Reviewed,
UniProtKB/Swiss-Prot P05202 (AATM_MOUSE)
Last modified
November 3, 2009.
Version 93.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aspartate aminotransferase, mitochondrial Short name=mAspAT EC=2.6.1.1 Alternative name(s): Transaminase A Glutamate oxaloacetate transaminase 2 Fatty acid-binding protein FABP-1 FABPpm | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Facilitates cellular uptake of long-chain free fatty acids. Ref.7 |
| Catalytic activity | L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. |
| Cofactor | Pyridoxal phosphate. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Post-translational modification | Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice. |
| Miscellaneous | In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 29 | 29 | Mitochondrion | ||||||
| Chain | 30 – 430 | 401 | Aspartate aminotransferase, mitochondrial | PRO_0000001216 | |||||
Amino acid modifications | |||||||||
| Modified residue | 73 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 90 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 94 | 1 | N6-acetyllysine Ref.9 | ||||||
| Modified residue | 96 | 1 | Nitrated tyrosine | ||||||
| Modified residue | 96 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 150 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 159 | 1 | N6-acetyllysine Ref.9 | ||||||
| Modified residue | 185 | 1 | N6-acetyllysine Ref.9 | ||||||
| Modified residue | 234 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 279 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
| Modified residue | 296 | 1 | N6-acetyllysine Ref.9 | ||||||
| Modified residue | 345 | 1 | N6-acetyllysine Ref.9 | ||||||
| Modified residue | 363 | 1 | N6-acetyllysine Ref.9 | ||||||
| Modified residue | 396 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 401 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 404 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 68 | 1 | R → G in BAE39800. Ref.4 | ||||||
| Sequence conflict | 146 | 1 | Q → E in AAB91426. Ref.3 | ||||||
| Sequence conflict | 153 | 1 | R → G in BAE39800. Ref.4 | ||||||
| Sequence conflict | 377 | 1 | Q → K in BAE39800. Ref.4 | ||||||
| Sequence conflict | 421 | 1 | L → I in BAE39800. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes." Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y. J. Biol. Chem. 261:16976-16983(1986) [PubMed: 3782150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Structural organization of the mouse mitochondrial aspartate aminotransferase gene." Tsuzuki T., Obaru K., Setoyama C., Shimada K. J. Mol. Biol. 198:21-31(1987) [PubMed: 2828632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/He. Tissue: Liver. |
| [3] | "Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA." Bradbury M.W., Berk P.D. Biochem. J. 345:423-427(2000) [PubMed: 10642497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Strain: FVB. Tissue: Liver. |
| [4] | "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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J and NOD. Tissue: Bone marrow macrophage, Cecum, Dendritic cell and Melanocyte. |
| [5] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain and Eye. |
| [6] | Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296; 310-345; 356-363 AND 397-404, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus. |
| [7] | "Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake." Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D. Proc. Soc. Exp. Biol. Med. 208:263-270(1995) [PubMed: 7878064] [Abstract] Cited for: FUNCTION. |
| [8] | "Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed: 16800626] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, MASS SPECTROMETRY. Tissue: Brain. |
| [9] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-159; LYS-185; LYS-296; LYS-345 AND LYS-363, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| J02622 mRNA. Translation: AAA37264.1. X06917 X06926 Genomic DNA. Translation: CAA30015.1. M37259 M37258 Genomic DNA. Translation: AAA37265.1. Sequence problems.U82470 mRNA. Translation: AAB91426.1. AK136556 mRNA. Translation: BAE23042.1. AK147953 mRNA. Translation: BAE28248.1. AK149886 mRNA. Translation: BAE29146.1. AK149926 mRNA. Translation: BAE29171.1. AK150194 mRNA. Translation: BAE29370.1. AK152921 mRNA. Translation: BAE31596.1. AK155075 mRNA. Translation: BAE33029.1. AK167767 mRNA. Translation: BAE39800.1. BC089015 mRNA. Translation: AAH89015.1. BC089341 mRNA. Translation: AAH89341.1. | |
| IPI | IPI00117312. |
| PIR | S01174. |
| RefSeq | NP_034455.1. |
| UniGene | Mm.230169 |
3D structure databases | |
| HSSP | HSSP built from PDB template 7AAT based on UniProtKB P00508. |
| SMR | P05202. Positions 30-430. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P05202. |
PTM databases | |
| PhosphoSite | P05202. |
Proteomic databases | |
| PRIDE | P05202. |
Genome annotation databases | |
| Ensembl | ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672; Mus musculus. [Genome view] |
| GeneID | 14719. |
| KEGG | mmu:14719. |
| UCSC | uc009mzi.1. mouse. |
Organism-specific databases | |
| CTD | 14719. |
| MGI | MGI:95792. Got2. |
Phylogenomic databases | |
| HOGENOM | P05202. |
| HOVERGEN | P05202. |
| OMA | IASSYSK. |
Enzyme and pathway databases | |
| BRENDA | 2.6.1.1. 244. |
Gene expression databases | |
| ArrayExpress | P05202. |
| Bgee | P05202. |
| Genevestigator | P05202. |
| GermOnline | ENSMUSG00000031672. Mus musculus. |
Family and domain databases | |
| InterPro | IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR11879. Asp_trans. 1 hit. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| PRINTS | PR00799. TRANSAMINASE. |
| PROSITE | PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 286731. |
| SOURCE | Search... |
Entry information
| Entry name | AATM_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P05202 Secondary accession number(s): O09188 Q5HZH5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


