ID NDUAD_HUMAN Reviewed; 144 AA. AC Q9P0J0; B4DF76; K7EK58; Q6PKI0; Q9H2L3; Q9Y327; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-FEB-2022, entry version 197. DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13; DE AltName: Full=Cell death regulatory protein GRIM-19; DE AltName: Full=Complex I-B16.6; DE Short=CI-B16.6; DE AltName: Full=Gene associated with retinoic and interferon-induced mortality 19 protein; DE Short=GRIM-19; DE Short=Gene associated with retinoic and IFN-induced mortality 19 protein; DE AltName: Full=NADH-ubiquinone oxidoreductase B16.6 subunit; GN Name=NDUFA13; Synonyms=GRIM19; ORFNames=CDA016, CGI-39; 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 1), AND TISSUE SPECIFICITY. RC TISSUE=Mammary carcinoma; RX PubMed=10924506; DOI=10.1074/jbc.m003929200; RA Angell J.E., Lindner D.J., Shapiro P.S., Hofmann E.R., Kalvakolanu D.V.; RT "Identification of GRIM-19, a novel cell death-regulatory gene induced by RT the interferon-beta and retinoic acid combination, using a genetic RT approach."; RL J. Biol. Chem. 275:33416-33426(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pheochromocytoma; RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.; RT "A novel gene expressed in human pheochromocytoma."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Skin; 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 [8] RP INTERACTION WITH HHV-8 IRF1; HPV-16 E6 AND SV40 LT (MICROBIAL INFECTION). RX PubMed=12163600; DOI=10.1128/jvi.76.17.8797-8807.2002; RA Seo T., Lee D., Shim Y.S., Angell J.E., Chidambaram N.V., Kalvakolanu D.V., RA Choe J.; RT "Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated RT herpesvirus interacts with a cell death regulator, GRIM19, and inhibits RT interferon/retinoic acid-induced cell death."; RL J. Virol. 76:8797-8807(2002). RN [9] RP FUNCTION, INTERACTION WITH STAT3, AND SUBCELLULAR LOCATION. RX PubMed=12628925; DOI=10.1093/emboj/cdg135; RA Lufei C., Ma J., Huang G., Zhang T., Novotny-Diermayr V., Ong C.T., Cao X.; RT "GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via RT functional interaction."; RL EMBO J. 22:1325-1335(2003). RN [10] RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12611891; DOI=10.1074/jbc.c300064200; RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., RA Ghosh S.S., Capaldi R.A.; RT "The subunit composition of the human NADH dehydrogenase obtained by rapid RT one-step immunopurification."; RL J. Biol. Chem. 278:13619-13622(2003). RN [11] RP FUNCTION, AND INTERACTION WITH STAT3. RX PubMed=12867595; DOI=10.1073/pnas.1633516100; RA Zhang J., Yang J., Roy S.K., Tininini S., Hu J., Bromberg J.F., Poli V., RA Stark G.R., Kalvakolanu D.V.; RT "The cell death regulator GRIM-19 is an inhibitor of signal transducer and RT activator of transcription 3."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9342-9347(2003). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=15367666; DOI=10.1128/mcb.24.19.8447-8456.2004; RA Huang G., Lu H., Hao A., Ng D.C.H., Ponniah S., Guo K., Lufei C., Zeng Q., RA Cao X.; RT "GRIM-19, a cell death regulatory protein, is essential for assembly and RT function of mitochondrial complex I."; RL Mol. Cell. Biol. 24:8447-8456(2004). RN [13] RP SUBCELLULAR LOCATION, AND INTERACTION WITH OLFM4. RX PubMed=15059901; DOI=10.1158/0008-5472.can-03-3443; RA Zhang X., Huang Q., Yang Z., Li Y., Li C.-Y.; RT "GW112, a novel antiapoptotic protein that promotes tumor growth."; RL Cancer Res. 64:2474-2481(2004). RN [14] RP FUNCTION, AND INTERACTION WITH CARD15. RX PubMed=15753091; DOI=10.1074/jbc.m413776200; RA Barnich N., Hisamatsu T., Aguirre J.E., Xavier R., Reinecker H.-C., RA Podolsky D.K.; RT "GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as RT downstream effector of anti-bacterial function in intestinal epithelial RT cells."; RL J. Biol. Chem. 280:19021-19026(2005). RN [15] 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 [16] 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 [17] RP FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX. RX PubMed=27626371; DOI=10.1038/nature19754; RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E., RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R., RA Salim A., Ryan M.T.; RT "Accessory subunits are integral for assembly and function of human RT mitochondrial complex I."; RL Nature 538:123-126(2016). RN [18] RP VARIANTS ASN-5 AND PRO-115, AND INVOLVEMENT IN SUSCEPTIBILITY TO HURTHLE RP CELL THYROID CARCINOMA. RX PubMed=15841082; DOI=10.1038/sj.bjc.6602547; RA Maximo V., Botelho T., Capela J., Soares P., Lima J., Taveira A., Amaro T., RA Barbosa A.P., Preto A., Harach H.R., Williams D., Sobrinho-Simoes M.; RT "Somatic and germline mutation in GRIM-19, a dual function gene involved in RT mitochondrial metabolism and cell death, is linked to mitochondrion-rich RT (Hurthle cell) tumours of the thyroid."; RL Br. J. Cancer 92:1892-1898(2005). RN [19] RP VARIANT MC1DN28 HIS-57, INVOLVEMENT IN MC1DN28, AND CHARACTERIZATION OF RP VARIANT MC1DN28 HIS-57. RX PubMed=25901006; DOI=10.1093/hmg/ddv133; RA Angebault C., Charif M., Guegen N., Piro-Megy C., Mousson de Camaret B., RA Procaccio V., Guichet P.O., Hebrard M., Manes G., Leboucq N., Rivier F., RA Hamel C.P., Lenaers G., Roubertie A.; RT "Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia and RT sensorial deficiencies, and mitochondrial complex I instability."; RL Hum. Mol. Genet. 24:3948-3955(2015). CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I), that is believed not to be CC involved in catalysis (PubMed:27626371). Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone CC (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid CC (IFN/RA) induced cell death. This apoptotic activity is inhibited by CC interaction with viral IRF1. Prevents the transactivation of STAT3 CC target genes. May play a role in CARD15-mediated innate mucosal CC responses and serve to regulate intestinal epithelial cell responses to CC microbes (PubMed:15753091). {ECO:0000269|PubMed:12628925, CC ECO:0000269|PubMed:12867595, ECO:0000269|PubMed:15753091, CC ECO:0000269|PubMed:27626371}. CC -!- SUBUNIT: Complex I is composed of 45 different subunits CC (PubMed:27626371). Interacts with CARD15, but not with CARD4 CC (PubMed:12611891, PubMed:15753091). Interacts with STAT3, but not with CC STAT1, STAT2 and STAT5A (PubMed:12628925, PubMed:12867595). Interacts CC with OLFM4 (PubMed:15059901). {ECO:0000269|PubMed:12163600, CC ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:12628925, CC ECO:0000269|PubMed:12867595, ECO:0000269|PubMed:15059901, CC ECO:0000269|PubMed:15753091, ECO:0000269|PubMed:27626371}. CC -!- SUBUNIT: (Microbial infection) Interacts with HHV-8 IRF1, in the CC nucleus, with HPV-16 E6 and SV40 LT (PubMed:12163600). CC {ECO:0000269|PubMed:12163600}. CC -!- INTERACTION: CC Q9P0J0; O43464: HTRA2; NbExp=7; IntAct=EBI-372742, EBI-517086; CC Q9P0J0; P42858: HTT; NbExp=4; IntAct=EBI-372742, EBI-466029; CC Q9P0J0; Q9HC29: NOD2; NbExp=6; IntAct=EBI-372742, EBI-7445625; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:15059901, CC ECO:0000269|PubMed:15367666}; Single-pass membrane protein CC {ECO:0000255}; Matrix side. Nucleus {ECO:0000269|PubMed:12628925}. CC Note=Localizes mainly in the mitochondrion (PubMed:12628925). May be CC translocated into the nucleus upon IFN/RA treatment. CC {ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:15059901}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9P0J0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P0J0-2; Sequence=VSP_056644; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in heart, CC skeletal muscle, liver, kidney and placenta. In intestinal mucosa, CC down-regulated in areas involved in Crohn disease and ulcerative CC colitis. {ECO:0000269|PubMed:10924506}. CC -!