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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   03-AUG-2022, entry version 236.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Saghbini M.,
RA   Scheffler I.E.;
RT   "Structural organization of the gene encoding the human iron-sulfur subunit
RT   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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   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 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 of
RT   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: isolation
RT   of partial cDNA or genomic clones encoding the iron-sulfur protein of
RT   succinate dehydrogenase from several species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
RN   [9]
RP   ERRATUM OF PUBMED:2494655.
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., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [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., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [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., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   INTERACTION WITH SDHAF1.
RX   PubMed=26749241; DOI=10.1016/j.cmet.2015.12.005;
RA   Maio N., Ghezzi D., Verrigni D., Rizza T., Bertini E., Martinelli D.,
RA   Zeviani M., Singh A., Carrozzo R., Rouault T.A.;
RT   "Disease-causing SDHAF1 mutations impair transfer of Fe-S clusters to
RT   SDHB.";
RL   Cell Metab. 23:292-302(2016).
RN   [14]
RP   INTERACTION WITH JC VIRUS SMALL T ANTIGEN (MICROBIAL INFECTION).
RX   PubMed=33092197; DOI=10.3390/v12101192;
RA   Saribas S., Safak M.;
RT   "A Comprehensive Proteomics Analysis of the JC Virus (JCV) Large and Small
RT   Tumor Antigen Interacting Proteins: Large T Primarily Targets the Host
RT   Protein Complexes with V-ATPase and Ubiquitin Ligase Activities While Small
RT   t Mostly Associates with Those Having Phosphatase and Chromatin-Remodeling
RT   Functions.";
RL   Viruses 12:0-0(2020).
RN   [15]
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   [16]
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 prolonged
RT   survival associated with mutation in the succinate dehydrogenase B gene.";
RL   J. Clin. Endocrinol. Metab. 87:4101-4105(2002).
RN   [17]
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 patients
RT   with head and neck paragangliomas.";
RL   J. Med. Genet. 39:178-183(2002).
RN   [18]
RP   VARIANTS PCC GLN-29 INS; GLY-46; TYR-101; ARG-192; TYR-196 AND 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., Franke G.,
RA   Schipper J., Klisch J., Altehoefer C., Zerres K., Januszewicz A.,
RA   Smith W.M., Munk R., Manz T., Glaesker S., Apel T.W., Treier M.,
RA   Reineke M., Walz M.K., Hoang-Vu C., Brauckhoff M., Klein-Franke A.,
RA   Klose P., Schmidt H., Maier-Woelfle M., Peczkowska M., Szmigielski C.,
RA   Eng C.;
RT   "Germ-line mutations in nonsyndromic pheochromocytoma.";
RL   N. Engl. J. Med. 346:1459-1466(2002).
RN   [19]
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., Crespin M.,
RA   Nau V., Khau Van Kien P., Corvol P., Plouin P.-F., 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   [20]
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., Eng C.,
RA   Evans D.G.R., Maher E.R.;
RT   "Genetic analysis of mitochondrial complex II subunits SDHD, SDHB and SDHC
RT   in paraganglioma and phaeochromocytoma susceptibility.";
RL   Clin. Endocrinol. (Oxf.) 59:728-733(2003).
RN   [21]
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   [22]
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 familial
RT   phaeochromocytoma and paraganglioma.";
RL   Clin. Endocrinol. (Oxf.) 61:510-514(2004).
RN   [23]
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 SDHB
RT   and SDHD gene mutations.";
RL   JAMA 292:943-951(2004).
RN   [24]
RP   ERRATUM OF PUBMED:15328326.
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   [25]
RP   VARIANT PGL4 PRO-132.
RX   PubMed=14715873; DOI=10.1210/jc.2003-031236;
RA   Maier-Woelfle M., Braendle M., Komminoth P., Saremaslani P., Schmid S.,
RA   Locher T., Heitz P.U., Krull I., Galeazzi R.L., Schmid C., Perren A.;
RT   "A novel succinate dehydrogenase subunit B gene mutation, H132P, causes
RT   familial malignant sympathetic extraadrenal paragangliomas.";
RL   J. Clin. Endocrinol. Metab. 89:362-367(2004).
RN   [26]
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   [27]
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   [28]
RP   VARIANTS GLY-3 AND PRO-163, AND CHARACTERIZATION OF VARIANTS GLY-3 AND
RP   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., Platzer P.,
RA   Orloff M.S., Waite K.A., Eng C.;
RT   "Germline mutations and variants in the succinate dehydrogenase genes in
RT   Cowden and Cowden-like syndromes.";
RL   Am. J. Hum. Genet. 83:261-268(2008).
RN   [29]
RP   VARIANT MC2DN4 VAL-48, AND INVOLVEMENT IN MC2DN4.
RX   PubMed=22972948; DOI=10.1136/jmedgenet-2012-101146;
RA   Alston C.L., Davison J.E., Meloni F., van der Westhuizen F.H., He L.,
RA   Hornig-Do H.T., Peet A.C., Gissen P., Goffrini P., Ferrero I., Wassmer E.,
RA   McFarland R., Taylor R.W.;
RT   "Recessive germline SDHA and SDHB mutations causing leukodystrophy and
RT   isolated mitochondrial complex II deficiency.";
RL   J. Med. Genet. 49:569-577(2012).
RN   [30]
RP   VARIANT MC2DN4 VAL-48, CHARACTERIZATION OF VARIANT MC2DN4 VAL-48,
RP   INVOLVEMENT IN MC2DN4, AND FUNCTION.
RX   PubMed=26925370; DOI=10.1016/j.ymgmr.2015.10.006;
RA   Ardissone A., Invernizzi F., Nasca A., Moroni I., Farina L., Ghezzi D.;
RT   "Mitochondrial leukoencephalopathy and complex II deficiency associated
RT   with a recessive SDHB mutation with reduced penetrance.";
RL   Mol. Genet. Metab. Rep. 5:51-54(2015).
RN   [31]
RP   VARIANTS MC2DN4 VAL-48 AND THR-103, AND INVOLVEMENT IN MC2DN4.
RX   PubMed=26642834; DOI=10.1002/ana.24572;
RG   SDH Study Group;
RA   Helman G., Caldovic L., Whitehead M.T., Simons C., Brockmann K.,
RA   Edvardson S., Bai R., Moroni I., Taylor J.M., Van Haren K., Taft R.J.,
RA   Vanderver A., van der Knaap M.S.;
RT   "Magnetic resonance imaging spectrum of succinate dehydrogenase-related
RT   infantile leukoencephalopathy.";
RL   Ann. Neurol. 79:379-386(2016).
RN   [32]
RP   VARIANTS MC2DN4 VAL-48; HIS-230 AND VAL-257, CHARACTERIZATION OF VARIANT
RP   MC2DN4 VAL-257, AND FUNCTION.
RX   PubMed=27604842; DOI=10.1007/8904_2016_582;
RA   Groenborg S., Darin N., Miranda M.J., Damgaard B., Cayuela J.A.,
RA   Oldfors A., Kollberg G., Hansen T.V.O., Ravn K., Wibrand F.,
RA   Oestergaard E.;
RT   "Leukoencephalopathy due to Complex II Deficiency and Bi-Allelic SDHB
RT   Mutations: Further Cases and Implications for Genetic Counselling.";
RL   JIMD Rep. 33:69-77(2017).
RN   [33]
RP   VARIANT MC2DN4 THR-102.
RX   PubMed=32124427; DOI=10.1111/ahg.12377;
RA   Kaur P., Sharma S., Kadavigere R., Girisha K.M., Shukla A.;
RT   "Novel variant p.(Ala102Thr) in SDHB causes mitochondrial complex II
RT   deficiency: Case report and review of the literature.";
RL   Ann. Hum. Genet. 84:345-351(2020).
CC   -!- FUNCTION: Iron-sulfur protein (IP) subunit of the succinate
CC       dehydrogenase complex (mitochondrial respiratory chain complex II),
CC       responsible for transferring electrons from succinate to ubiquinone
CC       (coenzyme Q). {ECO:0000269|PubMed:26925370,
CC       ECO:0000269|PubMed:27604842}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       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 cytochrome
CC       b560 composed of SDHC and SDHD (By similarity). Interacts with SDHAF1;
CC       the interaction is required for iron-sulfur cluster incorporation into
CC       SDHB (PubMed:26749241). {ECO:0000250|UniProtKB:Q007T0,
CC       ECO:0000269|PubMed:26749241}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with JC virus small t antigen.
CC       {ECO:0000269|PubMed:33092197}.
CC   -!- INTERACTION:
CC       P21912; Q8IWL3: HSCB; NbExp=21; IntAct=EBI-1056481, EBI-1805738;
CC       P21912; Q9H1K1: ISCU; NbExp=7; IntAct=EBI-1056481, EBI-1047335;
CC       P21912; P31040: SDHA; NbExp=9; IntAct=EBI-1056481, EBI-1057265;
CC       P21912; A6NFY7: SDHAF1; NbExp=12; IntAct=EBI-1056481, EBI-12011488;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Matrix side.
CC   -!- DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-producing
CC       tumor of chromaffin tissue of the adrenal medulla or sympathetic
CC       paraganglia. The cardinal symptom, reflecting the increased secretion
CC       of epinephrine and norepinephrine, is hypertension, which may be
CC       persistent or intermittent. {ECO:0000269|PubMed:11404820,
CC       ECO:0000269|PubMed:12000816, ECO:0000269|PubMed:12618761,
CC       ECO:0000269|PubMed:14500403, ECO:0000269|PubMed:14974914,
CC       ECO:0000269|PubMed:15328326, ECO:0000269|PubMed:17634472}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Paragangliomas 4 (PGL4) [MIM:115310]: A neural crest tumor
CC       usually derived from the chromoreceptor tissue of a paraganglion.
CC       Paragangliomas can develop at various body sites, including the head,
CC       neck, thorax and abdomen. Most commonly, they are located in the head
CC       and neck region, specifically at the carotid bifurcation, the jugular
CC       foramen, the vagal nerve, and in the middle ear.
CC       {ECO:0000269|PubMed:11404820, ECO:0000269|PubMed:11897817,
CC       ECO:0000269|PubMed:14715873, ECO:0000269|PubMed:14974914,
CC       ECO:0000269|PubMed:15328326}. Note=The disease is caused by variants
CC       affecting the gene 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 of a
CC       syndrome associated with other tumors, such as in the context of
CC       neurofibromatosis type 1 (NF1). Patients have both gastrointestinal
CC       stromal tumors and paragangliomas. Susceptibility to the tumors was
CC       inherited in an apparently autosomal dominant manner, with incomplete
CC       penetrance. {ECO:0000269|PubMed:17804857}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Mitochondrial complex II deficiency, nuclear type 4 (MC2DN4)
CC       [MIM:619224]: A form of mitochondrial complex II deficiency, a disorder
CC       with heterogeneous clinical manifestations. Some patients have
CC       multisystem involvement of the brain, heart, muscle, liver, and kidneys
CC       resulting in death in infancy, whereas others have only isolated
CC       cardiac or muscle involvement with onset in adulthood and normal
CC       cognition. Clinical features include psychomotor regression in infants,
CC       poor growth with lack of speech development, severe spastic
CC       quadriplegia, dystonia, progressive leukoencephalopathy, muscle
CC       weakness, exercise intolerance, cardiomyopathy. Some patients manifest
CC       Leigh syndrome or Kearns-Sayre syndrome. MC2DN4 is a severe, autosomal
CC       recessive form characterized by early-onset progressive
CC       neurodegeneration with leukoencephalopathy.
CC       {ECO:0000269|PubMed:22972948, ECO:0000269|PubMed:26642834,
CC       ECO:0000269|PubMed:26925370, ECO:0000269|PubMed:27604842,
CC       ECO:0000269|PubMed:32124427}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SDHBID388.html";
CC   -!- WEB RESOURCE: Name=TCA Cycle Gene Mutation Database;
CC       URL="https://databases.lovd.nl/shared/genes/SDHB";
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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   PDB; 7KCL; EM; 3.14 A; C=29-160.
