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

 SDHA_HUMAN              Reviewed;         664 AA.
P31040; A8K5J6; B4DJ60; E9PBJ5; Q16395; Q59GW8; Q8IW48; Q9UMY5;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
12-SEP-2018, entry version 208.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
EC=1.3.5.1 {ECO:0000305|PubMed:24781757};
AltName: Full=Flavoprotein subunit of complex II;
Short=Fp;
Flags: Precursor;
Name=SDHA; Synonyms=SDH2, SDHF;
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).
TISSUE=Liver;
PubMed=7798181;
Hirawake H., Wang H., Kuramochi T., Kojima S., Kita K.;
"Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning
of the flavoprotein (Fp) subunit of liver mitochondria.";
J. Biochem. 116:221-227(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PHE-629 AND
ILE-657.
TISSUE=Heart;
PubMed=8142412; DOI=10.1016/0005-2728(94)90203-8;
Morris A.A.M., Farnsworth L., Ackrell B.A.C., Turnbull D.M.,
Birch-MacHin M.A.;
"The cDNA sequence of the flavoprotein subunit of human heart
succinate dehydrogenase.";
Biochim. Biophys. Acta 1185:125-128(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LS VAL-524.
PubMed=10746566; DOI=10.1007/s004390051033;
Parfait B., Chretien D., Roetig A., Marsac C., Munnich A., Rustin P.;
"Compound heterozygous mutations in the flavoprotein gene of the
respiratory chain complex II in a patient with Leigh syndrome.";
Hum. Genet. 106:236-243(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
VAL-38.
TISSUE=Substantia nigra, and Tongue;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PHE-629.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
PHE-629.
TISSUE=Colon, and Placenta;
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).
[9]
PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
Malcovati M., Marchetti L., Zanelli E., Tenchini M.L.;
"Cloning of the flavoprotein subunit of human succinate
dehydrogenase.";
(In) Curti B., Ronchi S., Zanetti G. (eds.);
Flavins and flavoproteins 1990, pp.727-730, Walter de Gruyter, Berlin
(1991).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 546-562, AND VARIANT LS TRP-554.
PubMed=7550341; DOI=10.1038/ng1095-144;
Bourgeron T., Rustin P., Chretien D., Birch-MacHin M.A., Bourgeois M.,
Viegas-Pequignot E., Munnich A., Roetig A.;
"Mutation of a nuclear succinate dehydrogenase gene results in
mitochondrial respiratory chain deficiency.";
Nat. Genet. 11:144-149(1995).
[11]
PROTEIN SEQUENCE OF 76-92 AND 398-418.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[12]
INTERACTION WITH SDHAF2.
PubMed=19628817; DOI=10.1126/science.1175689;
Hao H.-X., Khalimonchuk O., Schraders M., Dephoure N., Bayley J.-P.,
Kunst H., Devilee P., Cremers C.W.R.J., Schiffman J.D., Bentz B.G.,
Gygi S.P., Winge D.R., Kremer H., Rutter J.;
"SDH5, a gene required for flavination of succinate dehydrogenase, is
mutated in paraganglioma.";
Science 325:1139-1142(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-335; LYS-541 AND
LYS-608, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
FUNCTION, VARIANT PGL5 TRP-589, AND CHARACTERIZATION OF VARIANT PGL5
TRP-589.
PubMed=20484225; DOI=10.1093/hmg/ddq206;
Burnichon N., Briere J.J., Libe R., Vescovo L., Riviere J.,
Tissier F., Jouanno E., Jeunemaitre X., Benit P., Tzagoloff A.,
Rustin P., Bertherat J., Favier J., Gimenez-Roqueplo A.P.;
"SDHA is a tumor suppressor gene causing paraganglioma.";
Hum. Mol. Genet. 19:3011-3020(2010).
[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]
PHOSPHORYLATION AT TYR-215 BY SRC.
PubMed=22823520; DOI=10.1042/BJ20120509;
Ogura M., Yamaki J., Homma M.K., Homma Y.;
"Mitochondrial c-Src regulates cell survival through phosphorylation
of respiratory chain components.";
Biochem. J. 447:281-289(2012).
[17]
INTERACTION WITH TRAP1.
PubMed=23747254; DOI=10.1016/j.cmet.2013.04.019;
Sciacovelli M., Guzzo G., Morello V., Frezza C., Zheng L., Nannini N.,
Calabrese F., Laudiero G., Esposito F., Landriscina M., Defilippi P.,
Bernardi P., Rasola A.;
"The mitochondrial chaperone TRAP1 promotes neoplastic growth by
inhibiting succinate dehydrogenase.";
Cell Metab. 17:988-999(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
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).
[20]
VARIANT MT-C2D GLU-555.
PubMed=12794685; DOI=10.1002/ajmg.a.10202;
Van Coster R., Seneca S., Smet J., Van Hecke R., Gerlo E.,
Devreese B., Van Beeumen J., Leroy J.G., De Meirleir L., Lissens W.;
"Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa
flavoprotein gene causes instability of the respiratory chain complex
II.";
Am. J. Med. Genet. A 120:13-18(2003).
[21]
VARIANT CMD1GG GLU-555.
PubMed=20551992; DOI=10.1038/ejhg.2010.83;
Levitas A., Muhammad E., Harel G., Saada A., Caspi V.C., Manor E.,
Beck J.C., Sheffield V., Parvari R.;
"Familial neonatal isolated cardiomyopathy caused by a mutation in the
flavoprotein subunit of succinate dehydrogenase.";
Eur. J. Hum. Genet. 18:1160-1165(2010).
[22]
VARIANT LS GLY-189, CHARACTERIZATION OF VARIANT LS GLY-189, FUNCTION,
CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=24781757; DOI=10.1038/ejhg.2014.80;
Renkema G.H., Wortmann S.B., Smeets R.J., Venselaar H., Antoine M.,
Visser G., Ben-Omran T., van den Heuvel L.P., Timmers H.J.,
Smeitink J.A., Rodenburg R.J.;
"SDHA mutations causing a multisystem mitochondrial disease: novel
mutations and genetic overlap with hereditary tumors.";
Eur. J. Hum. Genet. 23:202-209(2015).
-!- 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) (PubMed:24781757). Can act as
a tumor suppressor (PubMed:20484225).
{ECO:0000269|PubMed:20484225, ECO:0000305|PubMed:24781757}.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000305|PubMed:24781757}.
-!- 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:0000305|PubMed:24781757}.
-!- 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 (PubMed:19628817). Interacts with TRAP1
(PubMed:23747254). {ECO:0000250|UniProtKB:Q0QF01,
ECO:0000269|PubMed:19628817, ECO:0000269|PubMed:23747254}.
-!- INTERACTION:
P26045:PTPN3; NbExp=2; IntAct=EBI-1057265, EBI-1047946;
Q9NX18:SDHAF2; NbExp=2; IntAct=EBI-1057265, EBI-713250;
P21912:SDHB; NbExp=8; IntAct=EBI-1057265, EBI-1056481;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q0QF01}; Matrix side
{ECO:0000250|UniProtKB:Q0QF01}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P31040-1; Sequence=Displayed;
Name=2;
IsoId=P31040-2; Sequence=VSP_055077;
Note=No experimental confirmation available.;
Name=3;
IsoId=P31040-3; Sequence=VSP_055078;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation at Tyr-215 is important for efficient
electron transfer in complex II and the prevention of ROS
generation. {ECO:0000269|PubMed:22823520}.
-!- PTM: Acetylated. Deacetylated by SIRT3.
{ECO:0000250|UniProtKB:Q8K2B3}.
-!- DISEASE: Mitochondrial complex II deficiency (MT-C2D)
[MIM:252011]: A disorder of the mitochondrial respiratory chain
with heterogeneous clinical manifestations. Clinical features
include psychomotor regression in infants, poor growth with lack
of speech development, severe spastic quadriplegia, dystonia,
progressive leukoencephalopathy, muscle weakness, exercise
intolerance, cardiomyopathy. Some patients manifest Leigh syndrome
or Kearns-Sayre syndrome. Note=The disease is caused by mutations
affecting the gene represented in this entry.
{ECO:0000269|PubMed:12794685}.
-!- DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset
progressive neurodegenerative disorder characterized by the
presence of focal, bilateral lesions in one or more areas of the
central nervous system including the brainstem, thalamus, basal
ganglia, cerebellum and spinal cord. Clinical features depend on
which areas of the central nervous system are involved and include
subacute onset of psychomotor retardation, hypotonia, ataxia,
weakness, vision loss, eye movement abnormalities, seizures, and
dysphagia. {ECO:0000269|PubMed:10746566,
ECO:0000269|PubMed:24781757, ECO:0000269|PubMed:7550341}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cardiomyopathy, dilated 1GG (CMD1GG) [MIM:613642]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:20551992}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Paragangliomas 5 (PGL5) [MIM:614165]: A neural crest
tumor usually derived from the chromoreceptor tissue of a
paraganglion. Paragangliomas can develop at various body sites,
including the head, neck, thorax and abdomen. Most commonly, they
are located in the head and neck region, specifically at the
carotid bifurcation, the jugular foramen, the vagal nerve, and in
the middle ear. {ECO:0000269|PubMed:20484225}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92228.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA37886.1; Type=Miscellaneous discrepancy; Note=Differs extensively from that shown.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=TCA Cycle Gene Mutation Database;
URL="http://databases.lovd.nl/shared/genes/SDHA";
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EMBL; D30648; BAA06332.1; -; mRNA.
