Iscu
entrez
66383
canonical
uniprot
Q9D7P6
canonical
ensembl
ENSMUSG00000025825
resolver
ensp
ENSMUSP00000026937
resolver
ensp
ENSMUSP00000107930
resolver
ensp
ENSMUSP00000107931
resolver
enst
ENSMUST00000026937
resolver
enst
ENSMUST00000112311
resolver
enst
ENSMUST00000112312
resolver
genesymbol
Iscu
resolver
genesymbol_syn
Nifun
resolver
uniprot
D3Z7W0
resolver
uniprot
Q4VBC7
resolver
uniprot
Q8K344
resolver
uniprot_entry
D3Z7W0_MOUSE
resolver
uniprot_entry
ISCU_MOUSE
resolver
uniprot_sec
Q4VBC7
resolver
uniprot_sec
Q8K344
resolver
amino_acid_sequence
MAAATGAGRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQESKKEEPEKQ
uniprot
proteins
function
FUNCTION: Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5. Exists as two slow interchanging conformational states, a structured (S) and disordered (D) form. May modulate NFS1 desulfurase activity in a zinc-dependent manner. Modulates the interaction between FXN and the cysteine desulfurase complex. {ECO:0000250|UniProtKB:Q9H1K1}.
uniprot
proteins
mass_dalton
18098
uniprot
proteins
mutagenesis
MUTAGEN 70; /note="C->S: Does not affect core iron sulfur assembly complex formation. Abolishes sulhydratation."; /evidence="ECO:0000269|PubMed:25597503"; MUTAGEN 139; /note="C->S: Does not affect core iron sulfur assembly complex formation. Abolishes sulhydratation."; /evidence="ECO:0000269|PubMed:25597503
uniprot
proteins
post_translational_modification
PTM: Cysteine persulfide is reduced by thiol-containing molecules such as glutathione and L-cysteine. {ECO:0000269|PubMed:25597503}.; PTM: Phosphorylation at Ser-15 is required for ISCU protein stabilization in the cytosol, whereas dephosphorylation of Ser-15, due to the inhibition of mTORC1 (mammalian target of rapamycin complex 1) complex, leads to degradation of the precursor form and ultimately to a decrease in the mitochondrial mature form. {ECO:0000250|UniProtKB:Q9H1K1}.
uniprot
proteins
protein_family
NifU family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21298097
uniprot
proteins
pubmed
25597503
uniprot
proteins
sequence_length
168
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H1K1}.
uniprot
proteins