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Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp)

 SDHA_MOUSE              Reviewed;         664 AA.
Q8K2B3; Q0QF19; Q3UH25; Q3UKP7; Q3V4B1; Q921P5; Q9Z1Z4;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
12-SEP-2018, entry version 144.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
AltName: Full=Flavoprotein subunit of complex II;
Short=Fp;
Flags: Precursor;
Name=Sdha;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, Heart, Pancreas, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
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).
[3]
PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282;
313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND
637-647.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-609.
TISSUE=Liver;
PubMed=16751257; DOI=10.1093/molbev/msl027;
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
"Housekeeping genes for phylogenetic analysis of eutherian
relationships.";
Mol. Biol. Evol. 23:1493-1503(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
TISSUE=Heart;
Weinreich D.M.;
"OXPHOS genes in mammals and the molecular clock.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
ACETYLATION AT LYS-179; LYS-182; LYS-250; LYS-335; LYS-480; LYS-485;
LYS-498; LYS-547; LYS-550; LYS-598; LYS-608; LYS-624 AND LYS-633, AND
DEACETYLATION BY SIRT3.
PubMed=21858060; DOI=10.1371/journal.pone.0023295;
Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V.,
Gygi S.P., Haigis M.C.;
"Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase
activity.";
PLoS ONE 6:E23295-E23295(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-547,
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-250; LYS-335;
LYS-485; LYS-498; LYS-538; LYS-547 AND LYS-615, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-179; LYS-182;
LYS-335; LYS-423; LYS-498; LYS-517; LYS-538; LYS-547; LYS-608; LYS-636
AND LYS-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
(SDH) that is involved in complex II of the mitochondrial electron
transport chain and is responsible for transferring electrons from
succinate to ubiquinone (coenzyme Q). Can act as a tumor
suppressor. {ECO:0000250|UniProtKB:P31040}.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000250|UniProtKB:P31040}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:Q0QF01};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000250|UniProtKB:P31040}.
-!- SUBUNIT: Component of complex II composed of four subunits: the
flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
cytochrome b560 composed of SDHC and SDHD (By similarity).
Interacts with SDHAF2/SDH5; interaction is required for FAD
attachment (By similarity). Interacts with TRAP1 (By similarity).
{ECO:0000250|UniProtKB:P31040, ECO:0000250|UniProtKB:Q0QF01}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q0QF01}; Matrix side
{ECO:0000250|UniProtKB:Q0QF01}.
-!- PTM: Acetylation of Lys-498 and Lys-538 is observed in liver
mitochondria from fasted mice but not from fed mice. Deacetylated
by SIRT3. {ECO:0000269|PubMed:21858060}.
-!- PTM: Phosphorylation at Tyr-215 is important for efficient
electron transfer in complex II and the prevention of ROS
generation. {ECO:0000250|UniProtKB:P31040}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
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EMBL; AK029520; BAC26491.1; -; mRNA.
EMBL; AK034928; BAC28884.1; -; mRNA.
EMBL; AK049590; BAC33831.1; -; mRNA.
EMBL; AK050475; BAC34276.1; -; mRNA.
EMBL; AK075990; BAC36101.1; -; mRNA.
EMBL; AK145923; BAE26754.1; -; mRNA.
EMBL; AK147286; BAE27822.1; -; mRNA.
EMBL; AK147624; BAE28032.1; -; mRNA.
EMBL; AK153085; BAE31710.1; -; mRNA.
EMBL; AK162148; BAE36754.1; -; mRNA.
EMBL; AK169254; BAE41018.1; -; mRNA.
EMBL; AK004362; BAE43173.1; -; mRNA.
EMBL; BC011301; AAH11301.1; -; mRNA.
EMBL; BC031849; AAH31849.1; -; mRNA.
EMBL; DQ402975; ABD77308.1; -; mRNA.
EMBL; AF095938; AAC72373.1; -; mRNA.
CCDS; CCDS26643.1; -.
RefSeq; NP_075770.1; NM_023281.1.
UniGene; Mm.158231; -.
ProteinModelPortal; Q8K2B3; -.
SMR; Q8K2B3; -.
BioGrid; 211828; 2.
ComplexPortal; CPX-562; Mitochondrial respiratory chain complex II.
CORUM; Q8K2B3; -.
IntAct; Q8K2B3; 23.
MINT; Q8K2B3; -.
STRING; 10090.ENSMUSP00000022062; -.
CarbonylDB; Q8K2B3; -.
iPTMnet; Q8K2B3; -.
PhosphoSitePlus; Q8K2B3; -.
SwissPalm; Q8K2B3; -.
REPRODUCTION-2DPAGE; Q8K2B3; -.
EPD; Q8K2B3; -.
MaxQB; Q8K2B3; -.
PaxDb; Q8K2B3; -.
PeptideAtlas; Q8K2B3; -.
PRIDE; Q8K2B3; -.
Ensembl; ENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
GeneID; 66945; -.
KEGG; mmu:66945; -.
UCSC; uc007rfa.1; mouse.
CTD; 6389; -.
MGI; MGI:1914195; Sdha.
eggNOG; KOG2403; Eukaryota.
eggNOG; COG1053; LUCA.
GeneTree; ENSGT00910000144277; -.
HOVERGEN; HBG001461; -.
InParanoid; Q8K2B3; -.
KO; K00234; -.
OMA; GDSPWEH; -.
OrthoDB; EOG091G041Z; -.
PhylomeDB; Q8K2B3; -.
TreeFam; TF300763; -.
Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
UniPathway; UPA00223; UER01006.
ChiTaRS; Sdha; mouse.
PRO; PR:Q8K2B3; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021577; Expressed in 321 organ(s), highest expression level in brown adipose tissue.
ExpressionAtlas; Q8K2B3; baseline and differential.
Genevisible; Q8K2B3; MM.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
GO; GO:0007399; P:nervous system development; ISO:MGI.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