EMBL; L21936; AAA20683.1; -; mRNA.
EMBL; AF171030; AAD51006.1; -; Genomic_DNA.
EMBL; AF171017; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171018; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171019; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171020; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171021; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171022; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171023; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171024; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171025; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171026; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171027; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171028; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AF171029; AAD51006.1; JOINED; Genomic_DNA.
EMBL; AK291311; BAF84000.1; -; mRNA.
EMBL; AK295937; BAG58722.1; -; mRNA.
EMBL; AB208991; BAD92228.1; ALT_INIT; mRNA.
EMBL; AC021087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471235; EAW50983.1; -; Genomic_DNA.
EMBL; BC001380; AAH01380.1; -; mRNA.
EMBL; BC041016; AAH41016.1; -; mRNA.
EMBL; X53943; CAA37886.1; ALT_SEQ; mRNA.
EMBL; S79641; AAB35332.1; -; Genomic_DNA.
CCDS; CCDS3853.1; -. [P31040-1]
CCDS; CCDS77992.1; -. [P31040-2]
PIR; JX0336; JX0336.
PIR; S21302; S21302.
RefSeq; NP_001281261.1; NM_001294332.1. [P31040-2]
RefSeq; NP_004159.2; NM_004168.3. [P31040-1]
UniGene; Hs.440475; -.
ProteinModelPortal; P31040; -.
SMR; P31040; -.
BioGrid; 112290; 223.
ComplexPortal; CPX-561; Mitochondrial respiratory chain complex II.
CORUM; P31040; -.
DIP; DIP-45851N; -.
IntAct; P31040; 147.
MINT; P31040; -.
STRING; 9606.ENSP00000264932; -.
ChEMBL; CHEMBL5758; -.
DrugBank; DB04657; Carboxin.
DrugBank; DB00139; Succinic acid.
DrugBank; DB04795; Thenoyltrifluoroacetone.
DrugBank; DB08689; UBIQUINONE-1.
iPTMnet; P31040; -.
PhosphoSitePlus; P31040; -.
SwissPalm; P31040; -.
BioMuta; SDHA; -.
DMDM; 1169337; -.
REPRODUCTION-2DPAGE; IPI00305166; -.
EPD; P31040; -.
MaxQB; P31040; -.
PaxDb; P31040; -.
PeptideAtlas; P31040; -.
PRIDE; P31040; -.
ProteomicsDB; 54758; -.
TopDownProteomics; P31040-1; -. [P31040-1]
DNASU; 6389; -.
Ensembl; ENST00000264932; ENSP00000264932; ENSG00000073578. [P31040-1]
Ensembl; ENST00000510361; ENSP00000427703; ENSG00000073578. [P31040-2]
GeneID; 6389; -.
KEGG; hsa:6389; -.
UCSC; uc003jao.5; human. [P31040-1]
CTD; 6389; -.
DisGeNET; 6389; -.
EuPathDB; HostDB:ENSG00000073578.16; -.
GeneCards; SDHA; -.
GeneReviews; SDHA; -.
H-InvDB; HIX0120996; -.
HGNC; HGNC:10680; SDHA.
HPA; CAB034929; -.
HPA; HPA041981; -.
HPA; HPA064582; -.
MalaCards; SDHA; -.
MIM; 252011; phenotype.
MIM; 256000; phenotype.
MIM; 600857; gene.
MIM; 613642; phenotype.
MIM; 614165; phenotype.
neXtProt; NX_P31040; -.
OpenTargets; ENSG00000073578; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 44890; Gastrointestinal stromal tumor.
Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
Orphanet; 3208; Isolated succinate-CoQ reductase deficiency.
Orphanet; 255241; Leigh syndrome with leukodystrophy.
PharmGKB; PA35605; -.
eggNOG; KOG2403; Eukaryota.
eggNOG; COG1053; LUCA.
GeneTree; ENSGT00910000144277; -.
HOGENOM; HOG000160475; -.
HOVERGEN; HBG001461; -.
InParanoid; P31040; -.
KO; K00234; -.
OMA; GDSPWEH; -.
OrthoDB; EOG091G041Z; -.
PhylomeDB; P31040; -.
TreeFam; TF300763; -.
BioCyc; MetaCyc:ENSG00000073578-MONOMER; -.
Reactome; R-HSA-611105; Respiratory electron transport.
Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
SIGNOR; P31040; -.
UniPathway; UPA00223; UER01006.
ChiTaRS; SDHA; human.
GeneWiki; SDHA; -.
GenomeRNAi; 6389; -.
PRO; PR:P31040; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000073578; Expressed in 95 organ(s), highest expression level in apex of heart.
CleanEx; HS_SDHA; -.
ExpressionAtlas; P31040; baseline and differential.
Genevisible; P31040; HS.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
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; IMP: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; IMP:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0022904; P:respiratory electron transport chain; IDA:UniProtKB.
GO; GO:0006105; P:succinate metabolic process; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB.
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; Alternative splicing; Cardiomyopathy; Complete proteome;
Direct protein sequencing; Disease mutation; Electron transport; FAD;
Flavoprotein; Leigh syndrome; Membrane; Mitochondrion;
Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
Polymorphism; Primary mitochondrial disease; 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_0000010335.
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:0000250|UniProtKB:Q8K2B3}.
MOD_RES 179 179 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 179 179 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 215 215 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:22823520}.
MOD_RES 250 250 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 250 250 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 335 335 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 335 335 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 480 480 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 485 485 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 485 485 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 498 498 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 498 498 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 517 517 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 538 538 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 538 538 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 541 541 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 547 547 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 547 547 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 550 550 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 598 598 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 608 608 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 615 615 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 624 624 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 647 647 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
VAR_SEQ 105 152 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055077.
VAR_SEQ 126 270 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055078.
VARIANT 33 33 F -> V (in dbSNP:rs1061518).
/FTId=VAR_049214.
VARIANT 38 38 D -> V (in dbSNP:rs34635677).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_049215.
VARIANT 189 189 C -> G (in LS; decrease in succinate
dehydrogenase activity).
{ECO:0000269|PubMed:24781757}.
/FTId=VAR_074022.
VARIANT 240 240 E -> Q (in dbSNP:rs1041946).
/FTId=VAR_049216.
VARIANT 333 333 V -> I (in dbSNP:rs1062468).
/FTId=VAR_059307.
VARIANT 524 524 A -> V (in LS; dbSNP:rs137852767).
{ECO:0000269|PubMed:10746566}.
/FTId=VAR_016878.
VARIANT 554 554 R -> W (in LS; dbSNP:rs9809219).
{ECO:0000269|PubMed:7550341}.
/FTId=VAR_002449.
VARIANT 555 555 G -> E (in MT-C2D and CMD1GG;
dbSNP:rs137852768).
{ECO:0000269|PubMed:12794685,
ECO:0000269|PubMed:20551992}.
/FTId=VAR_016879.
VARIANT 589 589 R -> W (in PGL5; loss of activity;
dbSNP:rs387906780).
{ECO:0000269|PubMed:20484225}.
/FTId=VAR_065975.
VARIANT 629 629 Y -> F (in dbSNP:rs6960).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8142412,
ECO:0000269|Ref.5}.
/FTId=VAR_071037.
VARIANT 657 657 V -> I (in dbSNP:rs6962).
{ECO:0000269|PubMed:8142412}.
/FTId=VAR_049217.
CONFLICT 356 356 G -> D (in Ref. 3; AAD51006).
{ECO:0000305}.
CONFLICT 398 398 E -> D (in Ref. 3; AAD51006).
{ECO:0000305}.
CONFLICT 591 591 A -> T (in Ref. 3; AAD51006).
{ECO:0000305}.
CONFLICT 596 596 D -> G (in Ref. 3; AAD51006).
{ECO:0000305}.
CONFLICT 600 600 R -> Q (in Ref. 3; AAD51006).
{ECO:0000305}.
CONFLICT 618 618 F -> L (in Ref. 4; BAG58722).
{ECO:0000305}.
CONFLICT 640 640 E -> G (in Ref. 3; AAD51006).
{ECO:0000305}.
SEQUENCE 664 AA; 72692 MW; 180B664E3FFD0B34 CRC64;
MSGVRGLSRL LSARRLALAK AWPTVLQTGT RGFHFTVDGN KRASAKVSDS ISAQYPVVDH
EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK
VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS
KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVGTGKVTLE YRPVIDKTLN EADCATVPPA
IRSY


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