Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleoporin NUP84

Gene

NUP84

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization.2 Publications

GO - Molecular functioni

  • nucleocytoplasmic transporter activity Source: GO_Central
  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • double-strand break repair Source: SGD
  • maintenance of chromatin silencing at telomere Source: SGD
  • mRNA export from nucleus Source: SGD
  • mRNA export from nucleus in response to heat stress Source: SGD
  • nuclear pore distribution Source: SGD
  • positive regulation of transcription, DNA-templated Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  • protein import into nucleus Source: SGD
  • telomere tethering at nuclear periphery Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29516-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP84
Alternative name(s):
Nuclear pore protein NUP84
Gene namesi
Name:NUP84
Ordered Locus Names:YDL116W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL116W.
SGDiS000002274. NUP84.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore outer 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 – 726726Nucleoporin NUP84PRO_0000204884Add
BLAST

Proteomic databases

MaxQBiP52891.

PTM databases

iPTMnetiP52891.

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. NUP84 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
NUP133P361613EBI-12337,EBI-11722
NUP145P496875EBI-12337,EBI-11730

Protein-protein interaction databases

BioGridi31946. 246 interactions.
DIPiDIP-2430N.
IntActiP52891. 21 interactions.
MINTiMINT-426746.

Structurei

Secondary structure

1
726
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Helixi12 – 2312Combined sources
Helixi36 – 5520Combined sources
Helixi61 – 8727Combined sources
Helixi102 – 11211Combined sources
Helixi114 – 12815Combined sources
Helixi145 – 1495Combined sources
Helixi160 – 1634Combined sources
Helixi166 – 1683Combined sources
Helixi171 – 18919Combined sources
Helixi193 – 20210Combined sources
Helixi206 – 2138Combined sources
Turni221 – 2233Combined sources
Helixi225 – 2273Combined sources
Turni228 – 2303Combined sources
Beta strandi235 – 2373Combined sources
Helixi240 – 25213Combined sources
Beta strandi254 – 2563Combined sources
Helixi258 – 26811Combined sources
Helixi274 – 2774Combined sources
Helixi282 – 30423Combined sources
Helixi310 – 3123Combined sources
Helixi324 – 33411Combined sources
Helixi336 – 3405Combined sources
Helixi344 – 3518Combined sources
Helixi356 – 3649Combined sources
Helixi383 – 39917Combined sources
Helixi406 – 42217Combined sources
Helixi426 – 4283Combined sources
Helixi429 – 4335Combined sources
Helixi437 – 4415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IKOX-ray3.20C/F/I1-460[»]
3JROX-ray4.00C1-424[»]
4XMMX-ray7.38F1-451[»]
4XMNX-ray7.60F2-451[»]
ProteinModelPortaliP52891.
SMRiP52891. Positions 7-442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52891.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili563 – 58321Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the Nup84/Nup107 nucleoporin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000012080.
HOGENOMiHOG000113892.
InParanoidiP52891.
KOiK14301.
OMAiEENAYNE.
OrthoDBiEOG7KH9T3.

