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Reviewed, UniProtKB/Swiss-Prot Q02630 (NU116_YEAST)

Last modified November 24, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nucleoporin NUP116/NSP116
Alternative name(s):
    Nuclear pore protein NUP116/NSP116
Gene names
Name: NUP116
Synonyms: NSP116
Ordered Locus Names: YMR047C
ORF Names: YM9532.12C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1113 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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). NUP116 plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subunit structure

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. NUP116 interacts with the NUP82 subcomplex (NUP82, NSP1, NUP159) and GLE2. Through its FG repeats it interacts with numerous karyopherins including KAP95, PSE1 (GSP1-GDP dependent), MEX67, and to homopolymeric RNA. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.15 Ref.16 Ref.12

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Biased towards cytoplasmic side.

Domain

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 similarities

Belongs to the nucleoporin GLFG family.

Contains 1 peptidase S59 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11131113Nucleoporin NUP116/NSP116
PRO_0000204835

Regions

Repeat2 – 32FG 1
Repeat17 – 182FG 2
Repeat24 – 252FG 3
Repeat40 – 412FG 4
Repeat55 – 584GLFG 1; approximate
Repeat66 – 672FG 5
Repeat79 – 802FG 6
Repeat94 – 952FG 7
Repeat167 – 1682FG 8
Repeat189 – 1902FG 9
Repeat205 – 2084GLFG 2
Repeat214 – 2174GLFG 3; approximate
Repeat224 – 2274GLFG 4; approximate
Repeat235 – 2384GLFG 5
Repeat249 – 2502FG 10
Repeat259 – 2624GLFG 6
Repeat276 – 2794GLFG 7
Repeat288 – 2914GLFG 8
Repeat297 – 2982FG 11
Repeat306 – 3094GLFG 9; approximate
Repeat327 – 3304GLFG 10; approximate
Repeat339 – 3424GLFG 11; approximate
Repeat351 – 3522FG 12
Repeat359 – 3624GLFG 12
Repeat370 – 3712FG 13
Repeat382 – 3854GLFG 13
Repeat395 – 3984GLFG 14
Repeat407 – 4104GLFG 15
Repeat420 – 4234GLFG 16
Repeat431 – 4322FG 14
Repeat439 – 4424GLFG 17
Repeat448 – 4514GLFG 18
Repeat470 – 4712FG 15
Repeat482 – 4854GLFG 19
Repeat497 – 5004GLFG 20
Repeat510 – 5112FG 16
Repeat525 – 5262FG 17
Repeat532 – 5332FG 18
Repeat572 – 5754GLFG 21
Repeat585 – 5884GLFG 22
Repeat604 – 6074GLFG 23
Repeat616 – 6172FG 19
Repeat630 – 6334GLFG 24; approximate
Repeat648 – 6514GLFG 25
Repeat665 – 6684GLFG 26
Repeat683 – 6864GLFG 27
Domain967 – 1109143Peptidase S59
Region110 – 16657GLE2 binding sequence (GLEBS)
Region160 – 362203Interaction with MEX67, not KAP95
Region362 – 535174Sufficient for interaction with MEX67 and KAP95
Region536 – 732197Interaction with KAP95, not MEX67
Region967 – 1113147Interaction with NUP82 NPC subcomplex
Region969 – 1108140Nucleoporin RNA-binding motif (NRM)
Compositional bias27 – 5024Gln-rich
Compositional bias27 – 326Poly-Gln
Compositional bias164 – 712549Gly-rich
Compositional bias263 – 30442Asn-rich
Compositional bias280 – 567288Gln-rich
Compositional bias475 – 4784Poly-Gln
Compositional bias669 – 70739Asn-rich
Compositional bias669 – 6724Poly-Asn
Compositional bias716 – 74025Gln-rich
Compositional bias729 – 7357Poly-Gln

Experimental info

Sequence conflict261G → A in CAA78754. Ref.1
Sequence conflict5361S → G in CAA78754. Ref.1
Sequence conflict7201S → P in CAA78754. Ref.1
Sequence conflict10181S → Y in CAA78754. Ref.1
Sequence conflict10231I → Y in CAA78754. Ref.1

Secondary structure

............................... 1113
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02630-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: FBAB0B9AEA958213

FASTA1,113116,234
        10         20         30         40         50         60 
MFGVSRGAFP SATTQPFGST GSTFGGQQQQ QQPVANTSAF GLSQQTNTTQ APAFGNFGNQ 

        70         80         90        100        110        120 
TSNSPFGMSG STTANGTPFG QSQLTNNNAS GSIFGGMGNN TALSAGSASV VPNSTAGTSI 

       130        140        150        160        170        180 
KPFTTFEEKD PTTGVINVFQ SITCMPEYRN FSFEELRFQD YQAGRKFGTS QNGTGTTFNN 

       190        200        210        220        230        240 
PQGTTNTGFG IMGNNNSTTS ATTGGLFGQK PATGMFGTGT GSGGGFGSGA TNSTGLFGSS 

       250        260        270        280        290        300 
TNLSGNSAFG ANKPATSGGL FGNTTNNPTN GTNNTGLFGQ QNSNTNGGLF GQQQNSFGAN 

       310        320        330        340        350        360 
NVSNGGAFGQ VNRGAFPQQQ TQQGSGGIFG QSNANANGGA FGQQQGTGAL FGAKPASGGL 

       370        380        390        400        410        420 
FGQSAGSKAF GMNTNPTGTT GGLFGQTNQQ QSGGGLFGQQ QNSNAGGLFG QNNQSQNQSG 

       430        440        450        460        470        480 
LFGQQNSSNA FGQPQQQGGL FGSKPAGGLF GQQQGASTFA SGNAQNNSIF GQNNQQQQST 

       490        500        510        520        530        540 
GGLFGQQNNQ SQSQPGGLFG QTNQNNNQPF GQNGLQQPQQ NNSLFGAKPT GFGNTSLFSN 

       550        560        570        580        590        600 
STTNQSNGIS GNNLQQQSGG LFQNKQQPAS GGLFGSKPSN TVGGGLFGNN QVANQNNPAS 

       610        620        630        640        650        660 
TSGGLFGSKP ATGSLFGGTN STAPNASSGG IFGSNNASNT AATTNSTGLF GNKPVGAGAS 

       670        680        690        700        710        720 
TSAGGLFGNN NNSSLNNSNG STGLFGSNNT SQSTNAGGLF QNNTSTNTSG GGLFSQPSQS 

       730        740        750        760        770        780 
MAQSQNALQQ QQQQQRLQIQ NNNPYGTNEL FSKATVTNTV SYPIQPSATK IKADERKKAS 

       790        800        810        820        830        840 
LTNAYKMIPK TLFTAKLKTN NSVMDKAQIK VDPKLSISID KKNNQIAISN QQEENLDESI 

       850        860        870        880        890        900 
LKASELLFNP DKRSFKNLIN NRKMLIASEE KNNGSQNNDM NFKSKSEEQE TILGKPKMDE 

       910        920        930        940        950        960 
KETANGGERM VLSSKNDGED SATKHHSRNM DEENKENVAD LQKQEYSEDD KKAVFADVAE 

       970        980        990       1000       1010       1020 
KDASFINENY YISPSLDTLS SYSLLQLRKV PHLVVGHKSY GKIEFLEPVD LAGIPLTSLG 

      1030       1040       1050       1060       1070       1080 
GVIITFEPKT CIIYANLPNR PKRGEGINVR ARITCFNCYP VDKSTRKPIK DPNHQLVKRH 

      1090       1100       1110 
IERLKKNPNS KFESYDADSG TYVFIVNHAA EQT 

« Hide

References

« Hide 'large scale' references
[1]"A new family of yeast nuclear pore complex proteins."
Wente S.R., Rout M.P., Blobel G.
J. Cell Biol. 119:705-723(1992) [PubMed: 1385442] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1."
Wimmer C., Doye V., Grandi P., Nehrbass U., Hurt E.C.
EMBO J. 11:5051-5061(1992) [PubMed: 1464327] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed: 9169872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif."
Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C.
Cell 78:275-289(1994) [PubMed: 8044840] [Abstract]
Cited for: FUNCTION, HOMOPOLYMERIC RNA-BINDING.
[5]"Yeast nucleoporin mutants are defective in pre-tRNA splicing."
Sharma K., Fabre E., Tekotte H., Hurt E.C., Tollervey D.
Mol. Cell. Biol. 16:294-301(1996) [PubMed: 8524308] [Abstract]
Cited for: FUNCTION IN TRNA EXPORT.
[6]"Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p."
Bailer S.M., Siniossoglou S., Podtelejnikov A., Hellwig A., Mann M., Hurt E.C.
EMBO J. 17:1107-1119(1998) [PubMed: 9463388] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GLE2.
[7]"Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase."
Seedorf M., Damelin M., Kahana J., Taura T., Silver P.A.
Mol. Cell. Biol. 19:1547-1557(1999) [PubMed: 9891088] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PSE1.
[8]"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: 10891509] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NUP82.
[9]"Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export."
Straesser K., Bassler J., Hurt E.C.
J. Cell Biol. 150:695-706(2000) [PubMed: 10952996] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEX67/MTR2 HETERODIMER.
[10]"Factors affecting nuclear export of the 60S ribosomal subunit in vivo."
Stage-Zimmermann T., Schmidt U., Silver P.A.
Mol. Biol. Cell 11:3777-3789(2000) [PubMed: 11071906] [Abstract]
Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
[11]"Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex."
Bailer S.M., Balduf C., Katahira J., Podtelejnikov A., Rollenhagen C., Mann M., Pante N., Hurt E.C.
J. Biol. Chem. 275:23540-23548(2000) [PubMed: 10801828] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NUP82 NPC SUBCOMPLEX.
[12]"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: 10684247] [Abstract]
Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[13]"Proteomic analysis of nucleoporin interacting proteins."
Allen N.P., Huang L., Burlingame A., Rexach M.
J. Biol. Chem. 276:29268-29274(2001) [PubMed: 11387327] [Abstract]
Cited for: FUNCTION, NUCLEOPORIN INTERACTING PROTEINS.
[14]"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: 11689687] [Abstract]
Cited for: FUNCTION, NPC ASSEMBLY.
[15]"The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex."
Strawn L.A., Shen T.X., Wente S.R.
J. Biol. Chem. 276:6445-6452(2001) [PubMed: 11104765] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEX67 AND KAP95.
[16]"GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta."
Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.
J. Biol. Chem. 277:50597-50606(2002) [PubMed: 12372823] [Abstract]
Cited for: FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION, INTERACTION WITH KAP95.
[17]"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded."
Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.
Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003) [PubMed: 12604785] [Abstract]
Cited for: FUNCTION, FG REPEAT STRUCTURE.
[18]"Minimal nuclear pore complexes define FG repeat domains essential for transport."
Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.
Nat. Cell Biol. 6:197-206(2004) [PubMed: 15039779] [Abstract]
Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
[19]"Peering through the pore: nuclear pore complex structure, assembly, and function."
Suntharalingam M., Wente S.R.
Dev. Cell 4:775-789(2003) [PubMed: 12791264] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z15036 Genomic DNA. Translation: CAA78754.1.
X68108 Genomic DNA. Translation: CAA48228.1.
Z48502 Genomic DNA. Translation: CAA88413.1.
PIRS28925.
RefSeqNP_013762.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2AIVNMR-A967-1113[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2389N.
IntActQ02630. 151 interactions.
STRINGQ02630.

Protein family/group databases

TCDB9.A.14.1.1. nuclear pore complex (NPC) family.

Proteomic databases

PeptideAtlasQ02630.

Genome annotation databases

EnsemblYMR047C; YMR047C; YMR047C; Saccharomyces cerevisiae. [Genome view]
GeneID855066.
KEGGsce:YMR047C.
NMPDRfig|4932.3.peg.4809.

Organism-specific databases

CYGDYMR047c.
SGDS000004650. NUP116.

Phylogenomic databases

HOGENOMQ02630.
OMAHGGGSVF
OrthoDBEOG9PZKQ0

Gene expression databases

ArrayExpressQ02630.
GenevestigatorQ02630.
GermOnlineYMR047C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR007230. Peptidase_S59.
[Graphical view]
Gene3DG3DSA:3.30.1610.10. Peptidase_S59. 1 hit.
PfamPF04096. Nucleoporin2. 1 hit.
[Graphical view]
PROSITEPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio978329.

Entry information

Entry nameNU116_YEAST
AccessionPrimary (citable) accession number: Q02630
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: November 24, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents