P40477 (NU159_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoporin NUP159

Alternative name(s):
Nuclear pore protein NUP159

Gene names

Name:	NUP159
Synonyms:	NUP158, RAT7
Ordered Locus Names:	YIL115C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1460 AA.
Sequence status	Complete.
Protein existence	Evidence 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). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.24
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. 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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.24 Ref.25 Ref.26
Subcellular location	Nucleus › nuclear pore complex. Nucleus membrane; Peripheral membrane protein; 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: SXFG/PXFG repeats are especially abundant in NUPs on the cytoplasmic side.
Miscellaneous	Present with 1230 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NLS-bearing substrate import into nucleus Inferred from genetic interaction Ref.17. Source: SGD ncRNA export from nucleus Inferred from mutant phenotype PubMed 11352936. Source: SGD nuclear pore distribution Inferred from mutant phenotype Ref.1PubMed 9359887. Source: SGD poly(A)+ mRNA export from nucleus Inferred from mutant phenotype Ref.24Ref.1PubMed 9359887PubMed 9802895. Source: SGD protein export from nucleus Inferred from mutant phenotype PubMed 17347149. Source: SGD ribosomal large subunit export from nucleus Inferred from mutant phenotype PubMed 11071906Ref.12. Source: SGD ribosomal small subunit export from nucleus Inferred from mutant phenotype Ref.12. Source: SGD
Cellular_component	nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore central transport channel Inferred from direct assay PubMed 18046406. Source: SGD nuclear pore cytoplasmic filaments Inferred from direct assay Ref.9PubMed 14960378. Source: SGD
Molecular_function	adenyl-nucleotide exchange factor activity Inferred from mutant phenotype PubMed 21576266. Source: SGD nucleocytoplasmic transporter activity Inferred from physical interaction PubMed 17418788. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KAP95	Q06142	3	EBI-11747,EBI-9145
NUP82	P40368	6	EBI-11747,EBI-12331

