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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: 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)DescriptionActionsGraphical viewLength
Binding sitei467ATPPROSITE-ProRule annotation1
Active sitei561Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi444 – 452ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • intracellular signal transduction Source: GO_Central
  • negative regulation of endocytosis Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of nitrogen utilization Source: SGD
  • regulation of sphingolipid biosynthetic process Source: SGD
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL183C.
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

  • cytoplasm Source: SGD
  • Golgi apparatus Source: SGD
  • nucleus Source: GO_Central
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47S → A: Abolishes autophosphorylation; when associated with A-257 and A-357. 1 Publication1
Mutagenesisi257S → A: Abolishes autophosphorylation; when associated with A-47 and A-357. 1 Publication1
Mutagenesisi257S → D: Abolishes autophosphorylation. 1 Publication1
Mutagenesisi357S → A: Abolishes autophosphorylation; when associated with A-47 and A-257. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000864451 – 790Nitrogen permease reactivator proteinAdd BLAST790

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei47Phosphoserine; by autocatalysis1 Publication1
Modified residuei85Phosphoserine1 Publication1
Modified residuei90Phosphoserine1 Publication1
Modified residuei100Phosphoserine1 Publication1
Modified residuei111Phosphoserine1 Publication1
Modified residuei116Phosphoserine1 Publication1
Modified residuei125PhosphoserineCombined sources1 Publication1
Modified residuei137PhosphoserineCombined sources1 Publication1
Modified residuei141PhosphoserineCombined sources1 Publication1
Modified residuei257Phosphoserine; by autocatalysis1 Publication1
Modified residuei259Phosphoserine1 Publication1
Modified residuei260Phosphoserine1 Publication1
Modified residuei288Phosphoserine1 Publication1
Modified residuei292Phosphoserine1 Publication1
Modified residuei317Phosphoserine1 Publication1
Modified residuei320Phosphoserine1 Publication1
Modified residuei328Phosphoserine1 Publication1
Modified residuei334PhosphotyrosineCombined sources1
Modified residuei336Phosphoserine1 Publication1
Modified residuei353Phosphoserine1 Publication1
Modified residuei356Phosphoserine1 Publication1
Modified residuei357Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei385Phosphoserine1 Publication1

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22211.
PRIDEiP22211.

PTM databases

iPTMnetiP22211.

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. 136 interactors.
DIPiDIP-4327N.
IntActiP22211. 49 interactors.
MINTiMINT-556937.

Structurei

3D structure databases

ProteinModelPortaliP22211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini438 – 742Protein kinasePROSITE-ProRule annotationAdd BLAST305

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 339Ser-rich (may play a regulatory role)Add BLAST339
Compositional biasi51 – 58Poly-Ser8
Compositional biasi782 – 786Poly-Lys5

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

GeneTreeiENSGT00550000075309.
HOGENOMiHOG000093332.
InParanoidiP22211.
OMAiITGEYCI.
OrthoDBiEOG092C0ZCR.

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]
SMARTiSM00220. S_TKc. 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)DescriptionActionsGraphical viewLength
Sequence conflicti154T → A in CAA39564 (PubMed:2125693).Curated1
Sequence conflicti277S → P in CAA39564 (PubMed:2125693).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP22211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35649. 136 interactors.
DIPiDIP-4327N.
IntActiP22211. 49 interactors.
MINTiMINT-556937.

PTM databases

iPTMnetiP22211.

Proteomic databases

MaxQBiP22211.
PRIDEiP22211.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YNL183C.
SGDiS000005127. NPR1.

Phylogenomic databases

GeneTreeiENSGT00550000075309.
HOGENOMiHOG000093332.
InParanoidiP22211.
OMAiITGEYCI.
OrthoDBiEOG092C0ZCR.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP22211.

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]
SMARTiSM00220. S_TKc. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 157 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

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.