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Q9CZB0

- C560_MOUSE

UniProt

Q9CZB0 - C560_MOUSE

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Protein

Succinate dehydrogenase cytochrome b560 subunit, mitochondrial

Gene

Sdhc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Membrane-anchoring 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

Cofactori

hemeBy similarityNote: The heme is bound between the two transmembrane subunits SDHC and SDHD.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271Iron (heme axial ligand); shared with SDHDBy similarity

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. heme binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. succinate dehydrogenase activity Source: InterPro

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_249033. Citric acid cycle (TCA cycle).
REACT_262523. Respiratory electron transport.
UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
Alternative name(s):
Integral membrane protein CII-3
QPs-1
Short name:
QPs1
Gene namesi
Name:Sdhc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1913302. Sdhc.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 6233Mitochondrial matrixBy similarityAdd
BLAST
Transmembranei63 – 9230HelicalBy similarityAdd
BLAST
Topological domaini93 – 11220Mitochondrial intermembraneBy similarityAdd
BLAST
Transmembranei113 – 13725HelicalBy similarityAdd
BLAST
Topological domaini138 – 1447Mitochondrial matrixBy similarity
Transmembranei145 – 16622HelicalBy similarityAdd
BLAST
Topological domaini167 – 1693Mitochondrial intermembraneBy similarity

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial respiratory chain complex II Source: UniProtKB
  4. mitochondrion 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 – 2929MitochondrionBy similarityAdd
BLAST
Chaini30 – 169140Succinate dehydrogenase cytochrome b560 subunit, mitochondrialPRO_0000003635Add
BLAST

Proteomic databases

MaxQBiQ9CZB0.
PaxDbiQ9CZB0.
PRIDEiQ9CZB0.

PTM databases

PhosphoSiteiQ9CZB0.

Expressioni

Gene expression databases

BgeeiQ9CZB0.
ExpressionAtlasiQ9CZB0. baseline and differential.
GenevestigatoriQ9CZB0.

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

IntActiQ9CZB0. 4 interactions.
MINTiMINT-4089551.

Structurei

3D structure databases

ProteinModelPortaliQ9CZB0.
SMRiQ9CZB0. Positions 32-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome b560 family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2009.
GeneTreeiENSGT00390000000566.
HOGENOMiHOG000160253.
HOVERGENiHBG003187.
InParanoidiQ9CZB0.
KOiK00236.
OMAiWNKNTSS.
OrthoDBiEOG7SV0WV.
PhylomeDBiQ9CZB0.
TreeFamiTF313317.

Family and domain databases

InterProiIPR018495. Succ_DH_cyt_bsu_CS.
IPR014314. Succ_DH_cytb556.
IPR014361. Succ_DH_cytb560.
IPR000701. Succ_DH_Fumarate_Rdtase_TM-su.
[Graphical view]
PfamiPF01127. Sdh_cyt. 1 hit.
[Graphical view]
PIRSFiPIRSF000178. SDH_cyt_b560. 1 hit.
TIGRFAMsiTIGR02970. succ_dehyd_cytB. 1 hit.
PROSITEiPS01000. SDH_CYT_1. 1 hit.
PS01001. SDH_CYT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CZB0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAFLLRHVS RHCLRAHLNA QLCIRNAAPL GTTAKEEMER FWKKNTSSNR
60 70 80 90 100
PLSPHLTIYK WSLPMALSVC HRGSGIALSG GVSLFGLSAL LLPGNFESYL
110 120 130 140 150
MFVKSLCLGP TLIYSAKFVL VFPLMYHSLN GIRHLLWDLG KGLAIPQVWL
160
SGVAVVVLAV LSSGGLAAL
Length:169
Mass (Da):18,382
Last modified:June 1, 2001 - v1
Checksum:iD9BFBCF936D0B9F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41F → L in AAH05779. (PubMed:15489334)Curated
Sequence conflicti10 – 101S → G in AAH05779. (PubMed:15489334)Curated
Sequence conflicti22 – 221L → R in BAB22116. (PubMed:16141072)Curated
Sequence conflicti91 – 911L → V in AAH05779. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002459 mRNA. Translation: BAB22116.1.
AK012818 mRNA. Translation: BAB28491.1.
AK032458 mRNA. Translation: BAC27878.1.
AK135503 mRNA. Translation: BAE22557.1.
BC005779 mRNA. Translation: AAH05779.1.
CCDSiCCDS35772.1.
RefSeqiNP_079597.2. NM_025321.3.
UniGeneiMm.198138.

Genome annotation databases

EnsembliENSMUST00000111336; ENSMUSP00000106968; ENSMUSG00000058076.
GeneIDi66052.
KEGGimmu:66052.
UCSCiuc007dnb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002459 mRNA. Translation: BAB22116.1 .
AK012818 mRNA. Translation: BAB28491.1 .
AK032458 mRNA. Translation: BAC27878.1 .
AK135503 mRNA. Translation: BAE22557.1 .
BC005779 mRNA. Translation: AAH05779.1 .
CCDSi CCDS35772.1.
RefSeqi NP_079597.2. NM_025321.3.
UniGenei Mm.198138.

3D structure databases

ProteinModelPortali Q9CZB0.
SMRi Q9CZB0. Positions 32-169.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9CZB0. 4 interactions.
MINTi MINT-4089551.

PTM databases

PhosphoSitei Q9CZB0.

Proteomic databases

MaxQBi Q9CZB0.
PaxDbi Q9CZB0.
PRIDEi Q9CZB0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000111336 ; ENSMUSP00000106968 ; ENSMUSG00000058076 .
GeneIDi 66052.
KEGGi mmu:66052.
UCSCi uc007dnb.2. mouse.

Organism-specific databases

CTDi 6391.
MGIi MGI:1913302. Sdhc.

Phylogenomic databases

eggNOGi COG2009.
GeneTreei ENSGT00390000000566.
HOGENOMi HOG000160253.
HOVERGENi HBG003187.
InParanoidi Q9CZB0.
KOi K00236.
OMAi WNKNTSS.
OrthoDBi EOG7SV0WV.
PhylomeDBi Q9CZB0.
TreeFami TF313317.

Enzyme and pathway databases

UniPathwayi UPA00223 .
Reactomei REACT_249033. Citric acid cycle (TCA cycle).
REACT_262523. Respiratory electron transport.

Miscellaneous databases

ChiTaRSi Sdhc. mouse.
NextBioi 320482.
PROi Q9CZB0.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZB0.
ExpressionAtlasi Q9CZB0. baseline and differential.
Genevestigatori Q9CZB0.

Family and domain databases

InterProi IPR018495. Succ_DH_cyt_bsu_CS.
IPR014314. Succ_DH_cytb556.
IPR014361. Succ_DH_cytb560.
IPR000701. Succ_DH_Fumarate_Rdtase_TM-su.
[Graphical view ]
Pfami PF01127. Sdh_cyt. 1 hit.
[Graphical view ]
PIRSFi PIRSF000178. SDH_cyt_b560. 1 hit.
TIGRFAMsi TIGR02970. succ_dehyd_cytB. 1 hit.
PROSITEi PS01000. SDH_CYT_1. 1 hit.
PS01001. SDH_CYT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain, Embryo, Kidney and Muellerian duct.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiC560_MOUSE
AccessioniPrimary (citable) accession number: Q9CZB0
Secondary accession number(s): Q544Q9, Q99JP2, Q9DCU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 105 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, 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