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P22211 (NPR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 132. 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:
Nitrogen permease reactivator protein

EC=2.7.11.1
Alternative name(s):
Serine/threonine-protein kinase NPR1
Gene names
Name:NPR1
Ordered Locus Names:YNL183C
ORF Names:N1631
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length790 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nutrient-regulated protein kinase that promotes the activity of at least 6 distinct transport systems for nitrogenous nutrients under conditions of nitrogen catabolite derepression. Under poor nitrogen growth conditions, required for post-Golgi sorting of the general amino acid permease GAP1 and the three known ammonia permeases, MEP1/2/3, to the plasma membrane. Contributes also to the stability and the retention of GAP1 at the plasma membrane. Inversely, promotes the degradation of tryptophan permease TAT2 under the same conditions. Activity is regulated by the TOR signaling pathway via phosphatase SIT4. Although thought to be involved in regulation of GLN3-dependent transcription by nitrogen catabolite repression, this seems to be an indirect effect from the reduced uptake of the nitrogen-repressing compound. Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Dephosphorylation by SIT4 activates NPR1 kinase activity.

Subunit structure

Interacts with TIP41. Ref.8

Subcellular location

Cytoplasm. Note: Appears to be more concentrated in punctate structures reminiscent of the Golgi or of an endosomal compartment. Ref.7

Post-translational modification

Hyperphosphorylated in nitrogen-rich growth medium. Nitrogen limitation (or rapamycin treatment) leads to substantial, though not complete dephosphorylation. Autophosphorylation plays only a minor role and seems not to be regulated by the quality of the nitrogen source. Ref.4

Miscellaneous

Present with 284 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 790790Nitrogen permease reactivator protein
PRO_0000086445

Regions

Domain438 – 742305Protein kinase
Nucleotide binding444 – 4529ATP By similarity
Compositional bias1 – 339339Ser-rich (may play a regulatory role)
Compositional bias51 – 588Poly-Ser
Compositional bias782 – 7865Poly-Lys

Sites

Active site5611Proton acceptor By similarity
Binding site4671ATP By similarity

Amino acid modifications

Modified residue471Phosphoserine; by autocatalysis Ref.4
Modified residue851Phosphoserine Ref.4
Modified residue901Phosphoserine Ref.4
Modified residue1001Phosphoserine Ref.4
Modified residue1111Phosphoserine Ref.4
Modified residue1161Phosphoserine Ref.4
Modified residue1251Phosphoserine Ref.4 Ref.13 Ref.16
Modified residue1371Phosphoserine Ref.4 Ref.16
Modified residue1411Phosphoserine Ref.4 Ref.16
Modified residue2571Phosphoserine; by autocatalysis Ref.4
Modified residue2591Phosphoserine Ref.4
Modified residue2601Phosphoserine Ref.4
Modified residue2881Phosphoserine Ref.4
Modified residue2921Phosphoserine Ref.4
Modified residue3171Phosphoserine Ref.4
Modified residue3201Phosphoserine Ref.4
Modified residue3281Phosphoserine Ref.4
Modified residue3341Phosphotyrosine Ref.16
Modified residue3361Phosphoserine Ref.4
Modified residue3531Phosphoserine Ref.4
Modified residue3561Phosphoserine Ref.4
Modified residue3571Phosphoserine; by autocatalysis Ref.4 Ref.13
Modified residue3851Phosphoserine Ref.4

Experimental info

Mutagenesis471S → A: Abolishes autophosphorylation; when associated with A-257 and A-357. Ref.4
Mutagenesis2571S → A: Abolishes autophosphorylation; when associated with A-47 and A-357. Ref.4
Mutagenesis2571S → D: Abolishes autophosphorylation. Ref.4
Mutagenesis3571S → A: Abolishes autophosphorylation; when associated with A-47 and A-257. Ref.4
Sequence conflict1541T → A in CAA39564. Ref.1
Sequence conflict2771S → P in CAA39564. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22211 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 0ECFA33376740733

FASTA79085,990
        10         20         30         40         50         60 
MSSLTRLLQE KRKNETSNSS PRTSADTLTT TPESQSLDLH SRNKSSSHIG SVSNSSSSDR 

        70         80         90        100        110        120 
NRANVPVPGS VTTVTQIYSE EDSSSTAGSS LDDRNQFSSS FLNANFAHTA SFYGTSAQSR 

       130        140        150        160        170        180 
DRFGSLINDQ GTAGLSSHGG SFAAQNRITS RLSTTSHTSG RAIPSLSSSI PYSVPNSNKD 

       190        200        210        220        230        240 
NNSSNSNSSS LSSSWLETYA GGMPNNISAI DSNVISSPKV DSVEPRFVIS KQKLQKASMD 

       250        260        270        280        290        300 
SNNANATQSR SISRSGSFSS QLGNFFFSKN SKESSNSNSA GMSFSANSNG PSPNIKNPNV 

       310        320        330        340        350        360 
TNGSTPIPKP IRARQSSIYS ASRQPTGSYT DNFYGSPSSV HDHLPPSQSV PRSQHSSIGD 

       370        380        390        400        410        420 
LKRFFKKSSN SNLSSNSNNV IPNGSPLSSG IAVPSHSHSS SHFAAGNNSY STSYNGNGDT 

       430        440        450        460        470        480 
IYSHSHGGSG IPFSKRYIKT GADLGAGAGG SVKLAQRISD NKIFAVKEFR TKFENESKRD 

       490        500        510        520        530        540 
YVKKITSEYC IGTTLNHPNI IETIEIVYEN DRILQVMEYC EYDLFAIVMS NKMSYEEICC 

       550        560        570        580        590        600 
CFKQILTGVQ YLHSIGLAHR DLKLDNCVIN EKGIVKLIDF GAAVVFSYPF SKNLVEASGI 

       610        620        630        640        650        660 
VGSDPYLAPE VCIFAKYDPR PVDIWSSAII FACMILKKFP WKIPKLRDNS FKLFCSGRDC 

       670        680        690        700        710        720 
DSLSSLVTRT PDPPSYDESH STEKKKPESS SNNVSDPNNV NIGPQRLLHS LPEETQHIVG 

       730        740        750        760        770        780 
RMIDLAPACR GNIEEIMEDP WIRSIDMCHL VEDGLSFKVV RGEDHHHTQV DQSEAHIAGL 

       790 
EKKKKKQNNQ 

« Hide

References

« Hide 'large scale' references
[1]"The Saccharomyces cerevisiae NPR1 gene required for the activity of ammonia-sensitive amino acid permeases encodes a protein kinase homologue."
Vandenbol M., Jauniaux J.-C., Grenson M.
Mol. Gen. Genet. 222:393-399(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sigma 1278B.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification of the rapamycin-sensitive phosphorylation sites within the Ser/Thr-rich domain of the yeast Npr1 protein kinase."
Gander S., Bonenfant D., Altermatt P., Martin D.E., Hauri S., Moes S., Hall M.N., Jenoe P.
Rapid Commun. Mass Spectrom. 22:3743-3753(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-60; 63-120; 123-147; 255-269; 273-296; 315-362 AND 368-403, PHOSPHORYLATION AT SER-47; SER-85; SER-90; SER-100; SER-111; SER-116; SER-125; SER-137; SER-141; SER-257; SER-259; SER-260; SER-288; SER-292; SER-317; SER-320; SER-328; SER-336; SER-353; SER-356; SER-357 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-47; SER-257 AND SER-357.
[5]"Study of the positive control of the general amino-acid permease and other ammonia-sensitive uptake systems by the product of the NPR1 gene in the yeast Saccharomyces cerevisiae."
Grenson M.
Eur. J. Biochem. 133:141-144(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease."
Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.
EMBO J. 17:6924-6931(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease."
De Craene J.-O., Soetens O., Andre B.
J. Biol. Chem. 276:43939-43948(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"TIP41 interacts with TAP42 and negatively regulates the TOR signaling pathway."
Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.
Mol. Cell 8:1017-1026(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIP41.
[9]"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].
[10]"NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae."
Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B., Primig M., Hall M.N.
J. Biol. Chem. 279:37512-37517(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae."
Feller A., Boeckstaens M., Marini A.-M., Dubois E.
J. Biol. Chem. 281:28546-28554(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Ammonia-specific regulation of Gln3 localization in Saccharomyces cerevisiae by protein kinase Npr1."
Tate J.J., Rai R., Cooper T.G.
J. Biol. Chem. 281:28460-28469(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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-125 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[14]"The yeast ammonium transport protein Mep2 and its positive regulator, the Npr1 kinase, play an important role in normal and pseudohyphal growth on various nitrogen media through retrieval of excreted ammonium."
Boeckstaens M., Andre B., Marini A.M.
Mol. Microbiol. 64:534-546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-125; SER-137; SER-141 AND TYR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56084 Genomic DNA. Translation: CAA39564.1.
Z71459 Genomic DNA. Translation: CAA96076.1.
BK006947 Genomic DNA. Translation: DAA10369.1.
PIRS63138.
RefSeqNP_014216.1. NM_001183021.1.

3D structure databases

ProteinModelPortalP22211.
SMRP22211. Positions 432-757.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35649. 129 interactions.
DIPDIP-4327N.
IntActP22211. 48 interactions.
MINTMINT-556937.
STRING4932.YNL183C.

Proteomic databases

MaxQBP22211.
PaxDbP22211.
PeptideAtlasP22211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL183C; YNL183C; YNL183C.
GeneID855538.
KEGGsce:YNL183C.

Organism-specific databases

CYGDYNL183c.
SGDS000005127. NPR1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000075309.
HOGENOMHOG000093332.
KOK00924.
OMAITGEYCI.
OrthoDBEOG7008J9.

Enzyme and pathway databases

BioCycYEAST:G3O-33194-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorP22211.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979598.

Entry information

Entry nameNPR1_YEAST
AccessionPrimary (citable) accession number: P22211
Secondary accession number(s): D6W103
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families