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P22211

- NPR1_YEAST

UniProt

P22211 - NPR1_YEAST

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Protein

Nitrogen permease reactivator protein

Gene

NPR1

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

Functioni

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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Dephosphorylation by SIT4 activates NPR1 kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei467 – 4671ATPPROSITE-ProRule annotation
Active sitei561 – 5611Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi444 – 4529ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  1. negative regulation of endocytosis Source: SGD
  2. protein phosphorylation Source: SGD
  3. regulation of nitrogen utilization Source: SGD
  4. regulation of sphingolipid biosynthetic process Source: SGD
  5. regulation of transmembrane transporter activity Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33194-MONOMER.
BRENDAi2.7.11.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen permease reactivator protein (EC:2.7.11.1)
Alternative name(s):
Serine/threonine-protein kinase NPR1
Gene namesi
Name:NPR1
Ordered Locus Names:YNL183C
ORF Names:N1631
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL183c.
SGDiS000005127. NPR1.

Subcellular locationi

Cytoplasm 1 Publication
Note: Appears to be more concentrated in punctate structures reminiscent of the Golgi or of an endosomal compartment.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. Golgi apparatus Source: SGD
  3. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471S → A: Abolishes autophosphorylation; when associated with A-257 and A-357. 1 Publication
Mutagenesisi257 – 2571S → A: Abolishes autophosphorylation; when associated with A-47 and A-357. 1 Publication
Mutagenesisi257 – 2571S → D: Abolishes autophosphorylation. 1 Publication
Mutagenesisi357 – 3571S → A: Abolishes autophosphorylation; when associated with A-47 and A-257. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790Nitrogen permease reactivator proteinPRO_0000086445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Phosphoserine; by autocatalysis1 Publication
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei90 – 901Phosphoserine1 Publication
Modified residuei100 – 1001Phosphoserine1 Publication
Modified residuei111 – 1111Phosphoserine1 Publication
Modified residuei116 – 1161Phosphoserine1 Publication
Modified residuei125 – 1251Phosphoserine3 Publications
Modified residuei137 – 1371Phosphoserine2 Publications
Modified residuei141 – 1411Phosphoserine2 Publications
Modified residuei257 – 2571Phosphoserine; by autocatalysis1 Publication
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei260 – 2601Phosphoserine1 Publication
Modified residuei288 – 2881Phosphoserine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei317 – 3171Phosphoserine1 Publication
Modified residuei320 – 3201Phosphoserine1 Publication
Modified residuei328 – 3281Phosphoserine1 Publication
Modified residuei334 – 3341Phosphotyrosine1 Publication
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei356 – 3561Phosphoserine1 Publication
Modified residuei357 – 3571Phosphoserine; by autocatalysis2 Publications
Modified residuei385 – 3851Phosphoserine1 Publication

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22211.
PaxDbiP22211.
PeptideAtlasiP22211.

Expressioni

Gene expression databases

GenevestigatoriP22211.

Interactioni

Subunit structurei

Interacts with TIP41.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GCN2P154422EBI-12207,EBI-330
SNF1P067822EBI-12207,EBI-17516
TOR1P351692EBI-12207,EBI-19374

Protein-protein interaction databases

BioGridi35649. 133 interactions.
DIPiDIP-4327N.
IntActiP22211. 48 interactions.
MINTiMINT-556937.
STRINGi4932.YNL183C.

Structurei

3D structure databases

ProteinModelPortaliP22211.
SMRiP22211. Positions 437-757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 742305Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 339339Ser-rich (may play a regulatory role)Add
BLAST
Compositional biasi51 – 588Poly-Ser
Compositional biasi782 – 7865Poly-Lys

