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P40064

- NU157_YEAST

UniProt

P40064 - NU157_YEAST

Protein

Nucleoporin NUP157

Gene

NUP157

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 120 (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.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: SGD
    2. RNA binding Source: SGD
    3. structural constituent of nuclear pore Source: SGD

    GO - Biological processi

    1. mitotic spindle assembly checkpoint Source: SGD
    2. mRNA transport Source: UniProtKB-KW
    3. nuclear pore complex assembly Source: SGD
    4. nucleocytoplasmic transport Source: SGD
    5. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
    6. protein transport Source: UniProtKB-KW
    7. 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-30270-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoporin NUP157
    Alternative name(s):
    Nuclear pore protein NUP157
    Gene namesi
    Name:NUP157
    Ordered Locus Names:YER105C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER105c.
    SGDiS000000907. NUP157.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13911391Nucleoporin NUP157PRO_0000204848Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei1034 – 10341Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP40064.
    PaxDbiP40064.
    PeptideAtlasiP40064.

    Expressioni

    Gene expression databases

    GenevestigatoriP40064.

    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. NUP157 may be part of a NPC subcomplex containing NUP53, NUP170, and NUP59. In addition it may bind to MAD2.

    Protein-protein interaction databases

    BioGridi36851. 62 interactions.
    DIPiDIP-846N.
    IntActiP40064. 16 interactions.
    MINTiMINT-385200.
    STRINGi4932.YER105C.

    Structurei

    Secondary structure

    1
    1391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi90 – 10617
    Helixi114 – 1163
    Beta strandi122 – 1287
    Turni129 – 1324
    Helixi133 – 1353
    Beta strandi138 – 1458
    Helixi148 – 1514
    Turni152 – 1543
    Beta strandi161 – 1666
    Turni167 – 1704
    Beta strandi171 – 1766
    Beta strandi179 – 1846
    Turni185 – 1873
    Beta strandi191 – 1944
    Beta strandi201 – 2077
    Turni214 – 2174
    Beta strandi218 – 23720
    Beta strandi239 – 2413
    Beta strandi244 – 25411
    Turni256 – 2583
    Beta strandi260 – 2667
    Turni267 – 2704
    Beta strandi271 – 2766
    Beta strandi284 – 2863
    Beta strandi303 – 3075
    Beta strandi341 – 3488
    Turni349 – 3524
    Beta strandi353 – 3586
    Beta strandi363 – 3697
    Beta strandi372 – 3798
    Helixi381 – 39111
    Helixi397 – 3993
    Turni401 – 4033
    Beta strandi406 – 4116
    Turni414 – 4163
    Beta strandi418 – 4269
    Beta strandi431 – 4355
    Beta strandi447 – 4526
    Helixi483 – 4864
    Beta strandi500 – 5023
    Turni503 – 5053
    Beta strandi506 – 5127
    Beta strandi536 – 5438
    Helixi545 – 5517
    Beta strandi555 – 5606
    Beta strandi567 – 5748
    Beta strandi581 – 5833
    Turni584 – 5874
    Helixi589 – 5924
    Turni593 – 5953
    Beta strandi600 – 61415
    Helixi617 – 6237
    Turni624 – 6263
    Helixi629 – 6357
    Helixi637 – 64913
    Helixi655 – 66713
    Turni670 – 6723
    Helixi707 – 71913
    Turni720 – 7256
    Beta strandi726 – 7294
    Beta strandi745 – 7473
    Helixi749 – 76820
    Helixi770 – 7723
    Helixi787 – 81529
    Helixi816 – 8183
    Helixi819 – 82911
    Helixi838 – 8458
    Helixi849 – 8535
    Helixi857 – 87216
    Helixi879 – 89012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4MHCX-ray2.40A70-893[»]
    ProteinModelPortaliP40064.
    SMRiP40064. Positions 88-892.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5308.
    GeneTreeiENSGT00390000016532.
    HOGENOMiHOG000246581.
    OrthoDBiEOG7GXPKT.

    Family and domain databases

    InterProiIPR007187. Nucleoporin_Nup133/Nup155_C.
    IPR014908. Nucleoporin_Nup133/Nup155_N.
    IPR004870. Nucleoporin_Nup155.
    [Graphical view]
    PANTHERiPTHR10350. PTHR10350. 1 hit.
    PfamiPF03177. Nucleoporin_C. 1 hit.
    PF08801. Nucleoporin_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40064-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYSTPLKKRI DYDRETFTAS ASLGGNRLRN RPRDDQNNGK PNLSSRSFLS     50
    ERKTRKDVLN KYGEAGNTIE SELRDVTTHV KISGLTSSEP LQLASEFVQD 100
    LSFRDRNTPI LDNPDYYSKG LDYNFSDEVG GLGAFTPFQR QQVTNIPDEV 150
    LSQVSNTEIK SDMGIFLELN YCWITSDNKL ILWNINNSSE YHCIDEIEHT 200
    ILKVKLVKPS PNTFVSSVEN LLIVATLFDI YILTISFNDR THELNIFNTG 250
    LKVNVTGFNV SNIISYERTG QIFFTGATDG VNVWELQYNC SENLFNSKSN 300
    KICLTKSNLA NLLPTKLIPS IPGGKLIQKV LEGDAGTEEE TISQLEVDQS 350
    RGVLHTLSTK SIVRSYLITS NGLVGPVLID AAHIRRGMNA LGVKNSPLLS 400
    NRAFKIAKIV SISMCENNDL FLAVITTTGV RLYFKGSISR RSIGSLKLDS 450
    VKFPPTSISS SLEQNKSFII GHHPLNTHDT GPLSTQKASS TYINTTCAST 500
    IISPGIYFTC VRKRANSGEL SKGITNKALL ENKEEHKLYV SAPDYGILKN 550
    YGKYVENTAL LDTTDEIKEI VPLTRSFNYT STPQGYANVF ASQYSAEPLK 600
    VAVLTSNALE IYCYRTPDEV FESLIENPLP FIHSYGLSEA CSTALYLACK 650
    FNKSEHIKSS ALAFFSAGIP GVVEIKPKSS RESGSVPPIS QNLFDKSGEC 700
    DGIVLSPRFY GSALLITRLF SQIWEERVFV FKRASKTEKM DAFGISITRP 750
    QVEYYLSSIS VLADFFNIHR PSFVSFVPPK GSNAITASDA ESIAMNALIL 800
    LINSIKDALS LINVFYEDID AFKSLLNTLM GAGGVYDSKT REYFFDLKFH 850
    DLFTPNAKTK QLIKEILIEV VNANIASGTS ADYIVNVLKE RFGSFCHSAD 900
    ILCYRAGEHL EAAQKFEMID SKISRNHLDT AIDLYERCAE NIELCELRRV 950
    VDIMVKLNYQ PKTVGFLLRF ADKIDKGNQA QEYVSRGCNT ADPRKVFYDK 1000
    RINVYTLIFE IVKSVDDYTS IEQSPSIANI SIFSPASSLK KRVYSVIMNS 1050
    NNRFFHYCFY DWLVANKRQD YLLRLDSQFV LPYLKERAEK SLEISNLLWF 1100
    YLFKEEHFLE AADVLYALAS SDFDLKLSER IECLARANGL CDSSTSFDQK 1150
    PALVQLSENI HELFDIASIQ DDLLNLVRNE TRIDEDYRKQ LTLKLNGRVL 1200
    PLSDLFNDCA DPLDYYEIKL RIFKVSQFKD EKVIQGEWNR LLDSMKNAPS 1250
    PDVGSVGQES FLSSISNTLI RIGKTTRDTD VVFPVHFLMN KILESFIDKS 1300
    SAADGSVCSM FLLAGVSHLK LYYILSRIIE NSEGNVELAK KEMVWLIKDW 1350
    YQSDSDLRGS IAPEQIKKLE KYDPNTDPVQ DYVKDRHHGL K 1391
    Length:1,391
    Mass (Da):156,649
    Last modified:February 1, 1995 - v1
    Checksum:iCB47CEE27AB4FCE3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18839 Genomic DNA. Translation: AAB64660.1.
    BK006939 Genomic DNA. Translation: DAA07766.1.
    PIRiS50608.
    RefSeqiNP_011031.1. NM_001178996.1.

    Genome annotation databases

    EnsemblFungiiYER105C; YER105C; YER105C.
    GeneIDi856842.
    KEGGisce:YER105C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18839 Genomic DNA. Translation: AAB64660.1 .
    BK006939 Genomic DNA. Translation: DAA07766.1 .
    PIRi S50608.
    RefSeqi NP_011031.1. NM_001178996.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4MHC X-ray 2.40 A 70-893 [» ]
    ProteinModelPortali P40064.
    SMRi P40064. Positions 88-892.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36851. 62 interactions.
    DIPi DIP-846N.
    IntActi P40064. 16 interactions.
    MINTi MINT-385200.
    STRINGi 4932.YER105C.

    Protein family/group databases

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

    Proteomic databases

    MaxQBi P40064.
    PaxDbi P40064.
    PeptideAtlasi P40064.

    Protocols and materials databases

    DNASUi 856842.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER105C ; YER105C ; YER105C .
    GeneIDi 856842.
    KEGGi sce:YER105C.

    Organism-specific databases

    CYGDi YER105c.
    SGDi S000000907. NUP157.

    Phylogenomic databases

    eggNOGi COG5308.
    GeneTreei ENSGT00390000016532.
    HOGENOMi HOG000246581.
    OrthoDBi EOG7GXPKT.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30270-MONOMER.

    Miscellaneous databases

    NextBioi 983159.

    Gene expression databases

    Genevestigatori P40064.

    Family and domain databases

    InterProi IPR007187. Nucleoporin_Nup133/Nup155_C.
    IPR014908. Nucleoporin_Nup133/Nup155_N.
    IPR004870. Nucleoporin_Nup155.
    [Graphical view ]
    PANTHERi PTHR10350. PTHR10350. 1 hit.
    Pfami PF03177. Nucleoporin_C. 1 hit.
    PF08801. Nucleoporin_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p."
      Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W.
      J. Cell Biol. 131:1133-1148(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1016-1030 AND 1349-1367.
    4. "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.
    5. "The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint."
      Iouk T., Kerscher O., Scott R.J., Basrai M.A., Wozniak R.W.
      J. Cell Biol. 159:807-819(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NUP170 AND NUP53.
    6. Cited for: INTERACTION WITH MAD2 AND NUP53.
    7. "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.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNU157_YEAST
    AccessioniPrimary (citable) accession number: P40064
    Secondary accession number(s): D3DM12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 120 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 4420 molecules/cell in log phase SD medium.1 Publication

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

    External Data

    Dasty 3