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 NUP49/NSP49

Gene

NUP49

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport.8 Publications

Miscellaneous

Present with 4760 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • poly(A)+ mRNA export from nucleus Source: SGD
  • protein import into nucleus Source: SGD
  • ribosomal large subunit export from nucleus Source: SGD
  • tRNA export from nucleus Source: SGD

Keywordsi

Biological processmRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30660-MONOMER

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP49/NSP49
Alternative name(s):
Nuclear pore protein NUP49/NSP49
Gene namesi
Name:NUP49
Synonyms:NSP49
Ordered Locus Names:YGL172W
ORF Names:G1648
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL172W
SGDiS000003140 NUP49

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002048671 – 472Nucleoporin NUP49/NSP49Add BLAST472

Proteomic databases

MaxQBiQ02199
PaxDbiQ02199
PRIDEiQ02199

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, SEC13 and SEH1. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP49 is part of the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57) interacting with NUP57. Interacts through its FG repeats with karyopherins.

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi33081, 60 interactors
ComplexPortaliCPX-824 Nuclear pore complex
DIPiDIP-709N
IntActiQ02199, 25 interactors
MINTiQ02199
STRINGi4932.YGL172W

Structurei

3D structure databases

ProteinModelPortaliQ02199
SMRiQ02199
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati2 – 3FG 12
Repeati14 – 17GLFG 14
Repeati33 – 34FG 22
Repeati48 – 51GLFG 24
Repeati65 – 66FG 32
Repeati77 – 78FG 42
Repeati86 – 89GLFG 34
Repeati101 – 104GLFG 44
Repeati113 – 116SLFG 14
Repeati125 – 128GLFG 54
Repeati148 – 151GLFG 64
Repeati159 – 162SLFG 24
Repeati175 – 178GLFG 7; approximate4
Repeati185 – 188SLFG 34
Repeati199 – 202GLFG 84
Repeati210 – 213SLFG 44
Repeati233 – 236GLFG 94

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi13 – 207Gly-richAdd BLAST195
Compositional biasi67 – 73Poly-Gln7
Compositional biasi90 – 226Asn-richAdd BLAST137
Compositional biasi216 – 226Poly-AsnAdd BLAST11
Compositional biasi238 – 289Gln-richAdd BLAST52
Compositional biasi238 – 249Poly-GlnAdd BLAST12

Domaini

Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats are especially abundant in NUPs in the central region (lacking a charged environment but are enriched in Ser, Thr, Gln, and Asn).

Sequence similaritiesi

Belongs to the nucleoporin GLFG family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00730000113226
HOGENOMiHOG000246824
InParanoidiQ02199
KOiK14307
OMAiIPKDINY
OrthoDBiEOG092C3NRB

Family and domain databases

InterProiView protein in InterPro
IPR025574 Nucleoporin_FG_rpt
IPR037665 Nucleoporin_S59-like
PANTHERiPTHR23198 PTHR23198, 2 hits
PfamiView protein in Pfam
PF13634 Nucleoporin_FG, 1 hit

Sequencei

Sequence statusi: Complete.

Q02199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGLNKASST PAGGLFGQAS GASTGNANTG FSFGGTQTGQ NTGPSTGGLF
60 70 80 90 100
GAKPAGSTGG LGASFGQQQQ QSQTNAFGGS ATTGGGLFGN KPNNTANTGG
110 120 130 140 150
GLFGANSNSN SGSLFGSNNA QTSRGLFGNN NTNNINNSSS GMNNASAGLF
160 170 180 190 200
GSKPAGGTSL FGNTSTSSAP AQNQGMFGAK PAGTSLFGNN AGNTTTGGGL
210 220 230 240 250
FGSKPTGATS LFGSSNNNNN NNNSNNIMSA SGGLFGNQQQ QLQQQPQMQC
260 270 280 290 300
ALQNLSQLPI TPMTRISELP PQIRQEIEQL DQYIQKQVQI SHHLKADTID
310 320 330 340 350
HDELIDSIPR DVAYLLKSES ATSQYLKQDL KKISSFKSLI DEDLLDTQTF
360 370 380 390 400
SVLLQQLLTP GSKISSNDLD KFFQKKIHLY EKKLEDYCRI LSDIETAVNG
410 420 430 440 450
IDTDLFGAPN NPNSTAITAD LGSSEAENLL QLKTGLAAIV STVIEEFTLF
460 470
MDIAERIAVL HQKTKTLASL SI
Length:472
Mass (Da):49,142
Last modified:July 1, 1993 - v1
Checksum:i0CA7516FF5753CA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68109 Genomic DNA Translation: CAA48229.1
Z15040 Genomic DNA Translation: CAA78758.1
X84705 Genomic DNA Translation: CAA59181.1
Z72694 Genomic DNA Translation: CAA96884.1
BK006941 Genomic DNA Translation: DAA07941.1
PIRiS28026
RefSeqiNP_011343.1, NM_001181037.1

Genome annotation databases

EnsemblFungiiYGL172W; YGL172W; YGL172W
GeneIDi852703
KEGGisce:YGL172W

Similar proteinsi

Entry informationi

Entry nameiNUP49_YEAST
AccessioniPrimary (citable) accession number: Q02199
Secondary accession number(s): D6VTY0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 20, 2018
This is version 166 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health