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1460

1460

Nucleoporin NUP159

PRO_0000204849

Regions

Repeat

228 – 231

4

FG 1

Repeat

267 – 270

4

PXFG 1

Repeat

462 – 470

9

SXFGXPXFG 1

Repeat

503 – 511

9

SXFGXPXFG 2; approximate

Repeat

522 – 530

9

SXFGXPXFG 3; approximate

Repeat

532 – 535

4

PXFG 2

Repeat

548 – 556

9

SXFGXPXFG 4

Repeat

558 – 561

4

PXFG 3

Repeat

574 – 582

9

SXFGXPXFG 5

Repeat

584 – 587

4

PXFG 4

Repeat

600 – 608

9

SXFGXPXFG 6

Repeat

610 – 613

4

SXFG 1

Repeat

624 – 632

9

SXFGXPXFG 7; approximate

Repeat

642 – 645

4

FG 2

Repeat

687 – 690

4

FG 3

Repeat

704 – 707

4

FXFG 1

Repeat

709 – 712

4

SXFG 2

Repeat

728 – 731

4

FXFG 2

Repeat

842 – 845

4

PXFG 5

Repeat

873 – 876

4

FXFG 3

Region

1 – 500

500

Interaction with DBP5

Region

497 – 701

205

Interactions with CRM1 and GLE1

Region

1223 – 1460

238

Interaction with NUP82

Coiled coil

1279 – 1320

42

Coiled coil

1383 – 1418

36

Compositional bias

455 – 766

312

Ser-rich

Amino acid modifications

Modified residue

402

1

Phosphoserine Ref.22 Ref.23

Modified residue

404

1

Phosphoserine Ref.19 Ref.20 Ref.22 Ref.23

Modified residue

406

1

Phosphothreonine Ref.23

Modified residue

407

1

Phosphoserine Ref.23

Modified residue

654

1

Phosphothreonine Ref.23

Modified residue

657

1

Phosphoserine Ref.22 Ref.23

Modified residue

710

1

Phosphoserine Ref.23

Modified residue

724

1

Phosphoserine Ref.23

Modified residue

735

1

Phosphoserine Ref.19 Ref.20 Ref.23

Modified residue

745

1

Phosphoserine Ref.22 Ref.23

Modified residue

748

1

Phosphoserine Ref.22 Ref.23

Modified residue

749

1

Phosphoserine Ref.23

Modified residue

803

1

Phosphothreonine Ref.20 Ref.23

Modified residue

805

1

Phosphoserine Ref.20 Ref.23

Modified residue

819

1

Phosphoserine Ref.20 Ref.22 Ref.23

Modified residue

889

1

Phosphoserine Ref.23

Modified residue

938

1

Phosphotyrosine Ref.23

Modified residue

940

1

Phosphoserine Ref.22 Ref.23

Modified residue

942

1

Phosphoserine Ref.23

Modified residue

948

1

Phosphothreonine Ref.23

Modified residue

949

1

Phosphoserine Ref.23

Modified residue

951

1

Phosphoserine Ref.23

Modified residue

1041

1

Phosphoserine Ref.21 Ref.22

Modified residue

1042

1

Phosphoserine Ref.21

Modified residue

1209

1

Phosphoserine Ref.23

Modified residue

1420

1

Phosphoserine Ref.23

Secondary structure

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1460

Helix Strand Turn

Details...

Beta strand

10 – 15

6

Beta strand

17 – 25

9

Beta strand

42 – 45

4

Turn

46 – 49

4

Beta strand

50 – 55

6

Beta strand

58 – 63

6

Helix

64 – 72

9

Beta strand

73 – 75

3

Beta strand

81 – 85

5

Beta strand

89 – 95

7

Beta strand

98 – 114

17

Beta strand

118 – 123

6

Beta strand

128 – 133

6

Beta strand

135 – 142

8

Beta strand

145 – 151

7

Turn

152 – 154

3

Beta strand

157 – 169

13

Beta strand

171 – 178

8

Beta strand

183 – 189

7

Beta strand

192 – 199

8

Helix

203 – 206

4

Turn

210 – 212

3

Beta strand

213 – 231

19

Beta strand

245 – 253

9

Beta strand

256 – 265

10

Beta strand

278 – 284

7

Beta strand

286 – 288

3

Beta strand

292 – 298

7

Beta strand

305 – 307

3

Beta strand

309 – 317

9

Helix

318 – 320

3

Turn

328 – 330

3

Beta strand

336 – 342

7

Beta strand

364 – 369

6

Beta strand

372 – 380

9

Beta strand

1118 – 1123

6

Helix

1436 – 1454

19

Sequences

	Sequence		Length	Mass (Da)
	P40477 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: A33FFA52378F8205	FASTA	1,460	158,908
	10 20 30 40 50 60 MSSLKDEVPT ETSEDFGFKF LGQKQILPSF NEKLPFASLQ NLDISNSKSL FVAASGSKAV 70 80 90 100 110 120 VGELQLLRDH ITSDSTPLTF KWEKEIPDVI FVCFHGDQVL VSTRNALYSL DLEELSEFRT 130 140 150 160 170 180 VTSFEKPVFQ LKNVNNTLVI LNSVNDLSAL DLRTKSTKQL AQNVTSFDVT NSQLAVLLKD 190 200 210 220 230 240 RSFQSFAWRN GEMEKQFEFS LPSELEELPV EEYSPLSVTI LSPQDFLAVF GNVISETDDE 250 260 270 280 290 300 VSYDQKMYII KHIDGSASFQ ETFDITPPFG QIVRFPYMYK VTLSGLIEPD ANVNVLASSC 310 320 330 340 350 360 SSEVSIWDSK QVIEPSQDSE RAVLPISEET DKDTNPIGVA VDVVTSGTIL EPCSGVDTIE 370 380 390 400 410 420 RLPLVYILNN EGSLQIVGLF HVAAIKSGHY SINLESLEHE KSLSPTSEKI PIAGQEQEEK 430 440 450 460 470 480 KKNNESSKAL SENPFTSANT SGFTFLKTQP AAANSLQSQS SSTFGAPSFG SSAFKIDLPS 490 500 510 520 530 540 VSSTSTGVAS SEQDATDPAS AKPVFGKPAF GAIAKEPSTS EYAFGKPSFG APSFGSGKSS 550 560 570 580 590 600 VESPASGSAF GKPSFGTPSF GSGNSSVEPP ASGSAFGKPS FGTPSFGSGN SSAEPPASGS 610 620 630 640 650 660 AFGKPSFGTS AFGTASSNET NSGSIFGKAA FGSSSFAPAN NELFGSNFTI SKPTVDSPKE 670 680 690 700 710 720 VDSTSPFPSS GDQSEDESKS DVDSSSTPFG TKPNTSTKPK TNAFDFGSSS FGSGFSKALE 730 740 750 760 770 780 SVGSDTTFKF GTQASPFSSQ LGNKSPFSSF TKDDTENGSL SKGSTSEIND DNEEHESNGP 790 800 810 820 830 840 NVSGNDLTDS TVEQTSSTRL PETPSDEDGE VVEEEAQKSP IGKLTETIKK SANIDMAGLK 850 860 870 880 890 900 NPVFGNHVKA KSESPFSAFA TNITKPSSTT PAFSFGNSTM NKSNTSTVSP MEEADTKETS 910 920 930 940 950 960 EKGPITLKSV ENPFLPAKEE RTGESSKKDH NDDPKDGYVS GSEISVRTSE SAFDTTANEE 970 980 990 1000 1010 1020 IPKSQDVNNH EKSETDPKYS QHAVVDHDNK SKEMNETSKN NERSGQPNHG VQGDGIALKK 1030 1040 1050 1060 1070 1080 DNEKENFDSN MAIKQFEDHQ SSEEDASEKD SRQSSEVKES DDNMSLNSDR DESISESYDK 1090 1100 1110 1120 1130 1140 LEDINTDELP HGGEAFKARE VSASADFDVQ TSLEDNYAES GIQTDLSESS KENEVQTDAI 1150 1160 1170 1180 1190 1200 PVKHNSTQTV KKEAVDNGLQ TEPVETCNFS VQTFEGDENY LAEQCKPKQL KEYYTSAKVS 1210 1220 1230 1240 1250 1260 NIPFVSQNST LRLIESTFQT VEAEFTVLME NIRNMDTFFT DQSSIPLVKR TVRSINNLYT 1270 1280 1290 1300 1310 1320 WRIPEAEILL NIQNNIKCEQ MQITNANIQD LKEKVTDYVR KDIAQITEDV ANAKEEYLFL 1330 1340 1350 1360 1370 1380 MHFDDASSGY VKDLSTHQFR MQKTLRQKLF DVSAKINHTE ELLNILKLFT VKNKRLDDNP 1390 1400 1410 1420 1430 1440 LVAKLAKESL ARDGLLKEIK LLREQVSRLQ LEEKGKKASS FDASSSITKD MKGFKVVEVG 1450 1460 LAMNTKKQIG DFFKNLNMAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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] [Europe PMC] [Abstract] 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]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND SER-735, MASS SPECTROMETRY. Strain: YAL6B.
[20]	"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, MASS SPECTROMETRY. Strain: ADR376.
[21]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041 AND SER-1042, MASS SPECTROMETRY.
[22]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-404; SER-657; SER-745; SER-748; SER-819; SER-940 AND SER-1041, MASS SPECTROMETRY.
[23]	"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-402; SER-404; THR-406; SER-407; THR-654; SER-657; SER-710; SER-724; SER-735; SER-745; SER-748; SER-749; THR-803; SER-805; SER-819; SER-889; TYR-938; SER-940; SER-942; THR-948; SER-949; SER-951; SER-1209 AND SER-1420, MASS SPECTROMETRY.
[24]	"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.
[25]	"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.
[26]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L40634 Genomic DNA. Translation: AAC41652.1.
Z38125 Genomic DNA. Translation: CAA86265.1.
BK006942 Genomic DNA. Translation: DAA08438.1.

PIR

S48457.

RefSeq

NP_012151.1. NM_001179463.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P40477.

SMR

P40477. Positions 2-381, 1431-1458.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2314N.

IntAct

P40477. 17 interactions.

MINT

MINT-629459.

STRING

4932.YIL115C.

Protein family/group databases

TCDB

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

Proteomic databases

PaxDb

P40477.

Protocols and materials databases

DNASU

854691.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL115C; YIL115C; YIL115C.

GeneID

854691.

KEGG

sce:YIL115C.

Organism-specific databases

CYGD

YIL115c.

SGD

S000001377. NUP159.

Phylogenomic databases

eggNOG

COG5651.

GeneTree

ENSGT00700000105429.

HOGENOM

HOG000113875.

OMA

ESPFAKF.

OrthoDB

EOG4XWK6M.

Gene expression databases

Genevestigator

P40477.

GermOnline

YIL115C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P40477.

NextBio

977319.

Entry information

Entry name

NU159_YEAST

Accession

Primary (citable) accession number: P40477
Secondary accession number(s): D6VVH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program