Gene3D; 3.50.50.60; -; 2.
Gene3D; 3.90.700.10; -; 1.
InterPro; IPR003953; FAD-binding_2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR003952; FRD_SDH_FAD_BS.
InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
InterPro; IPR011281; Succ_DH_flav_su_fwd.
InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
Pfam; PF00890; FAD_binding_2; 1.
Pfam; PF02910; Succ_DH_flav_C; 1.
SUPFAM; SSF46977; SSF46977; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF56425; SSF56425; 1.
TIGRFAMs; TIGR01816; sdhA_forward; 1.
TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide; Transport;
Tricarboxylic acid cycle; Tumor suppressor.
TRANSIT 1 42 Mitochondrion.
{ECO:0000250|UniProtKB:Q0QF01}.
CHAIN 43 664 Succinate dehydrogenase [ubiquinone]
flavoprotein subunit, mitochondrial.
/FTId=PRO_0000010337.
NP_BIND 68 73 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
NP_BIND 91 106 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
NP_BIND 456 457 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
ACT_SITE 340 340 Proton acceptor.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 275 275 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
BINDING 296 296 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
BINDING 308 308 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
BINDING 407 407 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
BINDING 440 440 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
BINDING 451 451 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
MOD_RES 99 99 Tele-8alpha-FAD histidine.
{ECO:0000250|UniProtKB:Q0QF01}.
MOD_RES 167 167 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 179 179 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337,
ECO:0000269|PubMed:21858060}.
MOD_RES 179 179 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000244|PubMed:23576753,
ECO:0000269|PubMed:21858060}.
MOD_RES 215 215 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 250 250 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:21858060}.
MOD_RES 250 250 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 335 335 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000269|PubMed:21858060}.
MOD_RES 335 335 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 423 423 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 480 480 N6-acetyllysine.
{ECO:0000269|PubMed:21858060}.
MOD_RES 485 485 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:21858060}.
MOD_RES 485 485 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 498 498 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000269|PubMed:21858060}.
MOD_RES 498 498 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 517 517 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 538 538 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 538 538 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 547 547 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337,
ECO:0000269|PubMed:21858060}.
MOD_RES 547 547 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 550 550 N6-acetyllysine.
{ECO:0000269|PubMed:21858060}.
MOD_RES 598 598 N6-acetyllysine.
{ECO:0000269|PubMed:21858060}.
MOD_RES 608 608 N6-acetyllysine.
{ECO:0000244|PubMed:23576753,
ECO:0000269|PubMed:21858060}.
MOD_RES 615 615 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 624 624 N6-acetyllysine.
{ECO:0000269|PubMed:21858060}.
MOD_RES 633 633 N6-acetyllysine.
{ECO:0000269|PubMed:21858060}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 647 647 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
CONFLICT 69 69 A -> V (in Ref. 1; BAE26754).
{ECO:0000305}.
CONFLICT 246 246 R -> Q (in Ref. 1; BAE26754).
{ECO:0000305}.
CONFLICT 428 428 Q -> R (in Ref. 1; BAE26754).
{ECO:0000305}.
CONFLICT 501 501 F -> L (in Ref. 4; ABD77308).
{ECO:0000305}.
CONFLICT 517 517 K -> M (in Ref. 4; ABD77308).
{ECO:0000305}.
CONFLICT 571 571 L -> M (in Ref. 4; ABD77308).
{ECO:0000305}.
SEQUENCE 664 AA; 72585 MW; DDCE1535163C9449 CRC64;
MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA ISTQYPVVDH
EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
DGSIHRIRAK NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
VLKHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK
VPSIKANAGE ESVMNLDKLR FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS
QLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN EADCATVPPA
IRSY


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EIAAB26813 Bos taurus,Bovine,CI-51kD,Complex I-51kD,NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial,NADH dehydrogenase flavoprotein 1,NADH-ubiquinone oxidoreductase 51 kDa subunit,NDUFV1,UQOR1
PE019854h Recombinant human Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial protein 1mg
PE019854h Recombinant human Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial protein 50ug
H3490 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (SDHA), Human, ELISA Kit 96T
CSB-EL020903CH Chicken Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial(SDHA) ELISA kit 96T
CSB-RP019894h Recombinant human Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial protein 500ug
CSB-EL020903RA Rat Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial(SDHA) ELISA kit SpeciesRat 96T


 

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