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P21549

- SPYA_HUMAN

UniProt

P21549 - SPYA_HUMAN

Protein

Serine--pyruvate aminotransferase

Gene

AGXT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    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

    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

    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.16 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 3 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. 1 Publication
    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. 3 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. 3 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. 5 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; alternateBy similarity
    Modified residuei225 – 2251N6-succinyllysine; alternateBy similarity
    Modified residuei234 – 2341N6-acetyllysineBy similarity
    Modified residuei312 – 3121N6-acetyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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. 1 Publication
    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. 3 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. 1 Publication
    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. 3 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. 3 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. 5 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.

    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

    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: October 1, 2014
    This is version 146 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