FOG02499
EOG8WH72M
sce:MCH5
Genes: 85
Protein descriptionriboflavin transporter
SGD DescriptionPlasma membrane riboflavin transporter; facilitates the uptake of vitamin B2; required for FAD-dependent processes; sequence similarity to mammalian monocarboxylate permeases, however mutants are not deficient in monocarboxylate transport
AspGD DescriptionOrtholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Ortholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process|Ortholog(s) have riboflavin transporter activity, role in riboflavin transport and plasma membrane localization|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization
References
Bruschi GC, et al. (2001 Apr). Sensitivity to camptothecin in Aspergillus nidulans identifies a novel gene, scaA+, related to the cellular DNA damage response.
Makuc J, et al. (2001 Sep 15). The putative monocarboxylate permeases of the yeast Saccharomyces cerevisiae do not transport monocarboxylic acids across the plasma membrane.
Semighini CP, et al. (2004 Oct). Multi-copy suppression of an Aspergillus nidulans mutant sensitive to camptothecin by a putative monocarboxylate transporter.
Reihl P, et al. (2005 Dec 2). The monocarboxylate transporter homolog Mch5p catalyzes riboflavin (vitamin B2) uptake in Saccharomyces cerevisiae.
Kim H, et al. (2006 Jul 25). A global topology map of the Saccharomyces cerevisiae membrane proteome.
Colabardini AC, et al. (2014 Apr 1). Functional characterization of a xylose transporter in Aspergillus nidulans.
FOG02500
EOG8WH72M
sce:MCH4
Genes: 1
Protein descriptionuncharacterized
SGD DescriptionProtein with similarity to mammalian monocarboxylate permeases; monocarboxylate permeases are involved in transport of monocarboxylic acids across the plasma membrane but mutant is not deficient in monocarboxylate transport
References
Makuc J, et al. (2001 Sep 15). The putative monocarboxylate permeases of the yeast Saccharomyces cerevisiae do not transport monocarboxylic acids across the plasma membrane.
Kim H, et al. (2006 Jul 25). A global topology map of the Saccharomyces cerevisiae membrane proteome.
Starita LM, et al. (2012 Jan). Sites of ubiquitin attachment in Saccharomyces cerevisiae.
FOG02501
EOG8WH72M
sce:absent
Genes: 16
AspGD DescriptionHas domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Ortholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process|Ortholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process
References
Bruschi GC, et al. (2001 Apr). Sensitivity to camptothecin in Aspergillus nidulans identifies a novel gene, scaA+, related to the cellular DNA damage response.
Semighini CP, et al. (2004 Oct). Multi-copy suppression of an Aspergillus nidulans mutant sensitive to camptothecin by a putative monocarboxylate transporter.
FOG02502
EOG8WH72M
sce:absent
Genes: 16
AspGD DescriptionHas domain(s) with predicted role in transmembrane transport and integral component of membrane localization
FOG02503
EOG8WH72M
sce:absent
Genes: 8
AspGD DescriptionHas domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization
FOG02504
EOG8WH72M
sce:absent
Genes: 8
AspGD DescriptionHas domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization
FOG02505
EOG8WH72M
sce:absent
Genes: 3
AspGD DescriptionOrtholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process
References
Bruschi GC, et al. (2001 Apr). Sensitivity to camptothecin in Aspergillus nidulans identifies a novel gene, scaA+, related to the cellular DNA damage response.
Semighini CP, et al. (2004 Oct). Multi-copy suppression of an Aspergillus nidulans mutant sensitive to camptothecin by a putative monocarboxylate transporter.
FOG02506
EOG8WH72M
sce:absent
Genes: 3
AspGD DescriptionPredicted transmembrane transport, encoded in a secondary metabolite gene cluster involved in production of pyranonigirin E
References
Bruschi GC, et al. (2001 Apr). Sensitivity to camptothecin in Aspergillus nidulans identifies a novel gene, scaA+, related to the cellular DNA damage response.
Semighini CP, et al. (2004 Oct). Multi-copy suppression of an Aspergillus nidulans mutant sensitive to camptothecin by a putative monocarboxylate transporter.
FOG02507
EOG8WH72M
sce:absent
Genes: 3
FOG02508
EOG8WH72M
sce:absent
Genes: 2
AspGD DescriptionHas domain(s) with predicted role in transmembrane transport and integral component of membrane localization
FOG02509
EOG8WH72M
sce:absent
Genes: 11
AspGD DescriptionHas domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Protein of unknown function|Ortholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process|Ortholog(s) have role in cellular response to drug, secondary metabolite biosynthetic process|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization|Has domain(s) with predicted role in transmembrane transport and integral component of membrane localization
References
Bruschi GC, et al. (2001 Apr). Sensitivity to camptothecin in Aspergillus nidulans identifies a novel gene, scaA+, related to the cellular DNA damage response.
Semighini CP, et al. (2004 Oct). Multi-copy suppression of an Aspergillus nidulans mutant sensitive to camptothecin by a putative monocarboxylate transporter.