- DEVELOPMENTAL STAGE: Expressed in numerous fetal tissues. CC -!- INDUCTION: By IFNB1/IFN-beta combined with all-trans-retinoic acid CC (ATRA). CC -!- DISEASE: Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]: A rare CC type of thyroid cancer accounting for only about 3-10% of all CC differentiated thyroid cancers. These neoplasms are considered a CC variant of follicular carcinoma of the thyroid and are referred to as CC follicular carcinoma, oxyphilic type. {ECO:0000269|PubMed:15841082}. CC Note=Disease susceptibility is associated with variants affecting the CC gene represented in this entry. CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 28 (MC1DN28) CC [MIM:618249]: A form of mitochondrial complex I deficiency, the most CC common biochemical signature of mitochondrial disorders, a group of CC highly heterogeneous conditions characterized by defective oxidative CC phosphorylation, which collectively affects 1 in 5-10000 live births. CC Clinical disorders have variable severity, ranging from lethal neonatal CC disease to adult-onset neurodegenerative disorders. Phenotypes include CC macrocephaly with progressive leukodystrophy, non-specific CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh CC syndrome, Leber hereditary optic neuropathy, and some forms of CC Parkinson disease. MC1DN28 transmission pattern is consistent with CC autosomal recessive inheritance. {ECO:0000269|PubMed:25901006}. CC Note=The disease may be caused by variants affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the complex I NDUFA13 subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD27748.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAG44670.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH00589.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF286697; AAG28167.1; -; mRNA. DR EMBL; AF155662; AAF67481.1; -; mRNA. DR EMBL; AF132973; AAD27748.1; ALT_INIT; mRNA. DR EMBL; AF261134; AAG44670.1; ALT_INIT; mRNA. DR EMBL; AK293965; BAG57337.1; -; mRNA. DR EMBL; AC011448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000589; AAH00589.2; ALT_INIT; mRNA. DR EMBL; BC009189; AAH09189.1; -; mRNA. DR CCDS; CCDS12404.2; -. [Q9P0J0-1] DR RefSeq; NP_057049.5; NM_015965.6. [Q9P0J0-1] DR PDB; 5XTB; EM; 3.40 A; W=7-28. DR PDB; 5XTC; EM; 3.70 A; W=29-144. DR PDB; 5XTD; EM; 3.70 A; W=7-144. DR PDB; 5XTH; EM; 3.90 A; W=7-144. DR PDB; 5XTI; EM; 17.40 A; BW/W=7-144. DR PDBsum; 5XTB; -. DR PDBsum; 5XTC; -. DR PDBsum; 5XTD; -. DR PDBsum; 5XTH; -. DR PDBsum; 5XTI; -. DR SMR; Q9P0J0; -. DR BioGRID; 119270; 123. DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I. DR CORUM; Q9P0J0; -. DR DIP; DIP-31180N; -. DR IntAct; Q9P0J0; 91. DR MINT; Q9P0J0; -. DR STRING; 9606.ENSP00000423673; -. DR BindingDB; Q9P0J0; -. DR ChEMBL; CHEMBL4105781; -. DR DrugBank; DB00157; NADH. DR DrugCentral; Q9P0J0; -. DR iPTMnet; Q9P0J0; -. DR PhosphoSitePlus; Q9P0J0; -. DR BioMuta; NDUFA13; -. DR DMDM; 20139242; -. DR EPD; Q9P0J0; -. DR jPOST; Q9P0J0; -. DR MassIVE; Q9P0J0; -. DR MaxQB; Q9P0J0; -. DR PaxDb; Q9P0J0; -. DR PeptideAtlas; Q9P0J0; -. DR PRIDE; Q9P0J0; -. DR ProteomicsDB; 83552; -. [Q9P0J0-1] DR TopDownProteomics; Q9P0J0-1; -. [Q9P0J0-1] DR Antibodypedia; 28492; 291 antibodies from 35 providers. DR DNASU; 51079; -. DR Ensembl; ENST00000507754; ENSP00000423673; ENSG00000186010. DR GeneID; 51079; -. DR KEGG; hsa:51079; -. DR MANE-Select; ENST00000507754.9; ENSP00000423673.1; NM_015965.7; NP_057049.5. DR