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Q60597

- ODO1_MOUSE

UniProt

Q60597 - ODO1_MOUSE

Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

Ogdh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.

    Enzyme regulationi

    Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi154 – 1541CalciumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi154 – 1585By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. oxoglutarate dehydrogenase (NAD+) activity Source: MGI
    3. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
    4. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: Ensembl
    2. cerebellar cortex development Source: UniProtKB
    3. generation of precursor metabolites and energy Source: UniProtKB
    4. glycolytic process Source: UniProtKB-KW
    5. hippocampus development Source: UniProtKB
    6. NADH metabolic process Source: Ensembl
    7. olfactory bulb mitral cell layer development Source: UniProtKB
    8. pyramidal neuron development Source: UniProtKB
    9. striatum development Source: UniProtKB
    10. succinyl-CoA metabolic process Source: Ensembl
    11. tangential migration from the subventricular zone to the olfactory bulb Source: UniProtKB
    12. thalamus development Source: UniProtKB
    13. tricarboxylic acid cycle Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Calcium, Metal-binding, Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase, mitochondrial (EC:1.2.4.2)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E1
    Short name:
    OGDC-E1
    Alpha-ketoglutarate dehydrogenase
    Gene namesi
    Name:Ogdh
    Synonyms:Kiaa4192
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1098267. Ogdh.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrial membrane Source: UniProtKB
    3. mitochondrion Source: MGI
    4. oxoglutarate dehydrogenase complex Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040MitochondrionBy similarityAdd
    BLAST
    Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrialPRO_0000020434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741N6-succinyllysine1 Publication
    Modified residuei401 – 4011N6-acetyllysine1 Publication
    Cross-linki534 – 534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei564 – 5641N6-succinyllysine1 Publication
    Modified residuei970 – 9701N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ60597.
    PaxDbiQ60597.
    PRIDEiQ60597.

    2D gel databases

    REPRODUCTION-2DPAGEQ60597.

    PTM databases

    PhosphoSiteiQ60597.

    Expressioni

    Gene expression databases

    ArrayExpressiQ60597.
    BgeeiQ60597.
    CleanExiMM_OGDH.
    GenevestigatoriQ60597.

    Interactioni

    Protein-protein interaction databases

    IntActiQ60597. 5 interactions.
    MINTiMINT-1860288.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E2HX-ray3.80Q932-940[»]
    3TF7X-ray2.75B/F932-940[»]
    ProteinModelPortaliQ60597.
    SMRiQ60597. Positions 130-1014.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni933 – 9397Recognized by alloreactive CD8 cytotoxic T-lymphocytes in association with a class I MHC protein

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0567.
    GeneTreeiENSGT00530000063092.
    HOVERGENiHBG001892.
    KOiK00164.
    OMAiMLSGTHF.
    OrthoDBiEOG7FXZXH.
    PhylomeDBiQ60597.
    TreeFamiTF300695.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view]
    PANTHERiPTHR23152. PTHR23152. 1 hit.
    PfamiPF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q60597-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL     50
    SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS 100
    RSSLATMAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL 150
    GILDADLDSS VPADIISSTD KLGFYGLHES DLDKVFHLPT TTFIGGQEPA 200
    LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE 250
    KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN 300
    GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH 350
    LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG 400
    KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT 450
    DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRNTFHKD 500
    VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV 550
    NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR 600
    SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT 650
    VDWALAEYMA FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC 700
    IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF 750
    NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ 800
    MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH VLRRQILLPF 850
    RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR 900
    LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN 950
    AELAWCQEEH KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK 1000
    THLTELQRFL DTAFDLDAFK KFS 1023
    Length:1,023
    Mass (Da):116,449
    Last modified:May 1, 2007 - v3
    Checksum:iA0F3F8D36C7A76BC
    GO
    Isoform 2 (identifier: Q60597-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-172: IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL → VRGHHIAKSCVNFDDAPVTVSSNV

    Show »
    Length:1,013
    Mass (Da):115,419
    Checksum:i64CBC6F0E46B5D5F
    GO
    Isoform 3 (identifier: Q60597-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         172-172: L → LDLAVFKERLRMLTVG

    Note: No experimental confirmation available.

    Show »
    Length:1,038
    Mass (Da):118,179
    Checksum:i7DC3C47068B12D2C
    GO
    Isoform 4 (identifier: Q60597-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-172: IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL → VRGHHIAKLD...KERLRMLTVG

    Show »
    Length:1,034
    Mass (Da):117,758
    Checksum:i7023215EEEE9516B
    GO

    Sequence cautioni

    The sequence AAH31165.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD90530.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti416 – 4161G → V in AAH49104. (PubMed:15489334)Curated
    Sequence conflicti549 – 5491V → F in AAH49104. (PubMed:15489334)Curated
    Sequence conflicti552 – 5521Q → E in AAH57354. (PubMed:15489334)Curated
    Sequence conflicti576 – 5761E → K in BAE29234. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 17234IRGHH…STDKL → VRGHHIAKSCVNFDDAPVTV SSNV in isoform 2. 1 PublicationVSP_024799Add
    BLAST
    Alternative sequencei139 – 17234IRGHH…STDKL → VRGHHIAKLDPLGISCVNFD DAPVTVSSNVDLAVFKERLR MLTVG in isoform 4. 1 PublicationVSP_024800Add
    BLAST
    Alternative sequencei172 – 1721L → LDLAVFKERLRMLTVG in isoform 3. 1 PublicationVSP_024801

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147289 mRNA. Translation: BAE27824.1.
    AK150009 mRNA. Translation: BAE29234.1.
    AK169286 mRNA. Translation: BAE41044.1.
    AK220536 mRNA. Translation: BAD90530.1. Different initiation.
    AL607152 Genomic DNA. Translation: CAI24404.1.
    AL607152 Genomic DNA. Translation: CAI24405.1.
    AL607152 Genomic DNA. Translation: CAI24406.1.
    BC025040 mRNA. Translation: AAH25040.1.
    BC013670 mRNA. Translation: AAH13670.1.
    BC029143 mRNA. Translation: AAH29143.1.
    BC031165 mRNA. Translation: AAH31165.1. Different initiation.
    BC049104 mRNA. Translation: AAH49104.1.
    BC057354 mRNA. Translation: AAH57354.1.
    U02971 mRNA. Translation: AAC52130.1.
    CCDSiCCDS36106.1. [Q60597-1]
    CCDS56758.1. [Q60597-4]
    PIRiI48884. A41911.
    RefSeqiNP_001239211.1. NM_001252282.1. [Q60597-3]
    NP_001239212.1. NM_001252283.1. [Q60597-4]
    NP_001239216.1. NM_001252287.1. [Q60597-1]
    NP_001239217.1. NM_001252288.1.
    NP_035086.2. NM_010956.4. [Q60597-1]
    XP_006514645.1. XM_006514582.1. [Q60597-4]
    XP_006514646.1. XM_006514583.1. [Q60597-4]
    XP_006514647.1. XM_006514584.1. [Q60597-4]
    XP_006514648.1. XM_006514585.1. [Q60597-1]
    UniGeneiMm.276348.
    Mm.479411.
    Mm.490272.

    Genome annotation databases

    EnsembliENSMUST00000003461; ENSMUSP00000003461; ENSMUSG00000020456. [Q60597-1]
    ENSMUST00000093350; ENSMUSP00000091041; ENSMUSG00000020456. [Q60597-4]
    ENSMUST00000101554; ENSMUSP00000099090; ENSMUSG00000020456. [Q60597-1]
    GeneIDi18293.
    KEGGimmu:18293.
    UCSCiuc007hyf.2. mouse. [Q60597-1]
    uc007hyg.2. mouse. [Q60597-3]
    uc007hyh.2. mouse. [Q60597-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147289 mRNA. Translation: BAE27824.1 .
    AK150009 mRNA. Translation: BAE29234.1 .
    AK169286 mRNA. Translation: BAE41044.1 .
    AK220536 mRNA. Translation: BAD90530.1 . Different initiation.
    AL607152 Genomic DNA. Translation: CAI24404.1 .
    AL607152 Genomic DNA. Translation: CAI24405.1 .
    AL607152 Genomic DNA. Translation: CAI24406.1 .
    BC025040 mRNA. Translation: AAH25040.1 .
    BC013670 mRNA. Translation: AAH13670.1 .
    BC029143 mRNA. Translation: AAH29143.1 .
    BC031165 mRNA. Translation: AAH31165.1 . Different initiation.
    BC049104 mRNA. Translation: AAH49104.1 .
    BC057354 mRNA. Translation: AAH57354.1 .
    U02971 mRNA. Translation: AAC52130.1 .
    CCDSi CCDS36106.1. [Q60597-1 ]
    CCDS56758.1. [Q60597-4 ]
    PIRi I48884. A41911.
    RefSeqi NP_001239211.1. NM_001252282.1. [Q60597-3 ]
    NP_001239212.1. NM_001252283.1. [Q60597-4 ]
    NP_001239216.1. NM_001252287.1. [Q60597-1 ]
    NP_001239217.1. NM_001252288.1.
    NP_035086.2. NM_010956.4. [Q60597-1 ]
    XP_006514645.1. XM_006514582.1. [Q60597-4 ]
    XP_006514646.1. XM_006514583.1. [Q60597-4 ]
    XP_006514647.1. XM_006514584.1. [Q60597-4 ]
    XP_006514648.1. XM_006514585.1. [Q60597-1 ]
    UniGenei Mm.276348.
    Mm.479411.
    Mm.490272.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E2H X-ray 3.80 Q 932-940 [» ]
    3TF7 X-ray 2.75 B/F 932-940 [» ]
    ProteinModelPortali Q60597.
    SMRi Q60597. Positions 130-1014.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q60597. 5 interactions.
    MINTi MINT-1860288.

    Chemistry

    ChEMBLi CHEMBL2176831.

    PTM databases

    PhosphoSitei Q60597.

    2D gel databases

    REPRODUCTION-2DPAGE Q60597.

    Proteomic databases

    MaxQBi Q60597.
    PaxDbi Q60597.
    PRIDEi Q60597.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003461 ; ENSMUSP00000003461 ; ENSMUSG00000020456 . [Q60597-1 ]
    ENSMUST00000093350 ; ENSMUSP00000091041 ; ENSMUSG00000020456 . [Q60597-4 ]
    ENSMUST00000101554 ; ENSMUSP00000099090 ; ENSMUSG00000020456 . [Q60597-1 ]
    GeneIDi 18293.
    KEGGi mmu:18293.
    UCSCi uc007hyf.2. mouse. [Q60597-1 ]
    uc007hyg.2. mouse. [Q60597-3 ]
    uc007hyh.2. mouse. [Q60597-4 ]

    Organism-specific databases

    CTDi 4967.
    MGIi MGI:1098267. Ogdh.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0567.
    GeneTreei ENSGT00530000063092.
    HOVERGENi HBG001892.
    KOi K00164.
    OMAi MLSGTHF.
    OrthoDBi EOG7FXZXH.
    PhylomeDBi Q60597.
    TreeFami TF300695.

    Miscellaneous databases

    ChiTaRSi OGDH. mouse.
    NextBioi 293740.
    PROi Q60597.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60597.
    Bgeei Q60597.
    CleanExi MM_OGDH.
    Genevestigatori Q60597.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view ]
    PANTHERi PTHR23152. PTHR23152. 1 hit.
    Pfami PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
    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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Bone marrow.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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] (ISOFORMS 1; 2 AND 4).
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain, Colon, Mammary tumor and Salivary gland.
    5. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 123-135; 185-204; 311-319; 561-568; 616-633 AND 916-925, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    6. "A ubiquitous protein is the source of naturally occurring peptides that are recognized by a CD8+ T-cell clone."
      Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.
      Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4).
      Strain: BALB/c.
    7. "A naturally occurring peptide recognized by alloreactive CD8+ cytotoxic T lymphocytes in association with a class I MHC protein."
      Udaka K., Tsomides T.J., Eisen H.N.
      Cell 69:989-998(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 933-939.
    8. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiODO1_MOUSE
    AccessioniPrimary (citable) accession number: Q60597
    Secondary accession number(s): Q3UDM7
    , Q5DTI4, Q5SVX7, Q5SVX9, Q6PFZ2, Q80Y57, Q8K0K7, Q8K2Z3, Q8R3M2, Q91WP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3