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Protein

Nuclear localization sequence-binding protein

Gene

NSR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pre-rRNA processing. Specifically binds nuclear localization sequences. Candidate for a receptor at the nucleus that may be involved in both RNA and protein transport. Binds telomeric sequences of the type (TG[1-3])n in vitro.

GO - Molecular functioni

  • nuclear localization sequence binding Source: SGD
  • nucleotide binding Source: InterPro
  • RNA binding Source: SGD
  • single-stranded telomeric DNA binding Source: SGD

GO - Biological processi

  • ribosomal small subunit assembly Source: SGD
  • rRNA processing Source: SGD
Complete GO annotation...

Keywords - Biological processi

rRNA processing, Stress response

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30859-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear localization sequence-binding protein
Alternative name(s):
p67
Gene namesi
Name:NSR1
Ordered Locus Names:YGR159C
ORF Names:G7001
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR159C.
SGDiS000003391. NSR1.

Subcellular locationi

  • Nucleusnucleolus 1 Publication

GO - Cellular componenti

  • nuclear envelope Source: SGD
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Nuclear localization sequence-binding proteinPRO_0000081690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei353 – 3531Asymmetric dimethylarginine1 Publication
Modified residuei362 – 3621Asymmetric dimethylarginine1 Publication
Modified residuei366 – 3661Asymmetric dimethylarginine1 Publication
Modified residuei375 – 3751Asymmetric dimethylarginine1 Publication
Modified residuei379 – 3791Asymmetric dimethylarginine1 Publication
Modified residuei382 – 3821Asymmetric dimethylarginine1 Publication

Post-translational modificationi

Methylated by HMT1, forming asymmetric dimethylarginines (DMA) within a domain referred to as an RGG box, made up of repeated Gly-Gly dipeptides interspersed with Arg and aromatic residues.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP27476.
PeptideAtlasiP27476.

PTM databases

iPTMnetiP27476.

Expressioni

Inductioni

In response to low temperature (By cold-shock).

Interactioni

Protein-protein interaction databases

BioGridi33407. 74 interactions.
DIPiDIP-5537N.
IntActiP27476. 45 interactions.
MINTiMINT-543806.

Structurei

3D structure databases

ProteinModelPortaliP27476.
SMRiP27476. Positions 170-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 24679RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini267 – 34579RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni353 – 38432RGG-boxAdd
BLAST
Regioni366 – 38419RNA-binding RGG-boxBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi29 – 136108Asp/Glu/Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the RRM GAR family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00840000129894.
HOGENOMiHOG000113864.
InParanoidiP27476.
KOiK11294.
OMAiDGRPINC.
OrthoDBiEOG706125.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTTKVKGN KKEVKASKQA KEEKAKAVSS SSSESSSSSS SSSESESESE
60 70 80 90 100
SESESSSSSS SSDSESSSSS SSDSESEAET KKEESKDSSS SSSDSSSDEE
110 120 130 140 150
EEEEKEETKK EESKESSSSD SSSSSSSDSE SEKEESNDKK RKSEDAEEEE
160 170 180 190 200
DEESSNKKQK NEETEEPATI FVGRLSWSID DEWLKKEFEH IGGVIGARVI
210 220 230 240 250
YERGTDRSRG YGYVDFENKS YAEKAIQEMQ GKEIDGRPIN CDMSTSKPAG
260 270 280 290 300
NNDRAKKFGD TPSEPSDTLF LGNLSFNADR DAIFELFAKH GEVVSVRIPT
310 320 330 340 350
HPETEQPKGF GYVQFSNMED AKKALDALQG EYIDNRPVRL DFSSPRPNND
360 370 380 390 400
GGRGGSRGFG GRGGGRGGNR GFGGRGGARG GRGGFRPSGS GANTAPLGRS
410
RNTASFAGSK KTFD
Length:414
Mass (Da):44,535
Last modified:August 1, 1992 - v1
Checksum:i90DEEE7BBC20BC0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57185 Genomic DNA. Translation: CAA40472.1.
X85807 Genomic DNA. Translation: CAA59817.1.
Z72944 Genomic DNA. Translation: CAA97173.1.
Z72946 Genomic DNA. Translation: CAA97180.1.
BK006941 Genomic DNA. Translation: DAA08250.1.
PIRiA39205.
RefSeqiNP_011675.1. NM_001181288.1.

Genome annotation databases

EnsemblFungiiYGR159C; YGR159C; YGR159C.
GeneIDi853064.
KEGGisce:YGR159C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57185 Genomic DNA. Translation: CAA40472.1.
X85807 Genomic DNA. Translation: CAA59817.1.
Z72944 Genomic DNA. Translation: CAA97173.1.
Z72946 Genomic DNA. Translation: CAA97180.1.
BK006941 Genomic DNA. Translation: DAA08250.1.
PIRiA39205.
RefSeqiNP_011675.1. NM_001181288.1.

3D structure databases

ProteinModelPortaliP27476.
SMRiP27476. Positions 170-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33407. 74 interactions.
DIPiDIP-5537N.
IntActiP27476. 45 interactions.
MINTiMINT-543806.

PTM databases

iPTMnetiP27476.

Proteomic databases

MaxQBiP27476.
PeptideAtlasiP27476.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR159C; YGR159C; YGR159C.
GeneIDi853064.
KEGGisce:YGR159C.

Organism-specific databases

EuPathDBiFungiDB:YGR159C.
SGDiS000003391. NSR1.

Phylogenomic databases

GeneTreeiENSGT00840000129894.
HOGENOMiHOG000113864.
InParanoidiP27476.
KOiK11294.
OMAiDGRPINC.
OrthoDBiEOG706125.

Enzyme and pathway databases

BioCyciYEAST:G3O-30859-MONOMER.

Miscellaneous databases

PROiP27476.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs."
    Lee W.-C., Xue Z., Melese T.
    J. Cell Biol. 113:1-12(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Yeast NSR1 protein that has structural similarity to mammalian nucleolin is involved in pre-rRNA processing."
    Kondo K., Inouye M.
    J. Biol. Chem. 267:16252-16258(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
    Skala J., Nawrocki A., Goffeau A.
    Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Isolation and characterization of two Saccharomyces cerevisiae genes that encode proteins that bind to (TG1-3)n single strand telomeric DNA in vitro."
    Lin J.-J., Zakian V.A.
    Nucleic Acids Res. 22:4906-4913(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p."
    Xu C., Henry P.A., Setya A., Henry M.F.
    RNA 9:746-759(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, METHYLATION BY HMT1.

Entry informationi

Entry nameiNSR1_YEAST
AccessioniPrimary (citable) accession number: P27476
Secondary accession number(s): D6VUT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 8, 2016
This is version 149 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 77400 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.