P21912 (DHSB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
EC=1.3.5.1

Alternative name(s):
Iron-sulfur subunit of complex II
Short name=Ip

Gene names

Name:	SDHB
Synonyms:	SDH, SDH1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Subunit structure	Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Involvement in disease	Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Paragangliomas 4 (PGL4) [MIM:115310]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.12 Ref.15 Ref.18 Ref.20 Paraganglioma and gastric stromal sarcoma (PGGSS) [MIM:606864]: Gastrointestinal stromal tumors may be sporadic or inherited in an autosomal dominant manner, alone or as a component of a syndrome associated with other tumors, such as in the context of neurofibromatosis type 1 (NF1). Patients have both gastrointestinal stromal tumors and paragangliomas. Susceptibility to the tumors was inherited in an apparently autosomal dominant manner, with incomplete penetrance. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Cowden-like syndrome (CWDLS) [MIM:612359]: Cancer predisposition syndrome associated with elevated risk for tumors of the breast, thyroid, kidney and uterus. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23
Sequence similarities	Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	respiratory electron transport chain Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome succinate metabolic process Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Traceable author statement. Source: Reactome
Cellular_component	mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 3 iron, 4 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 4 iron, 4 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC ubiquinone binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SDHA	P31040	2	EBI-1056481,EBI-1057265

