NFU1_HUMAN
ID NFU1_HUMAN Reviewed; 254 AA.
AC Q9UMS0; B4DUL9; Q53QE5; Q6VNZ8; Q7Z5B1; Q7Z5B2; Q9Y322;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=NFU1 iron-sulfur cluster scaffold homolog, mitochondrial;
DE AltName: Full=HIRA-interacting protein 5 {ECO:0000303|PubMed:11342215};
DE Flags: Precursor;
GN Name=NFU1; Synonyms=HIRIP5 {ECO:0000303|PubMed:11342215};
GN ORFNames=CGI-33 {ECO:0000303|PubMed:10810093};
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] (ISOFORM 3).
RC TISSUE=Myeloid leukemia cell;
RX PubMed=11342215; DOI=10.1016/s0167-4781(00)00300-6;
RA Lorain S., Lecluse Y., Scamps C., Mattei M.-G., Lipinski M.;
RT "Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two
RT mammalian representatives in a family of phylogenetically conserved
RT proteins with a role in the biogenesis of Fe/S proteins.";
RL Biochim. Biophys. Acta 1517:376-383(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EPM2A, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT LYS-25.
RC TISSUE=Brain;
RX PubMed=12915448; DOI=10.1093/hmg/ddg253;
RA Ganesh S., Tsurutani N., Suzuki T., Ueda K., Agarwala K.L., Osada H.,
RA Delgado-Escueta A.V., Yamakawa K.;
RT "The Lafora disease gene product laforin interacts with HIRIP5, a
RT phylogenetically conserved protein containing a NifU-like domain.";
RL Hum. Mol. Genet. 12:2359-2368(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12886008; DOI=10.1073/pnas.1732541100;
RA Tong W.-H., Jameson G.N.L., Huynh B.H., Rouault T.A.;
RT "Subcellular compartmentalization of human Nfu, an iron-sulfur cluster
RT scaffold protein, and its ability to assemble a [4Fe-4S] cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9762-9767(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LYS-25.
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [9]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN MMDS1.
RX PubMed=21944046; DOI=10.1016/j.ajhg.2011.08.011;
RA Cameron J.M., Janer A., Levandovskiy V., Mackay N., Rouault T.A.,
RA Tong W.H., Ogilvie I., Shoubridge E.A., Robinson B.H.;
RT "Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a
RT fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase
RT enzymes.";
RL Am. J. Hum. Genet. 89:486-495(2011).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS 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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
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 [14]
RP INTERACTION WITH BOLA3.
RX PubMed=27532772; DOI=10.7554/elife.16673;
RA Uzarska M.A., Nasta V., Weiler B.D., Spantgar F., Ciofi-Baffoni S.,
RA Saviello M.R., Gonnelli L., Muehlenhoff U., Banci L., Lill R.;
RT "Mitochondrial Bol1 and Bol3 function as assembly factors for specific
RT iron-sulfur proteins.";
RL Elife 5:0-0(2016).
RN [15]
RP INTERACTION WITH HSPA9.
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 [16]
RP STRUCTURE BY NMR OF 59-155, SUBUNIT, AND FUNCTION.
RX PubMed=27818104; DOI=10.1016/j.str.2016.08.020;
RA Cai K., Liu G., Frederick R.O., Xiao R., Montelione G.T., Markley J.L.;
RT "Structural/functional properties of human NFU1, an intermediate [4Fe-4S]
RT carrier in human mitochondrial iron-sulfur cluster biogenesis.";
RL Structure 24:2080-2091(2016).
RN [17]
RP VARIANT MMDS1 CYS-208.
RX PubMed=22077971; DOI=10.1016/j.ajhg.2011.10.005;
RA Navarro-Sastre A., Tort F., Stehling O., Uzarska M.A., Arranz J.A.,
RA Del Toro M., Labayru M.T., Landa J., Font A., Garcia-Villoria J.,
RA Merinero B., Ugarte M., Gutierrez-Solana L.G., Campistol J.,
RA Garcia-Cazorla A., Vaquerizo J., Riudor E., Briones P., Elpeleg O.,
RA Ribes A., Lill R.;
RT "A fatal mitochondrial disease is associated with defective NFU1 function
RT in the maturation of a subset of mitochondrial Fe-S proteins.";
RL Am. J. Hum. Genet. 89:656-667(2011).
