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Protein Page:
AGXT (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
AGXT Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1); also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Note: This description may include information from UniProtKB.
Protein type: Amino Acid Metabolism - glycine, serine and threonine; Amino Acid Metabolism - alanine, aspartate and glutamate; Transferase; Mitochondrial; EC 2.6.1.51; Motility/polarity/chemotaxis; EC 2.6.1.44
Cellular Component: peroxisomal matrix; mitochondrial matrix; peroxisome
Molecular Function: amino acid binding; protein binding; protein homodimerization activity; alanine-glyoxylate transaminase activity; serine-pyruvate transaminase activity; transaminase activity; pyridoxal phosphate binding; receptor binding
Biological Process: pyruvate biosynthetic process; response to cAMP; glyoxylate catabolic process; protein targeting to peroxisome; glyoxylate metabolic process; glycine biosynthetic process, by transamination of glyoxylate; response to glucocorticoid stimulus; oxalic acid secretion; L-cysteine catabolic process; L-alanine catabolic process
Reference #:  P21549 (UniProtKB)
Alt. Names/Synonyms: AGT; AGT1; AGXT; AGXT1; Alanine--glyoxylate aminotransferase; alanine-glyoxylate aminotransferase; hepatic peroxisomal alanine:glyoxylate aminotransferase; L-alanine: glyoxylate aminotransferase 1; PH1; Serine--pyruvate aminotransferase; serine-pyruvate aminotransferase; serine:pyruvate aminotransferase; SPAT; SPT; SPYA; TLH6
Gene Symbols: AGXT
Molecular weight: 43,010 Da
Basal Isoelectric point: 8.61  Predict pI for various phosphorylation states
Select Structure to View Below

AGXT

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 G42 PRIMAAGGLQMIGSM
0 9 Y194-p SLGGTPLyMDRQGID
0 1 K225 SLISFSDKAKkKMYS
0 1 K228-m3 SFSDKAKkKMYSRKT
0 1 K236 KMYSRKTKPFSFYLD
0 1 W246 SFYLDIKWLANFWGC
0 2 Y260-p CDDQPRMyHHTIPVI
0 1 S275 SLYSLRESLALIAEQ
0 22 Y297-p QHREAAAyLHGRLQA
0 13 K312 LGLQLFVKDPALRLP
0 1 K312 LGLQLFVKDPALRLP
0 2 K389-a AALQHCPkKKL____
  mouse

 
S64-p PRVLAAGsLRMIGHM
Y216 SLGGVPIYMDQQGID
K247-u SLISFNDkAKYKVYS
Y250 SFNDkAKYKVYSRKT
K258-u KVYSRKTkPVSFYTD
Y268-p SFYTDITyLAKLWGC
I282 CEGETRVIHHTTPVT
S297-p SLYCLREsLALIAEQ
H319 RHREATAHLHKHLQE
K334-a MGLKFFVkDPEIRLP
K334-u MGLKFFVkDPEIRLP
K411 EALQHCPKNKL____
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