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 28	28	Mitochondrion
	Chain	29 – 280	252	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000010355
Regions
	Domain	40 – 133	94	2Fe-2S ferredoxin-type
	Domain	176 – 206	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	93	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	98	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	101	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	113	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	186	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	189	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	192	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	196	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	243	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	249	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	253	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	201	1	Ubiquinone; shared with DHSD By similarity
Natural variations
	Natural variant	3	1	A → G Found in an individual with features of Cowden-like syndrome and absence of PTEN mutations; associated with increased manganese superoxide dismutase expression; associated with normal reactive oxygen species; associated with a 1.2-fold increase in AKT expression and 1.3-fold change in MAPK expression. Ref.23 Corresponds to variant rs11203289 [ dbSNP | Ensembl ].		VAR_054374
	Natural variant	29	1	A → AQ in pheochromocytoma. Ref.13		VAR_035063
	Natural variant	40	1	K → E. Ref.17		VAR_054375
	Natural variant	43	1	A → P in pheochromocytoma. Ref.14		VAR_054376
	Natural variant	46	1	R → G in pheochromocytoma. Ref.13 Ref.14 Ref.18		VAR_035064
	Natural variant	46	1	R → Q in pheochromocytoma and PGL4. Ref.14 Ref.16 Ref.18		VAR_054377
	Natural variant	53	1	G → R in pheochromocytoma. Ref.18		VAR_054378
	Natural variant	65	1	L → H in pheochromocytoma. Ref.16		VAR_054379
	Natural variant	65	1	L → P in pheochromocytoma. Ref.18		VAR_054380
	Natural variant	87	1	L → S in pheochromocytoma. Ref.10 Ref.18		VAR_018517
	Natural variant	100	1	S → F in pheochromocytoma; absence of expression in tumor cells indicating complete loss of SDHB function. Ref.21		VAR_037620
	Natural variant	101	1	C → Y in pheochromocytoma. Ref.13 Ref.18		VAR_035065
	Natural variant	127	1	I → N in pheochromocytoma. Ref.15		VAR_054381
	Natural variant	131	1	P → R in PGL4. Ref.12		VAR_018518
	Natural variant	132	1	H → P in PGL4. Ref.20		VAR_037621
	Natural variant	163	1	S → P Found in two individuals with features of Cowden-like syndrome and absence of PTEN mutations; associated with increased manganese superoxide dismutase function; associated with increased reactive oxygen species; associated with a 2.7-fold change in AKT expression and a 1.7-fold increase in MAPK expression. Ref.23 Corresponds to variant rs33927012 [ dbSNP | Ensembl ].		VAR_054382
	Natural variant	192	1	C → R in pheochromocytoma. Ref.13 Ref.18		VAR_035066
	Natural variant	196	1	C → Y in pheochromocytoma. Ref.13 Ref.18		VAR_035067
	Natural variant	197	1	P → R in PGL4. Ref.10 Ref.15		VAR_017868
	Natural variant	230	1	R → C in pheochromocytoma. Ref.14		VAR_054383
	Natural variant	242	1	R → H in familial malignant paraganglioma and pheochromocytoma, pheochromocytoma and PGL4. Ref.11 Ref.13 Ref.18		VAR_017869
Experimental info
	Sequence conflict	19 – 21	3	GGA → WRT in AAA35708. Ref.6
	Sequence conflict	19 – 21	3	GGA → WRT in BAA01089. Ref.6
	Sequence conflict	62	1	E → K in AAA81167. Ref.1
	Sequence conflict	62	1	E → K in AAA35708. Ref.6
	Sequence conflict	62	1	E → K in BAA01089. Ref.6
	Sequence conflict	67	1	K → NR in AAA80581. Ref.1
	Sequence conflict	151	1	K → R no nucleotide entry Ref.7
	Sequence conflict	172	1	Q → E no nucleotide entry Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P21912 [UniParc]. Last modified May 2, 2002. Version 3. Checksum: ED12E7C3BA7B6D13	FASTA	280	31,630
	10 20 30 40 50 60 MAAVVALSLR RRLPATTLGG ACLQASRGAQ TAAATAPRIK KFAIYRWDPD KAGDKPHMQT 70 80 90 100 110 120 YEVDLNKCGP MVLDALIKIK NEVDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN 130 140 150 160 170 180 LNKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQEGKQQY LQSIEEREKL 190 200 210 220 230 240 DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL 250 260 270 280 YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKKASV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural organization of the gene encoding the human iron-sulfur subunit of succinate dehydrogenase." Au H.C., Ream-Robinson D., Bellew L.A., Broomfield P.L.E., Saghbini M., Scheffler I.E. Gene 159:249-253(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Liver.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur (Ip) subunit of liver mitochondria." Kita K., Oya H., Gennis R.B., Ackrell B.A.C., Kasahara M. Biochem. Biophys. Res. Commun. 166:101-108(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-280. Tissue: Liver.
[7]	"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species." Gould S.J., Subramani S., Scheffler I.E. Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 107-249. Tissue: Fibroblast.
[8]	Erratum Gould S.J., Subramani S., Scheffler I.E. Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma." Astuti D., Latif F., Dallol A., Dahia P.L.M., Douglas F., George E., Skoeldberg F., Husebye E.S., Eng C., Maher E.R. Am. J. Hum. Genet. 69:49-54(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGL4 ARG-197, VARIANT PHEOCHROMOCYTOMA SER-87.
[11]	"Familial malignant catecholamine-secreting paraganglioma with prolonged survival associated with mutation in the succinate dehydrogenase B gene." Young A.L., Baysal B.E., Deb A., Young W.F. Jr. J. Clin. Endocrinol. Metab. 87:4101-4105(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FAMILIAL MALIGNANT PARAGANGLIOMA HIS-242.
[12]	"Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic patients with head and neck paragangliomas." Baysal B.E., Willett-Brozick J.E., Lawrence E.C., Drovdlic C.M., Savul S.A., McLeod D.R., Yee H.A., Brackmann D.E., Slattery W.H. III, Myers E.N., Ferrell R.E., Rubinstein W.S. J. Med. Genet. 39:178-183(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGL4 ARG-131.
[13]	"Germ-line mutations in nonsyndromic pheochromocytoma." The Freiburg-Warsaw-Columbus pheochromocytoma study group Neumann H.P.H., Bausch B., McWhinney S.R., Bender B.U., Gimm O., Franke G., Schipper J., Klisch J., Altehoefer C., Zerres K., Januszewicz A., Smith W.M., Munk R., Manz T., Glaesker S., Apel T.W., Treier M., Reineke M. , Walz M.K., Hoang-Vu C., Brauckhoff M., Klein-Franke A., Klose P., Schmidt H., Maier-Woelfle M., Peczkowska M., Szmigielski C., Eng C. N. Engl. J. Med. 346:1459-1466(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHEOCHROMOCYTOMA GLN-29 INS; GLY-46; TYR-101; ARG-192; TYR-196 AND HIS-242.
[14]	"Mutations in the SDHB gene are associated with extra-adrenal and/or malignant phaeochromocytomas." Gimenez-Roqueplo A.-P., Favier J., Rustin P., Rieubland C., Crespin M., Nau V., Khau Van Kien P., Corvol P., Plouin P.-F., Jeunemaitre X. Cancer Res. 63:5615-5621(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHEOCHROMOCYTOMA PRO-43; GLN-46; GLY-46 AND CYS-230.
[15]	"Genetic analysis of mitochondrial complex II subunits SDHD, SDHB and SDHC in paraganglioma and phaeochromocytoma susceptibility." Astuti D., Hart-Holden N., Latif F., Lalloo F., Black G.C., Lim C., Moran A., Grossman A.B., Hodgson S.V., Freemont A., Ramsden R., Eng C., Evans D.G.R., Maher E.R. Clin. Endocrinol. (Oxf.) 59:728-733(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHEOCHROMOCYTOMA ASN-127, VARIANT PGL4 ARG-197.
[16]	"Novel succinate dehydrogenase subunit B (SDHB) mutations in familial phaeochromocytomas and paragangliomas, but an absence of somatic SDHB mutations in sporadic phaeochromocytomas." Benn D.E., Croxson M.S., Tucker K., Bambach C.P., Richardson A.L., Delbridge L., Pullan P.T., Hammond J., Marsh D.J., Robinson B.G. Oncogene 22:1358-1364(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHEOCHROMOCYTOMA GLN-46 AND HIS-65.
[17]	"K40E: a novel succinate dehydrogenase (SDH)B mutation causing familial phaeochromocytoma and paraganglioma." McDonnell C.M., Benn D.E., Marsh D.J., Robinson B.G., Zacharin M.R. Clin. Endocrinol. (Oxf.) 61:510-514(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLU-40.
[18]	"Distinct clinical features of paraganglioma syndromes associated with SDHB and SDHD gene mutations." Neumann H.P.H., Pawlu C., Peczkowska M., Bausch B., McWhinney S.R., Muresan M., Buchta M., Franke G., Klisch J., Bley T.A., Hoegerle S., Boedeker C.C., Opocher G., Schipper J., Januszewicz A., Eng C. JAMA 292:943-951(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHEOCHROMOCYTOMA GLY-46; GLN-46; ARG-53; PRO-65; SER-87; TYR-101; ARG-192; TYR-196 AND HIS-242, VARIANTS PGL4 GLN-46 AND HIS-242.
[19]	Erratum Neumann H.P.H., Pawlu C., Peczkowska M., Bausch B., McWhinney S.R., Muresan M., Buchta M., Franke G., Klisch J., Bley T.A., Hoegerle S., Boedeker C.C., Opocher G., Schipper J., Januszewicz A., Eng C. JAMA 292:1686-1686(2004)
[20]	"A novel succinate dehydrogenase subunit B gene mutation, H132P, causes familial malignant sympathetic extraadrenal paragangliomas." Maier-Woelfle M., Braendle M., Komminoth P., Saremaslani P., Schmid S., Locher T., Heitz P.U., Krull I., Galeazzi R.L., Schmid C., Perren A. J. Clin. Endocrinol. Metab. 89:362-367(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGL4 PRO-132.
[21]	"Somatic SDHB mutation in an extraadrenal pheochromocytoma." van Nederveen F.H., Korpershoek E., Lenders J.W.M., de Krijger R.R., Dinjens W.N.M. N. Engl. J. Med. 357:306-308(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHEOCHROMOCYTOMA PHE-100.
[22]	"Familial gastrointestinal stromal tumors and germ-line mutations." McWhinney S.R., Pasini B., Stratakis C.A. N. Engl. J. Med. 357:1054-1056(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PGGSS.
[23]	"Germline mutations and variants in the succinate dehydrogenase genes in Cowden and Cowden-like syndromes." Ni Y., Zbuk K.M., Sadler T., Patocs A., Lobo G., Edelman E., Platzer P., Orloff M.S., Waite K.A., Eng C. Am. J. Hum. Genet. 83:261-268(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLY-3 AND PRO-163, CHARACTERIZATION OF VARIANTS GLY-3 AND PRO-163, INVOLVEMENT IN CWDLS.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

TCA Cycle Gene Mutation Database

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17248 mRNA. Translation: AAA81167.1. U17886 , U17296, U17880, U17881, U17882, U17883, U17884, U17885 Genomic DNA. Translation: AAA80581.1. AK312056 mRNA. Translation: BAG34992.1. AL049569 Genomic DNA. Translation: CAB96822.1. CH471134 Genomic DNA. Translation: EAW94828.1. BC007840 mRNA. Translation: AAH07840.1. D10245 mRNA. Translation: BAA01089.1. M32246 mRNA. Translation: AAA35708.1.
IPI	IPI00294911.
PIR	I38895.
RefSeq	NP_002991.2. NM_003000.2.
UniGene	Hs.465924.
3D structure databases
ProteinModelPortal	P21912.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21912. 8 interactions.
MINT	MINT-3009566.
STRING	9606.ENSP00000364649.
PTM databases
PhosphoSite	P21912.
Polymorphism databases
DMDM	20455488.
2D gel databases
UCD-2DPAGE	P21912.
Proteomic databases
PaxDb	P21912.
PeptideAtlas	P21912.
PRIDE	P21912.
Protocols and materials databases
DNASU	6390.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375499; ENSP00000364649; ENSG00000117118.
GeneID	6390.
KEGG	hsa:6390.
UCSC	uc001bae.3. human.
Organism-specific databases
CTD	6390.
GeneCards	GC01M017345.
HGNC	HGNC:10681. SDHB.
HPA	CAB009822. HPA002867. HPA002868.
MIM	115310. phenotype. 171300. phenotype. 185470. gene. 606864. phenotype. 612359. phenotype.
neXtProt	NX_P21912.
Orphanet	97286. Carney-Stratakis syndrome. 201. Cowden syndrome. 44890. Gastrointestinal stromal tumor. 29072. Hereditary pheochromocytoma-paraganglioma. 3208. Isolated succinate-CoQ reductase deficiency.
PharmGKB	PA35606.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0479.
HOGENOM	HOG000160590.
HOVERGEN	HBG005483.
InParanoid	P21912.
KO	K00235.
OMA	NCSRTCP.
OrthoDB	EOG4T4CW4.
PhylomeDB	P21912.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000117118-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00223; UER01006.
Gene expression databases
ArrayExpress	P21912.
Bgee	P21912.
CleanEx	HS_SDHB.
Genevestigator	P21912.
GermOnline	ENSG00000117118. Homo sapiens.
Family and domain databases
Gene3D	1.10.1060.10. 1 hit. 3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. Beta-grasp_dom. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR004489. Succ_DH/fum_Rdtase_Fe-S. IPR025192. Succ_DH/fum_Rdtase_N. [Graphical view]
Pfam	PF13085. Fer2_3. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF46548. Helical_ferredxn. 1 hit.
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00139. Succinic acid.
GenomeRNAi	6390.
NextBio	24824.
SOURCE	Search...

Entry information

Entry name

DHSB_HUMAN

Accession

Primary (citable) accession number: P21912
Secondary accession number(s): B2R545, Q9NQ12

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 2, 2002
Last modified:	May 29, 2013
This is version 157 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.