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P40477

- NU159_YEAST

UniProt

P40477 - NU159_YEAST

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Protein

Nucleoporin NUP159

Gene

NUP159

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.13 Publications

GO - Molecular functioni

  1. adenyl-nucleotide exchange factor activity Source: SGD
  2. nucleocytoplasmic transporter activity Source: SGD

GO - Biological processi

  1. ncRNA export from nucleus Source: SGD
  2. NLS-bearing protein import into nucleus Source: SGD
  3. nuclear pore distribution Source: SGD
  4. poly(A)+ mRNA export from nucleus Source: SGD
  5. protein export from nucleus Source: SGD
  6. regulation of catalytic activity Source: GOC
  7. ribosomal large subunit export from nucleus Source: SGD
  8. 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-31369-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP159
Alternative name(s):
Nuclear pore protein NUP159
Gene namesi
Name:NUP159
Synonyms:NUP158, RAT7
Ordered Locus Names:YIL115C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL115c.
SGDiS000001377. NUP159.

Subcellular locationi

GO - Cellular componenti

  1. nuclear pore Source: SGD
  2. nuclear pore central transport channel Source: SGD
  3. 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 – 14601460Nucleoporin NUP159PRO_0000204849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei404 – 4041Phosphoserine2 Publications
Modified residuei657 – 6571Phosphoserine1 Publication
Modified residuei724 – 7241Phosphoserine1 Publication
Modified residuei735 – 7351Phosphoserine3 Publications
Modified residuei745 – 7451Phosphoserine1 Publication
Modified residuei803 – 8031Phosphothreonine2 Publications
Modified residuei805 – 8051Phosphoserine3 Publications
Modified residuei819 – 8191Phosphoserine3 Publications
Modified residuei889 – 8891Phosphoserine1 Publication
Modified residuei940 – 9401Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40477.
PaxDbiP40477.

Expressioni

Gene expression databases

GenevestigatoriP40477.

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. NUP159 is part of the NUP82 subcomplex (NUP82, NSP1, NUP159) interacting with NUP82 through its C-terminal coiled coil. This subcomplex is the base for interactions with NUP116 and GLE2 and with NUP42 and GLE1. Interacts through its FG repeats with karyopherins, such as heterodimeric mRNA transport factor MEX67/MTR2, CRM1 (XPO1), and PSE1 (GSP1-GDP dependent). Interaction with CRM1 (XPO1) is GSP1-GTP dependent and stimulated by RNA1. NUP159 also interacts with GLE1 and the ATP-dependent RNA helicase DBP5.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KAP95Q061423EBI-11747,EBI-9145
NUP82P403685EBI-11747,EBI-12331

Protein-protein interaction databases

BioGridi34876. 91 interactions.
DIPiDIP-2314N.
IntActiP40477. 17 interactions.
MINTiMINT-629459.
STRINGi4932.YIL115C.

Structurei

Secondary structure

1
1460
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156Combined sources
Beta strandi17 – 259Combined sources
Beta strandi42 – 454Combined sources
Turni46 – 494Combined sources
Beta strandi50 – 556Combined sources
Beta strandi58 – 636Combined sources
Helixi64 – 729Combined sources
Beta strandi73 – 753Combined sources
Beta strandi81 – 855Combined sources
Beta strandi89 – 957Combined sources
Beta strandi98 – 11417Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi145 – 1517Combined sources
Turni152 – 1543Combined sources
Beta strandi157 – 16913Combined sources
Beta strandi171 – 1788Combined sources
Beta strandi183 – 1897Combined sources
Beta strandi192 – 1998Combined sources
Helixi203 – 2064Combined sources
Turni210 – 2123Combined sources
Beta strandi213 – 23119Combined sources
Beta strandi245 – 2539Combined sources
Beta strandi256 – 26510Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi292 – 2987Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi309 – 3179Combined sources
Helixi318 – 3203Combined sources
Turni328 – 3303Combined sources
Beta strandi336 – 3427Combined sources
Beta strandi364 – 3696Combined sources
Beta strandi372 – 3809Combined sources
Beta strandi1118 – 11236Combined sources
Helixi1436 – 145419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XIPX-ray2.50A2-387[»]
3PBPX-ray2.60C/F/I/L1425-1460[»]
3RRMX-ray2.88C2-387[»]
3TKNX-ray3.40B/E/H1425-1460[»]
4DS1X-ray1.85B/D1116-1126[»]
ProteinModelPortaliP40477.
SMRiP40477. Positions 2-381, 1431-1458.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati228 – 2314FG 1
Repeati267 – 2704PXFG 1
Repeati462 – 4709SXFGXPXFG 1
Repeati503 – 5119SXFGXPXFG 2; approximate
Repeati522 – 5309SXFGXPXFG 3; approximate
Repeati532 – 5354PXFG 2
Repeati548 – 5569SXFGXPXFG 4
Repeati558 – 5614PXFG 3
Repeati574 – 5829SXFGXPXFG 5
Repeati584 – 5874PXFG 4
Repeati600 – 6089SXFGXPXFG 6
Repeati610 – 6134SXFG 1
Repeati624 – 6329SXFGXPXFG 7; approximate
Repeati642 – 6454FG 2
Repeati687 – 6904FG 3
Repeati704 – 7074FXFG 1
Repeati709 – 7124SXFG 2
Repeati728 – 7314FXFG 2
Repeati842 – 8454PXFG 5
Repeati873 – 8764FXFG 3

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 500500Interaction with DBP5Add
BLAST
Regioni497 – 701205Interactions with CRM1 and GLE1Add
BLAST
Regioni1223 – 1460238Interaction with NUP82Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1279 – 132042Add
BLAST
Coiled coili1383 – 141836Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi455 – 766312Ser-richAdd
BLAST

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: SXFG/PXFG repeats are especially abundant in NUPs on the cytoplasmic side.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5651.
GeneTreeiENSGT00730000113975.
HOGENOMiHOG000113875.
InParanoidiP40477.
OMAiFGESAFG.
OrthoDBiEOG754HXQ.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P40477-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSLKDEVPT ETSEDFGFKF LGQKQILPSF NEKLPFASLQ NLDISNSKSL
60 70 80 90 100
FVAASGSKAV VGELQLLRDH ITSDSTPLTF KWEKEIPDVI FVCFHGDQVL
110 120 130 140 150
VSTRNALYSL DLEELSEFRT VTSFEKPVFQ LKNVNNTLVI LNSVNDLSAL
160 170 180 190 200
DLRTKSTKQL AQNVTSFDVT NSQLAVLLKD RSFQSFAWRN GEMEKQFEFS
210 220 230 240 250
LPSELEELPV EEYSPLSVTI LSPQDFLAVF GNVISETDDE VSYDQKMYII
260 270 280 290 300
KHIDGSASFQ ETFDITPPFG QIVRFPYMYK VTLSGLIEPD ANVNVLASSC
310 320 330 340 350
SSEVSIWDSK QVIEPSQDSE RAVLPISEET DKDTNPIGVA VDVVTSGTIL
360 370 380 390 400
EPCSGVDTIE RLPLVYILNN EGSLQIVGLF HVAAIKSGHY SINLESLEHE
410 420 430 440 450
KSLSPTSEKI PIAGQEQEEK KKNNESSKAL SENPFTSANT SGFTFLKTQP
460 470 480 490 500
AAANSLQSQS SSTFGAPSFG SSAFKIDLPS VSSTSTGVAS SEQDATDPAS
510 520 530 540 550
AKPVFGKPAF GAIAKEPSTS EYAFGKPSFG APSFGSGKSS VESPASGSAF
560 570 580 590 600
GKPSFGTPSF GSGNSSVEPP ASGSAFGKPS FGTPSFGSGN SSAEPPASGS
610 620 630 640 650
AFGKPSFGTS AFGTASSNET NSGSIFGKAA FGSSSFAPAN NELFGSNFTI
660 670 680 690 700
SKPTVDSPKE VDSTSPFPSS GDQSEDESKS DVDSSSTPFG TKPNTSTKPK
710 720 730 740 750
TNAFDFGSSS FGSGFSKALE SVGSDTTFKF GTQASPFSSQ LGNKSPFSSF
760 770 780 790 800
TKDDTENGSL SKGSTSEIND DNEEHESNGP NVSGNDLTDS TVEQTSSTRL
810 820 830 840 850
PETPSDEDGE VVEEEAQKSP IGKLTETIKK SANIDMAGLK NPVFGNHVKA
860 870 880 890 900
KSESPFSAFA TNITKPSSTT PAFSFGNSTM NKSNTSTVSP MEEADTKETS
910 920 930 940 950
EKGPITLKSV ENPFLPAKEE RTGESSKKDH NDDPKDGYVS GSEISVRTSE
960 970 980 990 1000
SAFDTTANEE IPKSQDVNNH EKSETDPKYS QHAVVDHDNK SKEMNETSKN
1010 1020 1030 1040 1050
NERSGQPNHG VQGDGIALKK DNEKENFDSN MAIKQFEDHQ SSEEDASEKD
1060 1070 1080 1090 1100
SRQSSEVKES DDNMSLNSDR DESISESYDK LEDINTDELP HGGEAFKARE
1110 1120 1130 1140 1150
VSASADFDVQ TSLEDNYAES GIQTDLSESS KENEVQTDAI PVKHNSTQTV
1160 1170 1180 1190 1200
KKEAVDNGLQ TEPVETCNFS VQTFEGDENY LAEQCKPKQL KEYYTSAKVS
1210 1220 1230 1240 1250
NIPFVSQNST LRLIESTFQT VEAEFTVLME NIRNMDTFFT DQSSIPLVKR
1260 1270 1280 1290 1300
TVRSINNLYT WRIPEAEILL NIQNNIKCEQ MQITNANIQD LKEKVTDYVR
1310 1320 1330 1340 1350
KDIAQITEDV ANAKEEYLFL MHFDDASSGY VKDLSTHQFR MQKTLRQKLF
1360 1370 1380 1390 1400
DVSAKINHTE ELLNILKLFT VKNKRLDDNP LVAKLAKESL ARDGLLKEIK
1410 1420 1430 1440 1450
LLREQVSRLQ LEEKGKKASS FDASSSITKD MKGFKVVEVG LAMNTKKQIG
1460
DFFKNLNMAK
Length:1,460
Mass (Da):158,908
Last modified:February 1, 1995 - v1
Checksum:iA33FFA52378F8205
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40634 Genomic DNA. Translation: AAC41652.1.
Z38125 Genomic DNA. Translation: CAA86265.1.
BK006942 Genomic DNA. Translation: DAA08438.1.
PIRiS48457.
RefSeqiNP_012151.1. NM_001179463.1.

