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P39705 (NUP60_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 NUP60
Alternative name(s):
Nuclear pore protein NUP60
Gene names
Name:NUP60
Synonyms:FUN17
Ordered Locus Names:YAR002W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length539 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). Ref.6 Ref.7 Ref.9 Ref.10

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. Binds to NUP1 and NUP2 forming the nuclear basket and the distal ring. The interaction with NUP2 is GSP1-GTP-dependent. Interacts through its FG repeats with karyopherins, such as KAP123 and KAP95-SRP1 (KAP60). Also interacts with GSP1-GTP and SRM1 (PRP20), where NUP60 reduces SRM1 activity, thus inhibiting GSP1 guanine nucleotide dissociation. Ref.5 Ref.7

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Nuclear basket.

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.

Post-translational modification

Phosphorylated by CDC28. Ref.12

Miscellaneous

Present with 4590 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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Inferred from mutant phenotype Ref.7. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 21818277. Source: SGD

chromosome organization

Inferred from mutant phenotype PubMed 21818277. Source: SGD

double-strand break repair

Inferred from mutant phenotype PubMed 17538013. Source: SGD

intracellular mRNA localization

Inferred from mutant phenotype PubMed 21036941. Source: SGD

mRNA export from nucleus in response to heat stress

Inferred from mutant phenotype PubMed 18258809. Source: SGD

nucleocytoplasmic transport

Inferred from mutant phenotype Ref.7. Source: SGD

poly(A)+ mRNA export from nucleus

Inferred from mutant phenotype PubMed 12411502PubMed 21036941. Source: SGD

posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 20932479. Source: SGD

protein export from nucleus

Inferred from mutant phenotype Ref.7. Source: SGD

regulation of protein desumoylation

Inferred from genetic interaction PubMed 17403926. Source: SGD

telomere tethering at nuclear periphery

Inferred from mutant phenotype PubMed 11862215PubMed 21818277. Source: SGD

transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 20098417PubMed 20932479PubMed 21036941. Source: SGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 22932476. Source: SGD

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Inferred from direct assay Ref.5. Source: SGD

nuclear pore central transport channel

Inferred from direct assay PubMed 18046406. Source: SGD

nuclear pore nuclear basket

Inferred from direct assay Ref.5. Source: SGD

nucleus

Inferred from direct assay PubMed 22932476. Source: SGD

   Molecular_functionnucleocytoplasmic transporter activity

Inferred from genetic interaction Ref.6. Source: SGD

phospholipid binding

Inferred from direct assay PubMed 17897934. Source: SGD

structural constituent of nuclear pore

Inferred from mutant phenotype PubMed 17418788. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KAP95Q061424EBI-20731,EBI-9145
NUP2P324992EBI-20731,EBI-12401

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539Nucleoporin NUP60
PRO_0000204879

Regions

Repeat399 – 4013FXF 1
Repeat427 – 4293FXF 2
Repeat469 – 4713FXF 3
Repeat509 – 5113FXF 4
Coiled coil91 – 11828 Potential

Amino acid modifications

Modified residue101Phosphoserine Ref.14 Ref.15 Ref.16 Ref.17
Modified residue491Phosphoserine Ref.15
Modified residue811Phosphoserine Ref.14 Ref.16 Ref.17
Modified residue891Phosphoserine Ref.17
Modified residue1621Phosphoserine Ref.17
Modified residue1711Phosphoserine Ref.17
Modified residue2141Phosphoserine Ref.17
Modified residue2221Phosphoserine Ref.17
Modified residue3521Phosphoserine Ref.16 Ref.17
Modified residue3601Phosphoserine Ref.15
Modified residue3741Phosphoserine Ref.15
Modified residue3821Phosphoserine Ref.17
Modified residue4601Phosphothreonine Ref.16
Modified residue4801Phosphoserine Ref.15
Modified residue4831Phosphoserine Ref.15

Sequences

Sequence LengthMass (Da)Tools
P39705 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B9A28494A358A3E3

FASTA53959,039
        10         20         30         40         50         60 
MHRKSLRRAS ATVPSAPYRK QIISNAHNKP SLFSKIKTFF TQKDSARVSP RNNVANKQPR 

        70         80         90        100        110        120 
NESFNRRISS MPGGYFHSEI SPDSTVNRSV VVSAVGEARN DIENKEEEYD ETHETNISNA 

       130        140        150        160        170        180 
KLANFFSKKG NEPLSEIEIE GVMSLLQKSS KSMITSEGEQ KSAEGNNIDQ SLILKESGST 

       190        200        210        220        230        240 
PISISNAPTF NPKYDTSNAS MNTTLGSIGS RKYSFNYSSL PSPYKTTVYR YSAAKKIPDT 

       250        260        270        280        290        300 
YTANTSAQSI ASAKSVRSGV SKSAPSKKIS NTAAALVSLL DENDSKKNNA ASELANPYSS 

       310        320        330        340        350        360 
YVSQIRKHKR VSPNAAPRQE ISEEETTVKP LFQNVPEQGE EPMKQLNATK ISPSAPSKDS 

       370        380        390        400        410        420 
FTKYKPARSS SLRSNVVVAE TSPEKKDGGD KPPSSAFNFS FNTSRNVEPT ENAYKSENAP 

       430        440        450        460        470        480 
SASSKEFNFT NLQAKPLVGK PKTELTKGDS TPVQPDLSVT PQKSSSKGFV FNSVQKKSRS 

       490        500        510        520        530 
NLSQENDNEG KHISASIDND FSEEKAEEFD FNVPVVSKQL GNGLVDENKV EAFKSLYTF 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [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]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"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, NUCLEOPORIN INTERACTING PROTEINS.
[7]"The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex."
Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.
J. Cell Biol. 154:937-950(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GSP1-GTP; NUP2; SRM1; KAP123 AND KAP95-SRP1.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, FG REPEAT STRUCTURE.
[10]"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.
[11]"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.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CDC28.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[14]"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-10 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[15]"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-10; SER-49; SER-360; SER-374; SER-480 AND SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-10; SER-81; SER-352 AND THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-10; SER-81; SER-89; SER-162; SER-171; SER-214; SER-222; SER-352 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22015 Genomic DNA. Translation: AAC04957.1.
AY692943 Genomic DNA. Translation: AAT92962.1.
BK006935 Genomic DNA. Translation: DAA06986.1.
PIRS40900.
RefSeqNP_009401.1. NM_001178209.1.

3D structure databases

ProteinModelPortalP39705.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31790. 206 interactions.
DIPDIP-5821N.
IntActP39705. 12 interactions.
MINTMINT-629603.
STRING4932.YAR002W.

Protein family/group databases

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

Proteomic databases

PaxDbP39705.
PeptideAtlasP39705.

Protocols and materials databases

DNASU851263.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAR002W; YAR002W; YAR002W.
GeneID851263.
KEGGsce:YAR002W.

Organism-specific databases

CYGDYAR002w.
SGDS000000063. NUP60.

Phylogenomic databases

eggNOGNOG79863.
OMAHISASID.
OrthoDBEOG76HQCM.

Enzyme and pathway databases

BioCycYEAST:G3O-28867-MONOMER.

Gene expression databases

GenevestigatorP39705.

Family and domain databases

ProtoNetSearch...

Other

NextBio968225.

Entry information

Entry nameNUP60_YEAST
AccessionPrimary (citable) accession number: P39705
Secondary accession number(s): D6VPL6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 119 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 I

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

Yeast

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