Nitrogen permease reactivator protein - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P22211 (NPR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	790 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.12 Ref.13 Ref.15
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of endocytosis Inferred from mutant phenotype PubMed 22118465. Source: SGD regulation of nitrogen utilization Inferred from mutant phenotype Ref.7. Source: SGD regulation of transmembrane transporter activity Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 17095607. Source: SGD plasma membrane Inferred from direct assay PubMed 22118465. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay PubMed 19780626. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
GCN2	P15442	2	EBI-12207,EBI-330
SNF1	P06782	2	EBI-12207,EBI-17516
TOR1	P35169	2	EBI-12207,EBI-19374

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 790

790

Nitrogen permease reactivator protein

PRO_0000086445

Regions

Domain

438 – 742

305

Protein kinase

Nucleotide binding

444 – 452

ATP By similarity

Compositional bias

1 – 339

339

Ser-rich (may play a regulatory role)

Compositional bias

51 – 58

Poly-Ser

Compositional bias

782 – 786

Poly-Lys

Sites

Active site

561

Proton acceptor By similarity

Binding site

467

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.17

Modified residue

Phosphoserine; by autocatalysis Ref.4

Modified residue

Phosphoserine Ref.4

Modified residue

Phosphoserine Ref.4

Modified residue

100

Phosphoserine Ref.4 Ref.17

Modified residue

111

Phosphoserine Ref.4

Modified residue

116

Phosphoserine Ref.4 Ref.17

Modified residue

125

Phosphoserine Ref.4 Ref.14

Modified residue

137

Phosphoserine Ref.4

Modified residue

141

Phosphoserine Ref.4

Modified residue

159

Phosphoserine Ref.16

Modified residue

169

Phosphoserine Ref.17

Modified residue

249

Phosphoserine Ref.17

Modified residue

255

Phosphoserine Ref.17

Modified residue

257

Phosphoserine; by autocatalysis Ref.4

Modified residue

259

Phosphoserine Ref.4

Modified residue

260

Phosphoserine Ref.4

Modified residue

288

Phosphoserine Ref.4

Modified residue

292

Phosphoserine Ref.4

Modified residue

317

Phosphoserine Ref.4 Ref.9

Modified residue

320

Phosphoserine Ref.4

Modified residue

328

Phosphoserine Ref.4

Modified residue

336

Phosphoserine Ref.4

Modified residue

353

Phosphoserine Ref.4

Modified residue

356

Phosphoserine Ref.4 Ref.17

Modified residue

357

Phosphoserine; by autocatalysis Ref.4 Ref.14 Ref.17

Modified residue

385

Phosphoserine Ref.4

Modified residue

681

Phosphoserine Ref.17

Experimental info

Mutagenesis

S → A: Abolishes autophosphorylation; when associated with A-257 and A-357. Ref.4

Mutagenesis

257

S → A: Abolishes autophosphorylation; when associated with A-47 and A-357. Ref.4

Mutagenesis

257

S → D: Abolishes autophosphorylation. Ref.4

Mutagenesis

357

S → A: Abolishes autophosphorylation; when associated with A-47 and A-257. Ref.4

Sequence conflict

154

T → A in CAA39564. Ref.1

Sequence conflict

277

S → P in CAA39564. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P22211 [UniParc].

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

790

85,990

        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' referencesShow '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. Hani J. Nature 387:93-98(1997) [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]	"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, 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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, MASS SPECTROMETRY. Strain: 2124.
[10]	"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].
[11]	"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.
[12]	"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.
[13]	"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.
[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-125 AND SER-357, MASS SPECTROMETRY. Strain: ADR376.
[15]	"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.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, MASS SPECTROMETRY.
[17]	"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-45; SER-100; SER-116; SER-169; SER-249; SER-255; SER-356; SER-357 AND SER-681, MASS SPECTROMETRY.
+	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.
PIR	S63138.
RefSeq	NP_014216.1. NM_001183021.1.
3D structure databases
ProteinModelPortal	P22211.
SMR	P22211. Positions 437-757.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4327N.
IntAct	P22211. 47 interactions.
MINT	MINT-556937.
STRING	4932.YNL183C.
Proteomic databases
PaxDb	P22211.
PeptideAtlas	P22211.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL183C; YNL183C; YNL183C.
GeneID	855538.
KEGG	sce:YNL183C.
Organism-specific databases
CYGD	YNL183c.
SGD	S000005127. NPR1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000075309.
HOGENOM	HOG000093332.
KO	K00924.
OMA	RFVISKQ.
OrthoDB	EOG4C2MJV.
Enzyme and pathway databases
BioCyc	YEAST:G3O-33194-MONOMER.
BRENDA	2.7.11.1. 984.
Gene expression databases
Genevestigator	P22211.
GermOnline	YNL183C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979598.

Entry information

Entry name

NPR1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 123 of the entry and version 2 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

Yeast chromosome XIV

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents