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Q8BGT5 (ALAT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine aminotransferase 2

Short name=ALT2
EC=2.6.1.2
Alternative name(s):
Glutamate pyruvate transaminase 2
Short name=GPT 2
Glutamic--alanine transaminase 2
Glutamic--pyruvic transaminase 2
Gene names
Name:Gpt2
Synonyms:Aat2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.

Subunit structure

Homodimer By similarity.

Tissue specificity

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. Ref.1

Miscellaneous

May be responsible for increased ALT activity in hepatic steatosis.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Alanine aminotransferase 2
PRO_0000247533

Amino acid modifications

Modified residue3401N6-(pyridoxal phosphate)lysine By similarity
Modified residue4141N6-acetyllysine Ref.5
Modified residue5041N6-acetyllysine Ref.5
Modified residue5111N6-acetyllysine Ref.5

Experimental info

Sequence conflict2521R → W in AAH34219. Ref.4
Sequence conflict2521R → W in DAA05290. Ref.4
Sequence conflict4211D → N in BAC36035. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BGT5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 70FED064E5F6A92E

FASTA52257,944
        10         20         30         40         50         60 
MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE RSPRDRILTL ESMNPQVKAV 

        70         80         90        100        110        120 
EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA MGQQPITFLR QVMALCTYPN 

       130        140        150        160        170        180 
LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAFITRR DGVPADPDNI 

       190        200        210        220        230        240 
YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA VISELDAVQV NYYLDEENCW 

       250        260        270        280        290        300 
ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC IEDVIHFAWE EKLFLLADEV 

       310        320        330        340        350        360 
YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK GYMGECGYRG GYMEVINLHP 

       370        380        390        400        410        420 
EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ FSREKEFVLG NLAKKAKLTE 

       430        440        450        460        470        480 
DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA PDMFYCMKLL EETGICVVPG 

       490        500        510        520 
SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ YS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_776291.1. NM_173866.3.
UniGeneMm.200423.

3D structure databases

ProteinModelPortalQ8BGT5.
SMRQ8BGT5. Positions 48-521.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1859318.

PTM databases

PhosphoSiteQ8BGT5.

Proteomic databases

PaxDbQ8BGT5.
PRIDEQ8BGT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034136; ENSMUSP00000034136; ENSMUSG00000031700.
GeneID108682.
KEGGmmu:108682.
UCSCuc009mpx.1. mouse.

Organism-specific databases

CTD84706.
MGIMGI:1915391. Gpt2.

Phylogenomic databases

eggNOGCOG0436.
GeneTreeENSGT00650000093331.
HOGENOMHOG000215020.
HOVERGENHBG026148.
InParanoidQ8BGT5.
KOK00814.
OMAFPANPQD.
OrthoDBEOG76HQ18.
PhylomeDBQ8BGT5.
TreeFamTF300839.

Enzyme and pathway databases

UniPathwayUPA00528; UER00586.

Gene expression databases

ArrayExpressQ8BGT5.
BgeeQ8BGT5.
GenevestigatorQ8BGT5.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGPT2. mouse.
NextBio361219.
PROQ8BGT5.
SOURCESearch...

Entry information

Entry nameALAT2_MOUSE
AccessionPrimary (citable) accession number: Q8BGT5
Secondary accession number(s): Q8BVY7, Q8K1J3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot