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P21549

- SPYA_HUMAN

UniProt

P21549 - SPYA_HUMAN

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Protein

Serine--pyruvate aminotransferase

Gene
AGXT, AGT1, SPAT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.
L-alanine + glyoxylate = pyruvate + glycine.

Cofactori

Pyridoxal phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei360 – 3601Substrate

GO - Molecular functioni

  1. alanine-glyoxylate transaminase activity Source: UniProtKB
  2. amino acid binding Source: UniProtKB
  3. protein binding Source: HGNC
  4. protein homodimerization activity Source: UniProtKB
  5. pyridoxal phosphate binding Source: UniProtKB
  6. receptor binding Source: UniProtKB
  7. serine-pyruvate transaminase activity Source: UniProtKB-EC
  8. transaminase activity Source: UniProtKB

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. glycine biosynthetic process, by transamination of glyoxylate Source: UniProtKB
  3. glyoxylate catabolic process Source: UniProtKB
  4. glyoxylate metabolic process Source: HGNC
  5. L-alanine catabolic process Source: UniProtKB
  6. L-cysteine catabolic process Source: UniProtKB
  7. oxalic acid secretion Source: Ensembl
  8. protein targeting to peroxisome Source: HGNC
  9. pyruvate biosynthetic process Source: Ensembl
  10. response to cAMP Source: Ensembl
  11. response to glucocorticoid Source: Ensembl
  12. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS10525-MONOMER.
BRENDAi2.6.1.44. 2681.
ReactomeiREACT_16925. Glyoxylate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--pyruvate aminotransferase (EC:2.6.1.51)
Short name:
SPT
Alternative name(s):
Alanine--glyoxylate aminotransferase (EC:2.6.1.44)
Short name:
AGT
Gene namesi
Name:AGXT
Synonyms:AGT1, SPAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:341. AGXT.

Subcellular locationi

Peroxisome. Mitochondrion matrix
Note: Except in some HP1 patients where AGT is found in the mitochondrial matrix.

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. peroxisomal matrix Source: UniProtKB
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

Pathology & Biotechi

Involvement in diseasei

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.18 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91T → N in HP1. 2 Publications
VAR_060547
Natural varianti41 – 411G → R in HP1; protein destabilization and loss of activity in the presence of L-11. 4 Publications
VAR_000588
Natural varianti41 – 411G → V in HP1. 2 Publications
VAR_010969
Natural varianti82 – 821G → E in HP1; abolishes catalytic activity by interfering with pyridoxal phosphate binding. 2 Publications
VAR_008878
Natural varianti82 – 821G → R in HP1. 1 Publication
VAR_060548
Natural varianti95 – 951E → EE in HP1. 2 Publications
VAR_010970
Natural varianti108 – 1081W → R in HP1. 2 Publications
VAR_060549
Natural varianti112 – 1121A → D in HP1. 1 Publication
VAR_060550
Natural varianti116 – 1161G → R in HP1. 2 Publications
VAR_010971
Natural varianti139 – 1391Missing in HP1. 1 Publication
VAR_060551
Natural varianti152 – 1521F → I in HP1; protein destabilization and loss of activity in the presence of L-11. 4 Publications
VAR_000589
Natural varianti153 – 1531L → V in HP1. 1 Publication
VAR_060552
Natural varianti156 – 1561G → R in HP1. 5 Publications
VAR_010972
Natural varianti158 – 1581S → L in HP1. 1 Publication
VAR_060553
Natural varianti161 – 1611G → R in HP1. 1 Publication
VAR_060554
Natural varianti170 – 1701G → R in HP1; causes mistargeting when associated with L-11. 4 Publications
VAR_000590
Natural varianti173 – 1731C → Y in HP1. 1 Publication
VAR_060555
Natural varianti183 – 1831D → N in HP1. 1 Publication
VAR_010973
Natural varianti187 – 1871S → F in HP1. 1 Publication
VAR_000591
Natural varianti190 – 1901G → R in HP1. 4 Publications
VAR_060556
Natural varianti195 – 1951M → R in HP1. 1 Publication
VAR_060557
Natural varianti201 – 2011D → E in HP1. 1 Publication
VAR_060558
Natural varianti205 – 2051S → P in HP1. 1 Publication
VAR_000592
Natural varianti218 – 2181S → L in HP1. 1 Publication
VAR_060559
Natural varianti233 – 2331R → C in HP1. 2 Publications
VAR_008879
Natural varianti233 – 2331R → H in HP1. 1 Publication
VAR_008880
Natural varianti233 – 2331R → L in HP1. 1 Publication
VAR_060560
Natural varianti243 – 2431D → H in HP1. 1 Publication
VAR_060561
Natural varianti244 – 2441I → T in HP1; prevalent mutation in the Canary islands; protein misfolding and loss of activity when associated with P-11. 7 Publications
VAR_008881
Natural varianti253 – 2531C → R in HP1. 1 Publication
VAR_060562
Natural varianti279 – 2791I → M in HP1. 1 Publication
VAR_060563
Natural varianti287 – 2871S → T in HP1. 1 Publication
VAR_060566
Natural varianti289 – 2891R → C in HP1. 2 Publications
VAR_060567
Natural varianti296 – 2961Missing in HP1. 1 Publication
VAR_060568
Natural varianti298 – 2981L → P in HP1. 2 Publications
VAR_060569
Natural varianti336 – 3361V → D in HP1. 1 Publication
VAR_060571
Natural varianti350 – 3501G → D in HP1. 1 Publication
VAR_060572

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091K → R: Affects pyridoxal phosphate binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi259900. phenotype.
Orphaneti93598. Primary hyperoxaluria type 1.
PharmGKBiPA24633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392Serine--pyruvate aminotransferasePRO_0000150237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei209 – 2091N6-(pyridoxal phosphate)lysine
Modified residuei225 – 2251N6-acetyllysine; alternate By similarity
Modified residuei225 – 2251N6-succinyllysine; alternate By similarity
Modified residuei234 – 2341N6-acetyllysine By similarity
Modified residuei312 – 3121N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21549.
PaxDbiP21549.
PeptideAtlasiP21549.
PRIDEiP21549.

PTM databases

PhosphoSiteiP21549.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiP21549.
CleanExiHS_AGXT.
GenevestigatoriP21549.

Organism-specific databases

HPAiHPA035370.
HPA035371.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi106694. 4 interactions.
DIPiDIP-59650N.
IntActiP21549. 2 interactions.
MINTiMINT-1419187.
STRINGi9606.ENSP00000302620.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154
Beta strandi27 – 293
Helixi35 – 417
Helixi51 – 6818
Beta strandi73 – 808
Helixi82 – 9312
Beta strandi99 – 1068
Helixi107 – 11812
Beta strandi122 – 1276
Helixi136 – 14611
Beta strandi149 – 1579
Turni158 – 1614
Helixi169 – 1757
Beta strandi179 – 1835
Turni185 – 1906
Turni195 – 1995
Beta strandi201 – 2099
Beta strandi218 – 2225
Helixi224 – 2307
Helixi244 – 2507
Beta strandi254 – 2563
Helixi266 – 28217
Helixi284 – 30421
Beta strandi309 – 3113
Helixi314 – 3163
Beta strandi321 – 3255
Helixi332 – 34312
Helixi352 – 3543
Turni355 – 3573
Beta strandi358 – 3625
Helixi365 – 3673
Helixi370 – 38617

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP21549.
SMRiP21549. Positions 4-392.

Miscellaneous databases

EvolutionaryTraceiP21549.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0075.
HOGENOMiHOG000171815.
HOVERGENiHBG006907.
InParanoidiP21549.
KOiK00830.
OMAiHKYNCLL.
OrthoDBiEOG7CZK6B.
PhylomeDBiP21549.
TreeFamiTF313234.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. 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]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000524. SPT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21549-1 [UniParc]FASTAAdd to Basket

« Hide

MASHKLLVTP PKALLKPLSI PNQLLLGPGP SNLPPRIMAA GGLQMIGSMS    50
KDMYQIMDEI KEGIQYVFQT RNPLTLVISG SGHCALEAAL VNVLEPGDSF 100
LVGANGIWGQ RAVDIGERIG ARVHPMTKDP GGHYTLQEVE EGLAQHKPVL 150
LFLTHGESST GVLQPLDGFG ELCHRYKCLL LVDSVASLGG TPLYMDRQGI 200
DILYSGSQKA LNAPPGTSLI SFSDKAKKKM YSRKTKPFSF YLDIKWLANF 250
WGCDDQPRMY HHTIPVISLY SLRESLALIA EQGLENSWRQ HREAAAYLHG 300
RLQALGLQLF VKDPALRLPT VTTVAVPAGY DWRDIVSYVI DHFDIEIMGG 350
LGPSTGKVLR IGLLGCNATR ENVDRVTEAL RAALQHCPKK KL 392
Length:392
Mass (Da):43,010
Last modified:May 1, 1991 - v1
Checksum:i2987DDE85B2470B4
GO

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91T → N in HP1. 2 Publications
VAR_060547
Natural varianti11 – 111P → L Common polymorphism; reduction of specific activity in vitro; causes mistargeting when associated with R-170. 2 Publications
Corresponds to variant rs34116584 [ dbSNP | Ensembl ].
VAR_000587
Natural varianti22 – 221N → S.
Corresponds to variant rs34885252 [ dbSNP | Ensembl ].
VAR_048236
Natural varianti41 – 411G → R in HP1; protein destabilization and loss of activity in the presence of L-11. 4 Publications
VAR_000588
Natural varianti41 – 411G → V in HP1. 2 Publications
VAR_010969
Natural varianti82 – 821G → E in HP1; abolishes catalytic activity by interfering with pyridoxal phosphate binding. 2 Publications
VAR_008878
Natural varianti82 – 821G → R in HP1. 1 Publication
VAR_060548
Natural varianti95 – 951E → EE in HP1. 2 Publications
VAR_010970
Natural varianti108 – 1081W → R in HP1. 2 Publications
VAR_060549
Natural varianti112 – 1121A → D in HP1. 1 Publication
VAR_060550
Natural varianti116 – 1161G → R in HP1. 2 Publications
VAR_010971
Natural varianti139 – 1391Missing in HP1. 1 Publication
VAR_060551
Natural varianti152 – 1521F → I in HP1; protein destabilization and loss of activity in the presence of L-11. 4 Publications
VAR_000589
Natural varianti153 – 1531L → V in HP1. 1 Publication
VAR_060552
Natural varianti156 – 1561G → R in HP1. 5 Publications
VAR_010972
Natural varianti158 – 1581S → L in HP1. 1 Publication
VAR_060553
Natural varianti161 – 1611G → R in HP1. 1 Publication
VAR_060554
Natural varianti170 – 1701G → R in HP1; causes mistargeting when associated with L-11. 4 Publications
VAR_000590
Natural varianti173 – 1731C → Y in HP1. 1 Publication
VAR_060555
Natural varianti183 – 1831D → N in HP1. 1 Publication
VAR_010973
Natural varianti187 – 1871S → F in HP1. 1 Publication
VAR_000591
Natural varianti190 – 1901G → R in HP1. 4 Publications
VAR_060556
Natural varianti195 – 1951M → R in HP1. 1 Publication
VAR_060557
Natural varianti201 – 2011D → E in HP1. 1 Publication
VAR_060558
Natural varianti205 – 2051S → P in HP1. 1 Publication
VAR_000592
Natural varianti218 – 2181S → L in HP1. 1 Publication
VAR_060559
Natural varianti233 – 2331R → C in HP1. 2 Publications
VAR_008879
Natural varianti233 – 2331R → H in HP1. 1 Publication
VAR_008880
Natural varianti233 – 2331R → L in HP1. 1 Publication
VAR_060560
Natural varianti243 – 2431D → H in HP1. 1 Publication
VAR_060561
Natural varianti244 – 2441I → T in HP1; prevalent mutation in the Canary islands; protein misfolding and loss of activity when associated with P-11. 7 Publications
VAR_008881
Natural varianti253 – 2531C → R in HP1. 1 Publication
VAR_060562
Natural varianti279 – 2791I → M in HP1. 1 Publication
VAR_060563
Natural varianti279 – 2791I → T.1 Publication
Corresponds to variant rs140992177 [ dbSNP | Ensembl ].
VAR_060564
Natural varianti280 – 2801A → V.1 Publication
Corresponds to variant rs73106685 [ dbSNP | Ensembl ].
VAR_060565
Natural varianti287 – 2871S → T in HP1. 1 Publication
VAR_060566
Natural varianti289 – 2891R → C in HP1. 2 Publications
VAR_060567
Natural varianti295 – 2951A → T.
Corresponds to variant rs13408961 [ dbSNP | Ensembl ].
VAR_048237
Natural varianti296 – 2961Missing in HP1. 1 Publication
VAR_060568
Natural varianti298 – 2981L → P in HP1. 2 Publications
VAR_060569
Natural varianti326 – 3261V → I.1 Publication
Corresponds to variant rs115057148 [ dbSNP | Ensembl ].
VAR_060570
Natural varianti336 – 3361V → D in HP1. 1 Publication
VAR_060571
Natural varianti340 – 3401I → M Common polymorphism; associated with hyperoxaluria. 1 Publication
Corresponds to variant rs4426527 [ dbSNP | Ensembl ].
VAR_000593
Natural varianti350 – 3501G → D in HP1. 1 Publication
VAR_060572

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2543.1.
PIRiI39419. XNHUSP.
RefSeqiNP_000021.1. NM_000030.2.
UniGeneiHs.144567.

Genome annotation databases

EnsembliENST00000307503; ENSP00000302620; ENSG00000172482.
GeneIDi189.
KEGGihsa:189.
UCSCiuc002waa.4. human.

Polymorphism databases

DMDMi134855.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2543.1.
PIRi I39419. XNHUSP.
RefSeqi NP_000021.1. NM_000030.2.
UniGenei Hs.144567.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H0C X-ray 2.50 A 1-392 [» ]
1J04 X-ray 2.60 A 1-392 [» ]
2YOB X-ray 1.90 A/B 1-388 [» ]
3R9A X-ray 2.35 A/C 1-392 [» ]
4I8A X-ray 2.90 A/B/C/D 1-392 [» ]
ProteinModelPortali P21549.
SMRi P21549. Positions 4-392.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106694. 4 interactions.
DIPi DIP-59650N.
IntActi P21549. 2 interactions.
MINTi MINT-1419187.
STRINGi 9606.ENSP00000302620.

Chemistry

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

PTM databases

PhosphoSitei P21549.

Polymorphism databases

DMDMi 134855.

Proteomic databases

MaxQBi P21549.
PaxDbi P21549.
PeptideAtlasi P21549.
PRIDEi P21549.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307503 ; ENSP00000302620 ; ENSG00000172482 .
GeneIDi 189.
KEGGi hsa:189.
UCSCi uc002waa.4. human.

Organism-specific databases

CTDi 189.
GeneCardsi GC02P241807.
GeneReviewsi AGXT.
HGNCi HGNC:341. AGXT.
HPAi HPA035370.
HPA035371.
MIMi 259900. phenotype.
604285. gene.
neXtProti NX_P21549.
Orphaneti 93598. Primary hyperoxaluria type 1.
PharmGKBi PA24633.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0075.
HOGENOMi HOG000171815.
HOVERGENi HBG006907.
InParanoidi P21549.
KOi K00830.
OMAi HKYNCLL.
OrthoDBi EOG7CZK6B.
PhylomeDBi P21549.
TreeFami TF313234.

Enzyme and pathway databases

BioCyci MetaCyc:HS10525-MONOMER.
BRENDAi 2.6.1.44. 2681.
Reactomei REACT_16925. Glyoxylate metabolism.

Miscellaneous databases

EvolutionaryTracei P21549.
GeneWikii AGXT.
GenomeRNAii 189.
NextBioi 772.
PROi P21549.
SOURCEi Search...

Gene expression databases

Bgeei P21549.
CleanExi HS_AGXT.
Genevestigatori P21549.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi 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 ]
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF000524. SPT. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiSPYA_HUMAN
AccessioniPrimary (citable) accession number: P21549
Secondary accession number(s): Q53QU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: September 3, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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