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NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 (Cell death regulatory protein GRIM-19) (Complex I-B16.6) (CI-B16.6) (Gene associated with retinoic and interferon-induced mortality 19 protein) (GRIM-19) (Gene associated with retinoic and IFN-induced mortality 19 protein) (NADH-ubiquinone oxidoreductase B16.6 subunit)

 NDUAD_HUMAN             Reviewed;         144 AA.
Q9P0J0; B4DF76; K7EK58; Q6PKI0; Q9H2L3; Q9Y327;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 168.
RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13;
AltName: Full=Cell death regulatory protein GRIM-19;
AltName: Full=Complex I-B16.6;
Short=CI-B16.6;
AltName: Full=Gene associated with retinoic and interferon-induced mortality 19 protein;
Short=GRIM-19;
Short=Gene associated with retinoic and IFN-induced mortality 19 protein;
AltName: Full=NADH-ubiquinone oxidoreductase B16.6 subunit;
Name=NDUFA13; Synonyms=GRIM19; ORFNames=CDA016, CGI-39;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Mammary carcinoma;
PubMed=10924506; DOI=10.1074/jbc.M003929200;
Angell J.E., Lindner D.J., Shapiro P.S., Hofmann E.R.,
Kalvakolanu D.V.;
"Identification of GRIM-19, a novel cell death-regulatory gene induced
by the interferon-beta and retinoic acid combination, using a genetic
approach.";
J. Biol. Chem. 275:33416-33426(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pheochromocytoma;
Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
"A novel gene expressed in human pheochromocytoma.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH HHV-8 IRF1; HPV-16 E6 AND SV40 LT (MICROBIAL
INFECTION).
PubMed=12163600; DOI=10.1128/JVI.76.17.8797-8807.2002;
Seo T., Lee D., Shim Y.S., Angell J.E., Chidambaram N.V.,
Kalvakolanu D.V., Choe J.;
"Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated
herpesvirus interacts with a cell death regulator, GRIM19, and
inhibits interferon/retinoic acid-induced cell death.";
J. Virol. 76:8797-8807(2002).
[9]
FUNCTION, INTERACTION WITH STAT3, AND SUBCELLULAR LOCATION.
PubMed=12628925; DOI=10.1093/emboj/cdg135;
Lufei C., Ma J., Huang G., Zhang T., Novotny-Diermayr V., Ong C.T.,
Cao X.;
"GRIM-19, a death-regulatory gene product, suppresses Stat3 activity
via functional interaction.";
EMBO J. 22:1325-1335(2003).
[10]
IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12611891; DOI=10.1074/jbc.C300064200;
Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
Ghosh S.S., Capaldi R.A.;
"The subunit composition of the human NADH dehydrogenase obtained by
rapid one-step immunopurification.";
J. Biol. Chem. 278:13619-13622(2003).
[11]
FUNCTION, AND INTERACTION WITH STAT3.
PubMed=12867595; DOI=10.1073/pnas.1633516100;
Zhang J., Yang J., Roy S.K., Tininini S., Hu J., Bromberg J.F.,
Poli V., Stark G.R., Kalvakolanu D.V.;
"The cell death regulator GRIM-19 is an inhibitor of signal transducer
and activator of transcription 3.";
Proc. Natl. Acad. Sci. U.S.A. 100:9342-9347(2003).
[12]
SUBCELLULAR LOCATION.
PubMed=15367666; DOI=10.1128/MCB.24.19.8447-8456.2004;
Huang G., Lu H., Hao A., Ng D.C.H., Ponniah S., Guo K., Lufei C.,
Zeng Q., Cao X.;
"GRIM-19, a cell death regulatory protein, is essential for assembly
and function of mitochondrial complex I.";
Mol. Cell. Biol. 24:8447-8456(2004).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH OLFM4.
PubMed=15059901; DOI=10.1158/0008-5472.CAN-03-3443;
Zhang X., Huang Q., Yang Z., Li Y., Li C.-Y.;
"GW112, a novel antiapoptotic protein that promotes tumor growth.";
Cancer Res. 64:2474-2481(2004).
