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 NUP116/NSP116

Gene

NUP116

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. 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.14 Publications

GO - Molecular functioni

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

GO - Biological processi

  • mRNA export from nucleus Source: SGD
  • nuclear pore organization Source: SGD
  • 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
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32752-MONOMER.

Protein family/group databases

MEROPSiS59.951.
TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP116/NSP116
Alternative name(s):
Nuclear pore protein NUP116/NSP116
Gene namesi
Name:NUP116
Synonyms:NSP116
Ordered Locus Names:YMR047C
ORF Names:YM9532.12C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR047C.
SGDiS000004650. NUP116.

Subcellular locationi

GO - Cellular componenti

  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore central transport channel Source: SGD
  • nuclear pore cytoplasmic filaments Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11131113Nucleoporin NUP116/NSP116PRO_0000204835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei886 – 8861PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02630.
PeptideAtlasiQ02630.

PTM databases

iPTMnetiQ02630.

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. 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. Interacts with CEX1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-11703,EBI-11703
CEX1Q124535EBI-11703,EBI-31271
GLE2P400666EBI-11703,EBI-22648
KAP95Q061424EBI-11703,EBI-9145
MEX67Q992575EBI-11703,EBI-11642
NUP100Q026295EBI-11703,EBI-11698
NUP42P496862EBI-11703,EBI-12310
NUP57P488374EBI-11703,EBI-12324
NUP82P403684EBI-11703,EBI-12331

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi35221. 145 interactions.
DIPiDIP-2389N.
IntActiQ02630. 46 interactions.
MINTiMINT-441530.

Structurei

Secondary structure

1
1113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi970 – 9745Combined sources
Helixi976 – 9816Combined sources
Beta strandi988 – 9903Combined sources
Beta strandi994 – 9974Combined sources
Turni998 – 10003Combined sources
Beta strandi1001 – 10077Combined sources
Turni1019 – 10224Combined sources
Beta strandi1023 – 10275Combined sources
Beta strandi1030 – 10345Combined sources
Beta strandi1042 – 10443Combined sources
Beta strandi1051 – 10566Combined sources
Turni1063 – 10653Combined sources
Helixi1075 – 108410Combined sources
Beta strandi1088 – 10958Combined sources
Turni1097 – 10993Combined sources
Beta strandi1102 – 11076Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AIVNMR-A967-1113[»]
3PBPX-ray2.60B/E/H/K967-1113[»]
ProteinModelPortaliQ02630.
SMRiQ02630. Positions 967-1113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02630.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 32FG 1
Repeati17 – 182FG 2
Repeati24 – 252FG 3
Repeati40 – 412FG 4
Repeati55 – 584GLFG 1; approximate
Repeati66 – 672FG 5
Repeati79 – 802FG 6
Repeati94 – 952FG 7
Repeati167 – 1682FG 8
Repeati189 – 1902FG 9
Repeati205 – 2084GLFG 2
Repeati214 – 2174GLFG 3; approximate
Repeati224 – 2274GLFG 4; approximate
Repeati235 – 2384GLFG 5
Repeati249 – 2502FG 10
Repeati259 – 2624GLFG 6
Repeati276 – 2794GLFG 7
Repeati288 – 2914GLFG 8
Repeati297 – 2982FG 11
Repeati306 – 3094GLFG 9; approximate
Repeati327 – 3304GLFG 10; approximate
Repeati339 – 3424GLFG 11; approximate
Repeati351 – 3522FG 12
Repeati359 – 3624GLFG 12
Repeati370 – 3712FG 13
Repeati382 – 3854GLFG 13
Repeati395 – 3984GLFG 14
Repeati407 – 4104GLFG 15
Repeati420 – 4234GLFG 16
Repeati431 – 4322FG 14
Repeati439 – 4424GLFG 17
Repeati448 – 4514GLFG 18
Repeati470 – 4712FG 15
Repeati482 – 4854GLFG 19
Repeati497 – 5004GLFG 20
Repeati510 – 5112FG 16
Repeati525 – 5262FG 17
Repeati532 – 5332FG 18
Repeati572 – 5754GLFG 21
Repeati585 – 5884GLFG 22
Repeati604 – 6074GLFG 23
Repeati616 – 6172FG 19
Repeati630 – 6334GLFG 24; approximate
Repeati648 – 6514GLFG 25
Repeati665 – 6684GLFG 26
Repeati683 – 6864GLFG 27
Domaini967 – 1109143Peptidase S59PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 16657GLE2 binding sequence (GLEBS)Add
BLAST
Regioni160 – 362203Interaction with MEX67, not KAP95Add
BLAST
Regioni362 – 535174Sufficient for interaction with MEX67 and KAP95Add
BLAST
Regioni536 – 732197Interaction with KAP95, not MEX67Add
BLAST
Regioni967 – 1113147Interaction with NUP82 NPC subcomplexAdd
BLAST
Regioni969 – 1108140Nucleoporin RNA-binding motif (NRM)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 5024Gln-richAdd
BLAST
Compositional biasi27 – 326Poly-Gln
Compositional biasi164 – 712549Gly-richAdd
BLAST
Compositional biasi263 – 30442Asn-richAdd
BLAST
Compositional biasi280 – 567288Gln-richAdd
BLAST
Compositional biasi475 – 4784Poly-Gln
Compositional biasi669 – 70739Asn-richAdd
BLAST
Compositional biasi669 – 6724Poly-Asn
Compositional biasi716 – 74025Gln-richAdd
BLAST
Compositional biasi729 – 7357Poly-Gln

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
Contains 1 peptidase S59 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074799.
HOGENOMiHOG000093958.
InParanoidiQ02630.
KOiK14297.
OMAiFEPKTCI.
OrthoDBiEOG7CCC0W.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR025574. Nucleoporin_FG_rpt.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF13634. Nucleoporin_FG. 8 hits.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGVSRGAFP SATTQPFGST GSTFGGQQQQ QQPVANTSAF GLSQQTNTTQ
60 70 80 90 100
APAFGNFGNQ TSNSPFGMSG STTANGTPFG QSQLTNNNAS GSIFGGMGNN
110 120 130 140 150
TALSAGSASV VPNSTAGTSI KPFTTFEEKD PTTGVINVFQ SITCMPEYRN
160 170 180 190 200
FSFEELRFQD YQAGRKFGTS QNGTGTTFNN PQGTTNTGFG IMGNNNSTTS
210 220 230 240 250
ATTGGLFGQK PATGMFGTGT GSGGGFGSGA TNSTGLFGSS TNLSGNSAFG
260 270 280 290 300
ANKPATSGGL FGNTTNNPTN GTNNTGLFGQ QNSNTNGGLF GQQQNSFGAN
310 320 330 340 350
NVSNGGAFGQ VNRGAFPQQQ TQQGSGGIFG QSNANANGGA FGQQQGTGAL
360 370 380 390 400
FGAKPASGGL FGQSAGSKAF GMNTNPTGTT GGLFGQTNQQ QSGGGLFGQQ
410 420 430 440 450
QNSNAGGLFG QNNQSQNQSG LFGQQNSSNA FGQPQQQGGL FGSKPAGGLF
460 470 480 490 500
GQQQGASTFA SGNAQNNSIF GQNNQQQQST GGLFGQQNNQ SQSQPGGLFG
510 520 530 540 550
QTNQNNNQPF GQNGLQQPQQ NNSLFGAKPT GFGNTSLFSN STTNQSNGIS
560 570 580 590 600
GNNLQQQSGG LFQNKQQPAS GGLFGSKPSN TVGGGLFGNN QVANQNNPAS
610 620 630 640 650
TSGGLFGSKP ATGSLFGGTN STAPNASSGG IFGSNNASNT AATTNSTGLF
660 670 680 690 700
GNKPVGAGAS TSAGGLFGNN NNSSLNNSNG STGLFGSNNT SQSTNAGGLF
710 720 730 740 750
QNNTSTNTSG GGLFSQPSQS MAQSQNALQQ QQQQQRLQIQ NNNPYGTNEL
760 770 780 790 800
FSKATVTNTV SYPIQPSATK IKADERKKAS LTNAYKMIPK TLFTAKLKTN
810 820 830 840 850
NSVMDKAQIK VDPKLSISID KKNNQIAISN QQEENLDESI LKASELLFNP
860 870 880 890 900
DKRSFKNLIN NRKMLIASEE KNNGSQNNDM NFKSKSEEQE TILGKPKMDE
910 920 930 940 950
KETANGGERM VLSSKNDGED SATKHHSRNM DEENKENVAD LQKQEYSEDD
960 970 980 990 1000
KKAVFADVAE KDASFINENY YISPSLDTLS SYSLLQLRKV PHLVVGHKSY
1010 1020 1030 1040 1050
GKIEFLEPVD LAGIPLTSLG GVIITFEPKT CIIYANLPNR PKRGEGINVR
1060 1070 1080 1090 1100
ARITCFNCYP VDKSTRKPIK DPNHQLVKRH IERLKKNPNS KFESYDADSG
1110
TYVFIVNHAA EQT
Length:1,113
Mass (Da):116,234
Last modified:February 1, 1996 - v2
Checksum:iFBAB0B9AEA958213
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261G → A in CAA78754 (PubMed:1385442).Curated
Sequence conflicti536 – 5361S → G in CAA78754 (PubMed:1385442).Curated
Sequence conflicti720 – 7201S → P in CAA78754 (PubMed:1385442).Curated
Sequence conflicti1018 – 10181S → Y in CAA78754 (PubMed:1385442).Curated
Sequence conflicti1023 – 10231I → Y in CAA78754 (PubMed:1385442).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15036 Genomic DNA. Translation: CAA78754.1.
X68108 Genomic DNA. Translation: CAA48228.1.
Z48502 Genomic DNA. Translation: CAA88413.1.
BK006946 Genomic DNA. Translation: DAA09946.1.
PIRiS28925.
RefSeqiNP_013762.1. NM_001182544.1.

Genome annotation databases

EnsemblFungiiYMR047C; YMR047C; YMR047C.
GeneIDi855066.
KEGGisce:YMR047C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15036 Genomic DNA. Translation: CAA78754.1.
X68108 Genomic DNA. Translation: CAA48228.1.
Z48502 Genomic DNA. Translation: CAA88413.1.
BK006946 Genomic DNA. Translation: DAA09946.1.
PIRiS28925.
RefSeqiNP_013762.1. NM_001182544.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AIVNMR-A967-1113[»]
3PBPX-ray2.60B/E/H/K967-1113[»]
ProteinModelPortaliQ02630.
SMRiQ02630. Positions 967-1113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35221. 145 interactions.
DIPiDIP-2389N.
IntActiQ02630. 46 interactions.
MINTiMINT-441530.

Protein family/group databases

MEROPSiS59.951.
TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiQ02630.

Proteomic databases

MaxQBiQ02630.
PeptideAtlasiQ02630.

Protocols and materials databases

DNASUi855066.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR047C; YMR047C; YMR047C.
GeneIDi855066.
KEGGisce:YMR047C.

Organism-specific databases

EuPathDBiFungiDB:YMR047C.
SGDiS000004650. NUP116.

Phylogenomic databases

GeneTreeiENSGT00550000074799.
HOGENOMiHOG000093958.
InParanoidiQ02630.
KOiK14297.
OMAiFEPKTCI.
OrthoDBiEOG7CCC0W.

Enzyme and pathway databases

BioCyciYEAST:G3O-32752-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02630.
PROiQ02630.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR025574. Nucleoporin_FG_rpt.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF13634. Nucleoporin_FG. 8 hits.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMOPOLYMERIC RNA-BINDING.
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRNA EXPORT.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GLE2.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSE1.
  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 NUP82.
  10. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MEX67/MTR2 HETERODIMER.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
  12. Cited for: FUNCTION, INTERACTION WITH NUP82 NPC SUBCOMPLEX.
  13. "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.
  14. "Proteomic analysis of nucleoporin interacting proteins."
    Allen N.P., Huang L., Burlingame A., Rexach M.
    J. Biol. Chem. 276:29268-29274(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEOPORIN INTERACTING PROTEINS.
  15. "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.
  16. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MEX67 AND KAP95.
  17. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION, INTERACTION WITH KAP95.
  18. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEAT STRUCTURE.
  19. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
  20. "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.
  21. "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery."
    McGuire A.T., Mangroo D.
    EMBO J. 26:288-300(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEX1.
  22. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNU116_YEAST
AccessioniPrimary (citable) accession number: Q02630
Secondary accession number(s): D6VZM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.