NDUAD_HUMAN
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 03-AUG-2022, entry version 199.
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};
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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 AlphaFoldDB; Q9P0J0; -.
DR SMR; Q9P0J0; -.
DR BioGRID; 119270; 140.
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; 294 antibodies from 36 providers.
DR DNASU; 51079; -.
DR Ensembl; ENST00000507754.9; ENSP00000423673.1; ENSG00000186010.19. [Q9P0J0-1]
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 BioCyc; MetaCyc:HS05364-MON; -.
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; 201 hits in 1072 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 97 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:0009060; P:aerobic respiration; IC:ComplexPortal.
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:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
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
