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P04181

- OAT_HUMAN

UniProt

P04181 - OAT_HUMAN

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Protein

Ornithine aminotransferase, mitochondrial

Gene

OAT

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

Functioni

Catalytic activityi

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

Cofactori

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
Complete GO annotation...

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
Complete GO annotation...

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. 18 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 – 5011Combined sources
Beta strandi61 – 677Combined sources
Beta strandi69 – 724Combined sources
Beta strandi77 – 826Combined sources
Helixi83 – 864Combined sources
Turni87 – 904Combined sources
Helixi95 – 10511Combined sources
Beta strandi115 – 1195Combined sources
Helixi120 – 13112Combined sources
Beta strandi134 – 1418Combined sources
Helixi142 – 15918Combined sources
Beta strandi169 – 1735Combined sources
Helixi182 – 1854Combined sources
Helixi191 – 1944Combined sources
Beta strandi204 – 2074Combined sources
Helixi212 – 2187Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi231 – 2333Combined sources
Turni234 – 2374Combined sources
Helixi245 – 25511Combined sources
Beta strandi259 – 2635Combined sources
Turni265 – 2728Combined sources
Beta strandi273 – 2764Combined sources
Helixi277 – 2815Combined sources
Beta strandi286 – 2905Combined sources
Helixi292 – 2954Combined sources
Beta strandi302 – 3065Combined sources
Helixi308 – 3114Combined sources
Helixi327 – 34216Combined sources
Helixi345 – 36016Combined sources
Turni365 – 3673Combined sources
Beta strandi368 – 3747Combined sources
Beta strandi377 – 3826Combined sources
Helixi390 – 39910Combined sources
Beta strandi406 – 4149Combined sources
Helixi422 – 43716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00630000089895.
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

        10         20         30         40         50
MFSKLAHLQR FAVLSRGVHS SVASATSVAT KKTVQGPPTS DDIFEREYKY
60 70 80 90 100
GAHNYHPLPV ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA
110 120 130 140 150
LKSQVDKLTL TSRAFYNNVL GEYEEYITKL FNYHKVLPMN TGVEAGETAC
160 170 180 190 200
KLARKWGYTV KGIQKYKAKI VFAAGNFWGR TLSAISSSTD PTSYDGFGPF
210 220 230 240 250
MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV PDPGYLMGVR
260 270 280 290 300
ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP
310 320 330 340 350
VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD
360 370 380 390 400
KLGIILRNEL MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN
410 420 430
GLLAKPTHGD IIRFAPPLVI KEDELRESIE IINKTILSF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 18 interactions.
IntActi P04181. 9 interactions.
MINTi MINT-1387274.
STRINGi 9606.ENSP00000357838.

Chemistry

ChEMBLi CHEMBL5954.
DrugBanki DB00129. L-Ornithine.

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.
GeneTreei ENSGT00630000089895.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 172 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