NPR1/YNL183C Protein Information Help

Standard Name Npr1p 1
Systematic Name Ynl183cp
ORF Classification Verified
Description Protein kinase; stabilizes several plasma membrane amino acid transporters by antagonizing their ubiquitin-mediated degradation; phosphorylates Aly2p; negatively regulates Ldb19p-mediated endocytosis through phosphorylation of Ldb19p, which prevents its association with the plasma membrane; Npr1p activity is negatively regulated via phosphorylation by the TOR complex; NPR1 has a paralog, PRR2, that arose from the whole genome duplication (2, 3, 4, 5, 6)
Name Description Nitrogen Permease Reactivator 1
Experimental Data
Molecules/cell 284 7
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 790
Molecular Weight (Da) 85,989
Isoelectric Point (pI) 8.4

Click on image for expanded interactive view
pbrowse

Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Npr1p (InterPro)
Physical Interactions There are 51 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI00001303F4 | P22211
MIPS: YNL183C
NCBI: 1302168 | 1709340 | 4047 | 6324146 | NP_014216.1
GenBank/EMBL/DDBJ: DAA10369.1 | X56084 | Z71459
External Classifications EC: 2.7.11.1 [Non-specific serine/threonine protein kinase]
Amino Acid Sequence (or in FASTA format)
       1  MSSLTRLLQE KRKNETSNSS PRTSADTLTT TPESQSLDLH SRNKSSSHIG
      51  SVSNSSSSDR NRANVPVPGS VTTVTQIYSE EDSSSTAGSS LDDRNQFSSS
     101  FLNANFAHTA SFYGTSAQSR DRFGSLINDQ GTAGLSSHGG SFAAQNRITS
     151  RLSTTSHTSG RAIPSLSSSI PYSVPNSNKD NNSSNSNSSS LSSSWLETYA
     201  GGMPNNISAI DSNVISSPKV DSVEPRFVIS KQKLQKASMD SNNANATQSR
     251  SISRSGSFSS QLGNFFFSKN SKESSNSNSA GMSFSANSNG PSPNIKNPNV
     301  TNGSTPIPKP IRARQSSIYS ASRQPTGSYT DNFYGSPSSV HDHLPPSQSV
     351  PRSQHSSIGD LKRFFKKSSN SNLSSNSNNV IPNGSPLSSG IAVPSHSHSS
     401  SHFAAGNNSY STSYNGNGDT IYSHSHGGSG IPFSKRYIKT GADLGAGAGG
     451  SVKLAQRISD NKIFAVKEFR TKFENESKRD YVKKITSEYC IGTTLNHPNI
     501  IETIEIVYEN DRILQVMEYC EYDLFAIVMS NKMSYEEICC CFKQILTGVQ
     551  YLHSIGLAHR DLKLDNCVIN EKGIVKLIDF GAAVVFSYPF SKNLVEASGI
     601  VGSDPYLAPE VCIFAKYDPR PVDIWSSAII FACMILKKFP WKIPKLRDNS
     651  FKLFCSGRDC DSLSSLVTRT PDPPSYDESH STEKKKPESS SNNVSDPNNV
     701  NIGPQRLLHS LPEETQHIVG RMIDLAPACR GNIEEIMEDP WIRSIDMCHL
     751  VEDGLSFKVV RGEDHHHTQV DQSEAHIAGL EKKKKKQNNQ *         

external links for Npr1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Npr1p
1) Vandenbol M, et al.  (1987) Isolation of the NPR1 gene responsible for the reactivation of ammonia-sensitive amino-acid permeases in Saccharomyces cerevisiae. RNA analysis and gene dosage effects. Eur J Biochem 164(3):607-12
2) Schmidt A, et al.  (1998) The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease. EMBO J 17(23):6924-31
3) De Craene JO, et al.  (2001) The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease. J Biol Chem 276(47):43939-48
4) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
5) O'Donnell AF, et al.  (2010) {alpha}-Arrestins Aly1 and Aly2 Regulate Intracellular Trafficking in Response to Nutrient Signaling. Mol Biol Cell 21(20):3552-66
6) MacGurn JA, et al.  (2011) TORC1 regulates endocytosis via Npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor. Cell 147(5):1104-17
7) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41