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P40477 (NU159_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleoporin NUP159
Alternative name(s):
Nuclear pore protein NUP159
Gene names
Name:NUP159
Synonyms:NUP158, RAT7
Ordered Locus Names:YIL115C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1460 AA.
Sequence statusComplete.
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). 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.22

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.22 Ref.23 Ref.24

Subcellular location

Nucleusnuclear 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 processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentMembrane
Nuclear pore complex
Nucleus
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein 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.22Ref.1PubMed 9359887PubMed 9802895. Source: SGD

protein export from nucleus

Inferred from mutant phenotype PubMed 17347149. Source: SGD

regulation of catalytic activity

Inferred from direct assay PubMed 21576266. Source: GOC

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_componentnuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Inferred from direct assay Ref.9PubMed 7642562Ref.1. Source: SGD

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_functionadenyl-nucleotide exchange factor activity

Inferred from direct assay 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

KAP95Q061423EBI-11747,EBI-9145
NUP82P403685EBI-11747,EBI-12331

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14601460Nucleoporin NUP159
PRO_0000204849

Regions

Repeat228 – 2314FG 1
Repeat267 – 2704PXFG 1
Repeat462 – 4709SXFGXPXFG 1
Repeat503 – 5119SXFGXPXFG 2; approximate
Repeat522 – 5309SXFGXPXFG 3; approximate
Repeat532 – 5354PXFG 2
Repeat548 – 5569SXFGXPXFG 4
Repeat558 – 5614PXFG 3
Repeat574 – 5829SXFGXPXFG 5
Repeat584 – 5874PXFG 4
Repeat600 – 6089SXFGXPXFG 6
Repeat610 – 6134SXFG 1
Repeat624 – 6329SXFGXPXFG 7; approximate
Repeat642 – 6454FG 2
Repeat687 – 6904FG 3
Repeat704 – 7074FXFG 1
Repeat709 – 7124SXFG 2
Repeat728 – 7314FXFG 2
Repeat842 – 8454PXFG 5
Repeat873 – 8764FXFG 3
Region1 – 500500Interaction with DBP5
Region497 – 701205Interactions with CRM1 and GLE1
Region1223 – 1460238Interaction with NUP82
Coiled coil1279 – 132042
Coiled coil1383 – 141836
Compositional bias455 – 766312Ser-rich

Amino acid modifications

Modified residue4041Phosphoserine Ref.19 Ref.21
Modified residue6571Phosphoserine Ref.20
Modified residue7241Phosphoserine Ref.20
Modified residue7351Phosphoserine Ref.19 Ref.20 Ref.21
Modified residue7451Phosphoserine Ref.20
Modified residue8031Phosphothreonine Ref.19 Ref.21
Modified residue8051Phosphoserine Ref.19 Ref.20 Ref.21
Modified residue8191Phosphoserine Ref.19 Ref.20 Ref.21
Modified residue8891Phosphoserine Ref.20
Modified residue9401Phosphoserine Ref.20 Ref.21

Secondary structure

.................................................................... 1460
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40477 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A33FFA52378F8205

FASTA1,460158,908
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[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]"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.
+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.
PIRS48457.
RefSeqNP_012151.1. NM_001179463.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP40477.
SMRP40477. Positions 2-381, 1431-1458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34876. 91 interactions.
DIPDIP-2314N.
IntActP40477. 17 interactions.
MINTMINT-629459.
STRING4932.YIL115C.

Protein family/group databases

TCDB1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

PaxDbP40477.

Protocols and materials databases

DNASU854691.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL115C; YIL115C; YIL115C.
GeneID854691.
KEGGsce:YIL115C.

Organism-specific databases

CYGDYIL115c.
SGDS000001377. NUP159.

Phylogenomic databases

eggNOGCOG5651.
GeneTreeENSGT00730000113975.
HOGENOMHOG000113875.
OMAFGESAFG.
OrthoDBEOG754HXQ.

Enzyme and pathway databases

BioCycYEAST:G3O-31369-MONOMER.

Gene expression databases

GenevestigatorP40477.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40477.
NextBio977319.

Entry information

Entry nameNU159_YEAST
AccessionPrimary (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 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references