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P35729

- NU120_YEAST

UniProt

P35729 - NU120_YEAST

Protein

Nucleoporin NUP120

Gene

NUP120

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 133 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural constituent of nuclear pore Source: SGD

    GO - Biological processi

    1. double-strand break repair Source: SGD
    2. maintenance of chromatin silencing at telomere Source: SGD
    3. mRNA export from nucleus Source: SGD
    4. mRNA export from nucleus in response to heat stress Source: SGD
    5. negative regulation of transcription from RNA polymerase II promoter Source: SGD
    6. nuclear pore distribution Source: SGD
    7. positive regulation of transcription, DNA-templated Source: SGD
    8. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    9. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
    10. protein export from nucleus Source: SGD
    11. protein import into nucleus Source: SGD
    12. ribosomal large subunit export from nucleus Source: SGD
    13. telomere tethering at nuclear periphery Source: SGD

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31856-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoporin NUP120
    Alternative name(s):
    Nuclear pore protein NUP120
    Gene namesi
    Name:NUP120
    Synonyms:RAT2
    Ordered Locus Names:YKL057C
    ORF Names:YKL313, YKL314
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL057c.
    SGDiS000001540. NUP120.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear membrane Source: UniProtKB-SubCell
    2. nuclear pore Source: SGD
    3. nuclear pore outer ring Source: SGD

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10371037Nucleoporin NUP120PRO_0000204836Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei417 – 4171Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP35729.
    PaxDbiP35729.
    PeptideAtlasiP35729.

    Expressioni

    Gene expression databases

    GenevestigatoriP35729.

    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. NUP120 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NUP145P496873EBI-11713,EBI-11730
    NUP85P466733EBI-11713,EBI-12345

    Protein-protein interaction databases

    BioGridi34076. 203 interactions.
    DIPiDIP-2721N.
    IntActiP35729. 17 interactions.
    MINTiMINT-491139.
    STRINGi4932.YKL057C.

    Structurei

    Secondary structure

    1
    1037
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 109
    Turni11 – 144
    Beta strandi16 – 194
    Beta strandi23 – 264
    Beta strandi55 – 617
    Beta strandi63 – 653
    Beta strandi67 – 726
    Beta strandi78 – 836
    Helixi84 – 863
    Turni87 – 893
    Beta strandi92 – 965
    Beta strandi101 – 1033
    Helixi104 – 1074
    Beta strandi108 – 1125
    Beta strandi114 – 12613
    Beta strandi128 – 1347
    Helixi135 – 1395
    Turni158 – 1603
    Beta strandi163 – 1686
    Beta strandi170 – 1789
    Beta strandi179 – 1813
    Beta strandi183 – 1864
    Beta strandi187 – 1926
    Helixi203 – 2086
    Beta strandi216 – 2194
    Beta strandi223 – 2297
    Turni230 – 2323
    Beta strandi233 – 2386
    Beta strandi242 – 2476
    Turni248 – 2514
    Beta strandi252 – 2587
    Turni259 – 2624
    Beta strandi280 – 29112
    Beta strandi293 – 2953
    Beta strandi297 – 3048
    Beta strandi307 – 3093
    Beta strandi312 – 3143
    Beta strandi318 – 3203
    Turni325 – 3273
    Beta strandi330 – 3389
    Beta strandi343 – 3453
    Beta strandi348 – 35710
    Beta strandi360 – 3689
    Beta strandi370 – 3723
    Beta strandi375 – 3817
    Beta strandi383 – 3853
    Helixi386 – 3927
    Helixi406 – 41510
    Helixi417 – 42812
    Turni429 – 4313
    Helixi440 – 45718
    Beta strandi460 – 4667
    Turni467 – 4693
    Beta strandi470 – 4778
    Beta strandi480 – 4867
    Helixi489 – 4946
    Turni495 – 4995
    Helixi505 – 51713
    Helixi522 – 53716
    Beta strandi538 – 5403
    Beta strandi542 – 5443
    Helixi546 – 55712
    Turni558 – 5603
    Helixi564 – 57411
    Helixi579 – 58810
    Turni589 – 5913
    Helixi609 – 63931
    Turni644 – 6474
    Helixi648 – 67023
    Helixi672 – 6809
    Beta strandi681 – 6844
    Beta strandi685 – 6884
    Helixi695 – 71117
    Helixi719 – 72810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F7FX-ray2.60A/B/C/D1-729[»]
    3H7NX-ray3.00A/B/C/D1-729[»]
    3HXRX-ray3.00A1-757[»]
    ProteinModelPortaliP35729.
    SMRiP35729. Positions 1-729.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35729.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni131 – 15222Leucine-zipper 1Sequence AnalysisAdd
    BLAST
    Regioni290 – 31122Leucine-zipper 2Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG19505.
    HOGENOMiHOG000113870.
    OMAiCHLKIWD.
    OrthoDBiEOG7MKWFP.

    Family and domain databases

    InterProiIPR021717. Nucleoporin_Nup160.
    [Graphical view]
    PfamiPF11715. Nup160. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35729-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACLSRIDAN LLQYYEKPEP NNTVDLYVSN NSNNNGLKEG DKSISTPVPQ     50
    PYGSEYSNCL LLSNSEYICY HFSSRSTLLT FYPLSDAYHG KTINIHLPNA 100
    SMNQRYTLTI QEVEQQLLVN VILKDGSFLT LQLPLSFLFS SANTLNGEWF 150
    HLQNPYDFTV RVPHFLFYVS PQFSVVFLED GGLLGLKKVD GVHYEPLLFN 200
    DNSYLKSLTR FFSRSSKSDY DSVISCKLFH ERYLIVLTQN CHLKIWDLTS 250
    FTLIQDYDMV SQSDSDPSHF RKVEAVGEYL SLYNNTLVTL LPLENGLFQM 300
    GTLLVDSSGI LTYTFQNNIP TNLSASAIWS IVDLVLTRPL ELNVEASYLN 350
    LIVLWKSGTA SKLQILNVND ESFKNYEWIE SVNKSLVDLQ SEHDLDIVTK 400
    TGDVERGFCN LKSRYGTQIF ERAQQILSEN KIIMAHNEDE EYLANLETIL 450
    RDVKTAFNEA SSITLYGDEI ILVNCFQPYN HSLYKLNTTV ENWFYNMHSE 500
    TDGSELFKYL RTLNGFASTL SNDVLRSISK KFLDIITGEL PDSMTTVEKF 550
    TDIFKNCLEN QFEITNLKIL FDELNSFDIP VVLNDLINNQ MKPGIFWKKD 600
    FISAIKFDGF TSIISLESLH QLLSIHYRIT LQVLLTFVLF DLDTEIFGQH 650
    ISTLLDLHYK QFLLLNLYRQ DKCLLAEVLL KDSSEFSFGV KFFNYGQLIA 700
    YIDSLNSNVY NASITENSFF MTFFRSYIIE NTSHKNIRFF LENVECPFYL 750
    RHNEVQEFMF AMTLFSCGNF DQSYEIFQLH DYPEAINDKL PTFLEDLKSE 800
    NYHGDSIWKD LLCTFTVPYR HSAFYYQLSL LFDRNNSQEF ALKCISKSAE 850
    YSLKEIQIEE LQDFKEKQHI HYLNLLIHFR MFEEVLDVLR LGHECLSDTV 900
    RTNFLQLLLQ EDIYSRDFFS TLLRLCNAHS DNGELYLRTV DIKIVDSILS 950
    QNLRSGDWEC FKKLYCFRML NKSERAAAEV LYQYILMQAD LDVIRKRKCY 1000
    LMVINVLSSF DSAYDQWILN GSKVVTLTDL RDELRGL 1037
    Length:1,037
    Mass (Da):120,448
    Last modified:June 1, 1994 - v1
    Checksum:iD4655E6116C54503
    GO

    Sequence cautioni

    The sequence CAA53415.1 differs from that shown. Reason: Frameshift at position 442.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75781 Genomic DNA. Translation: CAA53414.1. Frameshift.
    X75781 Genomic DNA. Translation: CAA53415.1. Frameshift.
    Z28057 Genomic DNA. Translation: CAA81894.1.
    BK006944 Genomic DNA. Translation: DAA09100.1.
    PIRiS37879.
    RefSeqiNP_012866.1. NM_001179623.1.

    Genome annotation databases

    EnsemblFungiiYKL057C; YKL057C; YKL057C.
    GeneIDi853808.
    KEGGisce:YKL057C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75781 Genomic DNA. Translation: CAA53414.1 . Frameshift.
    X75781 Genomic DNA. Translation: CAA53415.1 . Frameshift.
    Z28057 Genomic DNA. Translation: CAA81894.1 .
    BK006944 Genomic DNA. Translation: DAA09100.1 .
    PIRi S37879.
    RefSeqi NP_012866.1. NM_001179623.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3F7F X-ray 2.60 A/B/C/D 1-729 [» ]
    3H7N X-ray 3.00 A/B/C/D 1-729 [» ]
    3HXR X-ray 3.00 A 1-757 [» ]
    ProteinModelPortali P35729.
    SMRi P35729. Positions 1-729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34076. 203 interactions.
    DIPi DIP-2721N.
    IntActi P35729. 17 interactions.
    MINTi MINT-491139.
    STRINGi 4932.YKL057C.

    Protein family/group databases

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

    Proteomic databases

    MaxQBi P35729.
    PaxDbi P35729.
    PeptideAtlasi P35729.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL057C ; YKL057C ; YKL057C .
    GeneIDi 853808.
    KEGGi sce:YKL057C.

    Organism-specific databases

    CYGDi YKL057c.
    SGDi S000001540. NUP120.

    Phylogenomic databases

    eggNOGi NOG19505.
    HOGENOMi HOG000113870.
    OMAi CHLKIWD.
    OrthoDBi EOG7MKWFP.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31856-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P35729.
    NextBioi 974969.

    Gene expression databases

    Genevestigatori P35729.

    Family and domain databases

    InterProi IPR021717. Nucleoporin_Nup160.
    [Graphical view ]
    Pfami PF11715. Nup160. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins."
      Rasmussen S.W.
      Yeast 10:S63-S68(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [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. "Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transport."
      Aitchison J.D., Blobel G., Rout M.P.
      J. Cell Biol. 131:1659-1676(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 189-206 AND 800-807, CHARACTERIZATION, NUCLEAR MRNA EXPORT.
    5. "Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene."
      Heath C.V., Copeland C.S., Amberg D.C., Del Priore V., Snyder M., Cole C.N.
      J. Cell Biol. 131:1677-1697(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NPC ASSEMBLY AND DISTRIBUTION.
    6. "A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores."
      Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C., Emig S., Segref A., Hurt E.C.
      Cell 84:265-275(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR ENVELOPE ORGANIZATION.
    7. "Factors affecting nuclear export of the 60S ribosomal subunit in vivo."
      Stage-Zimmermann T., Schmidt U., Silver P.A.
      Mol. Biol. Cell 11:3777-3789(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
    8. "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.
    9. "Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins."
      Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.
      EMBO J. 21:387-397(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
    10. "Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p."
      Gao H., Sumanaweera N., Bailer S.M., Stochaj U.
      J. Biol. Chem. 278:25331-25340(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR GSP1 IMPORT.
    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. "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 THR-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNU120_YEAST
    AccessioniPrimary (citable) accession number: P35729
    Secondary accession number(s): D6VXN0, P35730
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3