Genome annotation databases

EnsemblFungiiYIL115C; YIL115C; YIL115C.
GeneIDi854691.
KEGGisce:YIL115C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40634 Genomic DNA. Translation: AAC41652.1 .
Z38125 Genomic DNA. Translation: CAA86265.1 .
BK006942 Genomic DNA. Translation: DAA08438.1 .
PIRi S48457.
RefSeqi NP_012151.1. NM_001179463.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XIP X-ray 2.50 A 2-387 [» ]
3PBP X-ray 2.60 C/F/I/L 1425-1460 [» ]
3RRM X-ray 2.88 C 2-387 [» ]
3TKN X-ray 3.40 B/E/H 1425-1460 [» ]
4DS1 X-ray 1.85 B/D 1116-1126 [» ]
ProteinModelPortali P40477.
SMRi P40477. Positions 2-381, 1431-1458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34876. 91 interactions.
DIPi DIP-2314N.
IntActi P40477. 17 interactions.
MINTi MINT-629459.
STRINGi 4932.YIL115C.

Protein family/group databases

TCDBi 1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

MaxQBi P40477.
PaxDbi P40477.

Protocols and materials databases

DNASUi 854691.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL115C ; YIL115C ; YIL115C .
GeneIDi 854691.
KEGGi sce:YIL115C.

Organism-specific databases

CYGDi YIL115c.
SGDi S000001377. NUP159.

Phylogenomic databases

eggNOGi COG5651.
GeneTreei ENSGT00730000113975.
HOGENOMi HOG000113875.
InParanoidi P40477.
OMAi FGESAFG.
OrthoDBi EOG754HXQ.

Enzyme and pathway databases

BioCyci YEAST:G3O-31369-MONOMER.

Miscellaneous databases

EvolutionaryTracei P40477.
NextBioi 977319.

Gene expression databases

Genevestigatori P40477.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes."
    Gorsch L.C., Dockendorff T.C., Cole C.N.
    J. Cell Biol. 129:939-955(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex."
    Hurwitz M.E., Strambio-de-Castillia C., Blobel G.
    Proc. Natl. Acad. Sci. U.S.A. 95:11241-11245(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP82.
  5. "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 NSP1.
  6. "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.
  7. "Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells."
    Hodge C.A., Colot H.V., Stafford P., Cole C.N.
    EMBO J. 18:5778-5788(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GLE1; CRM1 AND DBP5.
  8. Cited for: FUNCTION, NUP82 NPC SUBCOMPLEX.
  9. "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.
  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. "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, INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS.
  12. "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.
  13. "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.
  14. "Deciphering networks of protein interactions at the nuclear pore complex."
    Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A., Lutzmann M., Hurt E.C., Rexach M.
    Mol. Cell. Proteomics 1:930-946(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CRM1 AND RNA1.
  15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  16. "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.
  17. "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.
  18. "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.
  19. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-735; THR-803; SER-805 AND SER-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  20. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; SER-724; SER-735; SER-745; SER-805; SER-819; SER-889 AND SER-940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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-404; SER-735; THR-803; SER-805; SER-819 AND SER-940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore."
    Weirich C.S., Erzberger J.P., Berger J.M., Weis K.
    Mol. Cell 16:749-760(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-387, FUNCTION, INTERACTION WITH DBP5.
  23. "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 1425-1460 IN COMPLEX WITH NUP82 AND NUP116, SUBUNIT.
  24. "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 1425-1460 IN COMPLEX WITH NUP82 AND THE MOUSE ORTHOLOG OF NUP145, SUBUNIT.

Entry informationi

Entry nameiNU159_YEAST
AccessioniPrimary (citable) accession number: P40477
Secondary accession number(s): D6VVH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 142 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 1230 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3