Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04181 (OAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine aminotransferase, mitochondrial

EC=2.6.1.13
Alternative name(s):
Ornithine delta-aminotransferase
Ornithine--oxo-acid aminotransferase
Gene names
Name:OAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF6P565371EBI-721662,EBI-372243

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04181-1)

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.
Isoform 2 (identifier: P04181-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion; in renal form Ref.3
Transit peptide1 – 2525Mitochondrion; in hepatic form
Chain26 – 439414Ornithine aminotransferase, hepatic form
PRO_0000001262
Chain36 – 439404Ornithine aminotransferase, renal form
PRO_0000001263

Amino acid modifications

Modified residue491N6-acetyllysine By similarity
Modified residue661N6-acetyllysine By similarity
Modified residue1021N6-succinyllysine By similarity
Modified residue1071N6-acetyllysine; alternate By similarity
Modified residue1071N6-succinyllysine; alternate By similarity
Modified residue2921N6-(pyridoxal phosphate)lysine Ref.13
Modified residue3621N6-acetyllysine; alternate By similarity
Modified residue3621N6-succinyllysine; alternate By similarity
Modified residue3861N6-acetyllysine By similarity
Modified residue3921N6-acetyllysine By similarity
Modified residue4051N6-acetyllysine; alternate By similarity
Modified residue4051N6-succinyllysine; alternate By similarity
Modified residue4211N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 138138Missing in isoform 2.
VSP_043085
Natural variant541N → K in HOGA. Ref.18
VAR_000565
Natural variant551Y → H in HOGA. Ref.21
VAR_000566
Natural variant891N → K in HOGA. Ref.21
VAR_000567
Natural variant901Q → E in HOGA; mistargeted, accumulates in cytoplasm. Ref.23
VAR_015648
Natural variant931C → F in HOGA. Ref.21
VAR_000568
Natural variant1541R → L in HOGA; complete loss of activity. Ref.21
VAR_000569
Natural variant1801R → T in HOGA; complete loss of activity. Ref.20 Ref.21
VAR_000570
Natural variant1841Missing in HOGA. Ref.21
VAR_000571
Natural variant2261A → V in HOGA. Ref.22
VAR_000572
Natural variant2411P → L in HOGA. Ref.20 Ref.21
VAR_000573
Natural variant2451Y → C in HOGA. Ref.21
VAR_000574
Natural variant2501R → P in HOGA. Ref.20 Ref.21
VAR_000575
Natural variant2671T → I in HOGA. Ref.21
VAR_000576
Natural variant2701A → P in HOGA.
VAR_000577
Natural variant2711R → K in HOGA. Ref.21
VAR_000578
Natural variant3191H → Y in HOGA. Ref.19
VAR_000579
Natural variant3321V → M in HOGA. Ref.18
VAR_000580
Natural variant3531G → D in HOGA. Ref.20 Ref.21
VAR_000581
Natural variant3751G → A in HOGA. Ref.21
VAR_000582
Natural variant3941C → R in HOGA. Ref.20 Ref.21
VAR_000583
Natural variant4021L → P in HOGA. Ref.21
Corresponds to variant rs121965043 [ dbSNP | Ensembl ].
VAR_000584
Natural variant4171P → L in HOGA. Ref.21
VAR_000585
Natural variant4371L → F. Ref.21
Corresponds to variant rs1800456 [ dbSNP | Ensembl ].
VAR_000586

Secondary structure

................................................................. 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: E9D0636824A83220

FASTA43948,535
        10         20         30         40         50         60 
MFSKLAHLQR FAVLSRGVHS SVASATSVAT KKTVQGPPTS DDIFEREYKY GAHNYHPLPV 

        70         80         90        100        110        120 
ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA LKSQVDKLTL TSRAFYNNVL 

       130        140        150        160        170        180 
GEYEEYITKL FNYHKVLPMN TGVEAGETAC KLARKWGYTV KGIQKYKAKI VFAAGNFWGR 

       190        200        210        220        230        240 
TLSAISSSTD PTSYDGFGPF MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV 

       250        260        270        280        290        300 
PDPGYLMGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP 

       310        320        330        340        350        360 
VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD KLGIILRNEL 

       370        380        390        400        410        420 
MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN GLLAKPTHGD IIRFAPPLVI 

       430 
KEDELRESIE IINKTILSF 

« Hide

Isoform 2 [UniParc].

Checksum: 9CFA7F66DDB264F0
Show »

FASTA30132,853

References

« Hide 'large scale' references
[1]"Molecular cloning of human ornithine aminotransferase mRNA."
Inana G., Totsuka S., Redmond M., Dougherty T., Nagle J., Shiono T., Ohura T., Kominami E., Katunuma N.
Proc. Natl. Acad. Sci. U.S.A. 83:1203-1207(1986) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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.
PIRXNHUO. A30806.
I55360.
RefSeqNP_000265.1. NM_000274.3.
NP_001165285.1. NM_001171814.1.
UniGeneHs.523332.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP04181.
SMRP04181. Positions 36-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110996. 16 interactions.
IntActP04181. 9 interactions.
MINTMINT-1387274.
STRING9606.ENSP00000357838.

Chemistry

ChEMBLCHEMBL5954.
DrugBankDB00129. L-Ornithine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP04181.

Polymorphism databases

DMDM129018.

2D gel databases

REPRODUCTION-2DPAGEIPI00022334.

Proteomic databases

PaxDbP04181.
PeptideAtlasP04181.
PRIDEP04181.

Protocols and materials databases

DNASU4942.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368845; ENSP00000357838; ENSG00000065154. [P04181-1]
ENST00000539214; ENSP00000439042; ENSG00000065154. [P04181-2]
GeneID4942.
KEGGhsa:4942.
UCSCuc001lhp.3. human. [P04181-1]

Organism-specific databases

CTD4942.
GeneCardsGC10M126075.
HGNCHGNC:8091. OAT.
HPACAB033576.
HPA040098.
MIM258870. phenotype.
613349. gene.
neXtProtNX_P04181.
Orphanet414. Gyrate atrophy of choroid and retina.
PharmGKBPA31880.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4992.
HOGENOMHOG000020206.
HOVERGENHBG000434.
InParanoidP04181.
KOK00819.
OMAHGAHNYH.
OrthoDBEOG7SJD4P.
PhylomeDBP04181.
TreeFamTF105720.

Enzyme and pathway databases

BioCycMetaCyc:HS00832-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP04181.
UniPathwayUPA00098; UER00358.

Gene expression databases

BgeeP04181.
CleanExHS_OAT.
GenevestigatorP04181.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR005814. Aminotrans_3.
IPR010164. Orn_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01885. Orn_aminotrans. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04181.
GenomeRNAi4942.
NextBio19041.
PROP04181.
SOURCESearch...

Entry information

Entry nameOAT_HUMAN
AccessionPrimary (citable) accession number: P04181
Secondary accession number(s): D3DRF0 expand/collapse secondary AC list , Q16068, Q16069, Q68CS0, Q6IAV9, Q9UD03
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: April 16, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM