SubmitCancel

Skip Header

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

Q60597

- ODO1_MOUSE

UniProt

Q60597 - ODO1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
2-oxoglutarate dehydrogenase, mitochondrial
Gene
Ogdh, Kiaa4192
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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 – 1541Calcium By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi154 – 1585 By 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. NADH metabolic process Source: Ensembl
  3. cerebellar cortex development Source: UniProtKB
  4. generation of precursor metabolites and energy Source: UniProtKB
  5. glycolytic process Source: UniProtKB-KW
  6. hippocampus development Source: UniProtKB
  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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040Mitochondrion By similarity
Add
BLAST
Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_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-acetyllysine By 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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 17234IRGHH…STDKL → VRGHHIAKSCVNFDDAPVTV SSNV in isoform 2.
VSP_024799Add
BLAST
Alternative sequencei139 – 17234IRGHH…STDKL → VRGHHIAKLDPLGISCVNFD DAPVTVSSNVDLAVFKERLR MLTVG in isoform 4.
VSP_024800Add
BLAST
Alternative sequencei172 – 1721L → LDLAVFKERLRMLTVG in isoform 3.
VSP_024801

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti416 – 4161G → V in AAH49104. 1 Publication
Sequence conflicti549 – 5491V → F in AAH49104. 1 Publication
Sequence conflicti552 – 5521Q → E in AAH57354. 1 Publication
Sequence conflicti576 – 5761E → K in BAE29234. 1 Publication

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

« 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: July 9, 2014
This is version 135 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