NDUV2_HUMAN
ID NDUV2_HUMAN Reviewed; 249 AA.
AC P19404; Q9BV41;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFV2;
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], AND VARIANT ALA-29.
RX PubMed=2500970; DOI=10.1021/bi00434a021;
RA Pilkington S.J., Walker J.E.;
RT "Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of
RT import precursors of the bovine and human 24-kDa subunit.";
RL Biochemistry 28:3257-3264(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION AT TYR-193.
RX PubMed=22823520; DOI=10.1042/bj20120509;
RA Ogura M., Yamaki J., Homma M.K., Homma Y.;
RT "Mitochondrial c-Src regulates cell survival through phosphorylation of
RT respiratory chain components.";
RL Biochem. J. 447:281-289(2012).
RN [6]
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 [7]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ASN-32, AND
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 [8]
RP INVOLVEMENT IN MC1DN7.
RX PubMed=12754703; DOI=10.1002/humu.10225;
RA Benit P., Beugnot R., Chretien D., Giurgea I., De Lonlay-Debeney P.,
RA Issartel J.P., Corral-Debrinski M., Kerscher S., Rustin P., Roetig A.,
RA Munnich A.;
RT "Mutant NDUFV2 subunit of mitochondrial complex I causes early onset
RT hypertrophic cardiomyopathy and encephalopathy.";
RL Hum. Mutat. 21:582-586(2003).
RN [9]
RP INVOLVEMENT IN MC1DN7.
RX PubMed=26008862; DOI=10.1016/j.ejpn.2015.05.002;
RA Cameron J.M., MacKay N., Feigenbaum A., Tarnopolsky M., Blaser S.,
RA Robinson B.H., Schulze A.;
RT "Exome sequencing identifies complex I NDUFV2 mutations as a novel cause of
RT Leigh syndrome.";
RL Eur. J. Paediatr. Neurol. 19:525-532(2015).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor. {ECO:0000250|UniProtKB:P04394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. This is a component of
CC the flavoprotein-sulfur (FP) fragment of the enzyme.
CC {ECO:0000269|PubMed:12611891}.
CC -!- INTERACTION:
CC P19404; P63010-2: AP2B1; NbExp=3; IntAct=EBI-713665, EBI-11529439;
CC P19404; Q9BZZ5-2: API5; NbExp=3; IntAct=EBI-713665, EBI-10989614;
CC P19404; P05067: APP; NbExp=3; IntAct=EBI-713665, EBI-77613;
CC P19404; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-713665, EBI-14199987;
CC P19404; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-713665, EBI-9089489;
CC P19404; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-713665, EBI-2410266;
CC P19404; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-713665, EBI-2837444;
CC P19404; P62158: CALM3; NbExp=3; IntAct=EBI-713665, EBI-397435;
CC P19404; P24863: CCNC; NbExp=6; IntAct=EBI-713665, EBI-395261;
CC P19404; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-713665, EBI-350590;
CC P19404; Q96HD1-2: CRELD1; NbExp=3; IntAct=EBI-713665, EBI-21536433;
CC P19404; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-713665, EBI-2872414;
CC P19404; P35222: CTNNB1; NbExp=3; IntAct=EBI-713665, EBI-491549;
CC P19404; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-713665, EBI-11526226;
CC P19404; P20042: EIF2S2; NbExp=3; IntAct=EBI-713665, EBI-711977;
CC P19404; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-713665, EBI-10973142;
CC P19404; O15287: FANCG; NbExp=3; IntAct=EBI-713665, EBI-81610;
CC P19404; Q9Y261-2: FOXA2; NbExp=3; IntAct=EBI-713665, EBI-25830360;
CC P19404; P06241-3: FYN; NbExp=3; IntAct=EBI-713665, EBI-10691738;
CC P19404; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-713665, EBI-712073;
CC P19404; Q7L7L0: H2AW; NbExp=3; IntAct=EBI-713665, EBI-5325551;
CC P19404; Q71DI3: H3C15; NbExp=3; IntAct=EBI-713665, EBI-750650;
CC P19404; P61978: HNRNPK; NbExp=3; IntAct=EBI-713665, EBI-304185;
CC P19404; Q8IWL3: HSCB; NbExp=6; IntAct=EBI-713665, EBI-1805738;
CC P19404; Q92613: JADE3; NbExp=3; IntAct=EBI-713665, EBI-10278909;
CC P19404; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-713665, EBI-714379;
CC P19404; Q14525: KRT33B; NbExp=3; IntAct=EBI-713665, EBI-1049638;
CC P19404; Q96PV6: LENG8; NbExp=3; IntAct=EBI-713665, EBI-739546;
CC P19404; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-713665, EBI-9088829;
CC P19404; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-713665, EBI-739832;
CC P19404; P43356: MAGEA2B; NbExp=3; IntAct=EBI-713665, EBI-5650739;
CC P19404; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-713665, EBI-8487781;
CC P19404; Q9Y3D2: MSRB2; NbExp=3; IntAct=EBI-713665, EBI-9092052;
