Skip Header

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

Alanine aminotransferase 2

Gene

GPT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.1 Publication

Catalytic activityi

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathway:iL-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 2 (GPT2), Alanine aminotransferase 1 (GPT)
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

BioCyciMetaCyc:HS09332-MONOMER.
ReactomeiREACT_238. 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, ALT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:18062. GPT2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 49 (MRT49)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT49 patients show a developmental encephalopathy characterized by rapid onset of failure to thrive and microcephaly, as well as profoundly delayed development.

See also OMIM:616281
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531S → R in MRT49; loss of function mutation. 1 Publication
VAR_073379

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi616281. phenotype.
PharmGKBiPA28948.

Chemistry

DrugBankiDB00160. L-Alanine.
DB00780. Phenelzine.

Polymorphism and mutation databases

BioMutaiGPT2.
DMDMi74730602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Alanine aminotransferase 2PRO_0000247532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei341 – 3411N6-(pyridoxal phosphate)lysine
Modified residuei415 – 4151N6-acetyllysineBy similarity
Modified residuei505 – 5051N6-acetyllysineBy similarity
Modified residuei512 – 5121N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8TD30.
PaxDbiQ8TD30.
PRIDEiQ8TD30.

PTM databases

PhosphoSiteiQ8TD30.

Expressioni

Tissue specificityi

Expressed at high levels in muscle, adipose tissue, kidney and brain and at lower levels in the liver and breast.1 Publication

Gene expression databases

BgeeiQ8TD30.
CleanExiHS_GPT2.
ExpressionAtlasiQ8TD30. baseline and differential.
GenevisibleiQ8TD30. HS.

Organism-specific databases

HPAiHPA051514.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi124217. 6 interactions.
IntActiQ8TD30. 3 interactions.
STRINGi9606.ENSP00000345282.

Structurei

Secondary structure

1
523
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 524Combined sources
Turni53 – 564Combined sources
Beta strandi57 – 648Combined sources
Helixi67 – 8014Combined sources
Beta strandi86 – 894Combined sources
Helixi107 – 11711Combined sources
Helixi119 – 1235Combined sources
Beta strandi125 – 1273Combined sources
Helixi129 – 14113Combined sources
Helixi157 – 17014Combined sources
Turni171 – 1733Combined sources
Helixi178 – 1803Combined sources
Beta strandi181 – 1866Combined sources
Helixi187 – 19812Combined sources
Helixi203 – 2053Combined sources
Beta strandi206 – 2149Combined sources
Helixi218 – 2258Combined sources
Beta strandi229 – 2346Combined sources
Helixi237 – 2393Combined sources
Helixi245 – 25511Combined sources
Turni256 – 2583Combined sources
Beta strandi259 – 26911Combined sources
Turni271 – 2733Combined sources
Helixi279 – 29214Combined sources
Beta strandi295 – 2995Combined sources
Turni301 – 3044Combined sources
Helixi316 – 3227Combined sources
Helixi325 – 3284Combined sources
Beta strandi333 – 34210Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi352 – 3587Combined sources
Helixi361 – 37313Combined sources
Helixi379 – 38810Combined sources
Helixi399 – 42527Combined sources
Beta strandi437 – 4415Combined sources
Helixi449 – 4579Combined sources
Helixi462 – 47413Combined sources
Helixi481 – 4833Combined sources
Beta strandi492 – 4965Combined sources
Helixi501 – 52121Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IHJX-ray2.30A49-523[»]
ProteinModelPortaliQ8TD30.
SMRiQ8TD30. Positions 48-522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TD30.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093331.
HOGENOMiHOG000215020.
HOVERGENiHBG026148.
InParanoidiQ8TD30.
KOiK00814.
OMAiEWVGSIV.
OrthoDBiEOG76HQ18.
PhylomeDBiQ8TD30.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TD30-1) [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

        10         20         30         40         50
MQRAAALVRR GCGPRTPSSW GRSQSSAAAE ASAVLKVRPE RSRRERILTL
60 70 80 90 100
ESMNPQVKAV EYAVRGPIVL KAGEIELELQ RGIKKPFTEV IRANIGDAQA
110 120 130 140 150
MGQQPITFLR QVMALCTYPN LLDSPSFPED AKKRARRILQ ACGGNSLGSY
160 170 180 190 200
SASQGVNCIR EDVAAYITRR DGGVPADPDN IYLTTGASDG ISTILKILVS
210 220 230 240 250
GGGKSRTGVM IPIPQYPLYS AVISELDAIQ VNYYLDEENC WALNVNELRR
260 270 280 290 300
AVQEAKDHCD PKVLCIINPG NPTGQVQSRK CIEDVIHFAW EEKLFLLADE
310 320 330 340 350
VYQDNVYSPD CRFHSFKKVL YEMGPEYSSN VELASFHSTS KGYMGECGYR
360 370 380 390 400
GGYMEVINLH PEIKGQLVKL LSVRLCPPVS GQAAMDIVVN PPVAGEESFE
410 420 430 440 450
QFSREKESVL GNLAKKAKLT EDLFNQVPGI HCNPLQGAMY AFPRIFIPAK
460 470 480 490 500
AVEAAQAHQM APDMFYCMKL LEETGICVVP GSGFGQREGT YHFRMTILPP
510 520
VEKLKTVLQK VKDFHINFLE KYA
Length:523
Mass (Da):57,904
Last modified:June 1, 2002 - v1
Checksum:i4DD87814C62C7DEA
GO
Isoform 2 (identifier: Q8TD30-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Show »
Length:423
Mass (Da):46,983
Checksum:iC76C2613BE0CC4BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841D → G in BAC04465 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531S → R in MRT49; loss of function mutation. 1 Publication
VAR_073379

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_020008Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029173 mRNA. Translation: AAK31794.2.
AK094971 mRNA. Translation: BAC04465.1.
AC018845 Genomic DNA. No translation available.
BC062555 mRNA. Translation: AAH62555.1.
CCDSiCCDS10725.1. [Q8TD30-1]
CCDS45478.1. [Q8TD30-2]
RefSeqiNP_001135938.1. NM_001142466.2. [Q8TD30-2]
NP_597700.1. NM_133443.3. [Q8TD30-1]
UniGeneiHs.460693.

Genome annotation databases

EnsembliENST00000340124; ENSP00000345282; ENSG00000166123.
ENST00000440783; ENSP00000413804; ENSG00000166123. [Q8TD30-2]
GeneIDi84706.
KEGGihsa:84706.
UCSCiuc002eel.3. human. [Q8TD30-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029173 mRNA. Translation: AAK31794.2.
AK094971 mRNA. Translation: BAC04465.1.
AC018845 Genomic DNA. No translation available.
BC062555 mRNA. Translation: AAH62555.1.
CCDSiCCDS10725.1. [Q8TD30-1]
CCDS45478.1. [Q8TD30-2]
RefSeqiNP_001135938.1. NM_001142466.2. [Q8TD30-2]
NP_597700.1. NM_133443.3. [Q8TD30-1]
UniGeneiHs.460693.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IHJX-ray2.30A49-523[»]
ProteinModelPortaliQ8TD30.
SMRiQ8TD30. Positions 48-522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124217. 6 interactions.
IntActiQ8TD30. 3 interactions.
STRINGi9606.ENSP00000345282.

Chemistry

DrugBankiDB00160. L-Alanine.
DB00780. Phenelzine.

PTM databases

PhosphoSiteiQ8TD30.

Polymorphism and mutation databases

BioMutaiGPT2.
DMDMi74730602.

Proteomic databases

MaxQBiQ8TD30.
PaxDbiQ8TD30.
PRIDEiQ8TD30.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340124; ENSP00000345282; ENSG00000166123.
ENST00000440783; ENSP00000413804; ENSG00000166123. [Q8TD30-2]
GeneIDi84706.
KEGGihsa:84706.
UCSCiuc002eel.3. human. [Q8TD30-1]

Organism-specific databases

CTDi84706.
GeneCardsiGC16P046918.
HGNCiHGNC:18062. GPT2.
HPAiHPA051514.
MIMi138210. gene.
616281. phenotype.
neXtProtiNX_Q8TD30.
PharmGKBiPA28948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093331.
HOGENOMiHOG000215020.
HOVERGENiHBG026148.
InParanoidiQ8TD30.
KOiK00814.
OMAiEWVGSIV.
OrthoDBiEOG76HQ18.
PhylomeDBiQ8TD30.
TreeFamiTF300839.

Enzyme and pathway databases

UniPathwayiUPA00528; UER00586.
BioCyciMetaCyc:HS09332-MONOMER.
ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSiGPT2. human.
EvolutionaryTraceiQ8TD30.
GenomeRNAii84706.
NextBioi74798.
PROiQ8TD30.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TD30.
CleanExiHS_GPT2.
ExpressionAtlasiQ8TD30. baseline and differential.
GenevisibleiQ8TD30. HS.

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. "cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase."
    Yang R.-Z., Blaileanu G., Hansen B.C., Shuldiner A.R., Gong D.-W.
    Genomics 79:445-450(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Adipose tissue.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hippocampus.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Lung.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Loss of function mutation in glutamic pyruvate transaminase 2 (GPT2) causes developmental encephalopathy."
    Celis K., Shuldiner S., Haverfield E.V., Cappell J., Yang R., Gong D.W., Chung W.K.
    J. Inherit. Metab. Dis. 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRT49, VARIANT MRT49 ARG-153, CHARACTERIZATION OF VARIANT MRT49 ARG-153.
  7. "Human glutamate pyruvate transaminase 2."
    Structural genomics consortium (SGC)
    Submitted (AUG-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 49-523 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR.

Entry informationi

Entry nameiALAT2_HUMAN
AccessioniPrimary (citable) accession number: Q8TD30
Secondary accession number(s): Q8N9E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: June 1, 2002
Last modified: July 22, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.