DR   PDB; 7KCM; EM; 3.43 A; C=29-160.
DR   PDB; 7KLU; EM; 3.50 A; B/C=19-160.
DR   PDB; 7KLV; EM; 3.10 A; B=19-160.
DR   PDBsum; 7KCL; -.
DR   PDBsum; 7KCM; -.
DR   PDBsum; 7KLU; -.
DR   PDBsum; 7KLV; -.
DR   AlphaFoldDB; P21912; -.
DR   SMR; P21912; -.
DR   BioGRID; 112291; 179.
DR   ComplexPortal; CPX-561; Mitochondrial respiratory chain complex II.
DR   DIP; DIP-39666N; -.
DR   IntAct; P21912; 66.
DR   MINT; P21912; -.
DR   STRING; 9606.ENSP00000364649; -.
DR   BindingDB; P21912; -.
DR   ChEMBL; CHEMBL4105824; -.
DR   DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR   DrugBank; DB08689; Ubiquinone Q1.
DR   TCDB; 3.D.10.1.7; the prokaryotic succinate dehydrogenase (sdh) family.
DR   iPTMnet; P21912; -.
DR   PhosphoSitePlus; P21912; -.
DR   SwissPalm; P21912; -.
DR   BioMuta; SDHB; -.
DR   DMDM; 20455488; -.
DR   UCD-2DPAGE; P21912; -.
DR   EPD; P21912; -.
DR   jPOST; P21912; -.
DR   MassIVE; P21912; -.
DR   MaxQB; P21912; -.
DR   PaxDb; P21912; -.
DR   PeptideAtlas; P21912; -.
DR   PRIDE; P21912; -.
DR   ProteomicsDB; 53939; -.
DR   Antibodypedia; 1264; 565 antibodies from 40 providers.
DR   DNASU; 6390; -.
DR   Ensembl; ENST00000375499.8; ENSP00000364649.3; ENSG00000117118.10.
DR   GeneID; 6390; -.
DR   KEGG; hsa:6390; -.
DR   MANE-Select; ENST00000375499.8; ENSP00000364649.3; NM_003000.3; NP_002991.2.
DR   UCSC; uc001bae.5; human.
DR   CTD; 6390; -.
DR   DisGeNET; 6390; -.
DR   GeneCards; SDHB; -.
DR   GeneReviews; SDHB; -.
DR   HGNC; HGNC:10681; SDHB.
DR   HPA; ENSG00000117118; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; SDHB; -.
DR   MIM; 115310; phenotype.
DR   MIM; 171300; phenotype.
DR   MIM; 185470; gene.
DR   MIM; 606864; phenotype.
DR   MIM; 619224; 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   Orphanet; 276621; Sporadic pheochromocytoma/secreting paraganglioma.
DR   PharmGKB; PA35606; -.
DR   VEuPathDB; HostDB:ENSG00000117118; -.
DR   eggNOG; KOG3049; Eukaryota.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; CLU_044838_0_2_1; -.
DR   InParanoid; P21912; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 1264157at2759; -.
DR   PhylomeDB; P21912; -.
DR   TreeFam; TF300754; -.
DR   BioCyc; MetaCyc:ENSG00000117118-MON; -.
DR   BRENDA; 1.3.5.1; 2681.
DR   PathwayCommons; P21912; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR   SignaLink; P21912; -.
DR   SIGNOR; P21912; -.
DR   UniPathway; UPA00223; UER01006.
DR   BioGRID-ORCS; 6390; 332 hits in 1078 CRISPR screens.
DR   ChiTaRS; SDHB; human.
DR   GeneWiki; SDHB; -.
DR   GenomeRNAi; 6390; -.
DR   Pharos; P21912; Tchem.
DR   PRO; PR:P21912; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P21912; protein.
DR   Bgee; ENSG00000117118; Expressed in heart left ventricle and 205 other tissues.
DR   ExpressionAtlas; P21912; baseline and differential.
DR   Genevisible; P21912; HS.
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; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IC:ComplexPortal.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
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:ProtInc.
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; 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; 3D-structure; 3Fe-4S; 4Fe-4S; Acetylation; Disease variant;
KW   Electron transport; Host-virus interaction; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Primary mitochondrial disease; Reference proteome; Transit peptide;
KW   Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           29..280
FT                   /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000010355"
FT   DOMAIN          40..133
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          176..206
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   REGION          146..218
FT                   /note="Interaction with SDHAF1"
FT                   /evidence="ECO:0000269|PubMed:26749241"
FT   BINDING         93
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with DHSD"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         51
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQA3"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQA3"
FT   VARIANT         3
FT                   /note="A -> G (found in a patient with a Cowden-like
FT                   phenotype; unknown pathological significance; associated
FT                   with increased manganese superoxide dismutase expression
FT                   and normal levels of reactive oxygen species; associated
FT                   with a 1.2-fold increase in AKT expression and 1.3-fold
FT                   change in MAPK expression; dbSNP:rs11203289)"
FT                   /evidence="ECO:0000269|PubMed:18678321"
FT                   /id="VAR_054374"
FT   VARIANT         29
FT                   /note="A -> AQ (in PCC)"
FT                   /evidence="ECO:0000269|PubMed:12000816"
FT                   /id="VAR_035063"
FT   VARIANT         40
FT                   /note="K -> E"
FT                   /evidence="ECO:0000269|PubMed:15473885"
FT                   /id="VAR_054375"
FT   VARIANT         43
FT                   /note="A -> P (in PCC)"
FT                   /evidence="ECO:0000269|PubMed:14500403"
FT                   /id="VAR_054376"
FT   VARIANT         46
FT                   /note="R -> G (in PCC; dbSNP:rs74315370)"
FT                   /evidence="ECO:0000269|PubMed:12000816,
FT                   ECO:0000269|PubMed:14500403, ECO:0000269|PubMed:15328326"
FT                   /id="VAR_035064"
FT   VARIANT         46
FT                   /note="R -> Q (in PCC and PGL4; dbSNP:rs772551056)"
FT                   /evidence="ECO:0000269|PubMed:12618761,
FT                   ECO:0000269|PubMed:14500403, ECO:0000269|PubMed:15328326"
FT                   /id="VAR_054377"
FT   VARIANT         48
FT                   /note="D -> V (in MC2DN4; decreased succinate dehydrogenase
FT                   (ubiquinone) activity in homozygous patient cells;
FT                   decreased protein levels in homozygous patient cells;
FT                   dbSNP:rs202101384)"
FT                   /evidence="ECO:0000269|PubMed:22972948,
FT                   ECO:0000269|PubMed:26642834, ECO:0000269|PubMed:26925370,
FT                   ECO:0000269|PubMed:27604842"
FT                   /id="VAR_085398"
FT   VARIANT         53
FT                   /note="G -> R (in PCC; dbSNP:rs1570958009)"
FT                   /evidence="ECO:0000269|PubMed:15328326"
FT                   /id="VAR_054378"
FT   VARIANT         65
FT                   /note="L -> H (in PCC; dbSNP:rs876659329)"
FT                   /evidence="ECO:0000269|PubMed:12618761"
FT                   /id="VAR_054379"
FT   VARIANT         65
FT                   /note="L -> P (in PCC; dbSNP:rs876659329)"
FT                   /evidence="ECO:0000269|PubMed:15328326"
FT                   /id="VAR_054380"
FT   VARIANT         87
FT                   /note="L -> S (in PCC; dbSNP:rs727504457)"
FT                   /evidence="ECO:0000269|PubMed:11404820,
FT                   ECO:0000269|PubMed:15328326"
FT                   /id="VAR_018517"
FT   VARIANT         100
FT                   /note="S -> F (in PCC; absence of expression in tumor cells
FT                   indicating complete loss of SDHB function;
