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Protein

Nucleoporin NUP82

Gene

NUP82

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. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.6 Publications

GO - Molecular functioni

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

GO - Biological processi

  • mRNA export from nucleus Source: SGD
  • protein export from nucleus Source: SGD
  • protein import into nucleus Source: SGD
  • ribosomal large subunit export from nucleus Source: SGD
  • ribosomal small subunit export from nucleus Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31523-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP82
Alternative name(s):
Nuclear pore protein NUP82
Gene namesi
Name:NUP82
Ordered Locus Names:YJL061W
ORF Names:HRB187, J1135
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL061W.
SGDiS000003597. NUP82.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore cytoplasmic filaments Source: SGD
  • nuclear pore linkers Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Nucleoporin NUP82PRO_0000204883Add
BLAST

Proteomic databases

MaxQBiP40368.

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. NUP82 is part of the NUP82 subcomplex (NUP82, NSP1, NUP159). This subcomplex is the base for interactions with NUP116 and GLE2 and with NUP42 and GLE1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NSP1P149078EBI-12331,EBI-12265
NUP116Q026304EBI-12331,EBI-11703
NUP159P404775EBI-12331,EBI-11747

Protein-protein interaction databases

BioGridi33693. 60 interactions.
DIPiDIP-913N.
IntActiP40368. 19 interactions.
MINTiMINT-498618.

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Turni11 – 133Combined sources
Beta strandi20 – 223Combined sources
Beta strandi24 – 296Combined sources
Turni30 – 334Combined sources
Beta strandi34 – 396Combined sources
Beta strandi42 – 476Combined sources
Turni48 – 503Combined sources
Beta strandi55 – 584Combined sources
Turni60 – 623Combined sources
Beta strandi70 – 734Combined sources
Beta strandi77 – 837Combined sources
Beta strandi85 – 928Combined sources
Helixi103 – 1075Combined sources
Beta strandi110 – 1156Combined sources
Helixi116 – 1183Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi127 – 1326Combined sources
Helixi137 – 1393Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi194 – 1985Combined sources
Beta strandi204 – 2107Combined sources
Beta strandi214 – 2174Combined sources
Helixi220 – 23516Combined sources
Beta strandi239 – 2413Combined sources
Helixi243 – 26220Combined sources
Turni265 – 2684Combined sources
Beta strandi269 – 2713Combined sources
Helixi274 – 2774Combined sources
Beta strandi286 – 2883Combined sources
Helixi293 – 2964Combined sources
Beta strandi299 – 3068Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi313 – 3197Combined sources
Turni320 – 3223Combined sources
Beta strandi323 – 3297Combined sources
Beta strandi347 – 3559Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi372 – 3765Combined sources
Beta strandi378 – 3858Combined sources
Helixi387 – 39913Combined sources
Helixi403 – 4053Combined sources
Beta strandi413 – 4197Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi434 – 4407Combined sources
Beta strandi445 – 4495Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PBPX-ray2.60A/D/G/J1-452[»]
3TKNX-ray3.40A/D/G1-452[»]
ProteinModelPortaliP40368.
SMRiP40368. Positions 2-452.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40368.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 409409Interaction with NUP116Add
BLAST
Regioni463 – 713251Interaction with NSP1 and NUP159Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili582 – 713132Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi607 – 62317Bipartite nuclear localization signalAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000113891.
InParanoidiP40368.
KOiK18719.
OMAiVLFHPKS.
OrthoDBiEOG7G7KXN.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSSRLSAL PIFQASLSAS QSPRYIFSSQ NGTRIVFIQD NIIRWYNVLT
60 70 80 90 100
DSLYHSLNFS RHLVLDDTFH VISSTSGDLL CLFNDNEIFV MEVPWGYSNV
110 120 130 140 150
EDVSIQDAFQ IFHYSIDEEE VGPKSSIKKV LFHPKSYRDS CIVVLKEDDT
160 170 180 190 200
ITMFDILNSQ EKPIVLNKPN NSFGLDARVN DITDLEFSKD GLTLYCLNTT
210 220 230 240 250
EGGDIFAFYP FLPSVLLLNE KDLNLILNKS LVMYESLDST TDVIVKRNVI
260 270 280 290 300
KQLQFVSKLH ENWNSRFGKV DIQKEYRLAK VQGPFTINPF PGELYDYTAT
310 320 330 340 350
NIATILIDNG QNEIVCVSFD DGSLILLFKD LEMSMSWDVD NYVYNNSLVL
360 370 380 390 400
IERVKLQREI KSLITLPEQL GKLYVISDNI IQQVNFMSWA STLSKCINES
410 420 430 440 450
DLNPLAGLKF ESKLEDIATI ERIPNLAYIN WNDQSNLALM SNKTLTFQNI
460 470 480 490 500
SSDMKPQSTA AETSISTEKS DTVGDGFKMS FTQPINEILI LNDNFQKACI
510 520 530 540 550
SPCERIIPSA DRQIPLKNEA SENQLEIFTD ISKEFLQRIV KAQTLGVSIH
560 570 580 590 600
NRIHEQQFEL TRQLQSTCKI ISKDDDLRRK FEAQNKKWDA QLSRQSELME
610 620 630 640 650
RFSKLSKKLS QIAESNKFKE KKISHGEMKW FKEIRNQILQ FNSFVHSQKS
660 670 680 690 700
LQQDLSYLKS ELTRIEAETI KVDKKSQNEW DELRKMLEID SKIIKECNEE
710
LLQVSQEFTT KTQ
Length:713
Mass (Da):82,085
Last modified:November 1, 1995 - v2
Checksum:iC379B5E111E26B50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31543 Genomic DNA. Translation: AAA85504.1.
X85970 Genomic DNA. Translation: CAA59957.1.
Z49336 Genomic DNA. Translation: CAA89352.1.
Z34288 Genomic DNA. Translation: CAA84062.1.
BK006943 Genomic DNA. Translation: DAA08737.1.
PIRiS56833.
RefSeqiNP_012474.1. NM_001181494.1.