RN [18]
RP VARIANTS MMDS1 PRO-21; TRP-182; ARG-189; ARG-190 AND CYS-208, AND
RP CHARACTERIZATION OF VARIANTS MMDS1 PRO-21; TRP-182 AND CYS-208.
RX PubMed=25918518; DOI=10.3389/fgene.2015.00123;
RA Ahting U., Mayr J.A., Vanlander A.V., Hardy S.A., Santra S., Makowski C.,
RA Alston C.L., Zimmermann F.A., Abela L., Plecko B., Rohrbach M.,
RA Spranger S., Seneca S., Rolinski B., Hagendorff A., Hempel M., Sperl W.,
RA Meitinger T., Smet J., Taylor R.W., Van Coster R., Freisinger P.,
RA Prokisch H., Haack T.B.;
RT "Clinical, biochemical, and genetic spectrum of seven patients with NFU1
RT deficiency.";
RL Front. Genet. 6:123-123(2015).
RN [19]
RP VARIANT MMDS1 ARG-189, CHARACTERIZATION OF VARIANT MMDS1 ARG-189,
RP MUTAGENESIS OF GLY-189, AND FUNCTION.
RX PubMed=28906594; DOI=10.1111/febs.14271;
RA Wesley N.A., Wachnowsky C., Fidai I., Cowan J.A.;
RT "Understanding the molecular basis for multiple mitochondrial dysfunctions
RT syndrome 1 (MMDS1): impact of a disease-causing Gly189Arg substitution on
RT NFU1.";
RL FEBS J. 284:3838-3848(2017).
RN [20]
RP CHARACTERIZATION OF VARIANT MMDS1 CYS-208.
RX PubMed=28161430; DOI=10.1016/j.jmb.2017.01.021;
RA Wachnowsky C., Wesley N.A., Fidai I., Cowan J.A.;
RT "Understanding the Molecular Basis of Multiple Mitochondrial Dysfunctions
RT Syndrome 1 (MMDS1)-Impact of a Disease-Causing Gly208Cys Substitution on
RT Structure and Activity of NFU1 in the Fe/S Cluster Biosynthetic Pathway.";
RL J. Mol. Biol. 429:790-807(2017).
CC -!- FUNCTION: Iron-sulfur cluster scaffold protein which can assemble [4Fe-
CC 4S] clusters and deliver them to target proteins.
CC {ECO:0000269|PubMed:12886008, ECO:0000269|PubMed:27818104,
CC ECO:0000269|PubMed:28906594}.
CC -!- SUBUNIT: Monomer and homohexamer; the apo-NFU1 is a monomer, while the
CC holo-NFU1 is a hexamer composed of a trimer of dimer that is probably
CC linked by some 4Fe-4S cluster (PubMed:27818104). Interacts with HIRA
CC and EPM2A/laforin (PubMed:12915448). Interacts with BOLA3
CC (PubMed:27532772). Interacts with HSPA9 (PubMed:26702583).
CC {ECO:0000269|PubMed:12915448, ECO:0000269|PubMed:26702583,
CC ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27818104}.
CC -!- INTERACTION:
CC Q9UMS0; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-725252, EBI-741181;
CC Q9UMS0; P02654: APOC1; NbExp=3; IntAct=EBI-725252, EBI-1220105;
CC Q9UMS0; P55056: APOC4; NbExp=3; IntAct=EBI-725252, EBI-18302142;
CC Q9UMS0; Q9Y3E2: BOLA1; NbExp=2; IntAct=EBI-725252, EBI-1049556;
CC Q9UMS0; Q53S33: BOLA3; NbExp=2; IntAct=EBI-725252, EBI-12086950;
CC Q9UMS0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-725252, EBI-739580;
CC Q9UMS0; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-725252, EBI-7062247;
CC Q9UMS0; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-725252, EBI-11522780;
CC Q9UMS0; P38432: COIL; NbExp=3; IntAct=EBI-725252, EBI-945751;
CC Q9UMS0; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-725252, EBI-12878374;
CC Q9UMS0; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-725252, EBI-3918971;
CC Q9UMS0; P21741: MDK; NbExp=3; IntAct=EBI-725252, EBI-722444;
CC Q9UMS0; Q6PF18: MORN3; NbExp=3; IntAct=EBI-725252, EBI-9675802;
CC Q9UMS0; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-725252, EBI-17589229;
CC Q9UMS0; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-725252, EBI-742426;
CC Q9UMS0; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-725252, EBI-1105213;
CC Q9UMS0; P36406: TRIM23; NbExp=3; IntAct=EBI-725252, EBI-740098;
CC Q9UMS0; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-725252, EBI-4395732;
CC Q9UMS0; Q9BUG6: ZSCAN5A; NbExp=3; IntAct=EBI-725252, EBI-8836980;
CC Q9UMS0; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-725252, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UMS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMS0-2; Sequence=VSP_041224;
CC Name=3;
CC IsoId=Q9UMS0-3; Sequence=VSP_041225;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression in adult lung is weak
CC compared to fetal lung. {ECO:0000269|PubMed:12915448}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and adult.
CC {ECO:0000269|PubMed:12915448}.
CC -!- DISEASE: Multiple mitochondrial dysfunctions syndrome 1 (MMDS1)
CC [MIM:605711]: A severe disorder of systemic energy metabolism,
CC resulting in weakness, respiratory failure, lack of neurologic
CC development, lactic acidosis, hyperglycinemia and early death. Some
CC patients show failure to thrive, pulmonary hypertension, hypotonia and
CC irritability. Biochemical features include severe combined deficiency
CC of the 2-oxoacid dehydrogenases, defective lipoic acid synthesis and
CC reduction in activity of mitochondrial respiratory chain complexes.
CC {ECO:0000269|PubMed:21944046, ECO:0000269|PubMed:22077971,
CC ECO:0000269|PubMed:25918518, ECO:0000269|PubMed:28161430,
CC ECO:0000269|PubMed:28906594}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27742.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAY14828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAG36716.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB53015.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ132584; CAB53015.1; ALT_INIT; mRNA.
DR EMBL; AY335194; AAQ73784.1; -; mRNA.
DR EMBL; AY286306; AAP92372.1; -; mRNA.
DR EMBL; AY286307; AAP92373.1; -; mRNA.
DR EMBL; AF132967; AAD27742.1; ALT_FRAME; mRNA.
DR EMBL; AK314004; BAG36716.1; ALT_INIT; mRNA.
DR EMBL; AK300700; BAG62381.1; -; mRNA.
DR EMBL; DB304061; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC114772; AAY14828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471053; EAW99849.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99850.1; -; Genomic_DNA.
DR EMBL; BC113692; AAI13693.1; -; mRNA.
DR EMBL; BC113694; AAI13695.1; -; mRNA.
DR CCDS; CCDS33217.1; -. [Q9UMS0-1]
DR CCDS; CCDS42694.1; -. [Q9UMS0-2]
DR CCDS; CCDS46315.1; -. [Q9UMS0-3]
DR RefSeq; NP_001002755.1; NM_001002755.2. [Q9UMS0-1]
DR RefSeq; NP_001002756.1; NM_001002756.2. [Q9UMS0-2]
DR RefSeq; NP_056515.2; NM_015700.3. [Q9UMS0-3]
DR RefSeq; XP_016859297.1; XM_017003808.1.
DR PDB; 2LTM; NMR; -; A=59-155.
DR PDB; 2M5O; NMR; -; A=162-247.
DR PDBsum; 2LTM; -.
DR PDBsum; 2M5O; -.
DR AlphaFoldDB; Q9UMS0; -.
DR BMRB; Q9UMS0; -.
DR SMR; Q9UMS0; -.
DR BioGRID; 118095; 51.
DR IntAct; Q9UMS0; 29.
DR MINT; Q9UMS0; -.
DR STRING; 9606.ENSP00000387219; -.
DR GlyGen; Q9UMS0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UMS0; -.
DR MetOSite; Q9UMS0; -.
DR PhosphoSitePlus; Q9UMS0; -.
DR BioMuta; NFU1; -.
DR DMDM; 205371805; -.
DR EPD; Q9UMS0; -.
DR jPOST; Q9UMS0; -.
DR MassIVE; Q9UMS0; -.
DR MaxQB; Q9UMS0; -.
DR PaxDb; Q9UMS0; -.
DR PeptideAtlas; Q9UMS0; -.
DR PRIDE; Q9UMS0; -.
DR ProteomicsDB; 85204; -. [Q9UMS0-1]
DR ProteomicsDB; 85205; -. [Q9UMS0-2]
DR ProteomicsDB; 85206; -. [Q9UMS0-3]
DR Antibodypedia; 48139; 46 antibodies from 18 providers.
DR DNASU; 27247; -.
DR Ensembl; ENST00000303698.7; ENSP00000306965.3; ENSG00000169599.13. [Q9UMS0-3]
DR Ensembl; ENST00000394305.5; ENSP00000377842.1; ENSG00000169599.13. [Q9UMS0-2]
DR Ensembl; ENST00000410022.7; ENSP00000387219.3; ENSG00000169599.13. [Q9UMS0-1]
DR Ensembl; ENST00000462320.5; ENSP00000418598.1; ENSG00000169599.13. [Q9UMS0-2]
DR GeneID; 27247; -.
DR KEGG; hsa:27247; -.
DR MANE-Select; ENST00000410022.7; ENSP00000387219.3; NM_001002755.4; NP_001002755.1.
DR UCSC; uc002sfj.4; human. [Q9UMS0-1]
DR CTD; 27247; -.
DR DisGeNET; 27247; -.
DR GeneCards; NFU1; -.
DR HGNC; HGNC:16287; NFU1.
DR HPA; ENSG00000169599; Low tissue specificity.
DR MalaCards; NFU1; -.
DR MIM; 605711; phenotype.
DR MIM; 608100; gene.
DR neXtProt; NX_Q9UMS0; -.
DR OpenTargets; ENSG00000169599; -.
DR Orphanet; 401869; Multiple mitochondrial dysfunctions syndrome type 1.
DR PharmGKB; PA162397454; -.
DR VEuPathDB; HostDB:ENSG00000169599; -.
DR eggNOG; KOG2358; Eukaryota.
DR GeneTree; ENSGT00390000011296; -.
DR HOGENOM; CLU_060555_0_2_1; -.
DR InParanoid; Q9UMS0; -.
DR OMA; AIMEHYM; -.
DR OrthoDB; 1016782at2759; -.
DR PhylomeDB; Q9UMS0; -.
DR TreeFam; TF315076; -.
DR PathwayCommons; Q9UMS0; -.
DR SignaLink; Q9UMS0; -.
DR BioGRID-ORCS; 27247; 71 hits in 1078 CRISPR screens.
DR ChiTaRS; NFU1; human.
DR GenomeRNAi; 27247; -.
DR Pharos; Q9UMS0; Tbio.
DR PRO; PR:Q9UMS0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UMS0; protein.
DR Bgee; ENSG00000169599; Expressed in heart right ventricle and 202 other tissues.
DR ExpressionAtlas; Q9UMS0; baseline and differential.
DR Genevisible; Q9UMS0; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:UniProtKB.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR Gene3D; 3.30.1370.70; -; 1.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR014824; Nfu/NifU_N.
DR InterPro; IPR036498; Nfu/NifU_N_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF08712; Nfu_N; 1.
DR Pfam; PF01106; NifU; 1.
DR SMART; SM00932; Nfu_N; 1.
DR SUPFAM; SSF110836; SSF110836; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Iron;
KW Iron-sulfur; Metal-binding; Mitochondrion; Primary mitochondrial disease;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..9
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 10..254
FT /note="NFU1 iron-sulfur cluster scaffold homolog,
FT mitochondrial"
FT /id="PRO_0000166191"
FT REGION 173..241
FT /note="NifU"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:27818104"
FT BINDING 213
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:27818104"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041224"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10810093,
FT ECO:0000303|PubMed:11342215, ECO:0000303|PubMed:12886008"
FT /id="VSP_041225"
FT VARIANT 21
FT /note="R -> P (in MMDS1; patient's skeletal muscles and
FT fibroblasts show deficiency of mitochondrial respiratory
FT chain complexes; dbSNP:rs776875884)"
FT /evidence="ECO:0000269|PubMed:25918518"
FT /id="VAR_079757"
FT VARIANT 25
FT /note="M -> K (in dbSNP:rs4453725)"
FT /evidence="ECO:0000269|PubMed:12915448,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_044429"
FT VARIANT 182
FT /note="R -> W (in MMDS1; patient's skin fibroblasts show
FT deficiency of lipoic acid synthase and reduced lipoic acid
FT content; dbSNP:rs1354126704)"
FT /evidence="ECO:0000269|PubMed:25918518"
FT /id="VAR_079758"
FT VARIANT 189
FT /note="G -> R (in MMDS1; alters protein structure;
FT increases likelihood of existing as monomer; decreases
FT ability to receive a Fe/S clusters from donor proteins;
FT decreases delivery rates of [2Fe-2S] cluster to target
FT proteins)"
FT /evidence="ECO:0000269|PubMed:25918518,
FT ECO:0000269|PubMed:28906594"
FT /id="VAR_079759"
FT VARIANT 190
FT /note="G -> R (in MMDS1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25918518"
FT /id="VAR_079760"
FT VARIANT 208
FT /note="G -> C (in MMDS1; patient's skeletal muscles and
FT fibroblasts show deficiency of mitochondrial respiratory
FT chain complexes; increases homodimerization; unable to
FT receive a Fe/S clusters from donor proteins; changes
FT delivery rates of [2Fe-2S] cluster to target proteins;
FT dbSNP:rs374514431)"
FT /evidence="ECO:0000269|PubMed:22077971,
FT ECO:0000269|PubMed:25918518, ECO:0000269|PubMed:28161430"
FT /id="VAR_066639"
FT MUTAGEN 189
FT /note="G->A: Alters protein structure. Increases likelihood
FT of existing as monomer. Decreases ability to receive a Fe/S
FT clusters from donor proteins. Decreases delivery rates of
FT [2Fe-2S] cluster to target proteins."
FT /evidence="ECO:0000269|PubMed:28906594"
FT MUTAGEN 189
FT /note="G->K: Alters protein structure. Increases likelihood
FT of existing as monomer. Decreases ability to receive a Fe/S
FT clusters from donor proteins. Decreases delivery rates of
FT [2Fe-2S] cluster to target proteins."
FT /evidence="ECO:0000269|PubMed:28906594"
FT CONFLICT 158
FT /note="S -> P (in Ref. 4; AAD27742)"
FT /evidence="ECO:0000305"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2LTM"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2LTM"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2LTM"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2LTM"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2LTM"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:2LTM"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2LTM"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:2LTM"
FT HELIX 130..147
FT /evidence="ECO:0007829|PDB:2LTM"
FT HELIX 167..188
FT /evidence="ECO:0007829|PDB:2M5O"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:2M5O"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:2M5O"
FT TURN 208..212
FT /evidence="ECO:0007829|PDB:2M5O"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:2M5O"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2M5O"
SQ SEQUENCE 254 AA; 28463 MW; E84B7F47A4A282CF CRC64;
MAATARRGWG AAAVAAGLRR RFCHMLKNPY TIKKQPLHQF VQRPLFPLPA AFYHPVRYMF
IQTQDTPNPN SLKFIPGKPV LETRTMDFPT PAAAFRSPLA RQLFRIEGVK SVFFGPDFIT
VTKENEELDW NLLKPDIYAT IMDFFASGLP LVTEETPSGE AGSEEDDEVV AMIKELLDTR
IRPTVQEDGG DVIYKGFEDG IVQLKLQGSC TSCPSSIITL KNGIQNMLQF YIPEVEGVEQ
VMDDESDEKE ANSP