[14]
FUNCTION, AND INTERACTION WITH CARD15.
PubMed=15753091; DOI=10.1074/jbc.M413776200;
Barnich N., Hisamatsu T., Aguirre J.E., Xavier R., Reinecker H.-C.,
Podolsky D.K.;
"GRIM-19 interacts with nucleotide oligomerization domain 2 and serves
as downstream effector of anti-bacterial function in intestinal
epithelial cells.";
J. Biol. Chem. 280:19021-19026(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE
COMPLEX.
PubMed=27626371; DOI=10.1038/nature19754;
Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
Salim A., Ryan M.T.;
"Accessory subunits are integral for assembly and function of human
mitochondrial complex I.";
Nature 538:123-126(2016).
[18]
VARIANTS ASN-5 AND PRO-115, AND INVOLVEMENT IN SUSCEPTIBILITY TO
HURTHLE CELL THYROID CARCINOMA.
PubMed=15841082; DOI=10.1038/sj.bjc.6602547;
Maximo V., Botelho T., Capela J., Soares P., Lima J., Taveira A.,
Amaro T., Barbosa A.P., Preto A., Harach H.R., Williams D.,
Sobrinho-Simoes M.;
"Somatic and germline mutation in GRIM-19, a dual function gene
involved in mitochondrial metabolism and cell death, is linked to
mitochondrion-rich (Hurthle cell) tumours of the thyroid.";
Br. J. Cancer 92:1892-1898(2005).
[19]
VARIANT HIS-57, AND INVOLVEMENT IN MITOCHONDRIAL COMPLEX I DEFICIENCY.
PubMed=25901006; DOI=10.1093/hmg/ddv133;
Angebault C., Charif M., Guegen N., Piro-Megy C.,
Mousson de Camaret B., Procaccio V., Guichet P.O., Hebrard M.,
Manes G., Leboucq N., Rivier F., Hamel C.P., Lenaers G., Roubertie A.;
"Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia
and sensorial deficiencies, and mitochondrial complex I instability.";
Hum. Mol. Genet. 24:3948-3955(2015).
-!- FUNCTION: Accessory subunit of the mitochondrial membrane
respiratory chain NADH dehydrogenase (Complex I), that is believed
not to be involved in catalysis (PubMed:27626371). Complex I
functions in the transfer of electrons from NADH to the
respiratory chain. The immediate electron acceptor for the enzyme
is believed to be ubiquinone (PubMed:27626371). Involved in the
interferon/all-trans-retinoic acid (IFN/RA) induced cell death.
This apoptotic activity is inhibited by interaction with viral
IRF1. Prevents the transactivation of STAT3 target genes. May play
a role in CARD15-mediated innate mucosal responses and serve to
regulate intestinal epithelial cell responses to microbes
(PubMed:15753091). {ECO:0000269|PubMed:12628925,
ECO:0000269|PubMed:12867595, ECO:0000269|PubMed:15753091,
ECO:0000269|PubMed:27626371}.
-!- SUBUNIT: Complex I is composed of 45 different subunits
(PubMed:27626371). Interacts with CARD15, but not with CARD4
(PubMed:12611891, PubMed:15753091). Interacts with STAT3, but not
with STAT1, STAT2 and STAT5A (PubMed:12628925, PubMed:12867595).
Interacts with OLFM4 (PubMed:15059901).
{ECO:0000269|PubMed:12163600, ECO:0000269|PubMed:12611891,
ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:12867595,
ECO:0000269|PubMed:15059901, ECO:0000269|PubMed:15753091,
ECO:0000269|PubMed:27626371}.
-!- SUBUNIT: (Microbial infection) Interacts with HHV-8 IRF1, in the
nucleus, with HPV-16 E6 and SV40 LT (PubMed:12163600).
{ECO:0000269|PubMed:12163600}.
-!- INTERACTION:
O43464:HTRA2; NbExp=6; IntAct=EBI-372742, EBI-517086;
Q9HC29:NOD2; NbExp=6; IntAct=EBI-372742, EBI-7445625;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:15059901,
ECO:0000269|PubMed:15367666}; Single-pass membrane protein
{ECO:0000255}; Matrix side. Nucleus {ECO:0000269|PubMed:12628925}.
Note=Localizes mainly in the mitochondrion (PubMed:12628925). May
be translocated into the nucleus upon IFN/RA treatment.
{ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:15059901}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9P0J0-1; Sequence=Displayed;
Name=2;
IsoId=Q9P0J0-2; Sequence=VSP_056644;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
heart, skeletal muscle, liver, kidney and placenta. In intestinal
mucosa, down-regulated in areas involved in Crohn disease and
ulcerative colitis. {ECO:0000269|PubMed:10924506}.
-!- DEVELOPMENTAL STAGE: Expressed in numerous fetal tissues.
-!- INDUCTION: By IFNB1/IFN-beta combined with all-trans-retinoic acid
(ATRA).
-!- DISEASE: Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]: A
rare type of thyroid cancer accounting for only about 3-10% of all
differentiated thyroid cancers. These neoplasms are considered a
variant of follicular carcinoma of the thyroid and are referred to
as follicular carcinoma, oxyphilic type.
{ECO:0000269|PubMed:15841082}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Note=Defects in NDUFA13 are a cause of a mitochondrial
complex I deficiency characterized by early onset hypotonia,
dyskinesia and sensorial deficiencies, as well as a severe optic
neuropathy. {ECO:0000269|PubMed:25901006}.
-!- SIMILARITY: Belongs to the complex I NDUFA13 subunit family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD27748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAG44670.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH00589.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF286697; AAG28167.1; -; mRNA.
EMBL; AF155662; AAF67481.1; -; mRNA.
EMBL; AF132973; AAD27748.1; ALT_INIT; mRNA.
EMBL; AF261134; AAG44670.1; ALT_INIT; mRNA.
EMBL; AK293965; BAG57337.1; -; mRNA.
EMBL; AC011448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000589; AAH00589.2; ALT_INIT; mRNA.
EMBL; BC009189; AAH09189.1; -; mRNA.
CCDS; CCDS12404.2; -. [Q9P0J0-1]
RefSeq; NP_057049.5; NM_015965.6. [Q9P0J0-1]
UniGene; Hs.534453; -.
PDB; 5XTB; EM; 3.40 A; W=7-28.
PDB; 5XTC; EM; 3.70 A; W=29-144.
PDB; 5XTD; EM; 3.70 A; W=7-144.
PDB; 5XTH; EM; 3.90 A; W=7-144.
PDB; 5XTI; EM; 17.40 A; BW/W=7-144.
PDBsum; 5XTB; -.
PDBsum; 5XTC; -.
PDBsum; 5XTD; -.
PDBsum; 5XTH; -.
PDBsum; 5XTI; -.
ProteinModelPortal; Q9P0J0; -.
SMR; Q9P0J0; -.
BioGrid; 119270; 76.
CORUM; Q9P0J0; -.
DIP; DIP-31180N; -.
IntAct; Q9P0J0; 56.
MINT; MINT-3077817; -.
STRING; 9606.ENSP00000423673; -.
ChEMBL; CHEMBL2363065; -.
DrugBank; DB00157; NADH.
iPTMnet; Q9P0J0; -.
PhosphoSitePlus; Q9P0J0; -.
BioMuta; NDUFA13; -.
DMDM; 20139242; -.
EPD; Q9P0J0; -.
MaxQB; Q9P0J0; -.
PaxDb; Q9P0J0; -.
PeptideAtlas; Q9P0J0; -.
PRIDE; Q9P0J0; -.
TopDownProteomics; Q9P0J0-1; -. [Q9P0J0-1]
Ensembl; ENST00000507754; ENSP00000423673; ENSG00000186010. [Q9P0J0-1]
GeneID; 51079; -.
KEGG; hsa:51079; -.
UCSC; uc021uqu.2; human. [Q9P0J0-1]
CTD; 51079; -.