FT                   dbSNP:rs121917755)"
FT                   /evidence="ECO:0000269|PubMed:17634472"
FT                   /id="VAR_037620"
FT   VARIANT         101
FT                   /note="C -> Y (in PCC; dbSNP:rs74315371)"
FT                   /evidence="ECO:0000269|PubMed:12000816,
FT                   ECO:0000269|PubMed:15328326"
FT                   /id="VAR_035065"
FT   VARIANT         102
FT                   /note="A -> T (in MC2DN4; unknown pathological
FT                   significance; dbSNP:rs777578399)"
FT                   /evidence="ECO:0000269|PubMed:32124427"
FT                   /id="VAR_085399"
FT   VARIANT         103
FT                   /note="M -> T (in MC2DN4; dbSNP:rs1553177765)"
FT                   /evidence="ECO:0000269|PubMed:26642834"
FT                   /id="VAR_085400"
FT   VARIANT         127
FT                   /note="I -> N (in PCC)"
FT                   /evidence="ECO:0000269|PubMed:14974914"
FT                   /id="VAR_054381"
FT   VARIANT         131
FT                   /note="P -> R (in PGL4)"
FT                   /evidence="ECO:0000269|PubMed:11897817"
FT                   /id="VAR_018518"
FT   VARIANT         132
FT                   /note="H -> P (in PGL4; dbSNP:rs74315372)"
FT                   /evidence="ECO:0000269|PubMed:14715873"
FT                   /id="VAR_037621"
FT   VARIANT         163
FT                   /note="S -> P (found in a patient with a Cowden-like
FT                   phenotype; unknown pathological significance; associated
FT                   with increased manganese superoxide dismutase function and
FT                   increased levels of reactive oxygen species; associated
FT                   with a 2.7-fold change in AKT expression and a 1.7-fold
FT                   increase in MAPK expression; dbSNP:rs33927012)"
FT                   /evidence="ECO:0000269|PubMed:18678321"
FT                   /id="VAR_054382"
FT   VARIANT         192
FT                   /note="C -> R (in PCC; dbSNP:rs786202732)"
FT                   /evidence="ECO:0000269|PubMed:12000816,
FT                   ECO:0000269|PubMed:15328326"
FT                   /id="VAR_035066"
FT   VARIANT         196
FT                   /note="C -> Y (in PCC; dbSNP:rs876658367)"
FT                   /evidence="ECO:0000269|PubMed:12000816,
FT                   ECO:0000269|PubMed:15328326"
FT                   /id="VAR_035067"
FT   VARIANT         197
FT                   /note="P -> R (in PGL4; dbSNP:rs74315367)"
FT                   /evidence="ECO:0000269|PubMed:11404820,
FT                   ECO:0000269|PubMed:14974914"
FT                   /id="VAR_017868"
FT   VARIANT         230
FT                   /note="R -> C (in PCC; dbSNP:rs138996609)"
FT                   /evidence="ECO:0000269|PubMed:14500403"
FT                   /id="VAR_054383"
FT   VARIANT         230
FT                   /note="R -> H (in MC2DN4; dbSNP:rs587782604)"
FT                   /evidence="ECO:0000269|PubMed:27604842"
FT                   /id="VAR_085401"
FT   VARIANT         242
FT                   /note="R -> H (in PGL4 and PCC; dbSNP:rs74315368)"
FT                   /evidence="ECO:0000269|PubMed:12000816,
FT                   ECO:0000269|PubMed:12213855, ECO:0000269|PubMed:15328326"
FT                   /id="VAR_017869"
FT   VARIANT         257
FT                   /note="L -> V (in MC2DN4; decreased succinate dehydrogenase
FT                   (ubiquinone) activity; decreased protein levels in
FT                   homozygous patient cells; dbSNP:rs761350633)"
FT                   /evidence="ECO:0000269|PubMed:27604842"
FT                   /id="VAR_085402"
FT   CONFLICT        19..21
FT                   /note="GGA -> WRT (in Ref. 7; AAA35708/BAA01089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="E -> K (in Ref. 1; AAA81167 and 7; AAA35708/
FT                   BAA01089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="K -> NR (in Ref. 1; AAA80581)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="K -> R (in Ref. 8; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="Q -> E (in Ref. 8; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:7KCM"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:7KCL"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:7KCL"
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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