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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

Sdhb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi95 – 951Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi100 – 1001Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi103 – 1031Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi115 – 1151Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi188 – 1881Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi191 – 1911Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi194 – 1941Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi198 – 1981Iron-sulfur 3 (3Fe-4S)By similarity
Binding sitei203 – 2031Ubiquinone; shared with DHSDBy similarity
Metal bindingi245 – 2451Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi251 – 2511Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi255 – 2551Iron-sulfur 2 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. 3 iron, 4 sulfur cluster binding Source: UniProtKB
  3. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  4. electron carrier activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  7. ubiquinone binding Source: UniProtKB

GO - Biological processi

  1. respiratory electron transport chain Source: Ensembl
  2. succinate metabolic process Source: Ensembl
  3. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_278797. Respiratory electron transport.
REACT_333358. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Sdhb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914930. Sdhb.

Subcellular locationi

Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) Source: UniProtKB
  4. mitochondrion Source: MGI
  5. respiratory chain complex II Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 282252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine1 Publication
Modified residuei57 – 571N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CQA3.
PaxDbiQ9CQA3.
PRIDEiQ9CQA3.

2D gel databases

REPRODUCTION-2DPAGEQ9CQA3.

PTM databases

PhosphoSiteiQ9CQA3.

Expressioni

Gene expression databases

BgeeiQ9CQA3.
ExpressionAtlasiQ9CQA3. baseline and differential.
GenevestigatoriQ9CQA3.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

BioGridi212362. 1 interaction.
IntActiQ9CQA3. 5 interactions.
MINTiMINT-1860322.

Structurei

3D structure databases

ProteinModelPortaliQ9CQA3.
SMRiQ9CQA3. Positions 39-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 135942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini178 – 208314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0479.
GeneTreeiENSGT00390000013558.
HOGENOMiHOG000160590.
HOVERGENiHBG005483.
InParanoidiQ9CQA3.
KOiK00235.
OMAiIDSHERM.
OrthoDBiEOG7H4DTN.
PhylomeDBiQ9CQA3.
TreeFamiTF300754.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATVGVSLK RGFPAAVLGR VGLQFQACRG AQTAAAAAPR IKKFAIYRWD
60 70 80 90 100
PDKTGDKPRM QTYEVDLNKC GPMVLDALIK IKNEVDSTLT FRRSCREGIC
110 120 130 140 150
GSCAMNINGG NTLACTRRID TDLSKVSKIY PLPHMYVIKD LVPDLSNFYA
160 170 180 190 200
QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE KLDGLYECIL CACCSTSCPS
210 220 230 240 250
YWWNGDKYLG PAVLMQAYRW MIDSRDDFTE ERLAKLQDPF SVYRCHTIMN
260 270 280
CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA
Length:282
Mass (Da):31,814
Last modified:May 31, 2001 - v1
Checksum:iA8616A911427AF8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401R → K in BAB22534 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003052 mRNA. Translation: BAB22534.1.
AK003533 mRNA. Translation: BAB22842.1.
AK009660 mRNA. Translation: BAB26422.1.
AK153045 mRNA. Translation: BAE31674.1.
AK169252 mRNA. Translation: BAE41016.1.
BC013509 mRNA. Translation: AAH13509.1.
BC051934 mRNA. Translation: AAH51934.1.
CCDSiCCDS18858.1.
PIRiPT0094.
RefSeqiNP_075863.2. NM_023374.3.
UniGeneiMm.246965.

Genome annotation databases

EnsembliENSMUST00000010007; ENSMUSP00000010007; ENSMUSG00000009863.
GeneIDi67680.
KEGGimmu:67680.
UCSCiuc008vnl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003052 mRNA. Translation: BAB22534.1.
AK003533 mRNA. Translation: BAB22842.1.
AK009660 mRNA. Translation: BAB26422.1.
AK153045 mRNA. Translation: BAE31674.1.
AK169252 mRNA. Translation: BAE41016.1.
BC013509 mRNA. Translation: AAH13509.1.
BC051934 mRNA. Translation: AAH51934.1.
CCDSiCCDS18858.1.
PIRiPT0094.
RefSeqiNP_075863.2. NM_023374.3.
UniGeneiMm.246965.

3D structure databases

ProteinModelPortaliQ9CQA3.
SMRiQ9CQA3. Positions 39-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212362. 1 interaction.
IntActiQ9CQA3. 5 interactions.
MINTiMINT-1860322.

PTM databases

PhosphoSiteiQ9CQA3.

2D gel databases

REPRODUCTION-2DPAGEQ9CQA3.

Proteomic databases

MaxQBiQ9CQA3.
PaxDbiQ9CQA3.
PRIDEiQ9CQA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000010007; ENSMUSP00000010007; ENSMUSG00000009863.
GeneIDi67680.
KEGGimmu:67680.
UCSCiuc008vnl.1. mouse.

Organism-specific databases

CTDi6390.
MGIiMGI:1914930. Sdhb.

Phylogenomic databases

eggNOGiCOG0479.
GeneTreeiENSGT00390000013558.
HOGENOMiHOG000160590.
HOVERGENiHBG005483.
InParanoidiQ9CQA3.
KOiK00235.
OMAiIDSHERM.
OrthoDBiEOG7H4DTN.
PhylomeDBiQ9CQA3.
TreeFamiTF300754.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
ReactomeiREACT_278797. Respiratory electron transport.
REACT_333358. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiSdhb. mouse.
NextBioi325239.
PROiQ9CQA3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQA3.
ExpressionAtlasiQ9CQA3. baseline and differential.
GenevestigatoriQ9CQA3.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Bone marrow, Brain and Tongue.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Colon.
  3. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 49-92; 118-153; 170-179; 208-232 AND 245-257, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSDHB_MOUSE
AccessioniPrimary (citable) accession number: Q9CQA3
Secondary accession number(s): Q3TF82, Q9DC91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2004
Last sequence update: May 31, 2001
Last modified: March 31, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.