CC P19404; Q99457: NAP1L3; NbExp=3; IntAct=EBI-713665, EBI-8645631;
CC P19404; Q6X4W1-6: NSMF; NbExp=3; IntAct=EBI-713665, EBI-25842707;
CC P19404; O15381-5: NVL; NbExp=3; IntAct=EBI-713665, EBI-18577082;
CC P19404; Q16625: OCLN; NbExp=3; IntAct=EBI-713665, EBI-2903088;
CC P19404; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-713665, EBI-1058491;
CC P19404; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-713665, EBI-25830200;
CC P19404; P32242: OTX1; NbExp=3; IntAct=EBI-713665, EBI-740446;
CC P19404; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-713665, EBI-10694433;
CC P19404; Q16549: PCSK7; NbExp=3; IntAct=EBI-713665, EBI-8059854;
CC P19404; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-713665, EBI-349819;
CC P19404; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-713665, EBI-2339674;
CC P19404; O75925: PIAS1; NbExp=3; IntAct=EBI-713665, EBI-629434;
CC P19404; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-713665, EBI-10694821;
CC P19404; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-713665, EBI-710402;
CC P19404; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-713665, EBI-25835994;
CC P19404; P57729: RAB38; NbExp=3; IntAct=EBI-713665, EBI-6552718;
CC P19404; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-713665, EBI-11984839;
CC P19404; Q9NS23-4: RASSF1; NbExp=6; IntAct=EBI-713665, EBI-438710;
CC P19404; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-713665, EBI-960502;
CC P19404; P57052: RBM11; NbExp=3; IntAct=EBI-713665, EBI-741332;
CC P19404; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-713665, EBI-25829984;
CC P19404; Q96D59: RNF183; NbExp=3; IntAct=EBI-713665, EBI-743938;
CC P19404; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-713665, EBI-11528848;
CC P19404; Q6AZY7-2: SCARA3; NbExp=3; IntAct=EBI-713665, EBI-21598366;
CC P19404; O95391: SLU7; NbExp=3; IntAct=EBI-713665, EBI-750559;
CC P19404; Q12824: SMARCB1; NbExp=3; IntAct=EBI-713665, EBI-358419;
CC P19404; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-713665, EBI-358489;
CC P19404; Q92673: SORL1; NbExp=3; IntAct=EBI-713665, EBI-1171329;
CC P19404; Q8NHS9: SPATA22; NbExp=3; IntAct=EBI-713665, EBI-7067260;
CC P19404; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-713665, EBI-2510414;
CC P19404; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-713665, EBI-5235340;
CC P19404; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-713665, EBI-7082156;
CC P19404; Q9BR01-2: SULT4A1; NbExp=3; IntAct=EBI-713665, EBI-25831443;
CC P19404; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-713665, EBI-741515;
CC P19404; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-713665, EBI-11525489;
CC P19404; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-713665, EBI-10259086;
CC P19404; P07437: TUBB; NbExp=3; IntAct=EBI-713665, EBI-350864;
CC P19404; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-713665, EBI-9088812;
CC P19404; P10599: TXN; NbExp=3; IntAct=EBI-713665, EBI-594644;
CC P19404; O75436: VPS26A; NbExp=3; IntAct=EBI-713665, EBI-1043891;
CC P19404; P58304: VSX2; NbExp=3; IntAct=EBI-713665, EBI-6427899;
CC P19404; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-713665, EBI-358545;
CC P19404; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-713665, EBI-7705033;
CC P19404; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-713665, EBI-12040603;
CC P19404; P17023: ZNF19; NbExp=3; IntAct=EBI-713665, EBI-12884200;
CC P19404; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-713665, EBI-749023;
CC P19404; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-713665, EBI-11741890;
CC P19404; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-713665, EBI-12010736;
CC P19404; P10073: ZSCAN22; NbExp=3; IntAct=EBI-713665, EBI-10178224;
CC P19404; Q86V28; NbExp=3; IntAct=EBI-713665, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04394}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04394}; Matrix side
CC {ECO:0000250|UniProtKB:P04394}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 7 (MC1DN7)
CC [MIM:618229]: 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. MC1DN7 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:12754703,
CC ECO:0000269|PubMed:26008862}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M22538; AAA75390.1; -; mRNA.
DR EMBL; BC001632; AAH01632.1; -; mRNA.
DR EMBL; BC017487; AAH17487.1; -; mRNA.
DR CCDS; CCDS11842.1; -.
DR PIR; A30113; A30113.
DR RefSeq; NP_066552.2; NM_021074.4.
DR PDB; 5XTB; EM; 3.40 A; O=36-247.
DR PDB; 5XTD; EM; 3.70 A; O=36-247.
DR PDB; 5XTH; EM; 3.90 A; O=36-247.
DR PDB; 5XTI; EM; 17.40 A; BO/O=36-247.
DR PDBsum; 5XTB; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P19404; -.
DR SMR; P19404; -.
DR BioGRID; 110807; 205.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; P19404; -.
DR IntAct; P19404; 134.
DR MINT; P19404; -.
DR STRING; 9606.ENSP00000327268; -.
DR BindingDB; P19404; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; P19404; -.
DR GlyGen; P19404; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19404; -.
DR PhosphoSitePlus; P19404; -.
DR SwissPalm; P19404; -.
DR BioMuta; NDUFV2; -.
DR DMDM; 20455499; -.
DR SWISS-2DPAGE; P19404; -.
DR UCD-2DPAGE; P19404; -.
DR EPD; P19404; -.
DR jPOST; P19404; -.
DR MassIVE; P19404; -.
DR MaxQB; P19404; -.
DR PaxDb; P19404; -.
DR PeptideAtlas; P19404; -.
DR PRIDE; P19404; -.
DR ProteomicsDB; 53655; -.
DR TopDownProteomics; P19404; -.
DR Antibodypedia; 1273; 287 antibodies from 32 providers.
DR DNASU; 4729; -.
DR Ensembl; ENST00000318388.11; ENSP00000327268.6; ENSG00000178127.13.
DR GeneID; 4729; -.
DR KEGG; hsa:4729; -.
DR MANE-Select; ENST00000318388.11; ENSP00000327268.6; NM_021074.5; NP_066552.2.
DR UCSC; uc002knu.3; human.
DR CTD; 4729; -.
DR DisGeNET; 4729; -.
DR GeneCards; NDUFV2; -.
DR HGNC; HGNC:7717; NDUFV2.
DR HPA; ENSG00000178127; Tissue enhanced (skeletal).
DR MalaCards; NDUFV2; -.
DR MIM; 600532; gene.
DR MIM; 618229; phenotype.
DR neXtProt; NX_P19404; -.
DR OpenTargets; ENSG00000178127; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR Orphanet; 255241; Leigh syndrome with leukodystrophy.
DR PharmGKB; PA31527; -.
DR VEuPathDB; HostDB:ENSG00000178127; -.
DR eggNOG; KOG3196; Eukaryota.
DR GeneTree; ENSGT00390000017580; -.
DR HOGENOM; CLU_054362_1_0_1; -.
DR InParanoid; P19404; -.
DR OMA; VGKFHVQ; -.
DR OrthoDB; 1396088at2759; -.
DR PhylomeDB; P19404; -.
DR TreeFam; TF300004; -.
DR BioCyc; MetaCyc:HS11253-MON; -.
DR PathwayCommons; P19404; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; P19404; -.
DR SIGNOR; P19404; -.
DR BioGRID-ORCS; 4729; 117 hits in 1092 CRISPR screens.
DR ChiTaRS; NDUFV2; human.
DR GeneWiki; NDUFV2; -.
DR GenomeRNAi; 4729; -.
DR Pharos; P19404; Tclin.
DR PRO; PR:P19404; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P19404; protein.
DR Bgee; ENSG00000178127; Expressed in apex of heart and 98 other tissues.
DR ExpressionAtlas; P19404; baseline and differential.
DR Genevisible; P19404; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Acetylation; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Phosphoprotein; Primary mitochondrial disease;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transport; Ubiquinone.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 33..249
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 2,
FT mitochondrial"
FT /id="PRO_0000020003"
FT REGION 213..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D6J6"
FT MOD_RES 193
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:22823520"
FT VARIANT 29
FT /note="V -> A (in dbSNP:rs906807)"
FT /evidence="ECO:0000269|PubMed:2500970"
FT /id="VAR_016167"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5XTB"
SQ SEQUENCE 249 AA; 27392 MW; AAF46ABB0908B177 CRC64;
MFFSAALRAR AAGLTAHWGR HVRNLHKTVM QNGAGGALFV HRDTPENNPD TPFDFTPENY
KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT
MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC
VNAPMVQIND NYYEDLTAKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG
PGFGVQAGL
