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P21912 (SDHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 + a quinone = fumarate + a quinol.

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.11 Ref.13 Ref.16 Ref.19 Ref.21

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.23

Cowden syndrome 2 (CWS2) [MIM:612359]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.24

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 processElectron transport
Transport
Tricarboxylic acid cycle
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Ligand2Fe-2S
3Fe-4S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaerobic respiration

Traceable author statement Ref.7. Source: ProtInc

cellular metabolic process

Traceable author statement. Source: Reactome

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: Ensembl

tricarboxylic acid cycle

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex II

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Traceable author statement Ref.7. Source: ProtInc

   Molecular_function2 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

protein binding

Inferred from physical interaction PubMed 15961414. Source: UniProtKB

succinate dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-EC

ubiquinone binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SDHAP310402EBI-1056481,EBI-1057265

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion
Chain29 – 280252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
PRO_0000010355

Regions

Domain40 – 133942Fe-2S ferredoxin-type
Domain176 – 206314Fe-4S ferredoxin-type

Sites

Metal binding931Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding981Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1011Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1131Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1861Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1891Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1921Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1961Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2431Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2491Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2531Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2011Ubiquinone; shared with DHSD By similarity

Amino acid modifications

Modified residue511N6-acetyllysine By similarity
Modified residue551N6-acetyllysine By similarity

Natural variations

Natural variant31A → G in CWS2; uncertain pathological significance; associated with increased manganese superoxide dismutase expression and normal levels of reactive oxygen species; associated with a 1.2-fold increase in AKT expression and 1.3-fold change in MAPK expression. Ref.24
Corresponds to variant rs11203289 [ dbSNP | Ensembl ].
VAR_054374
Natural variant291A → AQ in pheochromocytoma. Ref.14
VAR_035063
Natural variant401K → E. Ref.18
VAR_054375
Natural variant431A → P in pheochromocytoma. Ref.15
VAR_054376
Natural variant461R → G in pheochromocytoma. Ref.14 Ref.15 Ref.19
VAR_035064
Natural variant461R → Q in pheochromocytoma and PGL4. Ref.15 Ref.17 Ref.19
VAR_054377
Natural variant531G → R in pheochromocytoma. Ref.19
VAR_054378
Natural variant651L → H in pheochromocytoma. Ref.17
VAR_054379
Natural variant651L → P in pheochromocytoma. Ref.19
VAR_054380
Natural variant871L → S in pheochromocytoma. Ref.11 Ref.19
VAR_018517
Natural variant1001S → F in pheochromocytoma; absence of expression in tumor cells indicating complete loss of SDHB function. Ref.22
VAR_037620
Natural variant1011C → Y in pheochromocytoma. Ref.14 Ref.19
VAR_035065
Natural variant1271I → N in pheochromocytoma. Ref.16
VAR_054381
Natural variant1311P → R in PGL4. Ref.13
VAR_018518
Natural variant1321H → P in PGL4. Ref.21
VAR_037621
Natural variant1631S → P in CWS2; uncertain pathological significance; associated with increased manganese superoxide dismutase function and increased levels of reactive oxygen species; associated with a 2.7-fold change in AKT expression and a 1.7-fold increase in MAPK expression. Ref.24
Corresponds to variant rs33927012 [ dbSNP | Ensembl ].
VAR_054382
Natural variant1921C → R in pheochromocytoma. Ref.14 Ref.19
VAR_035066
Natural variant1961C → Y in pheochromocytoma. Ref.14 Ref.19
VAR_035067
Natural variant1971P → R in PGL4. Ref.11 Ref.16
VAR_017868
Natural variant2301R → C in pheochromocytoma. Ref.15
Corresponds to variant rs138996609 [ dbSNP | Ensembl ].
VAR_054383
Natural variant2421R → H in familial malignant paraganglioma and pheochromocytoma, pheochromocytoma and PGL4. Ref.12 Ref.14 Ref.19
VAR_017869

Experimental info

Sequence conflict19 – 213GGA → WRT in AAA35708. Ref.7
Sequence conflict19 – 213GGA → WRT in BAA01089. Ref.7
Sequence conflict621E → K in AAA81167. Ref.1
Sequence conflict621E → K in AAA35708. Ref.7
Sequence conflict621E → K in BAA01089. Ref.7
Sequence conflict671K → NR in AAA80581. Ref.1
Sequence conflict1511K → R no nucleotide entry Ref.8
Sequence conflict1721Q → E no nucleotide entry Ref.8

Sequences

Sequence LengthMass (Da)Tools
P21912 [UniParc].

Last modified May 2, 2002. Version 3.
Checksum: ED12E7C3BA7B6D13

FASTA28031,630
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-264.
[7]"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.
[8]"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.
[9]Erratum
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
[10]"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].
[11]"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.
[12]"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.
[13]"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.
[14]"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. expand/collapse author list , 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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]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)
[21]"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.
[22]"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.
[23]"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.
[24]"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 CWS2 GLY-3 AND PRO-163, CHARACTERIZATION OF VARIANTS CWS2 GLY-3 AND PRO-163.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17248 mRNA. Translation: AAA81167.1.
U17886 expand/collapse EMBL AC list , 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.
DQ403007 mRNA. Translation: ABD77140.1.
D10245 mRNA. Translation: BAA01089.1.
M32246 mRNA. Translation: AAA35708.1.
CCDSCCDS176.1.
PIRI38895.
RefSeqNP_002991.2. NM_003000.2.
UniGeneHs.465924.

3D structure databases

ProteinModelPortalP21912.
SMRP21912. Positions 37-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112291. 45 interactions.
IntActP21912. 9 interactions.
MINTMINT-3009566.
STRING9606.ENSP00000364649.

Chemistry

DrugBankDB00139. Succinic acid.

PTM databases

PhosphoSiteP21912.

Polymorphism databases

DMDM20455488.

2D gel databases

UCD-2DPAGEP21912.

Proteomic databases

MaxQBP21912.
PaxDbP21912.
PeptideAtlasP21912.
PRIDEP21912.

Protocols and materials databases

DNASU6390.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375499; ENSP00000364649; ENSG00000117118.
GeneID6390.
KEGGhsa:6390.
UCSCuc001bae.3. human.

Organism-specific databases

CTD6390.
GeneCardsGC01M017345.
GeneReviewsSDHB.
HGNCHGNC:10681. SDHB.
HPACAB009822.
HPA002867.
HPA002868.
MIM115310. phenotype.
171300. phenotype.
185470. gene.
606864. phenotype.
612359. phenotype.
neXtProtNX_P21912.
Orphanet97286. Carney-Stratakis syndrome.
201. Cowden syndrome.
44890. Gastrointestinal stromal tumor.
29072. Hereditary pheochromocytoma-paraganglioma.
3208. Isolated succinate-CoQ reductase deficiency.
PharmGKBPA35606.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
HOVERGENHBG005483.
InParanoidP21912.
KOK00235.
OMAIMNCSRT.
OrthoDBEOG7H4DTN.
PhylomeDBP21912.
TreeFamTF300754.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000117118-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00223; UER01006.

Gene expression databases

ArrayExpressP21912.
BgeeP21912.
CleanExHS_SDHB.
GenevestigatorP21912.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 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]
ProtoNetSearch...

Other

GeneWikiSDHB.
GenomeRNAi6390.
NextBio24824.
PROP21912.
SOURCESearch...

Entry information

Entry nameSDHB_HUMAN
AccessionPrimary (citable) accession number: P21912
Secondary accession number(s): B2R545, Q0QEY7, Q9NQ12
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM