Q8TD30 (ALAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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, ALT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Ref.1
Catalytic activity	L-alanine + 2-oxoglutarate = pyruvate + L-glutamate. Ref.1
Cofactor	Pyridoxal phosphate. Ref.5
Pathway	Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subunit structure	Homodimer By similarity.
Tissue specificity	Expressed at high levels in muscle, adipose tissue, kidney and brain and at lower levels in the liver and breast. Ref.1
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from direct assay Ref.1. Source: UniProtKB L-alanine metabolic process Inferred from direct assay Ref.1. Source: UniProtKB cellular amino acid biosynthetic process Traceable author statement. Source: Reactome
Cellular component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular function	L-alanine:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.1. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TD30-1)

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.

Isoform 2 (identifier: Q8TD30-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

Alanine aminotransferase 2

PRO_0000247532

Amino acid modifications

Modified residue

341

1

N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence

1 – 100

100

Missing in isoform 2.

VSP_020008

Experimental info

Sequence conflict

284

1

D → G in BAC04465. Ref.4

Secondary structure

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523

Helix Strand Turn

Details...

Beta strand

49 – 52

4

Turn

53 – 56

4

Beta strand

57 – 64

8

Helix

68 – 71

4

Helix

75 – 80

6

Beta strand

86 – 89

4

Helix

107 – 117

11

Helix

119 – 123

5

Beta strand

125 – 127

3

Helix

129 – 142

14

Helix

157 – 170

14

Helix

178 – 180

3

Helix

192 – 198

7

Beta strand

210 – 214

5

Helix

218 – 225

8

Beta strand

231 – 234

4

Helix

237 – 239

3

Helix

245 – 255

11

Turn

256 – 258

3

Beta strand

263 – 267

5

Helix

279 – 292

14

Beta strand

295 – 299

5

Turn

301 – 304

4

Helix

316 – 322

7

Turn

326 – 330

5

Beta strand

333 – 336

4

Beta strand

354 – 358

5

Turn

361 – 363

3

Helix

367 – 373

7

Helix

383 – 388

6

Helix

399 – 409

11

Helix

413 – 425

13

Helix

449 – 457

9

Helix

462 – 473

12

Beta strand

494 – 496

3

Helix

501 – 521

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 4DD87814C62C7DEA	FASTA	523	57,904
	10 20 30 40 50 60 MQRAAALVRR GCGPRTPSSW GRSQSSAAAE ASAVLKVRPE RSRRERILTL ESMNPQVKAV 70 80 90 100 110 120 EYAVRGPIVL KAGEIELELQ RGIKKPFTEV IRANIGDAQA MGQQPITFLR QVMALCTYPN 130 140 150 160 170 180 LLDSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAYITRR DGGVPADPDN 190 200 210 220 230 240 IYLTTGASDG ISTILKILVS GGGKSRTGVM IPIPQYPLYS AVISELDAIQ VNYYLDEENC 250 260 270 280 290 300 WALNVNELRR AVQEAKDHCD PKVLCIINPG NPTGQVQSRK CIEDVIHFAW EEKLFLLADE 310 320 330 340 350 360 VYQDNVYSPD CRFHSFKKVL YEMGPEYSSN VELASFHSTS KGYMGECGYR GGYMEVINLH 370 380 390 400 410 420 PEIKGQLVKL LSVRLCPPVS GQAAMDIVVN PPVAGEESFE QFSREKESVL GNLAKKAKLT 430 440 450 460 470 480 EDLFNQVPGI HCNPLQGAMY AFPRIFIPAK AVEAAQAHQM APDMFYCMKL LEETGICVVP 490 500 510 520 GSGFGQREGT YHFRMTILPP VEKLKTVLQK VKDFHINFLE KYA
	Isoform 2 [UniParc]. Checksum: C76C2613BE0CC4BF	FASTA	423	46,983
	10 20 30 40 50 60 MGQQPITFLR QVMALCTYPN LLDSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR 70 80 90 100 110 120 EDVAAYITRR DGGVPADPDN IYLTTGASDG ISTILKILVS GGGKSRTGVM IPIPQYPLYS 130 140 150 160 170 180 AVISELDAIQ VNYYLDEENC WALNVNELRR AVQEAKDHCD PKVLCIINPG NPTGQVQSRK 190 200 210 220 230 240 CIEDVIHFAW EEKLFLLADE VYQDNVYSPD CRFHSFKKVL YEMGPEYSSN VELASFHSTS 250 260 270 280 290 300 KGYMGECGYR GGYMEVINLH PEIKGQLVKL LSVRLCPPVS GQAAMDIVVN PPVAGEESFE 310 320 330 340 350 360 QFSREKESVL GNLAKKAKLT EDLFNQVPGI HCNPLQGAMY AFPRIFIPAK AVEAAQAHQM 370 380 390 400 410 420 APDMFYCMKL LEETGICVVP GSGFGQREGT YHFRMTILPP VEKLKTVLQK VKDFHINFLE KYA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11863375] [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: 14702039] [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: 15616553] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY029173 mRNA. Translation: AAK31794.2.
AK094971 mRNA. Translation: BAC04465.1.
AC018845 Genomic DNA. No translation available.
BC062555 mRNA. Translation: AAH62555.1.

IPI

IPI00152432.
IPI00784445.

RefSeq

NP_001135938.1. NM_001142466.1.
NP_597700.1. NM_133443.2.

UniGene

Hs.460693.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IHJ	X-ray	2.30	A	49-523	[»]

ProteinModelPortal

Q8TD30.

SMR

Q8TD30. Positions 48-522.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8TD30. 2 interactions.

STRING

Q8TD30.

PTM databases

PhosphoSite

Q8TD30.

Polymorphism databases

DMDM

74730602.

Proteomic databases

PRIDE

Q8TD30.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340124; ENSP00000345282; ENSG00000166123.

GeneID

84706.

KEGG

hsa:84706.

NMPDR

fig|9606.3.peg.12201.

UCSC

uc002eel.1. human.
uc002eem.1. human.

Organism-specific databases

CTD

84706.

GeneCards

GC16P046859.

H-InvDB

HIX0013003.

HGNC

HGNC:18062. GPT2.

MIM

138210. gene.

neXtProt

NX_Q8TD30.

PharmGKB

PA28948.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08965.

GeneTree

ENSGT00390000001465.

HOGENOM

HBG645860.

HOVERGEN

HBG026148.

InParanoid

Q8TD30.

OMA

QFSREKE.

OrthoDB

EOG41G33Z.

PhylomeDB

Q8TD30.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12786.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q8TD30.

Bgee

Q8TD30.

CleanEx

HS_GPT2.

Genevestigator

Q8TD30.

GermOnline

ENSG00000166123. Homo sapiens.

Family and domain databases

InterPro

IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

KO

K00814.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00160. L-Alanine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

NextBio

74798.

SOURCE

Search...

Entry information

Entry name

ALAT2_HUMAN

Accession

Primary (citable) accession number: Q8TD30
Secondary accession number(s): Q8N9E2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 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.