Reviewed,
UniProtKB/Swiss-Prot Q9BYV1 (AGT2_HUMAN)
Last modified
January 19, 2010.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alanine--glyoxylate aminotransferase 2, mitochondrial Short name=AGT 2 EC=2.6.1.44 Alternative name(s): (R)-3-amino-2-methylpropionate--pyruvate transaminase EC=2.6.1.40 Beta-alanine-pyruvate aminotransferase Beta-ALAAT II D-AIBAT | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 514 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)
| Catalytic activity | L-alanine + glyoxylate = pyruvate + glycine. (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine. |
| Cofactor | Pyridoxal phosphate. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Mitochondrion Potential. |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Coding sequence diversity | Polymorphism |
| Domain | Transit peptide |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | (R)-3-amino-2-methylpropionate-pyruvate transaminase activity Inferred from electronic annotation. Source: EC alanine-glyoxylate transaminase activityInferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 41 | 41 | Mitochondrion By similarity | ||||||
| Chain | 42 – 514 | 473 | Alanine--glyoxylate aminotransferase 2, mitochondrial | PRO_0000001269 | |||||
Amino acid modifications | |||||||||
| Modified residue | 129 | 1 | N6-acetyllysine Ref.4 | ||||||
| Modified residue | 350 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 102 | 1 | S → I: dbSNP rs37370. | VAR_061006 | |||||
| Natural variant | 102 | 1 | S → N: dbSNP rs37370. Ref.2 Ref.3 | VAR_023483 | |||||
| Natural variant | 102 | 1 | S → T: dbSNP rs37370. | VAR_061007 | |||||
| Natural variant | 132 | 1 | G → R: dbSNP rs16870794. | VAR_048231 | |||||
| Natural variant | 140 | 1 | V → I: dbSNP rs37369. Ref.2 Ref.3 | VAR_022140 | |||||
| Natural variant | 212 | 1 | T → I: dbSNP rs180749. Ref.2 Ref.3 | VAR_022141 | |||||
| Natural variant | 492 | 1 | P → R: dbSNP rs17245714. | VAR_048232 | |||||
| Natural variant | 498 | 1 | V → L: dbSNP rs16899974. Ref.3 | VAR_029513 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The human ortholog for rat alanine-glyoxylate aminotransferase 2." Jenne D.E. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Human beta-alanine-pyruvate aminotransferase cDNA." Matsuda K., Horikawa Y., Kaneko M., Sakata S., Tamaki N. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-102; ILE-140 AND ILE-212. |
| [3] | Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASN-102; ILE-140; ILE-212 AND LEU-498. Tissue: Kidney. |
| [4] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ292204 mRNA. Translation: CAC24841.1. AB193309 mRNA. Translation: BAD66662.1. AK223128 mRNA. Translation: BAD96848.1. AK223144 mRNA. No translation available. AK223375 mRNA. Translation: BAD97095.1. |
| IPI | IPI00011075. |
| RefSeq | NP_114106.1. |
| UniGene | Hs.34494 |
3D structure databases | |
| SMR | Q9BYV1. Positions 84-508. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9BYV1. |
PTM databases | |
| PhosphoSite | Q9BYV1. |
Proteomic databases | |
| PRIDE | Q9BYV1. |
Genome annotation databases | |
| Ensembl | ENST00000231420; ENSP00000231420; ENSG00000113492; Homo sapiens. [Genome view] |
| GeneID | 64902. |
| KEGG | hsa:64902. |
| UCSC | uc003jjf.1. human. |
Organism-specific databases | |
| CTD | 64902. |
| GeneCards | GC05M035033. |
| HGNC | HGNC:14412. AGXT2. |
| MIM | 612471. gene. |
| PharmGKB | PA24634. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG06182. |
| HOGENOM | HBG725944. |
| HOVERGEN | Q9BYV1. |
| InParanoid | Q9BYV1. |
| OMA | QKQLGRL. |
| OrthoDB | EOG9MWBRD. |
| PhylomeDB | Q9BYV1. |
Enzyme and pathway databases | |
| BRENDA | 2.6.1.40. 247. 2.6.1.44. 247. |
Gene expression databases | |
| ArrayExpress | Q9BYV1. |
| Bgee | Q9BYV1. |
| CleanEx | HS_AGXT2. |
| Genevestigator | Q9BYV1. |
| GermOnline | ENSG00000113492. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR11986. Aminotrans_3. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00145. Glycine. DB00160. L-Alanine. DB00114. Pyridoxal Phosphate. DB00119. Pyruvic acid. |
| NextBio | 67053. |
| SOURCE | Search... |
Entry information
| Entry name | AGT2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9BYV1 Secondary accession number(s): Q53FB4 Q5W7Q1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 5 Human chromosome 5: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


