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P39705

- NUP60_YEAST

UniProt

P39705 - NUP60_YEAST

Protein

Nucleoporin NUP60

Gene

NUP60

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 122 (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).4 Publications

    GO - Molecular functioni

    1. nucleocytoplasmic transporter activity Source: SGD
    2. phospholipid binding Source: SGD
    3. protein binding Source: IntAct
    4. structural constituent of nuclear pore Source: SGD

    GO - Biological processi

    1. chromatin silencing at silent mating-type cassette Source: SGD
    2. chromosome organization Source: SGD
    3. double-strand break repair Source: SGD
    4. intracellular mRNA localization Source: SGD
    5. mRNA export from nucleus in response to heat stress Source: SGD
    6. NLS-bearing protein import into nucleus Source: SGD
    7. nucleocytoplasmic transport Source: SGD
    8. poly(A)+ mRNA export from nucleus Source: SGD
    9. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
    10. protein export from nucleus Source: SGD
    11. regulation of protein desumoylation Source: SGD
    12. telomere tethering at nuclear periphery Source: SGD
    13. 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-28867-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoporin NUP60
    Alternative name(s):
    Nuclear pore protein NUP60
    Gene namesi
    Name:NUP60
    Synonyms:FUN17
    Ordered Locus Names:YAR002W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome I

    Organism-specific databases

    CYGDiYAR002w.
    SGDiS000000063. NUP60.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. nuclear membrane Source: UniProtKB-SubCell
    3. nuclear pore Source: SGD
    4. nuclear pore central transport channel Source: SGD
    5. nuclear pore nuclear basket Source: SGD
    6. nucleus Source: SGD

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 539539Nucleoporin NUP60PRO_0000204879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine5 Publications
    Modified residuei49 – 491Phosphoserine2 Publications
    Modified residuei81 – 811Phosphoserine4 Publications
    Modified residuei89 – 891Phosphoserine2 Publications
    Modified residuei162 – 1621Phosphoserine2 Publications
    Modified residuei171 – 1711Phosphoserine2 Publications
    Modified residuei214 – 2141Phosphoserine2 Publications
    Modified residuei222 – 2221Phosphoserine2 Publications
    Modified residuei352 – 3521Phosphoserine3 Publications
    Modified residuei360 – 3601Phosphoserine2 Publications
    Modified residuei374 – 3741Phosphoserine2 Publications
    Modified residuei382 – 3821Phosphoserine2 Publications
    Modified residuei460 – 4601Phosphothreonine2 Publications
    Modified residuei480 – 4801Phosphoserine2 Publications
    Modified residuei483 – 4831Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by CDC28.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39705.
    PaxDbiP39705.
    PeptideAtlasiP39705.

    Expressioni

    Gene expression databases

    GenevestigatoriP39705.

    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 NUP1 and NUP2 forming the nuclear basket and the distal ring. The interaction with NUP2 is GSP1-GTP-dependent. Interacts through its FG repeats with karyopherins, such as KAP123 and KAP95-SRP1 (KAP60). Also interacts with GSP1-GTP and SRM1 (PRP20), where NUP60 reduces SRM1 activity, thus inhibiting GSP1 guanine nucleotide dissociation.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KAP95Q061424EBI-20731,EBI-9145
    NUP2P324992EBI-20731,EBI-12401

    Protein-protein interaction databases

    BioGridi31790. 206 interactions.
    DIPiDIP-5821N.
    IntActiP39705. 12 interactions.
    MINTiMINT-629603.
    STRINGi4932.YAR002W.

    Structurei

    3D structure databases

    ProteinModelPortaliP39705.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati399 – 4013FXF 1
    Repeati427 – 4293FXF 2
    Repeati469 – 4713FXF 3
    Repeati509 – 5113FXF 4

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili91 – 11828Sequence AnalysisAdd
    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.

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG79863.
    OMAiHISASID.
    OrthoDBiEOG76HQCM.

    Sequencei

    Sequence statusi: Complete.

