Nucleoporin ASM4 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Nucleoporin ASM4

Alternative name(s):
Nuclear pore protein NUP59

Gene names

Name:	ASM4
Synonyms:	NUP59
Ordered Locus Names:	YDL088C
ORF Names:	D2420

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	528 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). May have a mitosis control function By similarity. Ref.6 Ref.9
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. ASM4 may form a subcomplex with NUP53, NDC1, and NUP170. Ref.7
Subcellular location	Nucleus › nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Symmetric distribution.
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. The RRM Nup35-type domain might be involved in the control of mitosis.
Post-translational modification	Phosphorylated by CDC28. Ref.13 Ref.14 Ref.15
Miscellaneous	Present with 2740 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Contains 1 RRM Nup35-type domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mRNA export from nucleus in response to heat stress Inferred from mutant phenotype. Source: SGD mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from direct assay Ref.7 Ref.6. Source: SGD
Molecular function	phospholipid binding Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct single-stranded DNA binding Inferred from direct assay. Source: SGD structural molecule activity Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDC1	P32500	3	EBI-3035,EBI-11950

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 528

528

Nucleoporin ASM4

PRO_0000204878

Regions

Repeat

2 – 3

2

FG 1

Repeat

61 – 62

2

FG 2

Repeat

195 – 196

2

FG 3

Domain

265 – 394

130

RRM Nup35-type

Repeat

274 – 275

2

FG 4

Repeat

291 – 292

2

FG 5

Repeat

523 – 524

2

FG 6

Coiled coil

490 – 510

21

Potential

Compositional bias

19 – 49

31

Gln-rich

Compositional bias

28 – 46

19

Poly-Gln

Compositional bias

63 – 178

116

Asn-rich

Compositional bias

84 – 87

4

Poly-Asn

Amino acid modifications

Modified residue

457

1

Phosphoserine Ref.15

Modified residue

458

1

Phosphoserine Ref.14 Ref.15

Experimental info

Sequence conflict

114

1

F → L in CAA54130. Ref.1

Sequence conflict

171

1

N → S in AAT92991. Ref.5

Sequence conflict

446 – 528

83

PAGHA…GWNDL → LPVMLVIQQIFQVQ in CAA54130. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q05166 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 84FE1F07FC1B0173
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FASTA

528

58,793

        10         20         30         40         50         60 
MFGIRSGNNN GGFTNLTSQA PQTTQMFQSQ SQLQPQPQPQ PQQQQQHLQF NGSSDASSLR 

        70         80         90        100        110        120 
FGNSLSNTVN ANNYSSNIGN NSINNNNIKN GTNNISQHGQ GNNPSWVNNP KKRFTPHTVI 

       130        140        150        160        170        180 
RRKTTKQNSS SDINQNDDSS SMNATMRNFS KQNQDSKHNE RNKSAANNDI NSLLSNFNDI 

       190        200        210        220        230        240 
PPSVTLQDWQ REDEFGSIPS LTTQFVTDKY TAKKTNRSAY DSKNTPNVFD KDSYVRIANI 

       250        260        270        280        290        300 
EQNHLDNNYN TAETNNKVHE TSSKSSSLSA IIVFGYPESI SNELIEHFSH FGHIMEDFQV 

       310        320        330        340        350        360 
LRLGRGINPN TFRIFHNHDT GCDENDSTVN KSITLKGRNN ESNNKKYPIF TGESWVKLTY 

       370        380        390        400        410        420 
NSPSSALRAL QENGTIFRGS LIGCIPYSKN AVEQLAGCKI DNVDDIGEFN VSMYQNSSTS 

       430        440        450        460        470        480 
STSNTPSPPN VIITDGTLLR EDDNTPAGHA GNPTNISSPI VANSPNKRLD VIDGKLPFMQ 

       490        500        510        520 
NAGPNSNIPN LLRNLESKMR QQEAKYRNNE PAGFTHKLSN WLFGWNDL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7862092] [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: 8923743] [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. Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] 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: 9864357] [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: 10684247] [Abstract] Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[8]	"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: 14562106] [Abstract] 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: 12604785] [Abstract] Cited for: FUNCTION, FG REPEAT STRUCTURE.
[10]	"A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae." Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A., Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M., Johnston M., Fields S., Rothberg J.M. Nature 403:623-627(2000) [PubMed: 10688190] [Abstract] 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: 11283351] [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: 12791264] [Abstract] Cited for: REVIEW.
[13]	"Targets of the cyclin-dependent kinase Cdk1." Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O. Nature 425:859-864(2003) [PubMed: 14574415] [Abstract] Cited for: PHOSPHORYLATION BY CDC28.
[14]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY.
[15]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-458, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S67624.
RefSeq	NP_010195.1. NM_001180147.1.
3D structure databases
ProteinModelPortal	Q05166.
SMR	Q05166. Positions 270-396.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1466N.
IntAct	Q05166. 13 interactions.
MINT	MINT-389482.
STRING	Q05166.
Protein family/group databases
TCDB	9.A.14.1.1. nuclear pore complex (NPC) family.
Proteomic databases
PeptideAtlas	Q05166.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL088C; YDL088C; YDL088C.
GeneID	851470.
KEGG	sce:YDL088C.
NMPDR	fig\|4932.3.peg.933.
Organism-specific databases
CYGD	YDL088c.
SGD	S000002246. ASM4.
Phylogenomic databases
eggNOG	fuNOG09269.
HOGENOM	HBG203083.
OMA	GCIPYSK.
OrthoDB	EOG4XH38N.
Gene expression databases
ArrayExpress	Q05166.
Genevestigator	Q05166.
GermOnline	YDL088C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007846. MPPN. [Graphical view]
Pfam	PF05172. MPPN. 1 hit. [Graphical view]
PROSITE	PS51472. RRM_NUP35. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968762.

Entry information

Entry name

NUP59_YEAST

Accession

Primary (citable) accession number: Q05166
Secondary accession number(s): D6VRR0, E9P903, Q12456

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents