HIS3/YOR202W Protein Information

Standard Name	His3p 1
Systematic Name	Yor202wp
Alias	His10p 2 , His8p 2
ORF Classification	Verified
Description	Imidazoleglycerol-phosphate dehydratase, catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p (1, 2, 3, 4, 5)
Name Description	HIStidine 1

Experimental Data
Molecules/cell	2100 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	220
Molecular Weight (Da)	23,833
Isoelectric Point (pI)	6.37

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 His3p (InterPro)
Physical Interactions	There are 11 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000053225 \| P06633 MIPS: YOR202W NCBI: 1197052 \| 1420477 \| 2190695 \| 2190699 \| 2506514 \| 3780 \| 45720014 \| 45720016 \| 45720018 \| 45720020 \| 45720022 \| 45720024 \| 45720026 \| 45720028 \| 45720030 \| 45720032 \| 45720034 \| 45720036 \| 45720038 \| 45720040 \| 45720042 \| 6324776 \| NP_014845.1 GenBank/EMBL/DDBJ: DAA10975.1 \| AJ585705 \| AJ585706 \| AJ585707 \| AJ585708 \| AJ585709 \| AJ585710 \| AJ585711 \| AJ585712 \| AJ585713 \| AJ585714 \| AJ585715 \| AJ585716 \| AJ585717 \| AJ585718 \| AJ585719 \| J01330 \| U89927 \| U89928 \| X03245 \| Z75110
External Classifications	EC: 4.2.1.19 [Imidazoleglycerol-phosphate dehydratase]

Amino Acid Sequence (or in FASTA format)
1 MTEQKALVKR ITNETKIQIA ISLKGGPLAI EHSIFPEKEA EAVAEQATQS 51 QVINVHTGIG FLDHMIHALA KHSGWSLIVE CIGDLHIDDH HTTEDCGIAL 101 GQAFKEALGA VRGVKRFGSG FAPLDEALSR AVVDLSNRPY AVVELGLQRE 151 KVGDLSCEMI PHFLESFAEA SRITLHVDCL RGKNDHHRSE SAFKALAVAI 201 REATSPNGTN DVPSTKGVLM *

Amino Acid Sequence (or in FASTA format)

       1  MTEQKALVKR ITNETKIQIA ISLKGGPLAI EHSIFPEKEA EAVAEQATQS
      51  QVINVHTGIG FLDHMIHALA KHSGWSLIVE CIGDLHIDDH HTTEDCGIAL
     101  GQAFKEALGA VRGVKRFGSG FAPLDEALSR AVVDLSNRPY AVVELGLQRE
     151  KVGDLSCEMI PHFLESFAEA SRITLHVDCL RGKNDHHRSE SAFKALAVAI
     201  REATSPNGTN DVPSTKGVLM *

external links for His3p

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

References cited on this page View Complete Literature Guide for His3p

1)	Struhl K and Davis RW (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9
2)	Fink GR (1964) GENE-ENZYME RELATIONS IN HISTIDINE BIOSYNTHESIS IN YEAST. Science 146(3643):525-7
3)	Hope IA and Struhl K (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88
4)	Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9
5)	Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41