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000075309.
HOGENOMiHOG000093332.
InParanoidiP22211.
OMAiITGEYCI.
OrthoDBiEOG7008J9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22211-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSLTRLLQE KRKNETSNSS PRTSADTLTT TPESQSLDLH SRNKSSSHIG
60 70 80 90 100
SVSNSSSSDR NRANVPVPGS VTTVTQIYSE EDSSSTAGSS LDDRNQFSSS
110 120 130 140 150
FLNANFAHTA SFYGTSAQSR DRFGSLINDQ GTAGLSSHGG SFAAQNRITS
160 170 180 190 200
RLSTTSHTSG RAIPSLSSSI PYSVPNSNKD NNSSNSNSSS LSSSWLETYA
210 220 230 240 250
GGMPNNISAI DSNVISSPKV DSVEPRFVIS KQKLQKASMD SNNANATQSR
260 270 280 290 300
SISRSGSFSS QLGNFFFSKN SKESSNSNSA GMSFSANSNG PSPNIKNPNV
310 320 330 340 350
TNGSTPIPKP IRARQSSIYS ASRQPTGSYT DNFYGSPSSV HDHLPPSQSV
360 370 380 390 400
PRSQHSSIGD LKRFFKKSSN SNLSSNSNNV IPNGSPLSSG IAVPSHSHSS
410 420 430 440 450
SHFAAGNNSY STSYNGNGDT IYSHSHGGSG IPFSKRYIKT GADLGAGAGG
460 470 480 490 500
SVKLAQRISD NKIFAVKEFR TKFENESKRD YVKKITSEYC IGTTLNHPNI
510 520 530 540 550
IETIEIVYEN DRILQVMEYC EYDLFAIVMS NKMSYEEICC CFKQILTGVQ
560 570 580 590 600
YLHSIGLAHR DLKLDNCVIN EKGIVKLIDF GAAVVFSYPF SKNLVEASGI
610 620 630 640 650
VGSDPYLAPE VCIFAKYDPR PVDIWSSAII FACMILKKFP WKIPKLRDNS
660 670 680 690 700
FKLFCSGRDC DSLSSLVTRT PDPPSYDESH STEKKKPESS SNNVSDPNNV
710 720 730 740 750
NIGPQRLLHS LPEETQHIVG RMIDLAPACR GNIEEIMEDP WIRSIDMCHL
760 770 780 790
VEDGLSFKVV RGEDHHHTQV DQSEAHIAGL EKKKKKQNNQ
Length:790
Mass (Da):85,990
Last modified:October 1, 1996 - v2
Checksum:i0ECFA33376740733
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541T → A in CAA39564. (PubMed:2125693)Curated
Sequence conflicti277 – 2771S → P in CAA39564. (PubMed:2125693)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56084 Genomic DNA. Translation: CAA39564.1.
Z71459 Genomic DNA. Translation: CAA96076.1.
BK006947 Genomic DNA. Translation: DAA10369.1.
PIRiS63138.
RefSeqiNP_014216.1. NM_001183021.1.

Genome annotation databases

EnsemblFungiiYNL183C; YNL183C; YNL183C.
GeneIDi855538.
KEGGisce:YNL183C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56084 Genomic DNA. Translation: CAA39564.1 .
Z71459 Genomic DNA. Translation: CAA96076.1 .
BK006947 Genomic DNA. Translation: DAA10369.1 .
PIRi S63138.
RefSeqi NP_014216.1. NM_001183021.1.

3D structure databases

ProteinModelPortali P22211.
SMRi P22211. Positions 437-757.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35649. 133 interactions.
DIPi DIP-4327N.
IntActi P22211. 48 interactions.
MINTi MINT-556937.
STRINGi 4932.YNL183C.

Proteomic databases

MaxQBi P22211.
PaxDbi P22211.
PeptideAtlasi P22211.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL183C ; YNL183C ; YNL183C .
GeneIDi 855538.
KEGGi sce:YNL183C.

Organism-specific databases

CYGDi YNL183c.
SGDi S000005127. NPR1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000075309.
HOGENOMi HOG000093332.
InParanoidi P22211.
OMAi ITGEYCI.
OrthoDBi EOG7008J9.

Enzyme and pathway databases

BioCyci YEAST:G3O-33194-MONOMER.
BRENDAi 2.7.11.1. 984.

Miscellaneous databases

NextBioi 979598.

Gene expression databases

Genevestigatori P22211.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiNPR1_YEAST
AccessioniPrimary (citable) accession number: P22211
Secondary accession number(s): D6W103
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 284 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3