Disease relevance of HIP1

• This protein is highly homologous with the AroP (general aromatic transport) system of E. coli (59.6% identity) and to a lesser extent with the yeast permeases CAN1 (arginine), PUT4 (proline), and HIP1 (histidine) of Saccharomyces cerevisiae [1].

High impact information on HIP1

• Shr3p was required for the packaging of Gap1p and Hip1p but was not itself incorporated into transport vesicles [2].
• Gap1p, and the histidine permease, Hip1p [2].
• A human cDNA library in lambda-yes plasmid was used to transform a strain of Saccharomyces cerevisiae with defects in histidine biosynthesis (his4-401) and histidine permease (hip1-614) and with the general amino acid permease (GAP) repressed by excess ammonium [3].
• Overexpression of the Hip1-related protein Sla2 delayed the formation of extended plasma membrane invaginations in sjl2ts cells, indicating that Sla2 may become limiting or misregulated in cells with impaired PI phosphatase activity [4].
• Both Scd5p and yeast clathrin physically associate with Sla2p, a homologue of the mammalian huntingtin interacting protein HIP1 and the related HIP1R [5].

Biological context of HIP1

• We sequenced a 2.4-kb subfragment of this BamHI-Sau3A fragment containing the HIP1 gene and identified a 1596-bp open reading frame (ORF) [6].
• The HIP1 gene maps to the right arm of chromosome VII, approx. 11 cM distal to the ADE3 gene [6].
• Analysis of the deduced amino acid sequences revealed that one (HIP1) of the two HCpro interactors is a novel RING finger protein [7].

Associations of HIP1 with chemical compounds

• The histidine-specific permease gene (HIP1) of Saccharomyces cerevisiae has been mapped, cloned, and sequenced [6].
• Our results suggest that the TAT1-encoded protein, previously characterized as the high-affinity tyrosine permease, also acts as the low affinity histidine permease [8].
• Involvement of histidine permease (Hip1p) in manganese transport in Saccharomyces cerevisiae [9].

Other interactions of HIP1

• In the aligned sequences HIP1 and CAN1, the postulated membrane-spanning alpha-helices often start at corresponding sites, even though the overall sequence similarity of the two proteins is only 30% [10].
• We report that mutations in the HIP1 and SHM1 genes exhibit synthetic lethality with ade3 deletions [11].
• This defect in histidine uptake, exhibited by the sln2 mutant in the absence but not in the presence of Ubr1p, was traced to the gene HIP1, which encodes the histidine transporter [12].
• Sequencing of the inserts revealed the presence of the HIP1 gene and also the presence of the TAT1 gene [8].

References