    P39705-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHRKSLRRAS ATVPSAPYRK QIISNAHNKP SLFSKIKTFF TQKDSARVSP    50
    RNNVANKQPR NESFNRRISS MPGGYFHSEI SPDSTVNRSV VVSAVGEARN 100
    DIENKEEEYD ETHETNISNA KLANFFSKKG NEPLSEIEIE GVMSLLQKSS 150
    KSMITSEGEQ KSAEGNNIDQ SLILKESGST PISISNAPTF NPKYDTSNAS 200
    MNTTLGSIGS RKYSFNYSSL PSPYKTTVYR YSAAKKIPDT YTANTSAQSI 250
    ASAKSVRSGV SKSAPSKKIS NTAAALVSLL DENDSKKNNA ASELANPYSS 300
    YVSQIRKHKR VSPNAAPRQE ISEEETTVKP LFQNVPEQGE EPMKQLNATK 350
    ISPSAPSKDS FTKYKPARSS SLRSNVVVAE TSPEKKDGGD KPPSSAFNFS 400
    FNTSRNVEPT ENAYKSENAP SASSKEFNFT NLQAKPLVGK PKTELTKGDS 450
    TPVQPDLSVT PQKSSSKGFV FNSVQKKSRS NLSQENDNEG KHISASIDND 500
    FSEEKAEEFD FNVPVVSKQL GNGLVDENKV EAFKSLYTF 539
    Length:539
    Mass (Da):59,039
    Last modified:February 1, 1995 - v1
    Checksum:iB9A28494A358A3E3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22015 Genomic DNA. Translation: AAC04957.1.
    AY692943 Genomic DNA. Translation: AAT92962.1.
    BK006935 Genomic DNA. Translation: DAA06986.1.
    PIRiS40900.
    RefSeqiNP_009401.1. NM_001178209.1.

    Genome annotation databases

    EnsemblFungiiYAR002W; YAR002W; YAR002W.
    GeneIDi851263.
    KEGGisce:YAR002W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22015 Genomic DNA. Translation: AAC04957.1 .
    AY692943 Genomic DNA. Translation: AAT92962.1 .
    BK006935 Genomic DNA. Translation: DAA06986.1 .
    PIRi S40900.
    RefSeqi NP_009401.1. NM_001178209.1.

    3D structure databases

    ProteinModelPortali P39705.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31790. 206 interactions.
    DIPi DIP-5821N.
    IntActi P39705. 12 interactions.
    MINTi MINT-629603.
    STRINGi 4932.YAR002W.

    Protein family/group databases

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

    Proteomic databases

    MaxQBi P39705.
    PaxDbi P39705.
    PeptideAtlasi P39705.

    Protocols and materials databases

    DNASUi 851263.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YAR002W ; YAR002W ; YAR002W .
    GeneIDi 851263.
    KEGGi sce:YAR002W.

    Organism-specific databases

    CYGDi YAR002w.
    SGDi S000000063. NUP60.

    Phylogenomic databases

    eggNOGi NOG79863.
    OMAi HISASID.
    OrthoDBi EOG76HQCM.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28867-MONOMER.

    Miscellaneous databases

    NextBioi 968225.

    Gene expression databases

    Genevestigatori P39705.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
      Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
      Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    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. "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, NUCLEOPORIN INTERACTING PROTEINS.
    7. "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 GSP1-GTP; NUP2; SRM1; KAP123 AND KAP95-SRP1.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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.
    10. "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.
    11. "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.
    12. Cited for: PHOSPHORYLATION BY CDC28.
    13. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    14. "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-10 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "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-10; SER-49; SER-360; SER-374; SER-480 AND SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-10; SER-81; SER-352 AND THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-10; SER-81; SER-89; SER-162; SER-171; SER-214; SER-222; SER-352 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNUP60_YEAST
    AccessioniPrimary (citable) accession number: P39705
    Secondary accession number(s): D6VPL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 122 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 4590 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome I
      Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

    External Data

    Dasty 3