P24298 (ALAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	496 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)

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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-alanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular amino acid biosynthetic process Traceable author statement. Source: Reactome cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome gluconeogenesis Non-traceable author statement. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	L-alanine:2-oxoglutarate aminotransferase activity Non-traceable author statement Ref.6. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 496	495	Alanine aminotransferase 1		PRO_0000123933
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6
	Modified residue	314	1	N6-(pyridoxal phosphate)lysine By similarity
Natural variations
	Natural variant	14	1	H → N in allele GPT*2. Ref.1 Ref.4 Corresponds to variant rs1063739 [ dbSNP | Ensembl ].		VAR_000561
Experimental info
	Sequence conflict	4 – 7	4	STGD → RRGN in BAA01186. Ref.7
	Sequence conflict	39	1	G → S in BAA01186. Ref.7
	Sequence conflict	222	1	H → A AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P24298 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 23705E7A3A4283B6	FASTA	496	54,637
	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

References

	« Hide 'large scale' referencesShow '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. , 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. 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.
IPI	IPI00217458.
PIR	A40465.
RefSeq	NP_005300.1. NM_005309.2.
UniGene	Hs.103502.
3D structure databases
ProteinModelPortal	P24298.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24298. 1 interaction.
STRING	9606.ENSP00000378408.
PTM databases
PhosphoSite	P24298.
Polymorphism databases
DMDM	46577683.
Proteomic databases
PaxDb	P24298.
PRIDE	P24298.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000394955; ENSP00000378408; ENSG00000167701. ENST00000528431; ENSP00000433586; ENSG00000167701.
GeneID	2875.
KEGG	hsa:2875.
UCSC	uc003zdh.4. human.
Organism-specific databases
CTD	2875.
GeneCards	GC08P145728.
HGNC	HGNC:4552. GPT.
HPA	CAB032997. CAB032999. HPA031059. HPA031060.
MIM	138200. gene.
neXtProt	NX_P24298.
PharmGKB	PA28947.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0436.
HOGENOM	HOG000215020.
HOVERGEN	HBG026148.
InParanoid	P24298.
KO	K00814.
OMA	LKLMSVR.
OrthoDB	EOG41G33Z.
PhylomeDB	P24298.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09610-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00528; UER00586.
Gene expression databases
Bgee	P24298.
CleanEx	HS_GPT.
Genevestigator	P24298.
GermOnline	ENSG00000167701. Homo sapiens.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL5929.
DrugBank	DB00160. L-Alanine. DB00142. L-Glutamic Acid. DB00114. Pyridoxal Phosphate.
GenomeRNAi	2875.
NextBio	11349.
SOURCE	Search...

Entry information

Entry name

ALAT1_HUMAN

Accession

Primary (citable) accession number: P24298
Secondary accession number(s): B0YJ18 , D3DWM7, P78398, Q93076

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.