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Q8K2B3

- SDHA_MOUSE

UniProt

Q8K2B3 - SDHA_MOUSE

Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

Sdha

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Flavoprotein (FP) 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). Can act as a tumor suppressor.By similarity

    Catalytic activityi

    Succinate + a quinone = fumarate + a quinol.

    Cofactori

    FAD.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei275 – 2751FADBy similarity
    Binding sitei296 – 2961SubstrateBy similarity
    Binding sitei308 – 3081SubstrateBy similarity
    Active sitei340 – 3401Proton acceptorBy similarity
    Binding sitei407 – 4071SubstrateBy similarity
    Binding sitei440 – 4401FADBy similarity
    Binding sitei451 – 4511SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi68 – 736FADBy similarity
    Nucleotide bindingi91 – 10616FADBy similarityAdd
    BLAST
    Nucleotide bindingi456 – 4572FADBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

    GO - Biological processi

    1. nervous system development Source: Ensembl
    2. respiratory electron transport chain Source: UniProtKB
    3. succinate metabolic process Source: UniProtKB
    4. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport, Tricarboxylic acid cycle

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER01006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1)
    Alternative name(s):
    Flavoprotein subunit of complex II
    Short name:
    Fp
    Gene namesi
    Name:Sdha
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1914195. Sdha.

    Subcellular locationi

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

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB
    2. mitochondrial respiratory chain complex II Source: UniProtKB
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343MitochondrionBy similarityAdd
    BLAST
    Chaini44 – 664621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000010337Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991Tele-8alpha-FAD histidineBy similarity
    Modified residuei167 – 1671N6-acetyllysine1 Publication
    Modified residuei179 – 1791N6-acetyllysine; alternate3 Publications
    Modified residuei179 – 1791N6-succinyllysine; alternate1 Publication
    Modified residuei182 – 1821N6-acetyllysine2 Publications
    Modified residuei215 – 2151Phosphotyrosine; by SRCBy similarity
    Modified residuei250 – 2501N6-acetyllysine; alternate1 Publication
    Modified residuei250 – 2501N6-succinyllysine; alternate1 Publication
    Modified residuei335 – 3351N6-acetyllysine; alternate2 Publications
    Modified residuei335 – 3351N6-succinyllysine; alternate1 Publication
    Modified residuei423 – 4231N6-acetyllysine1 Publication
    Modified residuei480 – 4801N6-acetyllysine1 Publication
    Modified residuei485 – 4851N6-acetyllysine; alternate1 Publication
    Modified residuei485 – 4851N6-succinyllysine; alternate1 Publication
    Modified residuei498 – 4981N6-acetyllysine; alternate2 Publications
    Modified residuei498 – 4981N6-succinyllysine; alternate1 Publication
    Modified residuei517 – 5171N6-acetyllysine1 Publication
    Modified residuei538 – 5381N6-acetyllysine; alternate1 Publication
    Modified residuei538 – 5381N6-succinyllysine; alternate1 Publication
    Modified residuei547 – 5471N6-acetyllysine; alternate3 Publications
    Modified residuei547 – 5471N6-succinyllysine; alternate1 Publication
    Modified residuei550 – 5501N6-acetyllysine1 Publication
    Modified residuei598 – 5981N6-acetyllysine1 Publication
    Modified residuei608 – 6081N6-acetyllysine2 Publications
    Modified residuei615 – 6151N6-succinyllysine1 Publication
    Modified residuei624 – 6241N6-acetyllysine1 Publication
    Modified residuei633 – 6331N6-acetyllysine1 Publication
    Modified residuei636 – 6361N6-acetyllysine1 Publication
    Modified residuei647 – 6471N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice. Deacetylated by SIRT3.3 Publications
    Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8K2B3.
    PaxDbiQ8K2B3.
    PRIDEiQ8K2B3.

    2D gel databases

    REPRODUCTION-2DPAGEQ8K2B3.

    PTM databases

    PhosphoSiteiQ8K2B3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8K2B3.
    BgeeiQ8K2B3.
    GenevestigatoriQ8K2B3.

    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. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity. Interacts with TRAP1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8K2B3. 7 interactions.
    MINTiMINT-4122544.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K2B3.
    SMRiQ8K2B3. Positions 52-664.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1053.
    GeneTreeiENSGT00390000010046.
    HOVERGENiHBG001461.
    InParanoidiQ8K2B3.
    KOiK00234.
    OMAiRTEQGRI.
    OrthoDBiEOG7MH0XJ.
    PhylomeDBiQ8K2B3.
    TreeFamiTF300763.

    Family and domain databases

    Gene3Di1.20.58.100. 1 hit.
    3.90.700.10. 1 hit.
    InterProiIPR003953. FAD_bind_dom.
    IPR003952. FRD_SDH_FAD_BS.
    IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    IPR011281. Succ_DH_flav_su_fwd.
    IPR014006. Succ_Dhase_FrdA_Gneg.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    PF02910. Succ_DH_flav_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF46977. SSF46977. 1 hit.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
    TIGR01812. sdhA_frdA_Gneg. 1 hit.
    PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8K2B3-1 [UniParc]FASTAAdd to Basket

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    MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA    50
    ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT 100
    VAAQGGINAA LGNMEEDNWR WHFYDTVKGS DWLGDQDAIH YMTEQAPASV 150
    VELENYGMPF SRTEDGKIYQ RAFGGQSLKF GKGGQAHRCC CVADRTGHSL 200
    LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE DGSIHRIRAK 250
    NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI 300
    YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE 350
    IREGRGCGPE KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI 400
    PVLPTVHYNM GGIPTNYKGQ VLKHVNGQDQ IVPGLYACGE AACASVHGAN 450
    RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKANAGE ESVMNLDKLR 500
    FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS QLYGDLKHLK 550
    TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR 600
    VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN 650
    EADCATVPPA IRSY 664
    Length:664
    Mass (Da):72,585
    Last modified:October 1, 2002 - v1
    Checksum:iDDCE1535163C9449
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691A → V in BAE26754. (PubMed:16141072)Curated
    Sequence conflicti246 – 2461R → Q in BAE26754. (PubMed:16141072)Curated
    Sequence conflicti428 – 4281Q → R in BAE26754. (PubMed:16141072)Curated
    Sequence conflicti501 – 5011F → L in ABD77308. (PubMed:16751257)Curated
    Sequence conflicti517 – 5171K → M in ABD77308. (PubMed:16751257)Curated
    Sequence conflicti571 – 5711L → M in ABD77308. (PubMed:16751257)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029520 mRNA. Translation: BAC26491.1.
    AK034928 mRNA. Translation: BAC28884.1.
    AK049590 mRNA. Translation: BAC33831.1.
    AK050475 mRNA. Translation: BAC34276.1.
    AK075990 mRNA. Translation: BAC36101.1.
    AK145923 mRNA. Translation: BAE26754.1.
    AK147286 mRNA. Translation: BAE27822.1.
    AK147624 mRNA. Translation: BAE28032.1.
    AK153085 mRNA. Translation: BAE31710.1.
    AK162148 mRNA. Translation: BAE36754.1.
    AK169254 mRNA. Translation: BAE41018.1.
    AK004362 mRNA. Translation: BAE43173.1.
    BC011301 mRNA. Translation: AAH11301.1.
    BC031849 mRNA. Translation: AAH31849.1.
    DQ402975 mRNA. Translation: ABD77308.1.
    AF095938 mRNA. Translation: AAC72373.1.
    CCDSiCCDS26643.1.
    RefSeqiNP_075770.1. NM_023281.1.
    UniGeneiMm.158231.

    Genome annotation databases

    EnsembliENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
    GeneIDi66945.
    KEGGimmu:66945.
    UCSCiuc007rfa.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029520 mRNA. Translation: BAC26491.1 .
    AK034928 mRNA. Translation: BAC28884.1 .
    AK049590 mRNA. Translation: BAC33831.1 .
    AK050475 mRNA. Translation: BAC34276.1 .
    AK075990 mRNA. Translation: BAC36101.1 .
    AK145923 mRNA. Translation: BAE26754.1 .
    AK147286 mRNA. Translation: BAE27822.1 .
    AK147624 mRNA. Translation: BAE28032.1 .
    AK153085 mRNA. Translation: BAE31710.1 .
    AK162148 mRNA. Translation: BAE36754.1 .
    AK169254 mRNA. Translation: BAE41018.1 .
    AK004362 mRNA. Translation: BAE43173.1 .
    BC011301 mRNA. Translation: AAH11301.1 .
    BC031849 mRNA. Translation: AAH31849.1 .
    DQ402975 mRNA. Translation: ABD77308.1 .
    AF095938 mRNA. Translation: AAC72373.1 .
    CCDSi CCDS26643.1.
    RefSeqi NP_075770.1. NM_023281.1.
    UniGenei Mm.158231.

    3D structure databases

    ProteinModelPortali Q8K2B3.
    SMRi Q8K2B3. Positions 52-664.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8K2B3. 7 interactions.
    MINTi MINT-4122544.

    PTM databases

    PhosphoSitei Q8K2B3.

    2D gel databases

    REPRODUCTION-2DPAGE Q8K2B3.

    Proteomic databases

    MaxQBi Q8K2B3.
    PaxDbi Q8K2B3.
    PRIDEi Q8K2B3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022062 ; ENSMUSP00000022062 ; ENSMUSG00000021577 .
    GeneIDi 66945.
    KEGGi mmu:66945.
    UCSCi uc007rfa.1. mouse.

    Organism-specific databases

    CTDi 6389.
    MGIi MGI:1914195. Sdha.

    Phylogenomic databases

    eggNOGi COG1053.
    GeneTreei ENSGT00390000010046.
    HOVERGENi HBG001461.
    InParanoidi Q8K2B3.
    KOi K00234.
    OMAi RTEQGRI.
    OrthoDBi EOG7MH0XJ.
    PhylomeDBi Q8K2B3.
    TreeFami TF300763.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01006 .

    Miscellaneous databases

    ChiTaRSi SdhA. mouse.
    NextBioi 323092.
    PROi Q8K2B3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8K2B3.
    Bgeei Q8K2B3.
    Genevestigatori Q8K2B3.

    Family and domain databases

    Gene3Di 1.20.58.100. 1 hit.
    3.90.700.10. 1 hit.
    InterProi IPR003953. FAD_bind_dom.
    IPR003952. FRD_SDH_FAD_BS.
    IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    IPR011281. Succ_DH_flav_su_fwd.
    IPR014006. Succ_Dhase_FrdA_Gneg.
    [Graphical view ]
    Pfami PF00890. FAD_binding_2. 1 hit.
    PF02910. Succ_DH_flav_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46977. SSF46977. 1 hit.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
    TIGR01812. sdhA_frdA_Gneg. 1 hit.
    PROSITEi PS00504. FRD_SDH_FAD_BINDING. 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: Bone marrow, Egg, Heart, Pancreas and Testis.
    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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary gland and Mammary tumor.
    3. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282; 313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND 637-647.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    4. "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 59-609.
      Tissue: Liver.
    5. "OXPHOS genes in mammals and the molecular clock."
      Weinreich D.M.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
      Tissue: Heart.
    6. "Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity."
      Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V., Gygi S.P., Haigis M.C.
      PLoS ONE 6:E23295-E23295(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-179; LYS-182; LYS-250; LYS-335; LYS-480; LYS-485; LYS-498; LYS-547; LYS-550; LYS-598; LYS-608; LYS-624 AND LYS-633, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-547, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-250; LYS-335; LYS-485; LYS-498; LYS-538; LYS-547 AND LYS-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    8. "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(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-179; LYS-182; LYS-335; LYS-423; LYS-498; LYS-517; LYS-538; LYS-547; LYS-608; LYS-636 AND LYS-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSDHA_MOUSE
    AccessioniPrimary (citable) accession number: Q8K2B3
    Secondary accession number(s): Q0QF19
    , Q3UH25, Q3UKP7, Q3V4B1, Q921P5, Q9Z1Z4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 111 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