ISCU_HUMAN
ID ISCU_HUMAN Reviewed; 167 AA.
AC Q9H1K1; Q6P713; Q99617; Q9H1K2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Iron-sulfur cluster assembly enzyme ISCU, mitochondrial;
DE AltName: Full=NifU-like N-terminal domain-containing protein;
DE AltName: Full=NifU-like protein;
DE Flags: Precursor;
GN Name=ISCU; Synonyms=NIFUN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH NFS1, TISSUE SPECIFICITY, AND VARIANT VAL-12.
RX PubMed=11060020; DOI=10.1093/emboj/19.21.5692;
RA Tong W.-H., Rouault T.;
RT "Distinct iron-sulfur cluster assembly complexes exist in the cytosol and
RT mitochondria of human cells.";
RL EMBO J. 19:5692-5700(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-12.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-167, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=8875867; DOI=10.1007/bf02337525;
RA Hwang D.M., Dempsey A., Tan K.-T., Liew C.-C.;
RT "A modular domain of NifU, a nitrogen fixation cluster protein, is highly
RT conserved in evolution.";
RL J. Mol. Evol. 43:536-540(1996).
RN [5]
RP INVOLVEMENT IN MEIS.
RX PubMed=18304497; DOI=10.1016/j.ajhg.2007.12.012;
RA Mochel F., Knight M.A., Tong W.-H., Hernandez D., Ayyad K., Taivassalo T.,
RA Andersen P.M., Singleton A., Rouault T.A., Fischbeck K.H., Haller R.G.;
RT "Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes
RT myopathy with exercise intolerance.";
RL Am. J. Hum. Genet. 82:652-660(2008).
RN [6]
RP INTERACTION WITH HSCB.
RX PubMed=20668094; DOI=10.1093/hmg/ddq301;
RA Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A.;
RT "Characterization of the human HSC20, an unusual DnaJ type III protein,
RT involved in iron-sulfur cluster biogenesis.";
RL Hum. Mol. Genet. 19:3816-3834(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP INTERACTION WITH GLRX5.
RX PubMed=26100117; DOI=10.1002/jcb.25267;
RA Liu G., Wang Y., Anderson G.J., Camaschella C., Chang Y., Nie G.;
RT "Functional analysis of GLRX5 mutants reveals distinct functionalities of
RT GLRX5 protein.";
RL J. Cell. Biochem. 117:207-217(2016).
RN [10]
RP INTERACTION WITH HSPA9, AND SUBCELLULAR LOCATION.
RX PubMed=26702583; DOI=10.1016/j.mito.2015.12.005;
RA Shan Y., Cortopassi G.;
RT "Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-
RT sulfur cluster assembly.";
RL Mitochondrion 26:94-103(2016).
RN [11]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH HSC20.
RX PubMed=29309586; DOI=10.1093/hmg/ddy004;
RA Kim K.S., Maio N., Singh A., Rouault T.A.;
RT "Cytosolic HSC20 integrates de novo iron-sulfur cluster biogenesis with the
RT CIAO1-mediated transfer to recipients.";
RL Hum. Mol. Genet. 27:837-852(2018).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur
CC (Fe-S) clusters within mitochondria, which is required for maturation
CC of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins
CC (PubMed:11060020). First, a [2Fe-2S] cluster is transiently assembled
CC on the scaffold protein ISCU. In a second step, the cluster is released
CC from ISCU, transferred to a glutaredoxin GLRX5, followed by the
CC formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S]
CC clusters and their target-specific insertion into the recipient
CC apoproteins. Cluster assembly on ISCU depends on the function of the
CC cysteine desulfurase complex NFS1-LYRM4/ISD11, which serves as the
CC sulfur donor for cluster synthesis, the iron-binding protein frataxin
CC as the putative iron donor, and the electron transfer chain comprised
CC of ferredoxin reductase and ferredoxin, which receive their electrons
CC from NADH (By similarity). {ECO:0000250|UniProtKB:Q03020,
CC ECO:0000269|PubMed:11060020}.
CC -!- FUNCTION: [Isoform 2]: Functions as a cytoplasmic scaffold protein for
CC the de novo synthesis of iron-sulfur clusters in the cytoplasm.
CC {ECO:0000269|PubMed:29309586}.
CC -!- SUBUNIT: Binds NFS1 (PubMed:11060020). Interacts with HSCB
CC (PubMed:20668094). Interacts with GLRX5 (PubMed:26100117). Interacts
CC with HSPA9 (PubMed:26702583). Interacts with HSC20 (PubMed:29309586).
CC {ECO:0000269|PubMed:11060020, ECO:0000269|PubMed:20668094,
CC ECO:0000269|PubMed:26100117, ECO:0000269|PubMed:26702583,
CC ECO:0000269|PubMed:29309586}.
CC -!- INTERACTION:
CC Q9H1K1; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-1047335, EBI-741181;
CC Q9H1K1; Q8N9N5: BANP; NbExp=3; IntAct=EBI-1047335, EBI-744695;
CC Q9H1K1; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-1047335, EBI-11524851;
CC Q9H1K1; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-1047335, EBI-2548868;
CC Q9H1K1; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-1047335, EBI-10175124;
CC Q9H1K1; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1047335, EBI-618309;
CC Q9H1K1; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1047335, EBI-5916454;
CC Q9H1K1; P00492: HPRT1; NbExp=4; IntAct=EBI-1047335, EBI-748210;
CC Q9H1K1; Q13422: IKZF1; NbExp=3; IntAct=EBI-1047335, EBI-745305;
CC Q9H1K1; O76011: KRT34; NbExp=3; IntAct=EBI-1047335, EBI-1047093;
CC Q9H1K1; Q6A162: KRT40; NbExp=3; IntAct=EBI-1047335, EBI-10171697;
CC Q9H1K1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1047335, EBI-739832;
CC Q9H1K1; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1047335, EBI-10172526;
CC Q9H1K1; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-1047335, EBI-10172876;
CC Q9H1K1; P37198: NUP62; NbExp=6; IntAct=EBI-1047335, EBI-347978;
CC Q9H1K1; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1047335, EBI-79165;
CC Q9H1K1; P21912: SDHB; NbExp=7; IntAct=EBI-1047335, EBI-1056481;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:11060020, ECO:0000269|PubMed:26702583}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus
CC {ECO:0000269|PubMed:11060020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ISCU2;
CC IsoId=Q9H1K1-1; Sequence=Displayed;
CC Name=2; Synonyms=ISCU1;
CC IsoId=Q9H1K1-2; Sequence=VSP_013492;
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, skeletal muscle, brain,
CC pancreas, kidney, lung and placenta. {ECO:0000269|PubMed:11060020,
CC ECO:0000269|PubMed:8875867}.
CC -!- DISEASE: Myopathy with exercise intolerance Swedish type (MEIS)
CC [MIM:255125]: Autosomal recessive metabolic disease characterized by
CC lifelong severe exercise intolerance, in which minor exertion causes
CC fatigue of active muscles, shortness of breath, and cardiac
CC palpitations in association with lactic acidosis. The biochemical
CC phenotype is characterized by a deficiency in mitochondrial iron-sulfur
CC proteins and impaired muscle oxidative metabolism.
CC {ECO:0000269|PubMed:18304497}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; AY009127; AAG37427.1; -; mRNA.
DR EMBL; AY009128; AAG37428.1; -; mRNA.
DR EMBL; AC008119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011906; AAH11906.1; -; mRNA.
DR EMBL; BC061903; AAH61903.1; -; mRNA.
DR EMBL; U47101; AAC50885.1; -; mRNA.
DR CCDS; CCDS44966.1; -. [Q9H1K1-1]
DR CCDS; CCDS9118.1; -. [Q9H1K1-2]
DR RefSeq; NP_001306971.1; NM_001320042.1.
DR RefSeq; NP_055116.1; NM_014301.4. [Q9H1K1-2]
DR RefSeq; NP_998760.1; NM_213595.3. [Q9H1K1-1]
DR PDB; 5KZ5; EM; 14.30 A; a/b/c/d/e/f/g/h/i/j/k/l=50-167.
DR PDB; 5WKP; X-ray; 3.15 A; D/H=38-167.
DR PDB; 5WLW; X-ray; 3.32 A; D/H=38-167.
DR PDB; 6NZU; EM; 3.20 A; D/H=34-157.
DR PDB; 6UXE; X-ray; 1.57 A; D=35-167.
DR PDB; 6W1D; X-ray; 1.79 A; D=35-167.
DR PDB; 6WI2; X-ray; 1.95 A; D=35-167.
DR PDB; 6WIH; X-ray; 1.90 A; D=35-167.
DR PDB; 7RTK; X-ray; 2.50 A; D=35-167.
DR PDBsum; 5KZ5; -.
DR PDBsum; 5WKP; -.
DR PDBsum; 5WLW; -.
DR PDBsum; 6NZU; -.
DR PDBsum; 6UXE; -.
DR PDBsum; 6W1D; -.
DR PDBsum; 6WI2; -.
DR PDBsum; 6WIH; -.
DR PDBsum; 7RTK; -.
DR AlphaFoldDB; Q9H1K1; -.
DR BMRB; Q9H1K1; -.
DR SASBDB; Q9H1K1; -.
DR SMR; Q9H1K1; -.
DR BioGRID; 117038; 44.
DR ComplexPortal; CPX-5641; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR DIP; DIP-39616N; -.
DR IntAct; Q9H1K1; 32.
DR MINT; Q9H1K1; -.
DR STRING; 9606.ENSP00000310623; -.
DR iPTMnet; Q9H1K1; -.
DR MetOSite; Q9H1K1; -.
DR PhosphoSitePlus; Q9H1K1; -.
DR BioMuta; ISCU; -.
DR DMDM; 313104118; -.
DR EPD; Q9H1K1; -.
DR jPOST; Q9H1K1; -.
DR MassIVE; Q9H1K1; -.
DR MaxQB; Q9H1K1; -.
DR PaxDb; Q9H1K1; -.
DR PeptideAtlas; Q9H1K1; -.
DR PRIDE; Q9H1K1; -.
DR ProteomicsDB; 80422; -. [Q9H1K1-1]
DR ProteomicsDB; 80423; -. [Q9H1K1-2]
DR TopDownProteomics; Q9H1K1-1; -. [Q9H1K1-1]
DR Antibodypedia; 30765; 272 antibodies from 28 providers.
DR DNASU; 23479; -.
DR Ensembl; ENST00000311893.14; ENSP00000310623.9; ENSG00000136003.16. [Q9H1K1-1]
DR Ensembl; ENST00000392807.8; ENSP00000376554.4; ENSG00000136003.16. [Q9H1K1-2]
DR GeneID; 23479; -.
DR KEGG; hsa:23479; -.
DR MANE-Select; ENST00000311893.14; ENSP00000310623.9; NM_213595.4; NP_998760.1.
DR UCSC; uc001tnc.5; human. [Q9H1K1-1]
DR CTD; 23479; -.
DR DisGeNET; 23479; -.
DR GeneCards; ISCU; -.
DR HGNC; HGNC:29882; ISCU.
DR HPA; ENSG00000136003; Low tissue specificity.
DR MalaCards; ISCU; -.
DR MIM; 255125; phenotype.
DR MIM; 611911; gene.
DR neXtProt; NX_Q9H1K1; -.
DR OpenTargets; ENSG00000136003; -.
DR Orphanet; 43115; Hereditary myopathy with lactic acidosis due to ISCU deficiency.
DR PharmGKB; PA162392328; -.
DR VEuPathDB; HostDB:ENSG00000136003; -.
DR eggNOG; KOG3361; Eukaryota.
DR GeneTree; ENSGT00390000015813; -.
DR HOGENOM; CLU_079283_1_2_1; -.
DR InParanoid; Q9H1K1; -.
DR OMA; YKNPRNY; -.
DR PhylomeDB; Q9H1K1; -.
DR TreeFam; TF105422; -.
DR PathwayCommons; Q9H1K1; -.
DR Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis. [Q9H1K1-1]
DR SignaLink; Q9H1K1; -.
DR SIGNOR; Q9H1K1; -.
DR BioGRID-ORCS; 23479; 755 hits in 1052 CRISPR screens.
DR ChiTaRS; ISCU; human.
DR GeneWiki; ISCU; -.
DR GenomeRNAi; 23479; -.
DR Pharos; Q9H1K1; Tbio.
DR PRO; PR:Q9H1K1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H1K1; protein.
DR Bgee; ENSG00000136003; Expressed in heart right ventricle and 209 other tissues.
DR ExpressionAtlas; Q9H1K1; baseline and differential.
DR Genevisible; Q9H1K1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:HGNC-UCL.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; TAS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:HGNC-UCL.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; TAS:UniProtKB.
DR GO; GO:1904439; P:negative regulation of iron ion import across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:1904234; P:positive regulation of aconitate hydratase activity; IMP:ARUK-UCL.
DR GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IMP:ARUK-UCL.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR01999; iscU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Iron; Metal-binding;
KW Mitochondrion; Nucleus; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..167
FT /note="Iron-sulfur cluster assembly enzyme ISCU,
FT mitochondrial"
FT /id="PRO_0000019692"
FT VAR_SEQ 1..38
FT /note="MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKK -> MVLIDMSVDL
FT STQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11060020"
FT /id="VSP_013492"
FT VARIANT 12
FT /note="A -> V (in dbSNP:rs2287555)"
FT /evidence="ECO:0000269|PubMed:11060020,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT /id="VAR_060728"
FT CONFLICT 7
FT /note="F -> G (in Ref. 1; AAG37428 and 3; AAH11906)"
FT /evidence="ECO:0000305"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6UXE"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5WLW"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6UXE"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6UXE"
FT STRAND 83..94
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6UXE"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:6UXE"
SQ SEQUENCE 167 AA; 17999 MW; 0166D3EC9F1EEB47 CRC64;
MAAAGAFRLR RAASALLLRS PRLPARELSA PARLYHKKVV DHYENPRNVG SLDKTSKNVG
TGLVGAPACG DVMKLQIQVD EKGKIVDARF KTFGCGSAIA SSSLATEWVK GKTVEEALTI
KNTDIAKELC LPPVKLHCSM LAEDAIKAAL ADYKLKQEPK KGEAEKK