UCSC; uc021uqu.2; human. [Q9P0J0-1] DR CTD; 51079; -. DR DisGeNET; 51079; -. DR GeneCards; NDUFA13; -. DR HGNC; HGNC:17194; NDUFA13. DR HPA; ENSG00000186010; Low tissue specificity. DR MalaCards; NDUFA13; -. DR MIM; 607464; phenotype. DR MIM; 609435; gene. DR MIM; 618249; phenotype. DR neXtProt; NX_Q9P0J0; -. DR OpenTargets; ENSG00000186010; -. DR Orphanet; 146; Differentiated thyroid carcinoma. DR Orphanet; 255241; Leigh syndrome with leukodystrophy. DR PharmGKB; PA142671270; -. DR VEuPathDB; HostDB:ENSG00000186010; -. DR eggNOG; KOG3300; Eukaryota. DR GeneTree; ENSGT00390000000719; -. DR HOGENOM; CLU_119720_0_0_1; -. DR InParanoid; Q9P0J0; -. DR OrthoDB; 1496781at2759; -. DR PhylomeDB; Q9P0J0; -. DR TreeFam; TF315182; -. DR PathwayCommons; Q9P0J0; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR Reactome; R-HSA-6799198; Complex I biogenesis. DR SignaLink; Q9P0J0; -. DR SIGNOR; Q9P0J0; -. DR BioGRID-ORCS; 51079; 196 hits in 1040 CRISPR screens. DR ChiTaRS; NDUFA13; human. DR GeneWiki; NDUFA13; -. DR GenomeRNAi; 51079; -. DR Pharos; Q9P0J0; Tclin. DR PRO; PR:Q9P0J0; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9P0J0; protein. DR Bgee; ENSG00000186010; Expressed in apex of heart and 236 other tissues. DR ExpressionAtlas; Q9P0J0; baseline and differential. DR Genevisible; Q9P0J0; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0005746; C:mitochondrial respirasome; IDA:UniProtKB. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:UniProtKB. DR GO; GO:0003954; F:NADH dehydrogenase activity; IMP:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:ParkinsonsUK-UCL. DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:ParkinsonsUK-UCL. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:ParkinsonsUK-UCL. DR GO; GO:0010952; P:positive regulation of peptidase activity; IC:ParkinsonsUK-UCL. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:ParkinsonsUK-UCL. DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB. DR InterPro; IPR009346; GRIM-19. DR PANTHER; PTHR12966; PTHR12966; 1. DR Pfam; PF06212; GRIM-19; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; KW Disease variant; Electron transport; Host-virus interaction; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Nucleus; KW Primary mitochondrial disease; Reference proteome; Respiratory chain; KW Transmembrane; Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q95KV7" FT CHAIN 2..144 FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex FT subunit 13" FT /id="PRO_0000118804" FT TRANSMEM 30..51 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 102..144 FT /note="Important for inducing cell death" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q95KV7" FT VAR_SEQ 143..144 FT /note="YT -> ALELQPPLADMGRAELSSNATTSLVQRRKQAWGRQSWLEQIWNAGP FT VCQRLHRGGSRPGAGAAGGLSLWAAAARGAVRSC (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056644" FT VARIANT 5 FT /note="K -> N (in a Hurthle cell variant of papillary FT carcinoma sample; dbSNP:rs137852869)" FT /evidence="ECO:0000269|PubMed:15841082" FT /id="VAR_045984" FT VARIANT 57 FT /note="R -> H (in MC1DN28; reduced NDUFA13 protein level FT resulting in complex I instability; dbSNP:rs752513525)" FT /evidence="ECO:0000269|PubMed:25901006" FT /id="VAR_078938" FT VARIANT 115 FT /note="R -> P (in a Hurthle cell variant of papillary FT carcinoma sample)" FT /evidence="ECO:0000269|PubMed:15841082" FT /id="VAR_045985" FT CONFLICT 2 FT /note="A -> P (in Ref. 3)" FT /evidence="ECO:0000305" SQ SEQUENCE 144 AA; 16698 MW; 058F608B235FF856 CRC64; MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMLAIGI GTLIYGHWSI MKWNRERRRL QIEDFEARIA LLPLLQAETD RRTLQMLREN LEEEAIIMKD VPDWKVGESV FHTTRWVPPL IGELYGLRTT EEALHASHGF MWYT //