Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P04181

- OAT_HUMAN

UniProt

P04181 - OAT_HUMAN

Protein

Ornithine aminotransferase, mitochondrial

Gene

OAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. ornithine-oxo-acid transaminase activity Source: Reactome
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. L-proline biosynthetic process Source: UniProtKB-UniPathway
    4. protein hexamerization Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. visual perception Source: ProtInc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00832-MONOMER.
    ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP04181.
    UniPathwayiUPA00098; UER00358.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine aminotransferase, mitochondrial (EC:2.6.1.13)
    Alternative name(s):
    Ornithine delta-aminotransferase
    Ornithine--oxo-acid aminotransferase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:OAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8091. OAT.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Hyperornithinemia with gyrate atrophy of choroid and retina (HOGA) [MIM:258870]: A disorder clinically characterized by a triad of progressive chorioretinal degeneration, early cataract formation, and type II muscle fiber atrophy. Characteristic chorioretinal atrophy with progressive constriction of the visual fields leads to blindness at the latest during the sixth decade of life. Patients generally have normal intelligence.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541N → K in HOGA. 1 Publication
    VAR_000565
    Natural varianti55 – 551Y → H in HOGA. 1 Publication
    VAR_000566
    Natural varianti89 – 891N → K in HOGA. 1 Publication
    VAR_000567
    Natural varianti90 – 901Q → E in HOGA; mistargeted, accumulates in cytoplasm. 1 Publication
    VAR_015648
    Natural varianti93 – 931C → F in HOGA. 1 Publication
    VAR_000568
    Natural varianti154 – 1541R → L in HOGA; complete loss of activity. 1 Publication
    VAR_000569
    Natural varianti180 – 1801R → T in HOGA; complete loss of activity. 2 Publications
    VAR_000570
    Natural varianti184 – 1841Missing in HOGA. 1 Publication
    VAR_000571
    Natural varianti226 – 2261A → V in HOGA. 1 Publication
    VAR_000572
    Natural varianti241 – 2411P → L in HOGA. 2 Publications
    VAR_000573
    Natural varianti245 – 2451Y → C in HOGA. 1 Publication
    VAR_000574
    Natural varianti250 – 2501R → P in HOGA. 2 Publications
    VAR_000575
    Natural varianti267 – 2671T → I in HOGA. 1 Publication
    VAR_000576
    Natural varianti270 – 2701A → P in HOGA.
    VAR_000577
    Natural varianti271 – 2711R → K in HOGA. 1 Publication
    VAR_000578
    Natural varianti319 – 3191H → Y in HOGA. 1 Publication
    VAR_000579
    Natural varianti332 – 3321V → M in HOGA. 1 Publication
    VAR_000580
    Natural varianti353 – 3531G → D in HOGA. 2 Publications
    VAR_000581
    Natural varianti375 – 3751G → A in HOGA. 1 Publication
    VAR_000582
    Natural varianti394 – 3941C → R in HOGA. 2 Publications
    VAR_000583
    Natural varianti402 – 4021L → P in HOGA. 1 Publication
    Corresponds to variant rs121965043 [ dbSNP | Ensembl ].
    VAR_000584
    Natural varianti417 – 4171P → L in HOGA. 1 Publication
    VAR_000585

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi258870. phenotype.
    Orphaneti414. Gyrate atrophy of choroid and retina.
    PharmGKBiPA31880.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535Mitochondrion; in renal form1 PublicationAdd
    BLAST
    Transit peptidei1 – 2525Mitochondrion; in hepatic formAdd
    BLAST
    Chaini26 – 439414Ornithine aminotransferase, hepatic formPRO_0000001262Add
    BLAST
    Chaini36 – 439404Ornithine aminotransferase, renal formPRO_0000001263Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491N6-acetyllysineBy similarity
    Modified residuei66 – 661N6-acetyllysineBy similarity
    Modified residuei102 – 1021N6-succinyllysineBy similarity
    Modified residuei107 – 1071N6-acetyllysine; alternateBy similarity
    Modified residuei107 – 1071N6-succinyllysine; alternateBy similarity
    Modified residuei292 – 2921N6-(pyridoxal phosphate)lysine1 Publication
    Modified residuei362 – 3621N6-acetyllysine; alternateBy similarity
    Modified residuei362 – 3621N6-succinyllysine; alternateBy similarity
    Modified residuei386 – 3861N6-acetyllysineBy similarity
    Modified residuei392 – 3921N6-acetyllysineBy similarity
    Modified residuei405 – 4051N6-acetyllysine; alternateBy similarity
    Modified residuei405 – 4051N6-succinyllysine; alternateBy similarity
    Modified residuei421 – 4211N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP04181.
    PaxDbiP04181.
    PeptideAtlasiP04181.
    PRIDEiP04181.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00022334.

    PTM databases

    PhosphoSiteiP04181.

    Expressioni

    Gene expression databases

    BgeeiP04181.
    CleanExiHS_OAT.
    GenevestigatoriP04181.

    Organism-specific databases

    HPAiCAB033576.
    HPA040098.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF6P565371EBI-721662,EBI-372243

    Protein-protein interaction databases

    BioGridi110996. 16 interactions.
    IntActiP04181. 9 interactions.
    MINTiMINT-1387274.
    STRINGi9606.ENSP00000357838.

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 5011
    Beta strandi61 – 677
    Beta strandi69 – 724
    Beta strandi77 – 826
    Helixi83 – 864
    Turni87 – 904
    Helixi95 – 10511
    Beta strandi115 – 1195
    Helixi120 – 13112
    Beta strandi134 – 1418
    Helixi142 – 15918
    Beta strandi169 – 1735
    Helixi182 – 1854
    Helixi191 – 1944
    Beta strandi204 – 2074
    Helixi212 – 2187
    Beta strandi224 – 2296
    Beta strandi231 – 2333
    Turni234 – 2374
    Helixi245 – 25511
    Beta strandi259 – 2635
    Turni265 – 2728
    Beta strandi273 – 2764
    Helixi277 – 2815
    Beta strandi286 – 2905
    Helixi292 – 2954
    Beta strandi302 – 3065
    Helixi308 – 3114
    Helixi327 – 34216
    Helixi345 – 36016
    Turni365 – 3673
    Beta strandi368 – 3747
    Beta strandi377 – 3826
    Helixi390 – 39910
    Beta strandi406 – 4149
    Helixi422 – 43716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GBNX-ray2.30A/B/C38-439[»]
    1OATX-ray2.50A/B/C1-439[»]
    2BYJX-ray3.02A/B/C1-439[»]
    2BYLX-ray2.15A/B/C1-439[»]
    2CANX-ray2.30A/B/C38-439[»]
    2OATX-ray1.95A/B/C1-439[»]
    ProteinModelPortaliP04181.
    SMRiP04181. Positions 36-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04181.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4992.
    HOGENOMiHOG000020206.
    HOVERGENiHBG000434.
    InParanoidiP04181.
    KOiK00819.
    OMAiHGERICA.
    OrthoDBiEOG7SJD4P.
    PhylomeDBiP04181.
    TreeFamiTF105720.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProiIPR005814. Aminotrans_3.
    IPR010164. Orn_aminotrans.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PTHR11986:SF18. PTHR11986:SF18. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01885. Orn_aminotrans. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04181-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFSKLAHLQR FAVLSRGVHS SVASATSVAT KKTVQGPPTS DDIFEREYKY    50
    GAHNYHPLPV ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA 100
    LKSQVDKLTL TSRAFYNNVL GEYEEYITKL FNYHKVLPMN TGVEAGETAC 150
    KLARKWGYTV KGIQKYKAKI VFAAGNFWGR TLSAISSSTD PTSYDGFGPF 200
    MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV PDPGYLMGVR 250
    ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP 300
    VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD 350
    KLGIILRNEL MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN 400
    GLLAKPTHGD IIRFAPPLVI KEDELRESIE IINKTILSF 439
    Length:439
    Mass (Da):48,535
    Last modified:March 20, 1987 - v1
    Checksum:iE9D0636824A83220
    GO
    Isoform 2 (identifier: P04181-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-138: Missing.

    Show »
    Length:301
    Mass (Da):32,853
    Checksum:i9CFA7F66DDB264F0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541N → K in HOGA. 1 Publication
    VAR_000565
    Natural varianti55 – 551Y → H in HOGA. 1 Publication
    VAR_000566
    Natural varianti89 – 891N → K in HOGA. 1 Publication
    VAR_000567
    Natural varianti90 – 901Q → E in HOGA; mistargeted, accumulates in cytoplasm. 1 Publication
    VAR_015648
    Natural varianti93 – 931C → F in HOGA. 1 Publication
    VAR_000568
    Natural varianti154 – 1541R → L in HOGA; complete loss of activity. 1 Publication
    VAR_000569
    Natural varianti180 – 1801R → T in HOGA; complete loss of activity. 2 Publications
    VAR_000570
    Natural varianti184 – 1841Missing in HOGA. 1 Publication
    VAR_000571
    Natural varianti226 – 2261A → V in HOGA. 1 Publication
    VAR_000572
    Natural varianti241 – 2411P → L in HOGA. 2 Publications
    VAR_000573
    Natural varianti245 – 2451Y → C in HOGA. 1 Publication
    VAR_000574
    Natural varianti250 – 2501R → P in HOGA. 2 Publications
    VAR_000575
    Natural varianti267 – 2671T → I in HOGA. 1 Publication
    VAR_000576
    Natural varianti270 – 2701A → P in HOGA.
    VAR_000577
    Natural varianti271 – 2711R → K in HOGA. 1 Publication
    VAR_000578
    Natural varianti319 – 3191H → Y in HOGA. 1 Publication
    VAR_000579
    Natural varianti332 – 3321V → M in HOGA. 1 Publication
    VAR_000580
    Natural varianti353 – 3531G → D in HOGA. 2 Publications
    VAR_000581
    Natural varianti375 – 3751G → A in HOGA. 1 Publication
    VAR_000582
    Natural varianti394 – 3941C → R in HOGA. 2 Publications
    VAR_000583
    Natural varianti402 – 4021L → P in HOGA. 1 Publication
    Corresponds to variant rs121965043 [ dbSNP | Ensembl ].
    VAR_000584
    Natural varianti417 – 4171P → L in HOGA. 1 Publication
    VAR_000585
    Natural varianti437 – 4371L → F.1 Publication
    Corresponds to variant rs1800456 [ dbSNP | Ensembl ].
    VAR_000586

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 138138Missing in isoform 2. 2 PublicationsVSP_043085Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12267 mRNA. Translation: AAA59956.1.
    M14963 mRNA. Translation: AAA59959.1.
    Y07511 mRNA. Translation: CAA68809.1.
    M23204 mRNA. Translation: AAA36386.1.
    M23205 Genomic DNA. No translation available.
    M88760 Genomic DNA. Translation: AAA59958.1. Sequence problems.
    M29927
    , M29919, M29920, M29921, M29922, M29923, M29924, M29925, M29926 Genomic DNA. Translation: AAA59957.1.
    AK296032 mRNA. Translation: BAH12241.1.
    AK312561 mRNA. Translation: BAG35458.1.
    AK315947 mRNA. Translation: BAH14318.1.
    CR457045 mRNA. Translation: CAG33326.1.
    CR749808 mRNA. Translation: CAH18668.1.
    AL445237 Genomic DNA. Translation: CAI17293.1.
    CH471066 Genomic DNA. Translation: EAW49271.1.
    CH471066 Genomic DNA. Translation: EAW49272.1.
    BC000964 mRNA. Translation: AAH00964.1.
    BC016928 mRNA. Translation: AAH16928.1.
    S66418 mRNA. Translation: AAB20298.1.
    S66421 mRNA. Translation: AAB20297.1.
    CCDSiCCDS53586.1. [P04181-2]
    CCDS7639.1. [P04181-1]
    PIRiA30806. XNHUO.
    I55360.
    RefSeqiNP_000265.1. NM_000274.3. [P04181-1]
    NP_001165285.1. NM_001171814.1. [P04181-2]
    XP_006717934.1. XM_006717871.1. [P04181-1]
    UniGeneiHs.523332.

    Genome annotation databases

    EnsembliENST00000368845; ENSP00000357838; ENSG00000065154. [P04181-1]
    ENST00000539214; ENSP00000439042; ENSG00000065154. [P04181-2]
    GeneIDi4942.
    KEGGihsa:4942.
    UCSCiuc001lhp.3. human. [P04181-1]

    Polymorphism databases

    DMDMi129018.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12267 mRNA. Translation: AAA59956.1 .
    M14963 mRNA. Translation: AAA59959.1 .
    Y07511 mRNA. Translation: CAA68809.1 .
    M23204 mRNA. Translation: AAA36386.1 .
    M23205 Genomic DNA. No translation available.
    M88760 Genomic DNA. Translation: AAA59958.1 . Sequence problems.
    M29927
    , M29919 , M29920 , M29921 , M29922 , M29923 , M29924 , M29925 , M29926 Genomic DNA. Translation: AAA59957.1 .
    AK296032 mRNA. Translation: BAH12241.1 .
    AK312561 mRNA. Translation: BAG35458.1 .
    AK315947 mRNA. Translation: BAH14318.1 .
    CR457045 mRNA. Translation: CAG33326.1 .
    CR749808 mRNA. Translation: CAH18668.1 .
    AL445237 Genomic DNA. Translation: CAI17293.1 .
    CH471066 Genomic DNA. Translation: EAW49271.1 .
    CH471066 Genomic DNA. Translation: EAW49272.1 .
    BC000964 mRNA. Translation: AAH00964.1 .
    BC016928 mRNA. Translation: AAH16928.1 .
    S66418 mRNA. Translation: AAB20298.1 .
    S66421 mRNA. Translation: AAB20297.1 .
    CCDSi CCDS53586.1. [P04181-2 ]
    CCDS7639.1. [P04181-1 ]
    PIRi A30806. XNHUO.
    I55360.
    RefSeqi NP_000265.1. NM_000274.3. [P04181-1 ]
    NP_001165285.1. NM_001171814.1. [P04181-2 ]
    XP_006717934.1. XM_006717871.1. [P04181-1 ]
    UniGenei Hs.523332.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GBN X-ray 2.30 A/B/C 38-439 [» ]
    1OAT X-ray 2.50 A/B/C 1-439 [» ]
    2BYJ X-ray 3.02 A/B/C 1-439 [» ]
    2BYL X-ray 2.15 A/B/C 1-439 [» ]
    2CAN X-ray 2.30 A/B/C 38-439 [» ]
    2OAT X-ray 1.95 A/B/C 1-439 [» ]
    ProteinModelPortali P04181.
    SMRi P04181. Positions 36-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110996. 16 interactions.
    IntActi P04181. 9 interactions.
    MINTi MINT-1387274.
    STRINGi 9606.ENSP00000357838.

    Chemistry

    ChEMBLi CHEMBL5954.
    DrugBanki DB00129. L-Ornithine.
    DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei P04181.

    Polymorphism databases

    DMDMi 129018.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00022334.

    Proteomic databases

    MaxQBi P04181.
    PaxDbi P04181.
    PeptideAtlasi P04181.
    PRIDEi P04181.

    Protocols and materials databases

    DNASUi 4942.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368845 ; ENSP00000357838 ; ENSG00000065154 . [P04181-1 ]
    ENST00000539214 ; ENSP00000439042 ; ENSG00000065154 . [P04181-2 ]
    GeneIDi 4942.
    KEGGi hsa:4942.
    UCSCi uc001lhp.3. human. [P04181-1 ]

    Organism-specific databases

    CTDi 4942.
    GeneCardsi GC10M126075.
    HGNCi HGNC:8091. OAT.
    HPAi CAB033576.
    HPA040098.
    MIMi 258870. phenotype.
    613349. gene.
    neXtProti NX_P04181.
    Orphaneti 414. Gyrate atrophy of choroid and retina.
    PharmGKBi PA31880.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4992.
    HOGENOMi HOG000020206.
    HOVERGENi HBG000434.
    InParanoidi P04181.
    KOi K00819.
    OMAi HGERICA.
    OrthoDBi EOG7SJD4P.
    PhylomeDBi P04181.
    TreeFami TF105720.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00358 .
    BioCyci MetaCyc:HS00832-MONOMER.
    Reactomei REACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RK P04181.

    Miscellaneous databases

    EvolutionaryTracei P04181.
    GenomeRNAii 4942.
    NextBioi 19041.
    PROi P04181.
    SOURCEi Search...

