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Protein

Alanine aminotransferase 2

Gene

Gpt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.By similarity

Catalytic activityi

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactori

Pathway: L-alanine degradation via transaminase pathway

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from L-alanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine aminotransferase 1 (Gpt), Alanine aminotransferase 2 (Gpt2)
This subpathway is part of the pathway L-alanine degradation via transaminase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from L-alanine, the pathway L-alanine degradation via transaminase pathway and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_309077. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00528; UER00586.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine aminotransferase 2 (EC:2.6.1.2)
Short name:
ALT2
Alternative name(s):
Glutamate pyruvate transaminase 2
Short name:
GPT 2
Glutamic--alanine transaminase 2
Glutamic--pyruvic transaminase 2
Gene namesi
Name:Gpt2
Synonyms:Aat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915391. Gpt2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Alanine aminotransferase 2PRO_0000247533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei340 – 3401N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei414 – 4141N6-acetyllysine1 Publication
Modified residuei504 – 5041N6-acetyllysine1 Publication
Modified residuei511 – 5111N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BGT5.
PaxDbiQ8BGT5.
PRIDEiQ8BGT5.

PTM databases

PhosphoSiteiQ8BGT5.

Expressioni

Tissue specificityi

Specifically induced in fatty liver. Highly expressed in muscle, liver and white adipose tissue. Moderately expressed in brain and kidney and expressed at low levels in the heart.1 Publication

Gene expression databases

BgeeiQ8BGT5.
ExpressionAtlasiQ8BGT5. baseline and differential.
GenevisibleiQ8BGT5. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-1859318.
STRINGi10090.ENSMUSP00000034136.

Structurei

3D structure databases

ProteinModelPortaliQ8BGT5.
SMRiQ8BGT5. Positions 48-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093331.
HOGENOMiHOG000215020.
HOVERGENiHBG026148.
InParanoidiQ8BGT5.
KOiK00814.
OMAiKAWGTDV.
OrthoDBiEOG76HQ18.
PhylomeDBiQ8BGT5.
TreeFamiTF300839.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BGT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE RSPRDRILTL
60 70 80 90 100
ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA
110 120 130 140 150
MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY
160 170 180 190 200
SASQGVNCIR EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG
210 220 230 240 250
GGKSRTGVMI PIPQYPLYSA VISELDAVQV NYYLDEENCW ALNVDELRRA
260 270 280 290 300
LRQAKDHCDP KVLCIINPGN PTGQVQSRKC IEDVIHFAWE EKLFLLADEV
310 320 330 340 350
YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK GYMGECGYRG
360 370 380 390 400
GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ
410 420 430 440 450
FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA
460 470 480 490 500
VEAAQSHKMA PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV
510 520
DKLKTVLHKV KDFHLKFLEQ YS
Length:522
Mass (Da):57,944
Last modified:March 1, 2003 - v1
Checksum:i70FED064E5F6A92E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521R → W in AAH34219 (PubMed:15489334).Curated
Sequence conflicti252 – 2521R → W in DAA05290 (PubMed:15489334).Curated
Sequence conflicti421 – 4211D → N in BAC36035 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033424 mRNA. Translation: BAC28282.1.
AK075894 mRNA. Translation: BAC36035.1.
AK076250 mRNA. Translation: BAC36274.1.
AK082030 mRNA. Translation: BAC38395.1.
BC034219 mRNA. Translation: AAH34219.1.
BK005128 mRNA. Translation: DAA05290.1.
CCDSiCCDS22499.1.
RefSeqiNP_776291.1. NM_173866.3.
UniGeneiMm.200423.

Genome annotation databases

EnsembliENSMUST00000034136; ENSMUSP00000034136; ENSMUSG00000031700.
GeneIDi108682.
KEGGimmu:108682.
UCSCiuc009mpx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033424 mRNA. Translation: BAC28282.1.
AK075894 mRNA. Translation: BAC36035.1.
AK076250 mRNA. Translation: BAC36274.1.
AK082030 mRNA. Translation: BAC38395.1.
BC034219 mRNA. Translation: AAH34219.1.
BK005128 mRNA. Translation: DAA05290.1.
CCDSiCCDS22499.1.
RefSeqiNP_776291.1. NM_173866.3.
UniGeneiMm.200423.

3D structure databases

ProteinModelPortaliQ8BGT5.
SMRiQ8BGT5. Positions 48-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1859318.
STRINGi10090.ENSMUSP00000034136.

PTM databases

PhosphoSiteiQ8BGT5.

Proteomic databases

MaxQBiQ8BGT5.
PaxDbiQ8BGT5.
PRIDEiQ8BGT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034136; ENSMUSP00000034136; ENSMUSG00000031700.
GeneIDi108682.
KEGGimmu:108682.
UCSCiuc009mpx.1. mouse.

Organism-specific databases

CTDi84706.
MGIiMGI:1915391. Gpt2.

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093331.
HOGENOMiHOG000215020.
HOVERGENiHBG026148.
InParanoidiQ8BGT5.
KOiK00814.
OMAiKAWGTDV.
OrthoDBiEOG76HQ18.
PhylomeDBiQ8BGT5.
TreeFamiTF300839.

Enzyme and pathway databases

UniPathwayiUPA00528; UER00586.
ReactomeiREACT_309077. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSiGpt2. mouse.
NextBioi361219.
PROiQ8BGT5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGT5.
ExpressionAtlasiQ8BGT5. baseline and differential.
GenevisibleiQ8BGT5. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Murine alanine aminotransferase: cDNA cloning, functional expression, and differential gene regulation in mouse fatty liver."
    Jadhao S.B., Yang R.-Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R., Gong D.-W.
    Hepatology 39:1297-1302(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. Erratum
    Jadhao S.B., Yang R.-Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R., Gong D.-W.
    Hepatology 40:269-269(2004)
  3. "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].
    Strain: C57BL/6J.
    Tissue: Colon, Head, Skin and Tongue.
  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].
    Strain: Czech II.
    Tissue: Mammary gland.
  5. "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-414; LYS-504 AND LYS-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiALAT2_MOUSE
AccessioniPrimary (citable) accession number: Q8BGT5
Secondary accession number(s): Q8BVY7, Q8K1J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

May be responsible for increased ALT activity in hepatic steatosis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.