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P21549 (SPYA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentMitochondrion
Peroxisome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-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

glyoxylate metabolic process

Inferred from mutant phenotype PubMed 3709805. Source: HGNC

oxalic acid secretion

Inferred from electronic annotation. Source: Ensembl

protein targeting to peroxisome

Inferred from mutant phenotype Ref.2. Source: HGNC

pyruvate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisomal matrix

Inferred from direct assay PubMed 22198249PubMed 3418107. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 9053548. Source: UniProtKB

   Molecular_functionalanine-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

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

serine-pyruvate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

transaminase activity

Inferred from direct assay PubMed 18492492PubMed 20133649. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Serine--pyruvate aminotransferase
PRO_0000150237

Sites

Binding site3601Substrate

Amino acid modifications

Modified residue2091N6-(pyridoxal phosphate)lysine
Modified residue2251N6-acetyllysine; alternate By similarity
Modified residue2251N6-succinyllysine; alternate By similarity
Modified residue2341N6-acetyllysine By similarity
Modified residue3121N6-acetyllysine By similarity

Natural variations

Natural variant91T → N in HP1. Ref.25 Ref.26
VAR_060547
Natural variant111P → 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 variant221N → S.
Corresponds to variant rs34885252 [ dbSNP | Ensembl ].
VAR_048236
Natural variant411G → 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 variant411G → V in HP1. Ref.17 Ref.18
VAR_010969
Natural variant821G → E in HP1; abolishes catalytic activity by interfering with pyridoxal phosphate binding. Ref.11 Ref.21
VAR_008878
Natural variant821G → R in HP1. Ref.24
VAR_060548
Natural variant951E → EE in HP1. Ref.17 Ref.18
VAR_010970
Natural variant1081W → R in HP1. Ref.16 Ref.26
VAR_060549
Natural variant1121A → D in HP1. Ref.22
VAR_060550
Natural variant1161G → R in HP1. Ref.17 Ref.18
VAR_010971
Natural variant1391Missing in HP1. Ref.25
VAR_060551
Natural variant1521F → 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 variant1531L → V in HP1. Ref.24
VAR_060552
Natural variant1561G → R in HP1. Ref.17 Ref.18 Ref.19 Ref.25 Ref.26
VAR_010972
Natural variant1581S → L in HP1. Ref.25
VAR_060553
Natural variant1611G → R in HP1. Ref.27
VAR_060554
Natural variant1701G → R in HP1; causes mistargeting when associated with L-11. Ref.2 Ref.20 Ref.21 Ref.24
VAR_000590
Natural variant1731C → Y in HP1. Ref.16
VAR_060555
Natural variant1831D → N in HP1. Ref.20
VAR_010973
Natural variant1871S → F in HP1. Ref.12
VAR_000591
Natural variant1901G → R in HP1. Ref.16 Ref.19 Ref.25 Ref.26
VAR_060556
Natural variant1951M → R in HP1. Ref.26
VAR_060557
Natural variant2011D → E in HP1. Ref.25
VAR_060558
Natural variant2051S → P in HP1. Ref.10
VAR_000592
Natural variant2181S → L in HP1. Ref.27
VAR_060559
Natural variant2331R → C in HP1. Ref.15 Ref.20
VAR_008879
Natural variant2331R → H in HP1. Ref.15
VAR_008880
Natural variant2331R → L in HP1. Ref.25
VAR_060560
Natural variant2431D → H in HP1. Ref.26
VAR_060561
Natural variant2441I → 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 variant2531C → R in HP1. Ref.25
VAR_060562
Natural variant2791I → M in HP1. Ref.26
VAR_060563
Natural variant2791I → T. Ref.27
Corresponds to variant rs140992177 [ dbSNP | Ensembl ].
VAR_060564
Natural variant2801A → V. Ref.27
Corresponds to variant rs73106685 [ dbSNP | Ensembl ].
VAR_060565
Natural variant2871S → T in HP1. Ref.26
VAR_060566
Natural variant2891R → C in HP1. Ref.19 Ref.26
VAR_060567
Natural variant2951A → T.
Corresponds to variant rs13408961 [ dbSNP | Ensembl ].
VAR_048237
Natural variant2961Missing in HP1. Ref.16
VAR_060568
Natural variant2981L → P in HP1. Ref.19 Ref.26
VAR_060569
Natural variant3261V → I. Ref.22
Corresponds to variant rs115057148 [ dbSNP | Ensembl ].
VAR_060570
Natural variant3361V → D in HP1. Ref.24
VAR_060571
Natural variant3401I → M Common polymorphism; associated with hyperoxaluria. Ref.2
Corresponds to variant rs4426527 [ dbSNP | Ensembl ].
VAR_000593
Natural variant3501G → D in HP1. Ref.16
VAR_060572

Experimental info

Mutagenesis2091K → R: Affects pyridoxal phosphate binding. Ref.21

Secondary structure

............................................................. 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21549 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 2987DDE85B2470B4

FASTA39243,010
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. 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 (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

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.
PIRXNHUSP. I39419.
RefSeqNP_000021.1. NM_000030.2.
UniGeneHs.144567.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0CX-ray2.50A1-392[»]
1J04X-ray2.60A1-392[»]
2YOBX-ray1.90A/B1-388[»]
3R9AX-ray2.35A/C1-392[»]
4I8AX-ray2.90A/B/C/D1-392[»]
ProteinModelPortalP21549.
SMRP21549. Positions 4-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106694. 4 interactions.
DIPDIP-59650N.
IntActP21549. 2 interactions.
MINTMINT-1419187.
STRING9606.ENSP00000302620.

Chemistry

DrugBankDB00145. Glycine.
DB00160. L-Alanine.
DB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP21549.

Polymorphism databases

DMDM134855.

Proteomic databases

PaxDbP21549.
PeptideAtlasP21549.
PRIDEP21549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307503; ENSP00000302620; ENSG00000172482.
GeneID189.
KEGGhsa:189.
UCSCuc002waa.4. human.

Organism-specific databases

CTD189.
GeneCardsGC02P241807.
HGNCHGNC:341. AGXT.
HPAHPA035370.
HPA035371.
MIM259900. phenotype.
604285. gene.
neXtProtNX_P21549.
Orphanet93598. Primary hyperoxaluria type 1.
PharmGKBPA24633.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0075.
HOGENOMHOG000171815.
HOVERGENHBG006907.
InParanoidP21549.
KOK00830.
OMAAYSCSQK.
OrthoDBEOG7CZK6B.
PhylomeDBP21549.
TreeFamTF313234.

Enzyme and pathway databases

BioCycMetaCyc:HS10525-MONOMER.
BRENDA2.6.1.44. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP21549.
CleanExHS_AGXT.
GenevestigatorP21549.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000192. 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]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000524. SPT. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21549.
GeneWikiAGXT.
GenomeRNAi189.
NextBio772.
PROP21549.
SOURCESearch...

Entry information

Entry nameSPYA_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 141 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM