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P24298 (ALAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine aminotransferase 1

Short name=ALT1
EC=2.6.1.2
Alternative name(s):
Glutamate pyruvate transaminase 1
Short name=GPT 1
Glutamic--alanine transaminase 1
Glutamic--pyruvic transaminase 1
Gene names
Name:GPT
Synonyms:AAT1, GPT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Liver, kidney, heart, and skeletal muscles. Expressed at moderate levels in the adipose tissue. Ref.8

Induction

By glucocorticoids.

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

Initiator methionine11Removed Ref.6
Chain2 – 496495Alanine aminotransferase 1
PRO_0000123933

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue3141N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant141H → N in allele GPT*2. Ref.1 Ref.4
Corresponds to variant rs1063739 [ dbSNP | Ensembl ].
VAR_000561

Experimental info

Sequence conflict4 – 74STGD → RRGN in BAA01186. Ref.7
Sequence conflict391G → S in BAA01186. Ref.7
Sequence conflict2221H → A AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
P24298 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 23705E7A3A4283B6

FASTA49654,637
        10         20         30         40         50         60 
MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF 

        70         80         90        100        110        120 
TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL 

       130        140        150        160        170        180 
GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT 

       190        200        210        220        230        240 
GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI 

       250        260        270        280        290        300 
NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY 

       310        320        330        340        350        360 
AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL 

       370        380        390        400        410        420 
VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL 

       430        440        450        460        470        480 
PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL 

       490 
LEKLSRFHAK FTLEYS 

« Hide

References

« Hide 'large scale' references
[1]"Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites."
Sohocki M.M., Sullivan L.S., Harrison W.R., Sodergren E.J., Elder F.F.B., Weinstock G., Tanase S., Daiger S.P.
Genomics 40:247-252(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-14.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-14.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods."
Ishiguro M., Takio K., Suzuki M., Oyama R., Matsuzawa T., Titani K.
Biochemistry 30:10451-10457(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-496, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
Tissue: Liver.
[7]"Human mRNA for alanine aminotransferase."
Funatsu M., Tanase S., Nakao J., Hamada F., Oka T., Morino Y.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-496.
Tissue: Liver.
[8]"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: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Alanine transaminase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70732 Genomic DNA. Translation: AAC51155.1.
BT006992 mRNA. Translation: AAP35638.1.
EF444981 Genomic DNA. Translation: ACA05996.1.
CH471162 Genomic DNA. Translation: EAW82077.1.
CH471162 Genomic DNA. Translation: EAW82078.1.
BC018207 mRNA. Translation: AAH18207.1.
D10355 mRNA. Translation: BAA01186.1.
CCDSCCDS6430.1.
PIRA40465.
RefSeqNP_005300.1. NM_005309.2.
UniGeneHs.103502.

3D structure databases

ProteinModelPortalP24298.
SMRP24298. Positions 21-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109133. 2 interactions.
IntActP24298. 1 interaction.
STRING9606.ENSP00000378408.

Chemistry

ChEMBLCHEMBL5929.
DrugBankDB00160. L-Alanine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP24298.

Polymorphism databases

DMDM46577683.

Proteomic databases

MaxQBP24298.
PaxDbP24298.
PRIDEP24298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394955; ENSP00000378408; ENSG00000167701.
ENST00000528431; ENSP00000433586; ENSG00000167701.
GeneID2875.
KEGGhsa:2875.
UCSCuc003zdh.4. human.

Organism-specific databases

CTD2875.
GeneCardsGC08P145728.
HGNCHGNC:4552. GPT.
HPACAB032997.
CAB032999.
HPA031059.
HPA031060.
MIM138200. gene.
neXtProtNX_P24298.
PharmGKBPA28947.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000215020.
HOVERGENHBG026148.
InParanoidP24298.
KOK00814.
OMAHAKFTLE.
OrthoDBEOG76HQ18.
PhylomeDBP24298.
TreeFamTF300839.

Enzyme and pathway databases

BioCycMetaCyc:HS09610-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00528; UER00586.

Gene expression databases

BgeeP24298.
CleanExHS_GPT.
GenevestigatorP24298.

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

GenomeRNAi2875.
NextBio11349.
PROP24298.
SOURCESearch...

Entry information

Entry nameALAT1_HUMAN
AccessionPrimary (citable) accession number: P24298
Secondary accession number(s): B0YJ18 expand/collapse secondary AC list , D3DWM7, P78398, Q93076
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM