Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000052

Gene Ontology annotation based on curation of immunofluorescence data

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:12886008

Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster.

NFU1 assembles approximately one [4Fe-4S] cluster per two monomers
Isoform I localizes to mitochondria; isoform II to cytosol and nucleus
Alternative splicing produces isoforms with distinct subcellular localizations

PMID:12915448

The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain.

NFU1 (HIRIP5) identified as cytosolic protein
Interacts with laforin through its C-terminal NifU-like domain

PMID:22190034

Global landscape of HIV-human protein complexes.

PMID:25416956

A proteome-scale map of the human interactome network.

PMID:26702583

Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly.

HSPA9 interacts with NFU1 as part of mitochondrial ISC biogenesis machinery
NFU1 is stabilized by HSPA9 interaction

PMID:27532772

Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins.

BOLA3 preferentially interacts with holo-NFU1
NFU1 and BOL proteins have distinct but overlapping functions in Fe-S protein maturation

PMID:27538573

Iron-sulfur cluster exchange reactions mediated by the human Nfu protein.

NFU1 binds [2Fe-2S] cluster as dimer with 2:1 protein to cluster ratio
Cluster can be transferred to apo ferredoxins at relatively fast rates
NFU1 implicated in MMDS1

PMID:28906594

Understanding the molecular basis for multiple mitochondrial dysfunctions syndrome 1 (MMDS1): impact of a disease-causing Gly189Arg substitution on NFU1.

G189R mutation alters protein structure and monomer-dimer equilibrium
Disease mutations impair ability to receive Fe-S clusters from donors

PMID:32296183

A reference map of the human binary protein interactome.

PMID:34800366

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

NFU1 confirmed as high-confidence mitochondrial protein

Reactome:R-HSA-6793591

LIAS synthesizes lipoyl-GCSH

NFU1 provides [4Fe-4S] cluster to LIAS in mitochondrial matrix
Required for lipoylation pathway

file:human/NFU1/NFU1-deep-research-falcon.md

Deep research report on NFU1