QRI1/YDL103C Protein Information

Standard Name	Qri1p 1
Systematic Name	Ydl103cp
Alias	Uap1p
ORF Classification	Verified
Description	UDP-N-acetylglucosamine pyrophosphorylase; catalyzes the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), which is important in cell wall biosynthesis, protein N-glycosylation, and GPI anchor biosynthesis; protein abundance increases in response to DNA replication stress (2, 3)

Experimental Data
Molecules/cell	5480 4

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	477
Molecular Weight (Da)	53,476
Isoelectric Point (pI)	7.42

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Qri1p (InterPro)
Physical Interactions	There are 19 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000013793D \| P43123 MIPS: YDL103C NCBI: 1172803 \| 1199546 \| 1431144 \| 3273318 \| 6320100 \| 683705 \| NP_010180.1 GenBank/EMBL/DDBJ: DAA11757.1 \| AB011272 \| X79380 \| X95644 \| Z74151
External Classifications	EC: 2.7.7.23 [UDP-N-acetylglucosamine diphosphorylase]

Amino Acid Sequence (or in FASTA format)
1 MTDTKQLFIE AGQSQLFHNW ESLSRKDQEE LLSNLEQISS KRSPAKLLED 51 CQNAIKFSLA NSSKDTGVEI SPLPPTSYES LIGNSKKENE YWRLGLEAIG 101 KGEVAVILMA GGQGTRLGSS QPKGCYDIGL PSKKSLFQIQ AEKLIRLQDM 151 VKDKKVEIPW YIMTSGPTRA ATEAYFQEHN YFGLNKEQIT FFNQGTLPAF 201 DLTGKHFLMK DPVNLSQSPD GNGGLYRAIK ENKLNEDFDR RGIKHVYMYC 251 VDNVLSKIAD PVFIGFAIKH GFELATKAVR KRDAHESVGL IATKNEKPCV 301 IEYSEISNEL AEAKDKDGLL KLRAGNIVNH YYLVDLLKRD LDQWCENMPY 351 HIAKKKIPAY DSVTGKYTKP TEPNGIKLEQ FIFDVFDTVP LNKFGCLEVD 401 RCKEFSPLKN GPGSKNDNPE TSRLAYLKLG TSWLEDAGAI VKDGVLVEVS 451 SKLSYAGENL SQFKGKVFDR SGIVLEK*

Amino Acid Sequence (or in FASTA format)

       1  MTDTKQLFIE AGQSQLFHNW ESLSRKDQEE LLSNLEQISS KRSPAKLLED
      51  CQNAIKFSLA NSSKDTGVEI SPLPPTSYES LIGNSKKENE YWRLGLEAIG
     101  KGEVAVILMA GGQGTRLGSS QPKGCYDIGL PSKKSLFQIQ AEKLIRLQDM
     151  VKDKKVEIPW YIMTSGPTRA ATEAYFQEHN YFGLNKEQIT FFNQGTLPAF
     201  DLTGKHFLMK DPVNLSQSPD GNGGLYRAIK ENKLNEDFDR RGIKHVYMYC
     251  VDNVLSKIAD PVFIGFAIKH GFELATKAVR KRDAHESVGL IATKNEKPCV
     301  IEYSEISNEL AEAKDKDGLL KLRAGNIVNH YYLVDLLKRD LDQWCENMPY
     351  HIAKKKIPAY DSVTGKYTKP TEPNGIKLEQ FIFDVFDTVP LNKFGCLEVD
     401  RCKEFSPLKN GPGSKNDNPE TSRLAYLKLG TSWLEDAGAI VKDGVLVEVS
     451  SKLSYAGENL SQFKGKVFDR SGIVLEK*

external links for Qri1p

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

References cited on this page View Complete Literature Guide for Qri1p

1)	Simon M, et al. (1994) Sequence of the PHO2-POL3 (CDC2) region of chromosome IV of Saccharomyces cerevisiae. Yeast 10(12):1653-6
2)	Mio T, et al. (1998) The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism. J Biol Chem 273(23):14392-7
3)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
4)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41