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 09-DEC-2015, entry version 185. 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 P31040:SDHA; NbExp=2; IntAct=EBI-1056481, EBI-1057265; 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. CC {ECO:0000269|PubMed:18678321}. Note=The disease may be caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00465}. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. 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://chromium.liacs.nl/LOVD2/SDH/home.php?select_db=SDHB"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CAB96822.1; -; 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; 37-275. DR BioGrid; 112291; 98. DR IntAct; P21912; 10. DR MINT; MINT-3009566; -. DR STRING; 9606.ENSP00000364649; -. DR DrugBank; DB00139; Succinic acid. DR PhosphoSite; P21912; -. DR BioMuta; SDHB; -. DR DMDM; 20455488; -. DR UCD-2DPAGE; 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.3; human. DR CTD; 6390; -. 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; HPA002867; -. 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 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; IDSHERM; -. DR OrthoDB; EOG7H4DTN; -. 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 UniPathway; UPA00223; UER01006. DR ChiTaRS; SDHB; human. DR GeneWiki; SDHB; -. DR GenomeRNAi; 6390; -. DR NextBio; 24824; -. DR PRO; PR:P21912; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P21912; -. 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: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 carrier 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:0044237; P:cellular metabolic process; TAS:Reactome. DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome. DR Gene3D; 3.10.20.30; -; 1. 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. 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). 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 {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). 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). 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). FT {ECO:0000269|PubMed:17634472}. FT /FTId=VAR_037620. FT VARIANT 101 101 C -> Y (in PCC). 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). 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). FT {ECO:0000269|PubMed:12000816, FT ECO:0000269|PubMed:15328326}. FT /FTId=VAR_035066. FT VARIANT 196 196 C -> Y (in PCC). FT {ECO:0000269|PubMed:12000816, FT ECO:0000269|PubMed:15328326}. FT /FTId=VAR_035067. FT VARIANT 197 197 P -> R (in PGL4). 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 {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 //