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Database: UniProt/SWISS-PROT
Entry: SDHB_HUMAN
LinkDB: SDHB_HUMAN
Original site: SDHB_HUMAN 
ID   SDHB_HUMAN              Reviewed;         280 AA.
AC   P21912; B2R545; Q0QEY7; Q9NQ12;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 3.
DT   20-DEC-2017, entry version 204.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II;
DE            Short=Ip;
DE   Flags: Precursor;
GN   Name=SDHB; Synonyms=SDH, SDH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Liver;
RX   PubMed=7622059; DOI=10.1016/0378-1119(95)00162-Y;
RA   Au H.C., Ream-Robinson D., Bellew L.A., Broomfield P.L.E.,
RA   Saghbini M., Scheffler I.E.;
RT   "Structural organization of the gene encoding the human iron-sulfur
RT   subunit of succinate dehydrogenase.";
RL   Gene 159:249-253(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-264.
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian
RT   relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-280.
RC   TISSUE=Liver;
RX   PubMed=2302193; DOI=10.1016/0006-291X(90)91916-G;
RA   Kita K., Oya H., Gennis R.B., Ackrell B.A.C., Kasahara M.;
RT   "Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning
RT   of iron sulfur (Ip) subunit of liver mitochondria.";
RL   Biochem. Biophys. Res. Commun. 166:101-108(1990).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 107-249.
RC   TISSUE=Fibroblast;
RX   PubMed=2494655; DOI=10.1073/pnas.86.6.1934;
RA   Gould S.J., Subramani S., Scheffler I.E.;
RT   "Use of the DNA polymerase chain reaction for homology probing:
RT   isolation of partial cDNA or genomic clones encoding the iron-sulfur
RT   protein of succinate dehydrogenase from several species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
RN   [9]
RP   ERRATUM.
RA   Gould S.J., Subramani S., Scheffler I.E.;
RL   Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
RN   [10]
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.,
RA   Buerckstuemmer T., 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   [11]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-28, 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.,
RA   Ayoub D., 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   [13]
RP   VARIANT PGL4 ARG-197, AND VARIANT PCC SER-87.
RX   PubMed=11404820; DOI=10.1086/321282;
RA   Astuti D., Latif F., Dallol A., Dahia P.L.M., Douglas F., George E.,
RA   Skoeldberg F., Husebye E.S., Eng C., Maher E.R.;
RT   "Gene mutations in the succinate dehydrogenase subunit SDHB cause
RT   susceptibility to familial pheochromocytoma and to familial
RT   paraganglioma.";
RL   Am. J. Hum. Genet. 69:49-54(2001).
RN   [14]
RP   VARIANT FAMILIAL MALIGNANT PARAGANGLIOMA HIS-242.
RX   PubMed=12213855; DOI=10.1210/jc.2002-020312;
RA   Young A.L., Baysal B.E., Deb A., Young W.F. Jr.;
RT   "Familial malignant catecholamine-secreting paraganglioma with
RT   prolonged survival associated with mutation in the succinate
RT   dehydrogenase B gene.";
RL   J. Clin. Endocrinol. Metab. 87:4101-4105(2002).
RN   [15]
RP   VARIANT PGL4 ARG-131.
RX   PubMed=11897817; DOI=10.1136/jmg.39.3.178;
RA   Baysal B.E., Willett-Brozick J.E., Lawrence E.C., Drovdlic C.M.,
RA   Savul S.A., McLeod D.R., Yee H.A., Brackmann D.E., Slattery W.H. III,
RA   Myers E.N., Ferrell R.E., Rubinstein W.S.;
RT   "Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic
RT   patients with head and neck paragangliomas.";
RL   J. Med. Genet. 39:178-183(2002).
RN   [16]
RP   VARIANTS PCC GLN-29 INS; GLY-46; TYR-101; ARG-192; TYR-196 AND
RP   HIS-242.
RX   PubMed=12000816; DOI=10.1056/NEJMoa020152;
RG   The Freiburg-Warsaw-Columbus pheochromocytoma study group;
RA   Neumann H.P.H., Bausch B., McWhinney S.R., Bender B.U., Gimm O.,
RA   Franke G., Schipper J., Klisch J., Altehoefer C., Zerres K.,
RA   Januszewicz A., Smith W.M., Munk R., Manz T., Glaesker S., Apel T.W.,
RA   Treier M., Reineke M., Walz M.K., Hoang-Vu C., Brauckhoff M.,
RA   Klein-Franke A., Klose P., Schmidt H., Maier-Woelfle M.,
RA   Peczkowska M., Szmigielski C., Eng C.;
RT   "Germ-line mutations in nonsyndromic pheochromocytoma.";
RL   N. Engl. J. Med. 346:1459-1466(2002).
RN   [17]
RP   VARIANTS PCC PRO-43; GLN-46; GLY-46 AND CYS-230.
RX   PubMed=14500403;
RA   Gimenez-Roqueplo A.-P., Favier J., Rustin P., Rieubland C.,
RA   Crespin M., Nau V., Khau Van Kien P., Corvol P., Plouin P.-F.,
RA   Jeunemaitre X.;
RT   "Mutations in the SDHB gene are associated with extra-adrenal and/or
RT   malignant phaeochromocytomas.";
RL   Cancer Res. 63:5615-5621(2003).
RN   [18]
RP   VARIANT PCC ASN-127, AND VARIANT PGL4 ARG-197.
RX   PubMed=14974914; DOI=10.1046/j.1365-2265.2003.01914.x;
RA   Astuti D., Hart-Holden N., Latif F., Lalloo F., Black G.C., Lim C.,
RA   Moran A., Grossman A.B., Hodgson S.V., Freemont A., Ramsden R.,
RA   Eng C., Evans D.G.R., Maher E.R.;
RT   "Genetic analysis of mitochondrial complex II subunits SDHD, SDHB and
RT   SDHC in paraganglioma and phaeochromocytoma susceptibility.";
RL   Clin. Endocrinol. (Oxf.) 59:728-733(2003).
RN   [19]
RP   VARIANTS PCC GLN-46 AND HIS-65.
RX   PubMed=12618761; DOI=10.1038/sj.onc.1206300;
RA   Benn D.E., Croxson M.S., Tucker K., Bambach C.P., Richardson A.L.,
RA   Delbridge L., Pullan P.T., Hammond J., Marsh D.J., Robinson B.G.;
RT   "Novel succinate dehydrogenase subunit B (SDHB) mutations in familial
RT   phaeochromocytomas and paragangliomas, but an absence of somatic SDHB
RT   mutations in sporadic phaeochromocytomas.";
RL   Oncogene 22:1358-1364(2003).
RN   [20]
RP   VARIANT GLU-40.
RX   PubMed=15473885; DOI=10.1111/j.1365-2265.2004.02122.x;
RA   McDonnell C.M., Benn D.E., Marsh D.J., Robinson B.G., Zacharin M.R.;
RT   "K40E: a novel succinate dehydrogenase (SDH)B mutation causing
RT   familial phaeochromocytoma and paraganglioma.";
RL   Clin. Endocrinol. (Oxf.) 61:510-514(2004).
RN   [21]
RP   VARIANTS PCC GLY-46; GLN-46; ARG-53; PRO-65; SER-87; TYR-101; ARG-192;
RP   TYR-196 AND HIS-242, AND VARIANTS PGL4 GLN-46 AND HIS-242.
RX   PubMed=15328326; DOI=10.1001/jama.292.8.943;
RA   Neumann H.P.H., Pawlu C., Peczkowska M., Bausch B., McWhinney S.R.,
RA   Muresan M., Buchta M., Franke G., Klisch J., Bley T.A., Hoegerle S.,
RA   Boedeker C.C., Opocher G., Schipper J., Januszewicz A., Eng C.;
RT   "Distinct clinical features of paraganglioma syndromes associated with
RT   SDHB and SDHD gene mutations.";
RL   JAMA 292:943-951(2004).
RN   [22]
RP   ERRATUM.
RA   Neumann H.P.H., Pawlu C., Peczkowska M., Bausch B., McWhinney S.R.,
RA   Muresan M., Buchta M., Franke G., Klisch J., Bley T.A., Hoegerle S.,
RA   Boedeker C.C., Opocher G., Schipper J., Januszewicz A., Eng C.;
RL   JAMA 292:1686-1686(2004).
RN   [23]
RP   VARIANT PGL4 PRO-132.
RX   PubMed=14715873; DOI=10.1210/jc.2003-031236;
RA   Maier-Woelfle M., Braendle M., Komminoth P., Saremaslani P.,
RA   Schmid S., Locher T., Heitz P.U., Krull I., Galeazzi R.L., Schmid C.,
RA   Perren A.;
RT   "A novel succinate dehydrogenase subunit B gene mutation, H132P,
RT   causes familial malignant sympathetic extraadrenal paragangliomas.";
RL   J. Clin. Endocrinol. Metab. 89:362-367(2004).
RN   [24]
RP   VARIANT PCC PHE-100.
RX   PubMed=17634472; DOI=10.1056/NEJMc070010;
RA   van Nederveen F.H., Korpershoek E., Lenders J.W.M., de Krijger R.R.,
RA   Dinjens W.N.M.;
RT   "Somatic SDHB mutation in an extraadrenal pheochromocytoma.";
RL   N. Engl. J. Med. 357:306-308(2007).
RN   [25]
RP   INVOLVEMENT IN PGGSS.
RX   PubMed=17804857; DOI=10.1056/NEJMc071191;
RA   McWhinney S.R., Pasini B., Stratakis C.A.;
RT   "Familial gastrointestinal stromal tumors and germ-line mutations.";
RL   N. Engl. J. Med. 357:1054-1056(2007).
RN   [26]
RP   VARIANTS CWS2 GLY-3 AND PRO-163, AND CHARACTERIZATION OF VARIANTS CWS2
RP   GLY-3 AND PRO-163.
RX   PubMed=18678321; DOI=10.1016/j.ajhg.2008.07.011;
RA   Ni Y., Zbuk K.M., Sadler T., Patocs A., Lobo G., Edelman E.,
RA   Platzer P., Orloff M.S., Waite K.A., Eng C.;
RT   "Germline mutations and variants in the succinate dehydrogenase genes
RT   in Cowden and Cowden-like syndromes.";
RL   Am. J. Hum. Genet. 83:261-268(2008).
CC   -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate
CC       dehydrogenase (SDH) that is involved in complex II of the
CC       mitochondrial electron transport chain and is responsible for
CC       transferring electrons from succinate to ubiquinone (coenzyme Q).
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
CC       cytochrome b560 composed of SDHC and SDHD.
CC   -!- INTERACTION:
CC       Q8IWL3:HSCB; NbExp=21; IntAct=EBI-1056481, EBI-1805738;
CC       Q9H1K1:ISCU; NbExp=7; IntAct=EBI-1056481, EBI-1047335;
CC       P31040:SDHA; NbExp=8; IntAct=EBI-1056481, EBI-1057265;
CC       A6NFY7:SDHAF1; NbExp=12; IntAct=EBI-1056481, EBI-12011488;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side.
CC   -!- DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-
CC       producing tumor of chromaffin tissue of the adrenal medulla or
CC       sympathetic paraganglia. The cardinal symptom, reflecting the
CC       increased secretion of epinephrine and norepinephrine, is
CC       hypertension, which may be persistent or intermittent.
CC       {ECO:0000269|PubMed:11404820, ECO:0000269|PubMed:12000816,
CC       ECO:0000269|PubMed:12618761, ECO:0000269|PubMed:14500403,
CC       ECO:0000269|PubMed:14974914, ECO:0000269|PubMed:15328326,
CC       ECO:0000269|PubMed:17634472}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Paragangliomas 4 (PGL4) [MIM:115310]: A neural crest
CC       tumor usually derived from the chromoreceptor tissue of a
CC       paraganglion. Paragangliomas can develop at various body sites,
CC       including the head, neck, thorax and abdomen. Most commonly, they
CC       are located in the head and neck region, specifically at the
CC       carotid bifurcation, the jugular foramen, the vagal nerve, and in
CC       the middle ear. {ECO:0000269|PubMed:11404820,
CC       ECO:0000269|PubMed:11897817, ECO:0000269|PubMed:14715873,
CC       ECO:0000269|PubMed:14974914, ECO:0000269|PubMed:15328326}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Paraganglioma and gastric stromal sarcoma (PGGSS)
CC       [MIM:606864]: Gastrointestinal stromal tumors may be sporadic or
CC       inherited in an autosomal dominant manner, alone or as a component
CC       of a syndrome associated with other tumors, such as in the context
CC       of neurofibromatosis type 1 (NF1). Patients have both
CC       gastrointestinal stromal tumors and paragangliomas. Susceptibility
CC       to the tumors was inherited in an apparently autosomal dominant
CC       manner, with incomplete penetrance. {ECO:0000269|PubMed:17804857}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Cowden syndrome 2 (CWS2) [MIM:612359]: A form of Cowden
CC       syndrome, a hamartomatous polyposis syndrome with age-related
CC       penetrance. Cowden syndrome is characterized by hamartomatous
CC       lesions affecting derivatives of ectodermal, mesodermal and
CC       endodermal layers, macrocephaly, facial trichilemmomas (benign
CC       tumors of the hair follicle infundibulum), acral keratoses,
CC       papillomatous papules, and elevated risk for development of
CC       several types of malignancy, particularly breast carcinoma in
CC       women and thyroid carcinoma in both men and women. Colon cancer
CC       and renal cell carcinoma have also been reported. Hamartomas can
CC       be found in virtually every organ, but most commonly in the skin,
CC       gastrointestinal tract, breast and thyroid. CWS2 inheritance is
CC       autosomal dominant. {ECO:0000269|PubMed:18678321}. Note=The
CC       disease may be caused by mutations affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SDHBID388.html";
CC   -!- WEB RESOURCE: Name=TCA Cycle Gene Mutation Database;
CC       URL="http://databases.lovd.nl/shared/genes/SDHB";
DR   EMBL; U17248; AAA81167.1; -; mRNA.
DR   EMBL; U17886; AAA80581.1; -; Genomic_DNA.
DR   EMBL; U17296; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; U17880; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; U17881; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; U17882; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; U17883; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; U17884; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; U17885; AAA80581.1; JOINED; Genomic_DNA.
DR   EMBL; AK312056; BAG34992.1; -; mRNA.
DR   EMBL; AL049569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471134; EAW94828.1; -; Genomic_DNA.
DR   EMBL; BC007840; AAH07840.1; -; mRNA.
DR   EMBL; DQ403007; ABD77140.1; -; mRNA.
DR   EMBL; D10245; BAA01089.1; -; mRNA.
DR   EMBL; M32246; AAA35708.1; -; mRNA.
DR   CCDS; CCDS176.1; -.
DR   PIR; I38895; I38895.
DR   RefSeq; NP_002991.2; NM_003000.2.
DR   UniGene; Hs.465924; -.
DR   ProteinModelPortal; P21912; -.
DR   SMR; P21912; -.
DR   BioGrid; 112291; 111.
DR   DIP; DIP-39666N; -.
DR   IntAct; P21912; 28.
DR   MINT; MINT-3009566; -.
DR   STRING; 9606.ENSP00000364649; -.
DR   DrugBank; DB00139; Succinic acid.
DR   DrugBank; DB08689; UBIQUINONE-1.
DR   iPTMnet; P21912; -.
DR   PhosphoSitePlus; P21912; -.
DR   SwissPalm; P21912; -.
DR   BioMuta; SDHB; -.
DR   DMDM; 20455488; -.
DR   UCD-2DPAGE; P21912; -.
DR   EPD; P21912; -.
DR   MaxQB; P21912; -.
DR   PaxDb; P21912; -.
DR   PeptideAtlas; P21912; -.
DR   PRIDE; P21912; -.
DR   DNASU; 6390; -.
DR   Ensembl; ENST00000375499; ENSP00000364649; ENSG00000117118.
DR   GeneID; 6390; -.
DR   KEGG; hsa:6390; -.
DR   UCSC; uc001bae.5; human.
