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P40064

- NU157_YEAST

UniProt

P40064 - NU157_YEAST

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Protein
Nucleoporin NUP157
Gene
NUP157, YER105C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. mRNA transport Source: UniProtKB-KW
  2. mitotic spindle assembly checkpoint Source: SGD
  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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13911391Nucleoporin NUP157
PRO_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 MAD2.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 119 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.

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

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