DisGeNET; 51079; -.
EuPathDB; HostDB:ENSG00000186010.18; -.
GeneCards; NDUFA13; -.
H-InvDB; HIX0213010; -.
HGNC; HGNC:17194; NDUFA13.
HPA; HPA041213; -.
MalaCards; NDUFA13; -.
MIM; 607464; phenotype.
MIM; 609435; gene.
neXtProt; NX_Q9P0J0; -.
OpenTargets; ENSG00000186010; -.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
PharmGKB; PA142671270; -.
eggNOG; KOG3300; Eukaryota.
eggNOG; ENOG4111KIB; LUCA.
GeneTree; ENSGT00390000000719; -.
HOGENOM; HOG000195836; -.
HOVERGEN; HBG019074; -.
InParanoid; Q9P0J0; -.
KO; K11353; -.
OMA; SGYSMFG; -.
PhylomeDB; Q9P0J0; -.
TreeFam; TF315182; -.
Reactome; R-HSA-611105; Respiratory electron transport.
Reactome; R-HSA-6799198; Complex I biogenesis.
ChiTaRS; NDUFA13; human.
GeneWiki; NDUFA13; -.
GenomeRNAi; 51079; -.
PRO; PR:Q9P0J0; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000186010; -.
CleanEx; HS_NDUFA13; -.
ExpressionAtlas; Q9P0J0; baseline and differential.
Genevisible; Q9P0J0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0005746; C:mitochondrial respiratory chain; IDA:UniProtKB.
GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:UniProtKB.
GO; GO:0003954; F:NADH dehydrogenase activity; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:ParkinsonsUK-UCL.
GO; GO:0071300; P:cellular response to retinoic acid; IDA:ParkinsonsUK-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:Reactome.
GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:ParkinsonsUK-UCL.
GO; GO:0010952; P:positive regulation of peptidase activity; IC:ParkinsonsUK-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:ParkinsonsUK-UCL.
GO; GO:0045039; P:protein import into mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
InterPro; IPR009346; GRIM-19.
PANTHER; PTHR12966; PTHR12966; 1.
Pfam; PF06212; GRIM-19; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Disease mutation; Electron transport; Membrane;
Mitochondrion; Mitochondrion inner membrane; Nucleus; Polymorphism;
Primary mitochondrial disease; Reference proteome; Respiratory chain;
Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q95KV7}.
CHAIN 2 144 NADH dehydrogenase [ubiquinone] 1 alpha
subcomplex subunit 13.
/FTId=PRO_0000118804.
TRANSMEM 30 51 Helical. {ECO:0000255}.
REGION 102 144 Important for inducing cell death.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q95KV7}.
VAR_SEQ 143 144 YT -> ALELQPPLADMGRAELSSNATTSLVQRRKQAWGRQ
SWLEQIWNAGPVCQRLHRGGSRPGAGAAGGLSLWAAAARGA
VRSC (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056644.
VARIANT 5 5 K -> N (in a Hurthle cell variant of
papillary carcinoma sample;
dbSNP:rs137852869).
{ECO:0000269|PubMed:15841082}.
/FTId=VAR_045984.
VARIANT 57 57 R -> H (probable disease-associated
mutation found in patients with
mitochondrial complex I deficiency;
dbSNP:rs752513525).
{ECO:0000269|PubMed:25901006}.
/FTId=VAR_078938.
VARIANT 115 115 R -> P (in a Hurthle cell variant of
papillary carcinoma sample).
{ECO:0000269|PubMed:15841082}.
/FTId=VAR_045985.
CONFLICT 2 2 A -> P (in Ref. 3). {ECO:0000305}.
SEQUENCE 144 AA; 16698 MW; 058F608B235FF856 CRC64;
MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMLAIGI GTLIYGHWSI MKWNRERRRL
QIEDFEARIA LLPLLQAETD RRTLQMLREN LEEEAIIMKD VPDWKVGESV FHTTRWVPPL
IGELYGLRTT EEALHASHGF MWYT


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