Family and domain databases

InterProiIPR007252. Nup84_Nup100.
[Graphical view]
PANTHERiPTHR13003. PTHR13003. 1 hit.
PfamiPF04121. Nup84_Nup100. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52891-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSPTYQTE RFTKFSDTLK EFKIEQNNEQ NPIDPFNIIR EFRSAAGQLA
60 70 80 90 100
LDLANSGDES NVISSKDWEL EARFWHLVEL LLVFRNADLD LDEMELHPYN
110 120 130 140 150
SRGLFEKKLM QDNKQLYQIW IVMVWLKENT YVMERPKNVP TSKWLNSITS
160 170 180 190 200
GGLKSCDLDF PLRENTNVLD VKDKEEDHIF FKYIYELILA GAIDEALEEA
210 220 230 240 250
KLSDNISICM ILCGIQEYLN PVIDTQIANE FNTQQGIKKH SLWRRTVYSL
260 270 280 290 300
SQQAGLDPYE RAIYSYLSGA IPNQEVLQYS DWESDLHIHL NQILQTEIEN
310 320 330 340 350
YLLENNQVGT DELILPLPSH ALTVQEVLNR VASRHPSESE HPIRVLMASV
360 370 380 390 400
ILDSLPSVIH SSVEMLLDVV KGTEASNDII DKPYLLRIVT HLAICLDIIN
410 420 430 440 450
PGSVEEVDKS KLITTYISLL KLQGLYENIP IYATFLNESD CLEACSFILS
460 470 480 490 500
SLEDPQVRKK QIETINFLRL PASNILRRTT QRVFDETEQE YSPSNEISIS
510 520 530 540 550
FDVNNIDMHL IYGVEWLIEG KLYVDAVHSI IALSRRFLLN GRVKALEQFM
560 570 580 590 600
ERNNIGEICK NYELEKIADN ISKDENEDQF LEEITQYEHL IKGIREYEEW
610 620 630 640 650
QKSVSLLSSE SNIPTLIEKL QGFSKDTFEL IKTFLVDLTS SNFADSADYE
660 670 680 690 700
ILYEIRALYT PFLLMELHKK LVEAAKLLKI PKFISEALAF TSLVANENDK
710 720
IYLLFQSSGK LKEYLDLVAR TATLSN
Length:726
Mass (Da):83,635
Last modified:October 1, 1996 - v1
Checksum:iF45BAAF9B976EEFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90993 Genomic DNA. Translation: CAA62479.1.
Z74164 Genomic DNA. Translation: CAA98684.1.
BK006938 Genomic DNA. Translation: DAA11744.1.
PIRiS62180.
RefSeqiNP_010167.1. NM_001180175.1.

Genome annotation databases

EnsemblFungiiYDL116W; YDL116W; YDL116W.
GeneIDi851441.
KEGGisce:YDL116W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90993 Genomic DNA. Translation: CAA62479.1.
Z74164 Genomic DNA. Translation: CAA98684.1.
BK006938 Genomic DNA. Translation: DAA11744.1.
PIRiS62180.
RefSeqiNP_010167.1. NM_001180175.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IKOX-ray3.20C/F/I1-460[»]
3JROX-ray4.00C1-424[»]
4XMMX-ray7.38F1-451[»]
4XMNX-ray7.60F2-451[»]
ProteinModelPortaliP52891.
SMRiP52891. Positions 7-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31946. 246 interactions.
DIPiDIP-2430N.
IntActiP52891. 21 interactions.
MINTiMINT-426746.

Protein family/group databases

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

PTM databases

iPTMnetiP52891.

Proteomic databases

MaxQBiP52891.

Protocols and materials databases

DNASUi851441.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL116W; YDL116W; YDL116W.
GeneIDi851441.
KEGGisce:YDL116W.

Organism-specific databases

EuPathDBiFungiDB:YDL116W.
SGDiS000002274. NUP84.

Phylogenomic databases

GeneTreeiENSGT00390000012080.
HOGENOMiHOG000113892.
InParanoidiP52891.
KOiK14301.
OMAiEENAYNE.
OrthoDBiEOG7KH9T3.

Enzyme and pathway databases

BioCyciYEAST:G3O-29516-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP52891.
PROiP52891.

Family and domain databases

InterProiIPR007252. Nup84_Nup100.
[Graphical view]
PANTHERiPTHR13003. PTHR13003. 1 hit.
PfamiPF04121. Nup84_Nup100. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN NUCLEAR MRNA EXPORT; NPC ASSEMBLY; NPC DISTRIBUTION AND NUCLEAR ENVELOPE ORGANIZATION.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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 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. "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.
  6. "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.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUP84_YEAST
AccessioniPrimary (citable) accession number: P52891
Secondary accession number(s): D6VRN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 139 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 8580 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.