Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q05166

- NUP59_YEAST

UniProt

Q05166 - NUP59_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Nucleoporin ASM4

Gene

ASM4

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). May have a mitosis control function (By similarity).By similarity

GO - Molecular functioni

  1. nucleocytoplasmic transporter activity Source: SGD
  2. phospholipid binding Source: SGD
  3. single-stranded DNA binding Source: SGD

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. mitotic spindle assembly checkpoint Source: SGD
  3. mRNA export from nucleus in response to heat stress Source: SGD
  4. nuclear pore organization Source: SGD
  5. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29496-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin ASM4
Alternative name(s):
Nuclear pore protein NUP59
Gene namesi
Name:ASM4
Synonyms:NUP59
Ordered Locus Names:YDL088C
ORF Names:D2420
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL088c.
SGDiS000002246. ASM4.

Subcellular locationi

GO - Cellular componenti

  1. nuclear pore Source: SGD
  2. nuclear pore central transport channel Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Nucleoporin ASM4PRO_0000204878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei458 – 4581Phosphoserine1 Publication
Modified residuei464 – 4641Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CDC28.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05166.
PaxDbiQ05166.
PeptideAtlasiQ05166.

Expressioni

Gene expression databases

GenevestigatoriQ05166.

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. ASM4 may form a subcomplex with NUP53, NDC1, and NUP170.

Binary interactionsi

WithEntry#Exp.IntActNotes
NDC1P325003EBI-3035,EBI-11950

Protein-protein interaction databases

BioGridi31972. 80 interactions.
DIPiDIP-1466N.
IntActiQ05166. 13 interactions.
MINTiMINT-389482.

Structurei

3D structure databases

ProteinModelPortaliQ05166.
SMRiQ05166. Positions 270-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 32FG 11 Publication
Repeati61 – 622FG 21 Publication
Repeati195 – 1962FG 31 Publication
Domaini265 – 394130RRM Nup35-typePROSITE-ProRule annotationAdd
BLAST
Repeati274 – 2752FG 41 Publication
Repeati291 – 2922FG 51 Publication
Repeati523 – 5242FG 61 Publication

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili490 – 51021Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 4931Gln-richAdd
BLAST
Compositional biasi28 – 4619Poly-GlnAdd
BLAST
Compositional biasi63 – 178116Asn-richAdd
BLAST
Compositional biasi84 – 874Poly-Asn

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.
The RRM Nup35-type domain might be involved in the control of mitosis.

Sequence similaritiesi

Contains 1 RRM Nup35-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG43865.
GeneTreeiENSGT00530000067349.
HOGENOMiHOG000113890.
InParanoidiQ05166.
OMAiTRNENTI.
OrthoDBiEOG7S4XG6.

Family and domain databases

InterProiIPR007846. RRM_NUP35_dom.
[Graphical view]
PfamiPF05172. Nup35_RRM. 1 hit.
[Graphical view]
PROSITEiPS51472. RRM_NUP35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05166-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFGIRSGNNN GGFTNLTSQA PQTTQMFQSQ SQLQPQPQPQ PQQQQQHLQF
60 70 80 90 100
NGSSDASSLR FGNSLSNTVN ANNYSSNIGN NSINNNNIKN GTNNISQHGQ
110 120 130 140 150
GNNPSWVNNP KKRFTPHTVI RRKTTKQNSS SDINQNDDSS SMNATMRNFS
160 170 180 190 200
KQNQDSKHNE RNKSAANNDI NSLLSNFNDI PPSVTLQDWQ REDEFGSIPS
210 220 230 240 250
LTTQFVTDKY TAKKTNRSAY DSKNTPNVFD KDSYVRIANI EQNHLDNNYN
260 270 280 290 300
TAETNNKVHE TSSKSSSLSA IIVFGYPESI SNELIEHFSH FGHIMEDFQV
310 320 330 340 350
LRLGRGINPN TFRIFHNHDT GCDENDSTVN KSITLKGRNN ESNNKKYPIF
360 370 380 390 400
TGESWVKLTY NSPSSALRAL QENGTIFRGS LIGCIPYSKN AVEQLAGCKI
410 420 430 440 450
DNVDDIGEFN VSMYQNSSTS STSNTPSPPN VIITDGTLLR EDDNTPAGHA
460 470 480 490 500
GNPTNISSPI VANSPNKRLD VIDGKLPFMQ NAGPNSNIPN LLRNLESKMR
510 520
QQEAKYRNNE PAGFTHKLSN WLFGWNDL
Length:528
Mass (Da):58,793
Last modified:November 1, 1997 - v1
Checksum:i84FE1F07FC1B0173
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141F → L in CAA54130. (PubMed:7862092)Curated
Sequence conflicti171 – 1711N → S in AAT92991. (PubMed:17322287)Curated
Sequence conflicti446 – 52883PAGHA…GWNDL → LPVMLVIQQIFQVQ in CAA54130. (PubMed:7862092)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76709 Genomic DNA. Translation: CAA54130.1.
X95644 Genomic DNA. Translation: CAA64923.1.
Z74136 Genomic DNA. Translation: CAA98654.1.
AY692972 Genomic DNA. Translation: AAT92991.1.
BK006938 Genomic DNA. Translation: DAA11770.1.
PIRiS67624.
RefSeqiNP_010195.1. NM_001180147.1.

Genome annotation databases

EnsemblFungiiYDL088C; YDL088C; YDL088C.
GeneIDi851470.
KEGGisce:YDL088C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76709 Genomic DNA. Translation: CAA54130.1 .
X95644 Genomic DNA. Translation: CAA64923.1 .
Z74136 Genomic DNA. Translation: CAA98654.1 .
AY692972 Genomic DNA. Translation: AAT92991.1 .
BK006938 Genomic DNA. Translation: DAA11770.1 .
PIRi S67624.
RefSeqi NP_010195.1. NM_001180147.1.

3D structure databases

ProteinModelPortali Q05166.
SMRi Q05166. Positions 270-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31972. 80 interactions.
DIPi DIP-1466N.
IntActi Q05166. 13 interactions.
MINTi MINT-389482.

Protein family/group databases

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

Proteomic databases

MaxQBi Q05166.
PaxDbi Q05166.
PeptideAtlasi Q05166.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL088C ; YDL088C ; YDL088C .
GeneIDi 851470.
KEGGi sce:YDL088C.

Organism-specific databases

CYGDi YDL088c.
SGDi S000002246. ASM4.

Phylogenomic databases

eggNOGi NOG43865.
GeneTreei ENSGT00530000067349.
HOGENOMi HOG000113890.
InParanoidi Q05166.
OMAi TRNENTI.
OrthoDBi EOG7S4XG6.

Enzyme and pathway databases

BioCyci YEAST:G3O-29496-MONOMER.

Miscellaneous databases

NextBioi 968762.

Gene expression databases

Genevestigatori Q05166.

Family and domain databases

InterProi IPR007846. RRM_NUP35_dom.
[Graphical view ]
Pfami PF05172. Nup35_RRM. 1 hit.
[Graphical view ]
PROSITEi PS51472. RRM_NUP35. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Suppressors of thermosensitive mutations in the DNA polymerase delta gene of Saccharomyces cerevisiae."
    Giot L., Simon M., Dubois C., Faye G.
    Mol. Gen. Genet. 246:212-222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
    Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
    Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p."
    Marelli M., Aitchison J.D., Wozniak R.W.
    J. Cell Biol. 143:1813-1830(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCOMPLEX WITH NUP170 AND NUP53, INTERACTION WITH KARYOPHERIN PSE1.
  7. "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.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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.
  10. Cited for: INTERACTION.
  11. "A comprehensive two-hybrid analysis to explore the yeast protein interactome."
    Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.
    Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION.
  12. "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.
  13. Cited for: PHOSPHORYLATION BY CDC28.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-458 AND SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUP59_YEAST
AccessioniPrimary (citable) accession number: Q05166
Secondary accession number(s): D6VRR0, E9P903, Q12456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 122 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 2740 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3