Genome annotation databases

EnsemblFungiiYJL061W; YJL061W; YJL061W.
GeneIDi853385.
KEGGisce:YJL061W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31543 Genomic DNA. Translation: AAA85504.1.
X85970 Genomic DNA. Translation: CAA59957.1.
Z49336 Genomic DNA. Translation: CAA89352.1.
Z34288 Genomic DNA. Translation: CAA84062.1.
BK006943 Genomic DNA. Translation: DAA08737.1.
PIRiS56833.
RefSeqiNP_012474.1. NM_001181494.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PBPX-ray2.60A/D/G/J1-452[»]
3TKNX-ray3.40A/D/G1-452[»]
ProteinModelPortaliP40368.
SMRiP40368. Positions 2-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33693. 60 interactions.
DIPiDIP-913N.
IntActiP40368. 19 interactions.
MINTiMINT-498618.

Protein family/group databases

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

Proteomic databases

MaxQBiP40368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL061W; YJL061W; YJL061W.
GeneIDi853385.
KEGGisce:YJL061W.

Organism-specific databases

EuPathDBiFungiDB:YJL061W.
SGDiS000003597. NUP82.

Phylogenomic databases

HOGENOMiHOG000113891.
InParanoidiP40368.
KOiK18719.
OMAiVLFHPKS.
OrthoDBiEOG7G7KXN.

Enzyme and pathway databases

BioCyciYEAST:G3O-31523-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40368.
PROiP40368.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA export."
    Hurwitz M.E., Blobel G.
    J. Cell Biol. 130:1275-1281(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200912 / DF5.
  2. "A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p."
    Grandi P., Emig S., Weise C., Hucho F., Pohl T.M., Hurt E.C.
    J. Cell Biol. 130:1263-1273(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN MRNA EXPORT.
  3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces cerevisiae includes the mitochondrial ribosomal protein L8."
    Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.
    Yeast 11:57-60(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187.
    Strain: ATCC 204508 / S288c.
  6. "Functional characterization of a Nup159p-containing nuclear pore subcomplex."
    Belgareh N., Snay-Hodge C., Pasteau F., Dagher S., Cole C.N., Doye V.
    Mol. Biol. Cell 9:3475-3492(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP159 AND NSP1.
  7. Cited for: FUNCTION, NUP82 NPC SUBCOMPLEX.
  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. "Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p."
    Ho A.K., Shen T.X., Ryan K.J., Kiseleva E., Levy M.A., Allen T.D., Wente S.R.
    Mol. Cell. Biol. 20:5736-5748(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP116.
  10. "Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex."
    Gleizes P.-E., Noaillac-Depeyre J., Leger-Silvestre I., Teulieres F., Dauxois J.-Y., Pommet D., Azum-Gelade M.-C., Gas N.
    J. Cell Biol. 155:923-936(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
  11. "The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport."
    Bailer S.M., Balduf C., Hurt E.C.
    Mol. Cell. Biol. 21:7944-7955(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NPC ASSEMBLY.
  12. "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.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex."
    Yoshida K., Seo H.S., Debler E.W., Blobel G., Hoelz A.
    Proc. Natl. Acad. Sci. U.S.A. 108:16571-16576(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-452 IN COMPLEX WITH NUP116 AND NUP159, SUBUNIT.
  15. "Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex."
    Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.
    J. Mol. Biol. 419:330-346(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-452 IN COMPLEX WITH NUP159 AND THE MOUSE ORTHOLOG OF NUP145, SUBUNIT.

Entry informationi

Entry nameiNUP82_YEAST
AccessioniPrimary (citable) accession number: P40368
Secondary accession number(s): D6VWC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9470 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.