P21549 (SPYA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine--pyruvate aminotransferase
Short name=SPT
EC=2.6.1.51

Alternative name(s):
Alanine--glyoxylate aminotransferase
Short name=AGT
EC=2.6.1.44

Gene names

Name:	AGXT
Synonyms:	AGT1, SPAT

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	392 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-serine + pyruvate = 3-hydroxypyruvate + L-alanine. L-alanine + glyoxylate = pyruvate + glycine.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer. Ref.9
Subcellular location	Peroxisome. Mitochondrion matrix. Note: Except in some HP1 patients where AGT is found in the mitochondrial matrix.
Tissue specificity	Liver.
Polymorphism	Polymorphism at position 11 acts synergistically with different mutations in AGXT producing specific enzymic phenotypes in HP1 patients. The combined presence of Leu-11 and Met-340 polymorphisms defines the minor AGXT allele, whereas their absence defines the major allele. The minor allele has frequencies of 20% in normal European and North American populations, and 50% in HP1 patients.
Involvement in disease	Hyperoxaluria primary 1 (HP1) [MIM:259900]: An inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and progressive tissue accumulation of insoluble calcium oxalate. Affected individuals are at risk for nephrolithiasis, nephrocalcinosis and early onset end-stage renal disease. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion Peroxisome
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-alanine catabolic process Inferred from direct assay PubMed 17696873PubMed 18492492PubMed 22198249. Source: UniProtKB L-cysteine catabolic process Inferred from direct assay PubMed 18492492. Source: UniProtKB cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome glycine biosynthetic process, by transamination of glyoxylate Inferred from direct assay PubMed 22198249. Source: UniProtKB glyoxylate catabolic process Inferred from direct assay PubMed 22198249. Source: UniProtKB oxalic acid secretion Inferred from electronic annotation. Source: Compara protein targeting to peroxisome Inferred from mutant phenotype Ref.2. Source: HGNC pyruvate biosynthetic process Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisomal matrix Inferred from direct assay PubMed 22198249PubMed 3418107. Source: UniProtKB
Molecular_function	alanine-glyoxylate transaminase activity Inferred from direct assay PubMed 17696873PubMed 18492492PubMed 22198249. Source: UniProtKB amino acid binding Inferred from direct assay PubMed 18492492. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 20133649. Source: UniProtKB pyridoxal phosphate binding Inferred from direct assay PubMed 17696873PubMed 20133649. Source: UniProtKB serine-pyruvate transaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 392

392

Serine--pyruvate aminotransferase

PRO_0000150237

Sites

Binding site

360

1

Substrate

Amino acid modifications

Modified residue

209

1

N6-(pyridoxal phosphate)lysine

Natural variations

Natural variant

9

1

T → N in HP1. Ref.25 Ref.26

VAR_060547

Natural variant

11

1

P → L Common polymorphism; reduction of specific activity in vitro; causes mistargeting when associated with R-170. Ref.2 Ref.21
Corresponds to variant rs34116584 [ dbSNP | Ensembl ].

VAR_000587

Natural variant

22

1

N → S.
Corresponds to variant rs34885252 [ dbSNP | Ensembl ].

VAR_048236

Natural variant

41

1

G → R in HP1; protein destabilization and loss of activity in the presence of L-11. Ref.13 Ref.19 Ref.21 Ref.26

VAR_000588

Natural variant

41

1

G → V in HP1. Ref.17 Ref.18

VAR_010969

Natural variant

82

1

G → E in HP1; abolishes catalytic activity by interfering with pyridoxal phosphate binding. Ref.11 Ref.21

VAR_008878

Natural variant

82

1

G → R in HP1. Ref.24

VAR_060548

Natural variant

95

1

E → EE in HP1. Ref.17 Ref.18

VAR_010970

Natural variant

108

1

W → R in HP1. Ref.16 Ref.26

VAR_060549

Natural variant

112

1

A → D in HP1. Ref.22

VAR_060550

Natural variant

116

1

G → R in HP1. Ref.17 Ref.18

VAR_010971

Natural variant

139

1

Missing in HP1. Ref.25

VAR_060551

Natural variant

152

1

F → I in HP1; protein destabilization and loss of activity in the presence of L-11. Ref.13 Ref.20 Ref.21 Ref.24

VAR_000589

Natural variant

153

1

L → V in HP1. Ref.24

VAR_060552

Natural variant

156

1

G → R in HP1. Ref.17 Ref.18 Ref.19 Ref.25 Ref.26

VAR_010972

Natural variant

158

1

S → L in HP1. Ref.25

VAR_060553

Natural variant

161

1

G → R in HP1. Ref.27

VAR_060554

Natural variant

170

1

G → R in HP1; causes mistargeting when associated with L-11. Ref.2 Ref.20 Ref.21 Ref.24

VAR_000590

Natural variant

173

1

C → Y in HP1. Ref.16

VAR_060555

Natural variant

183

1

D → N in HP1. Ref.20

VAR_010973

Natural variant

187

1

S → F in HP1. Ref.12

VAR_000591

Natural variant

190

1

G → R in HP1. Ref.16 Ref.19 Ref.25 Ref.26

VAR_060556

Natural variant

195

1

M → R in HP1. Ref.26

VAR_060557

Natural variant

201

1

D → E in HP1. Ref.25

VAR_060558

Natural variant

205

1

S → P in HP1. Ref.10

VAR_000592

Natural variant

218

1

S → L in HP1. Ref.27

VAR_060559

Natural variant

233

1

R → C in HP1. Ref.15 Ref.20

VAR_008879

Natural variant

233

1

R → H in HP1. Ref.15

VAR_008880

Natural variant

233

1

R → L in HP1. Ref.25

VAR_060560

Natural variant

243

1

D → H in HP1. Ref.26

VAR_060561

Natural variant

244

1

I → T in HP1; prevalent mutation in the Canary islands; protein misfolding and loss of activity when associated with P-11. Ref.15 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26

VAR_008881

Natural variant

253

1

C → R in HP1. Ref.25

VAR_060562

Natural variant

279

1

I → M in HP1. Ref.26

VAR_060563

Natural variant

279

1

I → T. Ref.27

VAR_060564

Natural variant

280

1

A → V. Ref.27

VAR_060565

Natural variant

287

1

S → T in HP1. Ref.26

VAR_060566

Natural variant

289

1

R → C in HP1. Ref.19 Ref.26

VAR_060567

Natural variant

295

1

A → T.
Corresponds to variant rs13408961 [ dbSNP | Ensembl ].

VAR_048237

Natural variant

296

1

Missing in HP1. Ref.16

VAR_060568

Natural variant

298

1

L → P in HP1. Ref.19 Ref.26

VAR_060569

Natural variant

326

1

V → I. Ref.22

VAR_060570

Natural variant

336

1

V → D in HP1. Ref.24

VAR_060571

Natural variant

340

1

I → M Common polymorphism; associated with hyperoxaluria. Ref.2
Corresponds to variant rs4426527 [ dbSNP | Ensembl ].

VAR_000593

Natural variant

350

1

G → D in HP1. Ref.16

VAR_060572

Experimental info

Mutagenesis

209

1

K → R: Affects pyridoxal phosphate binding. Ref.21

Secondary structure

1

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392

Helix Strand Turn

Details...

Helix

13 – 15

3

Beta strand

27 – 29

3

Helix

35 – 40

6

Helix

51 – 68

18

Beta strand

73 – 80

8

Helix

82 – 93

12

Beta strand

100 – 106

7

Helix

107 – 118

12

Beta strand

123 – 127

5

Helix

136 – 146

11

Beta strand

149 – 157

9

Turn

158 – 161

4

Helix

169 – 175

7

Beta strand

179 – 183

5

Turn

185 – 190

6

Turn

195 – 199

5

Beta strand

201 – 209

9

Beta strand

218 – 222

5

Helix

224 – 232

9

Helix

244 – 250

7

Beta strand

254 – 256

3

Helix

266 – 282

17

Helix

284 – 305

22

Beta strand

309 – 311

3

Helix

314 – 316

3

Beta strand

321 – 325

5

Helix

332 – 343

12

Helix

352 – 354

3

Turn

355 – 357

3

Beta strand

358 – 362

5

Helix

365 – 367

3

Helix

370 – 386

17

Sequences

	Sequence		Length	Mass (Da)
	P21549 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 2987DDE85B2470B4	FASTA	392	43,010
	10 20 30 40 50 60 MASHKLLVTP PKALLKPLSI PNQLLLGPGP SNLPPRIMAA GGLQMIGSMS KDMYQIMDEI 70 80 90 100 110 120 KEGIQYVFQT RNPLTLVISG SGHCALEAAL VNVLEPGDSF LVGANGIWGQ RAVDIGERIG 130 140 150 160 170 180 ARVHPMTKDP GGHYTLQEVE EGLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL 190 200 210 220 230 240 LVDSVASLGG TPLYMDRQGI DILYSGSQKA LNAPPGTSLI SFSDKAKKKM YSRKTKPFSF 250 260 270 280 290 300 YLDIKWLANF WGCDDQPRMY HHTIPVISLY SLRESLALIA EQGLENSWRQ HREAAAYLHG 310 320 330 340 350 360 RLQALGLQLF VKDPALRLPT VTTVAVPAGY DWRDIVSYVI DHFDIEIMGG LGPSTGKVLR 370 380 390 IGLLGCNATR ENVDRVTEAL RAALQHCPKK KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase." Nishiyama K., Berstein G., Oda T., Ichiyama A. Eur. J. Biochem. 194:9-18(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1." Purdue P.E., Takada Y., Danpure C.J. J. Cell Biol. 111:2341-2351(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-11 AND MET-340, VARIANT HP1 ARG-170.
[3]	"Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon." Takada Y., Kaneko N., Esumi H., Purdue P.E., Danpure C.J. Biochem. J. 268:517-520(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase." Purdue P.E., Lumb M.J., Fox M., Griffo G., Hamon-Benais C., Povey S., Danpure C.J. Genomics 10:34-42(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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]. Tissue: Liver.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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].
[9]	"Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1." Zhang X., Roe S.M., Hou Y., Bartlam M., Rao Z., Pearl L.H., Danpure C.J. J. Mol. Biol. 331:643-652(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND AMINO-OXYACETIC ACID, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-209.
[10]	"Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene." Nishiyama K., Funai T., Katafuchi R., Hattori F., Onoyama K., Ichiyama A. Biochem. Biophys. Res. Commun. 176:1093-1099(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HP1 PRO-205.
[11]	"A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1." Purdue P.E., Lumb M.J., Allsop J., Minatogawa Y., Danpure C.J. Genomics 13:215-218(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HP1 GLU-82.
[12]	"A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1." Minatogawa Y., Tone S., Allsop J., Purdue P.E., Takada Y., Danpure C.J., Kido R. Hum. Mol. Genet. 1:643-644(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HP1 PHE-187.
[13]	"Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation." Danpure C.J., Purdue P.E., Fryer P., Griffiths S., Allsop J., Lumb M.J., Guttridge K.M., Jennings P.R., Scheinman J.I., Mauer S.M., Davidson N.O. Am. J. Hum. Genet. 53:417-432(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ARG-41 AND ILE-152.
[14]	"Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase." Danpure C.J. Biochimie 75:309-315(1993) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON HP1.
[15]	"Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene." von Schnakenburg C., Rumsby G. J. Med. Genet. 34:489-492(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 CYS-233; HIS-233 AND THR-244.
[16]	"Identification of new mutations in primary hyperoxaluria type 1 (PH1)." von Schnakenburg C., Rumsby G. J. Nephrol. 11:15-17(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ARG-108; TYR-173; ARG-190; ALA-296 DEL AND ASP-350.
[17]	"Gene symbol: AGXT. Disease: primary hyperoxaluria type I." Amoroso A., Pirulli D., Puzzer D., Ferri L., Crovella S., Ferrettini C., Marangella M., Mazzola G., Florian F. Hum. Genet. 104:441-441(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 VAL-41; GLU-95 INS; ARG-116 AND ARG-156.
[18]	"Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene." Pirulli D., Puzzer D., Ferri L., Crovella S., Amoroso A., Ferrettini C., Marangella M., Mazzola G., Florian F. Hum. Genet. 104:523-525(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 VAL-41; GLU-95 INS; ARG-116 AND ARG-156.
[19]	"Primary hyperoxaluria type I: a model for multiple mutations in a monogenic disease within a distinct ethnic group." Rinat C., Wanders R.J.A., Drukker A., Halle D., Frishberg Y. J. Am. Soc. Nephrol. 10:2352-2358(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ARG-41; ARG-156; ARG-190; THR-244; CYS-289 AND PRO-298.
[20]	"Identification of 5 novel mutations in the AGXT gene." Basmaison O., Rolland M.-O., Cochat P., Bozon D. Hum. Mutat. 15:577-577(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ILE-152; ARG-170; ASN-183; CYS-233 AND THR-244.
[21]	"Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations." Lumb M.J., Danpure C.J. J. Biol. Chem. 275:36415-36422(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-41; GLU-82; ILE-152; ARG-170 AND THR-244, CHARACTERIZATION OF VARIANT LEU-11, MUTAGENESIS OF LYS-209.
[22]	"The AGT gene in Africa: a distinctive minor allele haplotype, a polymorphism (V326I), and a novel PH1 mutation (A112D) in Black Africans." Coulter-Mackie M.B., Tung A., Henderson H.E., Toone J.R., Applegarth D.A. Mol. Genet. Metab. 78:44-50(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HP1 ASP-112, VARIANT ILE-326.
[23]	"Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase." Santana A., Salido E., Torres A., Shapiro L.J. Proc. Natl. Acad. Sci. U.S.A. 100:7277-7282(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT HP1 THR-244.
[24]	"Clinical implications of mutation analysis in primary hyperoxaluria type 1." van Woerden C.S., Groothoff J.W., Wijburg F.A., Annink C., Wanders R.J.A., Waterham H.R. Kidney Int. 66:746-752(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ARG-82; ILE-152; VAL-153; ARG-170 AND ASP-336.
[25]	"Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria." Monico C.G., Olson J.B., Milliner D.S. Am. J. Nephrol. 25:183-188(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ASN-9; VAL-139 DEL; ARG-156; LEU-158; ARG-190; GLU-201; LEU-233; THR-244 AND ARG-253.
[26]	"Intra-familial clinical heterogeneity: absence of genotype-phenotype correlation in primary hyperoxaluria type 1 in Israel." Frishberg Y., Rinat C., Shalata A., Khatib I., Feinstein S., Becker-Cohen R., Weismann I., Wanders R.J.A., Rumsby G., Roels F., Mandel H. Am. J. Nephrol. 25:269-275(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ASN-9; ARG-41; ARG-108; ARG-156; ARG-190; ARG-195; HIS-243; THR-244; MET-279; THR-287; CYS-289 AND PRO-298.
[27]	"The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1." Coulter-Mackie M.B., Lian Q., Applegarth D., Toone J. Mol. Genet. Metab. 86:172-178(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HP1 ARG-161 AND LEU-218, VARIANTS THR-279 AND VAL-280.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56092 mRNA. Translation: CAA39572.1.
X53414 mRNA. Translation: CAA37493.1.
D13368 mRNA. Translation: BAA02632.1.
M61763 Genomic DNA. Translation: AAA51680.1.
AK292754 mRNA. Translation: BAF85443.1.
AC104809 Genomic DNA. Translation: AAY24168.1.
CH471063 Genomic DNA. Translation: EAW71222.1.
BC132819 mRNA. Translation: AAI32820.1.

IPI

IPI00009367.

PIR

XNHUSP. I39419.

RefSeq

NP_000021.1. NM_000030.2.

UniGene

Hs.144567.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H0C	X-ray	2.50	A	1-392	[»]
1J04	X-ray	2.60	A	1-392	[»]
3R9A	X-ray	2.35	A/C	1-392	[»]

ProteinModelPortal

P21549.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59650N.

IntAct

P21549. 2 interactions.

MINT

MINT-1419187.

STRING

9606.ENSP00000302620.

PTM databases

PhosphoSite

P21549.

Polymorphism databases

DMDM

134855.

Proteomic databases

PaxDb

P21549.

PeptideAtlas

P21549.

PRIDE

P21549.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307503; ENSP00000302620; ENSG00000172482.

GeneID

189.

KEGG

hsa:189.

UCSC

uc002waa.4. human.

Organism-specific databases

CTD

189.

GeneCards

GC02P241807.

HGNC

HGNC:341. AGXT.

HPA

HPA035370.

MIM

259900. phenotype.
604285. gene.

neXtProt

NX_P21549.

Orphanet

93598. Primary hyperoxaluria type 1.

PharmGKB

PA24633.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0075.

HOGENOM

HOG000171815.

HOVERGEN

HBG006907.

InParanoid

P21549.

KO

K00830.

OMA

VFGRFGH.

OrthoDB

EOG4BVRTQ.

PhylomeDB

P21549.

Enzyme and pathway databases

BRENDA

2.6.1.44. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P21549.

CleanEx

HS_AGXT.

Genevestigator

P21549.

GermOnline

ENSG00000172482. Homo sapiens.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR024169. SP_NH2Trfase/AEP_transaminase.
[Graphical view]

Pfam

PF00266. Aminotran_5. 1 hit.
[Graphical view]

PIRSF

PIRSF000524. SPT. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00145. Glycine.
DB00160. L-Alanine.
DB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

P21549.

GenomeRNAi

189.

NextBio

772.

SOURCE

Search...

Entry information

Entry name

SPYA_HUMAN

Accession

Primary (citable) accession number: P21549
Secondary accession number(s): Q53QU6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 132 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.