – 7451Phosphoserine1 Publication
    Modified residuei803 – 8031Phosphothreonine2 Publications
    Modified residuei805 – 8051Phosphoserine3 Publications
    Modified residuei819 – 8191Phosphoserine3 Publications
    Modified residuei889 – 8891Phosphoserine1 Publication
    Modified residuei940 – 9401Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40477.
    PaxDbiP40477.

    Expressioni

    Gene expression databases

    GenevestigatoriP40477.

    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. NUP159 is part of the NUP82 subcomplex (NUP82, NSP1, NUP159) interacting with NUP82 through its C-terminal coiled coil. This subcomplex is the base for interactions with NUP116 and GLE2 and with NUP42 and GLE1. Interacts through its FG repeats with karyopherins, such as heterodimeric mRNA transport factor MEX67/MTR2, CRM1 (XPO1), and PSE1 (GSP1-GDP dependent). Interaction with CRM1 (XPO1) is GSP1-GTP dependent and stimulated by RNA1. NUP159 also interacts with GLE1 and the ATP-dependent RNA helicase DBP5.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KAP95Q061423EBI-11747,EBI-9145
    NUP82P403685EBI-11747,EBI-12331

    Protein-protein interaction databases

    BioGridi34876. 91 interactions.
    DIPiDIP-2314N.
    IntActiP40477. 17 interactions.
    MINTiMINT-629459.
    STRINGi4932.YIL115C.

    Structurei

    Secondary structure

    1
    1460
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 156
    Beta strandi17 – 259
    Beta strandi42 – 454
    Turni46 – 494
    Beta strandi50 – 556
    Beta strandi58 – 636
    Helixi64 – 729
    Beta strandi73 – 753
    Beta strandi81 – 855
    Beta strandi89 – 957
    Beta strandi98 – 11417
    Beta strandi118 – 1236
    Beta strandi128 – 1336
    Beta strandi135 – 1428
    Beta strandi145 – 1517
    Turni152 – 1543
    Beta strandi157 – 16913
    Beta strandi171 – 1788
    Beta strandi183 – 1897
    Beta strandi192 – 1998
    Helixi203 – 2064
    Turni210 – 2123
    Beta strandi213 – 23119
    Beta strandi245 – 2539
    Beta strandi256 – 26510
    Beta strandi278 – 2847
    Beta strandi286 – 2883
    Beta strandi292 – 2987
    Beta strandi305 – 3073
    Beta strandi309 – 3179
    Helixi318 – 3203
    Turni328 – 3303
    Beta strandi336 – 3427
    Beta strandi364 – 3696
    Beta strandi372 – 3809
    Beta strandi1118 – 11236
    Helixi1436 – 145419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XIPX-ray2.50A2-387[»]
    3PBPX-ray2.60C/F/I/L1425-1460[»]
    3RRMX-ray2.88C2-387[»]
    3TKNX-ray3.40B/E/H1425-1460[»]
    4DS1X-ray1.85B/D1116-1126[»]
    ProteinModelPortaliP40477.
    SMRiP40477. Positions 2-381, 1431-1458.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40477.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati228 – 2314FG 1
    Repeati267 – 2704PXFG 1
    Repeati462 – 4709SXFGXPXFG 1
    Repeati503 – 5119SXFGXPXFG 2; approximate
    Repeati522 – 5309SXFGXPXFG 3; approximate
    Repeati532 – 5354PXFG 2
    Repeati548 – 5569SXFGXPXFG 4
    Repeati558 – 5614PXFG 3
    Repeati574 – 5829SXFGXPXFG 5
    Repeati584 – 5874PXFG 4
    Repeati600 – 6089SXFGXPXFG 6
    Repeati610 – 6134SXFG 1
    Repeati624 – 6329SXFGXPXFG 7; approximate
    Repeati642 – 6454FG 2
    Repeati687 – 6904FG 3
    Repeati704 – 7074FXFG 1
    Repeati709 – 7124SXFG 2
    Repeati728 – 7314FXFG 2
    Repeati842 – 8454PXFG 5
    Repeati873 – 8764FXFG 3

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 500500Interaction with DBP5Add
    BLAST
    Regioni497 – 701205Interactions with CRM1 and GLE1Add
    BLAST
    Regioni1223 – 1460238Interaction with NUP82Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1279 – 132042Add
    BLAST
    Coiled coili1383 – 141836Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi455 – 766312Ser-richAdd
    BLAST

    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: SXFG/PXFG repeats are especially abundant in NUPs on the cytoplasmic side.

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5651.
    GeneTreeiENSGT00730000113975.
    HOGENOMiHOG000113875.
    OMAiFGESAFG.
    OrthoDBiEOG754HXQ.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSLKDEVPT ETSEDFGFKF LGQKQILPSF NEKLPFASLQ NLDISNSKSL     50
    FVAASGSKAV VGELQLLRDH ITSDSTPLTF KWEKEIPDVI FVCFHGDQVL 100
    VSTRNALYSL DLEELSEFRT VTSFEKPVFQ LKNVNNTLVI LNSVNDLSAL 150
    DLRTKSTKQL AQNVTSFDVT NSQLAVLLKD RSFQSFAWRN GEMEKQFEFS 200
    LPSELEELPV EEYSPLSVTI LSPQDFLAVF GNVISETDDE VSYDQKMYII 250
    KHIDGSASFQ ETFDITPPFG QIVRFPYMYK VTLSGLIEPD ANVNVLASSC 300
    SSEVSIWDSK QVIEPSQDSE RAVLPISEET DKDTNPIGVA VDVVTSGTIL 350
    EPCSGVDTIE RLPLVYILNN EGSLQIVGLF HVAAIKSGHY SINLESLEHE 400
    KSLSPTSEKI PIAGQEQEEK KKNNESSKAL SENPFTSANT SGFTFLKTQP 450
    AAANSLQSQS SSTFGAPSFG SSAFKIDLPS VSSTSTGVAS SEQDATDPAS 500
    AKPVFGKPAF GAIAKEPSTS EYAFGKPSFG APSFGSGKSS VESPASGSAF 550
    GKPSFGTPSF GSGNSSVEPP ASGSAFGKPS FGTPSFGSGN SSAEPPASGS 600
    AFGKPSFGTS AFGTASSNET NSGSIFGKAA FGSSSFAPAN NELFGSNFTI 650
    SKPTVDSPKE VDSTSPFPSS GDQSEDESKS DVDSSSTPFG TKPNTSTKPK 700
    TNAFDFGSSS FGSGFSKALE SVGSDTTFKF GTQASPFSSQ LGNKSPFSSF 750
    TKDDTENGSL SKGSTSEIND DNEEHESNGP NVSGNDLTDS TVEQTSSTRL 800
    PETPSDEDGE VVEEEAQKSP IGKLTETIKK SANIDMAGLK NPVFGNHVKA 850
    KSESPFSAFA TNITKPSSTT PAFSFGNSTM NKSNTSTVSP MEEADTKETS 900
    EKGPITLKSV ENPFLPAKEE RTGESSKKDH NDDPKDGYVS GSEISVRTSE 950
    SAFDTTANEE IPKSQDVNNH EKSETDPKYS QHAVVDHDNK SKEMNETSKN 1000
    NERSGQPNHG VQGDGIALKK DNEKENFDSN MAIKQFEDHQ SSEEDASEKD 1050
    SRQSSEVKES DDNMSLNSDR DESISESYDK LEDINTDELP HGGEAFKARE 1100
    VSASADFDVQ TSLEDNYAES GIQTDLSESS KENEVQTDAI PVKHNSTQTV 1150
    KKEAVDNGLQ TEPVETCNFS VQTFEGDENY LAEQCKPKQL KEYYTSAKVS 1200
    NIPFVSQNST LRLIESTFQT VEAEFTVLME NIRNMDTFFT DQSSIPLVKR 1250
    TVRSINNLYT WRIPEAEILL NIQNNIKCEQ MQITNANIQD LKEKVTDYVR 1300
    KDIAQITEDV ANAKEEYLFL MHFDDASSGY VKDLSTHQFR MQKTLRQKLF 1350
    DVSAKINHTE ELLNILKLFT VKNKRLDDNP LVAKLAKESL ARDGLLKEIK 1400
    LLREQVSRLQ LEEKGKKASS FDASSSITKD MKGFKVVEVG LAMNTKKQIG 1450
    DFFKNLNMAK 1460
    Length:1,460
    Mass (Da):158,908
    Last modified:February 1, 1995 - v1
    Checksum:iA33FFA52378F8205
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40634 Genomic DNA. Translation: AAC41652.1.
    Z38125 Genomic DNA. Translation: CAA86265.1.
    BK006942 Genomic DNA. Translation: DAA08438.1.
    PIRiS48457.
    RefSeqiNP_012151.1. NM_001179463.1.

    Genome annotation databases

    EnsemblFungiiYIL115C; YIL115C; YIL115C.
    GeneIDi854691.
    KEGGisce:YIL115C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40634 Genomic DNA. Translation: AAC41652.1 .
    Z38125 Genomic DNA. Translation: CAA86265.1 .
    BK006942 Genomic DNA. Translation: DAA08438.1 .
    PIRi S48457.
    RefSeqi NP_012151.1. NM_001179463.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XIP X-ray 2.50 A 2-387 [» ]
    3PBP X-ray 2.60 C/F/I/L 1425-1460 [» ]
    3RRM X-ray 2.88 C 2-387 [» ]
    3TKN X-ray 3.40 B/E/H 1425-1460 [» ]
    4DS1 X-ray 1.85 B/D 1116-1126 [» ]
    ProteinModelPortali P40477.
    SMRi P40477. Positions 2-381, 1431-1458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34876. 91 interactions.
    DIPi DIP-2314N.
    IntActi P40477. 17 interactions.
    MINTi MINT-629459.
    STRINGi 4932.YIL115C.

    Protein family/group databases

    TCDBi 1.I.1.1.1. the nuclear pore complex (npc) family.

    Proteomic databases

    MaxQBi P40477.
    PaxDbi P40477.

    Protocols and materials databases

    DNASUi 854691.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIL115C ; YIL115C ; YIL115C .
    GeneIDi 854691.
    KEGGi sce:YIL115C.

    Organism-specific databases

    CYGDi YIL115c.
    SGDi S000001377. NUP159.

    Phylogenomic databases

    eggNOGi COG5651.
    GeneTreei ENSGT00730000113975.
    HOGENOMi HOG000113875.
    OMAi FGESAFG.
    OrthoDBi EOG754HXQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31369-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P40477.
    NextBioi 977319.

    Gene expression databases

    Genevestigatori P40477.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes."
      Gorsch L.C., Dockendorff T.C., Cole C.N.
      J. Cell Biol. 129:939-955(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex."
      Hurwitz M.E., Strambio-de-Castillia C., Blobel G.
      Proc. Natl. Acad. Sci. U.S.A. 95:11241-11245(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NUP82.
    5. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NSP1.
    6. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PSE1.
    7. "Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells."
      Hodge C.A., Colot H.V., Stafford P., Cole C.N.
      EMBO J. 18:5778-5788(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GLE1; CRM1 AND DBP5.
    8. Cited for: FUNCTION, NUP82 NPC SUBCOMPLEX.
    9. "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.
    10. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MEX67/MTR2 HETERODIMER.
    11. "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 WITH KARYOPHERINS THROUGH FG REPEATS.
    12. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
    13. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NPC ASSEMBLY.
    14. "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 CRM1 AND RNA1.
    15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    16. "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.
    17. "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.
    18. "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.
    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-404; SER-735; THR-803; SER-805 AND SER-819, 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-657; SER-724; SER-735; SER-745; SER-805; SER-819; SER-889 AND SER-940, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-735; THR-803; SER-805; SER-819 AND SER-940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore."
      Weirich C.S., Erzberger J.P., Berger J.M., Weis K.
      Mol. Cell 16:749-760(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-387, FUNCTION, INTERACTION WITH DBP5.
    23. "Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex."
      Yoshida K., Seo H.S., Debler E.W., Blobel G., Hoelz A.
      Proc. Natl. Acad. Sci. U.S.A. 108:16571-16576(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1425-1460 IN COMPLEX WITH NUP82 AND NUP116, SUBUNIT.
    24. "Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex."
      Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.
      J. Mol. Biol. 419:330-346(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1425-1460 IN COMPLEX WITH NUP82 AND THE MOUSE ORTHOLOG OF NUP145, SUBUNIT.

    Entry informationi

    Entry nameiNU159_YEAST
    AccessioniPrimary (citable) accession number: P40477
    Secondary accession number(s): D6VVH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1230 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. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3