DR   CTD; 6390; -.
DR   DisGeNET; 6390; -.
DR   EuPathDB; HostDB:ENSG00000117118.9; -.
DR   GeneCards; SDHB; -.
DR   GeneReviews; SDHB; -.
DR   HGNC; HGNC:10681; SDHB.
DR   HPA; CAB009822; -.
DR   HPA; CAB068233; -.
DR   HPA; CAB068234; -.
DR   HPA; CAB068235; -.
DR   HPA; HPA002868; -.
DR   MalaCards; SDHB; -.
DR   MIM; 115310; phenotype.
DR   MIM; 171300; phenotype.
DR   MIM; 185470; gene.
DR   MIM; 606864; phenotype.
DR   MIM; 612359; phenotype.
DR   neXtProt; NX_P21912; -.
DR   OpenTargets; ENSG00000117118; -.
DR   Orphanet; 97286; Carney-Stratakis syndrome.
DR   Orphanet; 201; Cowden syndrome.
DR   Orphanet; 44890; Gastrointestinal stromal tumor.
DR   Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
DR   Orphanet; 3208; Isolated succinate-CoQ reductase deficiency.
DR   PharmGKB; PA35606; -.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; HOG000160590; -.
DR   HOVERGEN; HBG005483; -.
DR   InParanoid; P21912; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; EOG091G0EKC; -.
DR   PhylomeDB; P21912; -.
DR   TreeFam; TF300754; -.
DR   BioCyc; MetaCyc:ENSG00000117118-MONOMER; -.
DR   BRENDA; 1.3.5.1; 2681.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR   SIGNOR; P21912; -.
DR   UniPathway; UPA00223; UER01006.
DR   ChiTaRS; SDHB; human.
DR   GeneWiki; SDHB; -.
DR   GenomeRNAi; 6390; -.
DR   PRO; PR:P21912; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000117118; -.
DR   CleanEx; HS_SDHB; -.
DR   ExpressionAtlas; P21912; baseline and differential.
DR   Genevisible; P21912; HS.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   Pfam; PF13085; Fer2_3; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Acetylation; Complete proteome;
KW   Disease mutation; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Polymorphism; Reference proteome; Transit peptide;
KW   Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     28       Mitochondrion.
FT                                {ECO:0000244|PubMed:25944712}.
FT   CHAIN        29    280       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000010355.
FT   DOMAIN       40    133       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      176    206       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        93     93       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        98     98       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       101    101       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       113    113       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       186    186       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       189    189       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       192    192       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       196    196       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       243    243       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       249    249       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       253    253       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     201    201       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250}.
FT   MOD_RES      51     51       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9CQA3}.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9CQA3}.
FT   VARIANT       3      3       A -> G (in CWS2; uncertain pathological
FT                                significance; associated with increased
FT                                manganese superoxide dismutase expression
FT                                and normal levels of reactive oxygen
FT                                species; associated with a 1.2-fold
FT                                increase in AKT expression and 1.3-fold
FT                                change in MAPK expression;
FT                                dbSNP:rs11203289).
FT                                {ECO:0000269|PubMed:18678321}.
FT                                /FTId=VAR_054374.
FT   VARIANT      29     29       A -> AQ (in PCC).
FT                                {ECO:0000269|PubMed:12000816}.
FT                                /FTId=VAR_035063.
FT   VARIANT      40     40       K -> E. {ECO:0000269|PubMed:15473885}.
FT                                /FTId=VAR_054375.
FT   VARIANT      43     43       A -> P (in PCC).
FT                                {ECO:0000269|PubMed:14500403}.
FT                                /FTId=VAR_054376.
FT   VARIANT      46     46       R -> G (in PCC; dbSNP:rs74315370).
FT                                {ECO:0000269|PubMed:12000816,
FT                                ECO:0000269|PubMed:14500403,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_035064.
FT   VARIANT      46     46       R -> Q (in PCC and PGL4;
FT                                dbSNP:rs772551056).
FT                                {ECO:0000269|PubMed:12618761,
FT                                ECO:0000269|PubMed:14500403,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_054377.
FT   VARIANT      53     53       G -> R (in PCC).
FT                                {ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_054378.
FT   VARIANT      65     65       L -> H (in PCC; dbSNP:rs876659329).
FT                                {ECO:0000269|PubMed:12618761}.
FT                                /FTId=VAR_054379.
FT   VARIANT      65     65       L -> P (in PCC).
FT                                {ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_054380.
FT   VARIANT      87     87       L -> S (in PCC; dbSNP:rs727504457).
FT                                {ECO:0000269|PubMed:11404820,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_018517.
FT   VARIANT     100    100       S -> F (in PCC; absence of expression in
FT                                tumor cells indicating complete loss of
FT                                SDHB function; dbSNP:rs121917755).
FT                                {ECO:0000269|PubMed:17634472}.
FT                                /FTId=VAR_037620.
FT   VARIANT     101    101       C -> Y (in PCC; dbSNP:rs74315371).
FT                                {ECO:0000269|PubMed:12000816,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_035065.
FT   VARIANT     127    127       I -> N (in PCC).
FT                                {ECO:0000269|PubMed:14974914}.
FT                                /FTId=VAR_054381.
FT   VARIANT     131    131       P -> R (in PGL4).
FT                                {ECO:0000269|PubMed:11897817}.
FT                                /FTId=VAR_018518.
FT   VARIANT     132    132       H -> P (in PGL4; dbSNP:rs74315372).
FT                                {ECO:0000269|PubMed:14715873}.
FT                                /FTId=VAR_037621.
FT   VARIANT     163    163       S -> P (in CWS2; uncertain pathological
FT                                significance; associated with increased
FT                                manganese superoxide dismutase function
FT                                and increased levels of reactive oxygen
FT                                species; associated with a 2.7-fold
FT                                change in AKT expression and a 1.7-fold
FT                                increase in MAPK expression;
FT                                dbSNP:rs33927012).
FT                                {ECO:0000269|PubMed:18678321}.
FT                                /FTId=VAR_054382.
FT   VARIANT     192    192       C -> R (in PCC; dbSNP:rs786202732).
FT                                {ECO:0000269|PubMed:12000816,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_035066.
FT   VARIANT     196    196       C -> Y (in PCC; dbSNP:rs876658367).
FT                                {ECO:0000269|PubMed:12000816,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_035067.
FT   VARIANT     197    197       P -> R (in PGL4; dbSNP:rs74315367).
FT                                {ECO:0000269|PubMed:11404820,
FT                                ECO:0000269|PubMed:14974914}.
FT                                /FTId=VAR_017868.
FT   VARIANT     230    230       R -> C (in PCC; dbSNP:rs138996609).
FT                                {ECO:0000269|PubMed:14500403}.
FT                                /FTId=VAR_054383.
FT   VARIANT     242    242       R -> H (in PGL4 and PCC;
FT                                dbSNP:rs74315368).
FT                                {ECO:0000269|PubMed:12000816,
FT                                ECO:0000269|PubMed:12213855,
FT                                ECO:0000269|PubMed:15328326}.
FT                                /FTId=VAR_017869.
FT   CONFLICT     19     21       GGA -> WRT (in Ref. 7; AAA35708/
FT                                BAA01089). {ECO:0000305}.
FT   CONFLICT     62     62       E -> K (in Ref. 1; AAA81167 and 7;
FT                                AAA35708/BAA01089). {ECO:0000305}.
FT   CONFLICT     67     67       K -> NR (in Ref. 1; AAA80581).
FT                                {ECO:0000305}.
FT   CONFLICT    151    151       K -> R (in Ref. 8; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    172    172       Q -> E (in Ref. 8; no nucleotide entry).
FT                                {ECO:0000305}.
SQ   SEQUENCE   280 AA;  31630 MW;  ED12E7C3BA7B6D13 CRC64;
     MAAVVALSLR RRLPATTLGG ACLQASRGAQ TAAATAPRIK KFAIYRWDPD KAGDKPHMQT
     YEVDLNKCGP MVLDALIKIK NEVDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN
     LNKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQEGKQQY LQSIEEREKL
     DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL
     YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKKASV
//
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