    Gene expression databases

    Bgeei P04181.
    CleanExi HS_OAT.
    Genevestigatori P04181.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProi IPR005814. Aminotrans_3.
    IPR010164. Orn_aminotrans.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    PTHR11986:SF18. PTHR11986:SF18. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01885. Orn_aminotrans. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase."
      Ramesh V., Shaffer M.M., Allaire J.M., Shih V.E., Gusella J.F.
      DNA 5:493-501(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase. An examination of ornithine aminotransferase isozymes between liver and kidney."
      Kobayashi T., Nishii M., Takagi Y., Titani T., Matsuzawa T.
      FEBS Lett. 255:300-304(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 36-40, PROTEOLYTIC PROCESSING.
      Tissue: Kidney.
    4. "Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene."
      Mitchell G.A., Looney J.E., Brody L.C., Steel G., Suchanek M., Engelhardt J.F., Willard H.F., Valle D.
      J. Biol. Chem. 263:14288-14295(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    5. "Analysis of the human ornithine aminotransferase gene family."
      Zintz C.B., Inana G.
      Exp. Eye Res. 50:759-770(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain, Brain cortex and Subthalamic nucleus.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain cortex.
    9. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM 1).
      Tissue: Placenta and Uterus.
    12. "Molecular pathology of gyrate atrophy of the choroid and retina due to ornithine aminotransferase deficiency."
      Ramesh V., Gusella J.F., Shih V.E.
      Mol. Biol. Med. 8:81-93(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-58 AND 328-336 (ISOFORM 1).
    13. "The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis."
      Simmaco M., John R.A., Barra D., Bossa F.
      FEBS Lett. 199:39-42(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, PYRIDOXAL PHOSPHATE AT LYS-292, PROTEOLYTIC PROCESSING.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition."
      Shah S.A., Shen B.W., Brunger A.T.
      Structure 5:1067-1075(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    16. "Crystal structure of human recombinant ornithine aminotransferase."
      Shen B.W., Hennig M., Hohenester E., Jansonius J.N., Schirmer T.
      J. Mol. Biol. 277:81-102(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    17. "Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine."
      Storici P., Capitani G., Mueller R., Schirmer T., Jansonius J.N.
      J. Mol. Biol. 285:297-309(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    18. "Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy."
      Ramesh V., McClatchey A.I., Ramesh N., Benoit L.A., Berson E.L., Shih V.E., Gusella J.F.
      Proc. Natl. Acad. Sci. U.S.A. 85:3777-3780(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HOGA LYS-54 AND MET-332.
    19. "Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy."
      Inana G., Chambers C., Hotta Y., Inouye L., Filpula D., Pulford S., Shiono T.
      J. Biol. Chem. 264:17432-17436(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HOGA TYR-319.
    20. "Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene."
      Michaud J., Brody L.C., Steel G., Fontaine G., Martin L.S., Valle D., Mitchell G.
      Genomics 13:389-394(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HOGA THR-180; LEU-241; PRO-250; ASP-353 AND ARG-394.
    21. "Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences."
      Brody L.C., Mitchell G.A., Obie C., Michaud J., Steel G., Fontaine G., Robert M.-F., Sipila I., Kaiser-Kupfer M., Valle D.
      J. Biol. Chem. 267:3302-3307(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HOGA HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; LEU-241; CYS-245; PRO-250; ILE-267; LYS-271; ASP-353; ALA-375; ARG-394; PRO-402 AND LEU-417, VARIANT PHE-437.
    22. "Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V."
      Michaud J., Thompson G.N., Brody L.C., Steel G., Obie C., Fontaine G., Schappert K., Keith C.G., Valle D., Mitchell G.A.
      Am. J. Hum. Genet. 56:616-622(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HOGA VAL-226.
    23. "A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor."
      Kobayashi T., Ogawa H., Kasahara M., Shiozawa Z., Matsuzawa T.
      Am. J. Hum. Genet. 57:284-291(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HOGA GLU-90.

    Entry informationi

    Entry nameiOAT_HUMAN
    AccessioniPrimary (citable) accession number: P04181
    Secondary accession number(s): D3DRF0
    , Q16068, Q16069, Q68CS0, Q6IAV9, Q9UD03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 170 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3