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P32499

- NUP2_YEAST

UniProt

P32499 - NUP2_YEAST

Protein

Nucleoporin NUP2

Gene

NUP2

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 155 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      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). As one of the FG repeat nucleoporins NUP2 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 NUP1 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, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading.12 Publications

    GO - Molecular functioni

    1. nucleocytoplasmic transporter activity Source: SGD
    2. protein binding Source: IntAct
    3. Ran GTPase binding Source: SGD

    GO - Biological processi

    1. chromatin silencing at silent mating-type cassette Source: SGD
    2. maintenance of chromatin silencing at telomere Source: SGD
    3. mRNA export from nucleus in response to heat stress Source: SGD
    4. NLS-bearing protein import into nucleus Source: SGD
    5. poly(A)+ mRNA export from nucleus Source: SGD
    6. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
    7. protein export from nucleus Source: SGD
    8. protein import into nucleus, substrate release Source: SGD
    9. protein targeting to nuclear inner membrane Source: SGD
    10. transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32414-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoporin NUP2
    Alternative name(s):
    Nuclear pore protein NUP2
    p95
    Gene namesi
    Name:NUP2
    Ordered Locus Names:YLR335W
    ORF Names:L8300.9
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR335w.
    SGDiS000004327. NUP2.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear membrane Source: UniProtKB-SubCell
    2. nuclear pore cytoplasmic filaments Source: SGD
    3. nuclear pore nuclear basket Source: SGD

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 720720Nucleoporin NUP2PRO_0000204903Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171Phosphoserine4 Publications
    Modified residuei20 – 201Phosphoserine4 Publications
    Modified residuei137 – 1371Phosphoserine1 Publication
    Modified residuei165 – 1651Phosphoserine1 Publication
    Modified residuei203 – 2031Phosphoserine4 Publications
    Modified residuei205 – 2051Phosphoserine3 Publications
    Modified residuei348 – 3481Phosphoserine1 Publication
    Modified residuei351 – 3511Phosphoserine1 Publication
    Modified residuei361 – 3611Phosphothreonine1 Publication
    Modified residuei581 – 5811Phosphoserine1 Publication
    Modified residuei590 – 5901Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32499.
    PaxDbiP32499.
    PeptideAtlasiP32499.

    Expressioni

    Gene expression databases

    GenevestigatoriP32499.

    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. Binds to the nuclear basket of the NPC through NUP60 in a (GSP1, GSP2) GTPase-GTP-dependent manner. Interacts through its FG repeats with nuclear transport factors. Interacts with KAP122.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KAP95Q061425EBI-12401,EBI-9145
    NUP60P397052EBI-12401,EBI-20731
    SRP1Q028213EBI-12401,EBI-1797

    Protein-protein interaction databases

    BioGridi31599. 89 interactions.
    DIPiDIP-859N.
    IntActiP32499. 30 interactions.
    MINTiMINT-395606.
    STRINGi4932.YLR335W.

    Structurei

    Secondary structure

    1
    720
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni12 – 143
    Helixi34 – 374
    Turni47 – 493

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UN0X-ray2.60C/D1-51[»]
    2C1TX-ray2.60C/D1-51[»]
    DisProtiDP00222.
    ProteinModelPortaliP32499.
    SMRiP32499. Positions 2-46, 606-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32499.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati67 – 693FXF 1
    Repeati189 – 1924FXFG 1
    Repeati216 – 2183FXF 2
    Repeati247 – 2493FXF 3
    Repeati285 – 2884FXFG 2
    Repeati302 – 3054FXFG 3
    Repeati318 – 3214FXFG 4
    Repeati352 – 3543FXF 4
    Repeati369 – 3724FXFG 5
    Repeati386 – 3894FXFG 6
    Repeati438 – 4414FXFG 7
    Repeati474 – 4774FXFG 8
    Repeati493 – 4964FXFG 9
    Repeati511 – 5144FXFG 10
    Repeati524 – 5274FXFG 11
    Repeati550 – 5523FXF 5
    Domaini583 – 720138RanBD1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 5016Interaction with SRP1 NLS binding site 1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi333 – 37745Ser-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: FXFG repeats are especially abundant in NUPs on the nucleoplasmic side (in a highly charged environment and enriched in Ser and Thr).

    Sequence similaritiesi

    Contains 1 RanBD1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5171.
    GeneTreeiENSGT00730000113442.
    HOGENOMiHOG000248337.
    OMAiENEDTVI.
    OrthoDBiEOG7TF7N6.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR015007. NUP2/50/61.
    IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    [Graphical view]
    PfamiPF08911. NUP50. 1 hit.
    PF00638. Ran_BP1. 1 hit.
    [Graphical view]
    SMARTiSM00160. RanBD. 1 hit.
    [Graphical view]
    PROSITEiPS50196. RANBD1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32499-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKRVADAQI QRETYDSNES DDDVTPSTKV ASSAVMNRRK IAMPKRRMAF    50
    KPFGSAKSDE TKQASSFSFL NRADGTGEAQ VDNSPTTESN SRLKALNLQF 100
    KAKVDDLVLG KPLADLRPLF TRYELYIKNI LEAPVKSIEN PTQTKGNDAK 150
    PAKVEDVQKS SDSSSEDEVK VEGPKFTIDA KPPISDSVFS FGPKKENRKK 200
    DESDSENDIE IKGPEFKFSG TVSSDVFKLN PSTDKNEKKT ETNAKPFSFS 250
    SATSTTEQTK SKNPLSLTEA TKTNVDNNSK AEASFTFGTK HAADSQNNKP 300
    SFVFGQAAAK PSLEKSSFTF GSTTIEKKND ENSTSNSKPE KSSDSNDSNP 350
    SFSFSIPSKN TPDASKPSFS FGVPNSSKNE TSKPVFSFGA ATPSAKEASQ 400
    EDDNNNVEKP SSKPAFNLIS NAGTEKEKES KKDSKPAFSF GISNGSESKD 450
    SDKPSLPSAV DGENDKKEAT KPAFSFGINT NTTKTADTKA PTFTFGSSAL 500
    ADNKEDVKKP FSFGTSQPNN TPSFSFGKTT ANLPANSSTS PAPSIPSTGF 550
    KFSLPFEQKG SQTTTNDSKE ESTTEATGNE SQDATKVDAT PEESKPINLQ 600
    NGEEDEVALF SQKAKLMTFN AETKSYDSRG VGEMKLLKKK DDPSKVRLLC 650
    RSDGMGNVLL NATVVDSFKY EPLAPGNDNL IKAPTVAADG KLVTYIVKFK 700
    QKEEGRSFTK AIEDAKKEMK 720
    Length:720
    Mass (Da):77,881
    Last modified:May 16, 2003 - v2
    Checksum:i467210F14FA73311
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371S → F in CAA49587. (PubMed:8443417)Curated
    Sequence conflicti370 – 3701S → N in CAA49587. (PubMed:8443417)Curated
    Sequence conflicti418 – 4181L → F in CAA49587. (PubMed:8443417)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69964 Genomic DNA. Translation: CAA49587.1.
    U19028 Genomic DNA. Translation: AAB67259.1.
    BK006945 Genomic DNA. Translation: DAA09641.1.
    PIRiS51340.
    RefSeqiNP_013439.1. NM_001182224.1.

    Genome annotation databases

    EnsemblFungiiYLR335W; YLR335W; YLR335W.
    GeneIDi851048.
    KEGGisce:YLR335W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69964 Genomic DNA. Translation: CAA49587.1 .
    U19028 Genomic DNA. Translation: AAB67259.1 .
    BK006945 Genomic DNA. Translation: DAA09641.1 .
    PIRi S51340.
    RefSeqi NP_013439.1. NM_001182224.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UN0 X-ray 2.60 C/D 1-51 [» ]
    2C1T X-ray 2.60 C/D 1-51 [» ]
    DisProti DP00222.
    ProteinModelPortali P32499.
    SMRi P32499. Positions 2-46, 606-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31599. 89 interactions.
    DIPi DIP-859N.
    IntActi P32499. 30 interactions.
    MINTi MINT-395606.
    STRINGi 4932.YLR335W.

    Protein family/group databases

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

    Proteomic databases

    MaxQBi P32499.
    PaxDbi P32499.
    PeptideAtlasi P32499.

    Protocols and materials databases

    DNASUi 851048.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR335W ; YLR335W ; YLR335W .
    GeneIDi 851048.
    KEGGi sce:YLR335W.

    Organism-specific databases

    CYGDi YLR335w.
    SGDi S000004327. NUP2.

    Phylogenomic databases

    eggNOGi COG5171.
    GeneTreei ENSGT00730000113442.
    HOGENOMi HOG000248337.
    OMAi ENEDTVI.
    OrthoDBi EOG7TF7N6.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32414-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32499.
    NextBioi 967658.

    Gene expression databases

    Genevestigatori P32499.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR015007. NUP2/50/61.
    IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    [Graphical view ]
    Pfami PF08911. NUP50. 1 hit.
    PF00638. Ran_BP1. 1 hit.
    [Graphical view ]
    SMARTi SM00160. RanBD. 1 hit.
    [Graphical view ]
    PROSITEi PS50196. RANBD1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex."
      Loeb J.D.J., Davis L.I., Fink G.R.
      Mol. Biol. Cell 4:209-222(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "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.
    5. "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.
    6. "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.
    7. "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.
    8. "Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex."
      Dilworth D.J., Suprapto A., Padovan J.C., Chait B.T., Wozniak R.W., Rout M.P., Aitchison J.D.
      J. Cell Biol. 153:1465-1478(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH NPC.
    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 THROUH FG REPEATS.
    12. "Chromatin boundaries in budding yeast: the nuclear pore connection."
      Ishii K., Arib G., Lin C., Van Houwe G., Laemmli U.K.
      Cell 109:551-562(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHROMATIN BOUNDARY ACTIVITY.
    13. "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, SRP1-KAP95 NUCLEAR IMPORT COMPLEX DISASSEMBLY.
    14. "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, FG REPEAT AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
    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. "Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm."
      Gilchrist D., Rexach M.
      J. Biol. Chem. 278:51937-51949(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRP1.
    18. "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.
    19. "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.
    20. "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-17; SER-20; SER-165; SER-203 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    21. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-137; SER-203; SER-205 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-17; SER-20; SER-203; SER-348; THR-361; SER-581 AND THR-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import."
      Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.
      EMBO J. 22:5358-5369(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 36-50 IN COMPLEX WITH SRP1.

    Entry informationi

    Entry nameiNUP2_YEAST
    AccessioniPrimary (citable) accession number: P32499
    Secondary accession number(s): D6VYX5, Q06130
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2960 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. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3