P-POD: Princeton Protein Orthology Database: GO3/Nens1509

This family has 17 members: 3 Arabidopsis thaliana, 1 Caenorhabditis elegans, 3 Danio rerio, 1 Dictyostelium discoideum, 1 Drosophila melanogaster, 1 Escherichia coli, 1 Homo sapiens, 2 Mus musculus, 1 Rattus norvegicus, 2 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

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GO3/Nens1509
17 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_192317.1 · TAIR:locus:2136612 (T24H24.11 · AT4G04080 · ATISU3 · T24H24_11 · ISU3)ISCU-LIKE 3⌘
A. thalianaNCBI:NP_186751.1 · TAIR:locus:2102122 (T4P13_30 · T4P13.30 · ATISU2 · ISU2 · AT3G01020)ISCU-LIKE 2⌘
A. thalianaNCBI:NP_193953.1 · TAIR:locus:2132090 (ATISU1 · AT4G22220 · ISU1 · T10I14.50 · T10I14_50)⌘
C. elegansWB:WBGene00012885 (Y45F10D.4) · UniProtKB:O45948⌘
D. rerioZFIN:ZDB-GENE-050417-332 (zgc:110331) · UniProtKB:Q568F2⌘
D. rerioENSEMBL:ENSDARG00000035596 · UniProtKB:Q6DC82
D. rerioUniProtKB:Q6DC82 · ENSEMBL:ENSDARG00000067946
D. discoideumdictyBase:DDB_G0283003 · UniProtKB:Q54RP2
D. melanogasterFB:FBgn0037637 (CG9836) · UniProtKB:Q9VHK6⌘
E. coliUniProtKB:P0ACD4 · ECOLI:G7324-MONOMER (iscU · IscU · yfhN · b2529 · ECK2526 · nifU)scaffold protein involved in iron-sulfur cluster assembly⌘
H. sapiensENSEMBL:ENSG00000136003 · UniProtKB:Q9H1K1 (Q9H1K1 · NIFUN · ISCU_HUMAN · IPI00022240 · IPI00164885 · ISCU)Iron-sulfur cluster assembly enzyme ISCU, mitochondrial⌘
M. musculusNCBI:XP_001473902 · MGI:MGI:3644508
M. musculusUniProtKB:Q9D7P6 · MGI:MGI:1913633 (Nifun · Iscu)IscU iron-sulfur cluster scaffold homolog (E. coli)⌘
R. norvegicusNCBI:XP_213811 · RGD:1309562 (Iscu)iron-sulfur cluster scaffold homolog (E. coli)⌘
S. cerevisiaeUniProtKB:Q03020 · SGD:S000006056 (NUA1 · ISU1 · YPL135W)Conserved protein of the mitochondrial matrix, performs a scaffolding function during assembly of iron-sulfur clusters, interacts physically and functionally with yeast frataxin (Yfh1p)⌘
S. cerevisiaeUniProtKB:Q12056 · SGD:S000005752 (YOR226C · ISU2 · NUA2)Conserved protein of the mitochondrial matrix, required for synthesis of mitochondrial and cytosolic iron-sulfur proteins, performs a scaffolding function in mitochondria during Fe/S cluster assembly⌘
S. pombeUniProtKB:Q9UTC6 · GeneDB_Spombe:SPAC227.13c (isu1 · SPAC227.13c)mitochondrial iron-sulfur cluster assembly scaffold protein Isu1⌘
ProteinPublicationCurator Notes
UniProtKB:Q03020 · SGD:S000006056PMID:15792798 Léon S, et al. Mitochondrial localization of Arabidopsis thaliana Isu Fe-S scaffold proteins. FEBS Lett. 2005 Mar 28;579(9):1930-4.The A. thaliana protein AT4G22220.1 complements a homologous mutation in S. cerevisiae. Arabidopsis Isu1 complements a yeast isu1 mutant in an nfu1 background.
UniProtKB:Q12056 · SGD:S000005752PMID:15143178 Gerber J, et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004 Jun;24(11):4848-57.The E. coli protein iscU complements a homologous mutation in S. cerevisiae. E. coli iscU partially complements a yeast isu1 isu2 double mutant.
UniProtKB:Q03020 · SGD:S000006056PMID:15143178 Gerber J, et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004 Jun;24(11):4848-57.The E. coli protein iscU complements a homologous mutation in S. cerevisiae. E. coli iscU partially complements a yeast isu1 isu2 double mutant.
UniProtKB:Q03020 · SGD:S000006056PMID:15792798 Léon S, et al. Mitochondrial localization of Arabidopsis thaliana Isu Fe-S scaffold proteins. FEBS Lett. 2005 Mar 28;579(9):1930-4.The A. thaliana protein AT3G01020.1 complements a homologous mutation in S. cerevisiae. Arabidopsis Isu2 complements a yeast isu1 mutant in an nfu1 background.
UniProtKB:Q03020 · SGD:S000006056PMID:15792798 Léon S, et al. Mitochondrial localization of Arabidopsis thaliana Isu Fe-S scaffold proteins. FEBS Lett. 2005 Mar 28;579(9):1930-4.The A. thaliana protein AT4G04080.1 complements a homologous mutation in S. cerevisiae. Arabidopsis Isu3 complements a yeast isu1 mutant in an nfu1 background.
UniProtKB:Q12056 · SGD:S000005752PMID:15143178 Gerber J, et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004 Jun;24(11):4848-57.The H. sapiens protein Q9H1K1 complements a homologous mutation in S. cerevisiae. When the human mitochondrial targeting sequence is replaced with one from yeast, hIsu2 complements a yeast isu1 isu2 double mutant.
UniProtKB:Q03020 · SGD:S000006056PMID:15143178 Gerber J, et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004 Jun;24(11):4848-57.The H. sapiens protein Q9H1K1 complements a homologous mutation in S. cerevisiae. When the human mitochondrial targeting sequence is replaced with one from yeast, hIsu2 complements a yeast isu1 isu2 double mutant.
UniProtKB:Q12056 · SGD:S000005752PMID:15143178 Gerber J, et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004 Jun;24(11):4848-57.The H. sapiens protein Q9H1K1 complements a homologous mutation in S. cerevisiae. When tagged with a mitochondrial targeting sequence, hIsu1 partially complements a yeast isu1 isu2 mutant.
UniProtKB:Q03020 · SGD:S000006056PMID:15143178 Gerber J, et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004 Jun;24(11):4848-57.The H. sapiens protein Q9H1K1 complements a homologous mutation in S. cerevisiae. When tagged with a mitochondrial targeting sequence, hIsu1 partially complements a yeast isu1 isu2 mutant.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
OMIM (1)
ENSEMBL:ENSG00000136003 · UniProtKB:Q9H1K1#255125 MYOPATHY WITH EXERCISE INTOLERANCE, SWEDISH TYPE;;MYOPATHY WITH DEFICIENCY OF SUCCINATE DEHYDROGENASE AND ACONITASE;;MYOGLOBINURIA DUE TO ABNORMAL GLYCOLYSIS;;MYOPATHY WITH LACTIC ACIDOSIS, HEREDITARY; HML
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