Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

Ogdh

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

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

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

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: Ensembl
  • cerebellar cortex development Source: UniProtKB
  • generation of precursor metabolites and energy Source: UniProtKB
  • glycolytic process Source: UniProtKB-KW
  • hippocampus development Source: UniProtKB
  • NADH metabolic process Source: Ensembl
  • olfactory bulb mitral cell layer development Source: UniProtKB
  • pyramidal neuron development Source: UniProtKB
  • striatum development Source: UniProtKB
  • succinyl-CoA metabolic process Source: Ensembl
  • tangential migration from the subventricular zone to the olfactory bulb Source: UniProtKB
  • thalamus development Source: UniProtKB
  • tricarboxylic acid cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Calcium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_329568. Lysine catabolism.
REACT_333358. Citric acid cycle (TCA cycle).

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 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1098267. Ogdh.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

BgeeiQ60597.
CleanExiMM_OGDH.
ExpressionAtlasiQ60597. baseline and differential.
GenevestigatoriQ60597.

Interactioni

Protein-protein interaction databases

IntActiQ60597. 5 interactions.
MINTiMINT-1860288.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ60597.
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. AlignAdd to basket

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

        10         20         30         40         50
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL
60 70 80 90 100
SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS
110 120 130 140 150
RSSLATMAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL
160 170 180 190 200
GILDADLDSS VPADIISSTD KLGFYGLHES DLDKVFHLPT TTFIGGQEPA
210 220 230 240 250
LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE
260 270 280 290 300
KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN
310 320 330 340 350
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH
360 370 380 390 400
LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG
410 420 430 440 450
KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT
460 470 480 490 500
DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRNTFHKD
510 520 530 540 550
VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV
560 570 580 590 600
NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
610 620 630 640 650
SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT
660 670 680 690 700
VDWALAEYMA FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC
710 720 730 740 750
IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF
760 770 780 790 800
NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ
810 820 830 840 850
MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH VLRRQILLPF
860 870 880 890 900
RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR
910 920 930 940 950
LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN
960 970 980 990 1000
AELAWCQEEH KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK
1010 1020
THLTELQRFL DTAFDLDAFK KFS
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. Curated
The sequence BAD90530.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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_006514583.2. [Q60597-4]
XP_006514647.1. XM_006514584.2. [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:
EMBLi
GenBanki
DDBJi
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_006514583.2. [Q60597-4]
XP_006514647.1. XM_006514584.2. [Q60597-4]
XP_006514648.1. XM_006514585.1. [Q60597-1]
UniGeneiMm.276348.
Mm.479411.
Mm.490272.

3D structure databases

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

Protein-protein interaction databases

IntActiQ60597. 5 interactions.
MINTiMINT-1860288.

Chemistry

ChEMBLiCHEMBL2176831.

PTM databases

PhosphoSiteiQ60597.

2D gel databases

REPRODUCTION-2DPAGEQ60597.

Proteomic databases

MaxQBiQ60597.
PaxDbiQ60597.
PRIDEiQ60597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi4967.
MGIiMGI:1098267. Ogdh.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
HOVERGENiHBG001892.
InParanoidiQ60597.
KOiK00164.
OMAiMLSGTHF.
OrthoDBiEOG7FXZXH.
PhylomeDBiQ60597.
TreeFamiTF300695.

Enzyme and pathway databases

ReactomeiREACT_329568. Lysine catabolism.
REACT_333358. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiOgdh. mouse.
NextBioi293740.
PROiQ60597.
SOURCEiSearch...

Gene expression databases

BgeeiQ60597.
CleanExiMM_OGDH.
ExpressionAtlasiQ60597. baseline and differential.
GenevestigatoriQ60597.

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.
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(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: April 1, 2015
This is version 142 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

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.