UniProtKB - P04181 (OAT_HUMAN)
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- BLAST>sp|P04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial OS=Homo sapiens OX=9606 GN=OAT PE=1 SV=1 MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPV ALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVL GEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGR TLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVV PDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYP VSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNEL MKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVI KEDELRESIEIINKTILSF
- Align
Ornithine aminotransferase, mitochondrial
OAT
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"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), COFACTOR.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-proline biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-ornithine.Proteins known to be involved in this subpathway in this organism are:
- Ornithine aminotransferase, mitochondrial (OAT)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-ornithine, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: GO_Central
- ornithine-oxo-acid transaminase activity Source: ReactomeInferred from experimenti
- pyridoxal phosphate binding Source: GO_Central
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cellular amino acid biosynthetic process Source: Reactome
- L-proline biosynthetic process Source: UniProtKB-UniPathway
- protein hexamerization Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- visual perception Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Aminotransferase, Transferase |
| Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS00832-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.6.1.13 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-70614 Amino acid synthesis and interconversion (transamination) |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P04181 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00098; UER00358 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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: |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:OAT |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000065154.11 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8091 OAT |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613349 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P04181 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Mitochondrion
- Mitochondrion matrix 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Functional analysis of missense mutations of OAT, causing gyrate atrophy of choroid and retina."
Doimo M., Desbats M.A., Baldoin M.C., Lenzini E., Basso G., Murphy E., Graziano C., Seri M., Burlina A., Sartori G., Trevisson E., Salviati L.
Hum. Mutat. 34:229-236(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOGA ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417; ASN-436 AND PHE-437, CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226; LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437, SUBUNIT, SUBCELLULAR LOCATION.
- Mitochondrion matrix 1 Publication
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: HPA
Nucleus
- nucleoplasm Source: HPA
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Mitochondrion<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Hyperornithinemia with gyrate atrophy of choroid and retina (HOGA)7 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.20"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. - Ref.21"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. - Ref.22"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. - Ref.23"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. - Ref.24"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. - Ref.25"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. - Ref.26"Functional analysis of missense mutations of OAT, causing gyrate atrophy of choroid and retina."
Doimo M., Desbats M.A., Baldoin M.C., Lenzini E., Basso G., Murphy E., Graziano C., Seri M., Burlina A., Sartori G., Trevisson E., Salviati L.
Hum. Mutat. 34:229-236(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOGA ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417; ASN-436 AND PHE-437, CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226; LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437, SUBUNIT, SUBCELLULAR LOCATION.
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]
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]
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]
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]
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]
Kobayashi T., Ogawa H., Kasahara M., Shiozawa Z., Matsuzawa T.
Am. J. Hum. Genet. 57:284-291(1995) [PubMed] [Europe PMC] [Abstract]
Doimo M., Desbats M.A., Baldoin M.C., Lenzini E., Basso G., Murphy E., Graziano C., Seri M., Burlina A., Sartori G., Trevisson E., Salviati L.
Hum. Mutat. 34:229-236(2013) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071924 | 51 | G → D in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000565 | 54 | N → K in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000566 | 55 | Y → H in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000567 | 89 | N → K in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_015648 | 90 | Q → E in HOGA; mistargeted, accumulates in cytoplasm. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000568 | 93 | C → F in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071925 | 104 | Q → R in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000569 | 154 | R → L in HOGA; complete loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000570 | 180 | R → T in HOGA; complete loss of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000571 | 184 | Missing in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071926 | 199 | P → Q in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000572 | 226 | A → V in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000573 | 241 | P → L in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000574 | 245 | Y → C in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000575 | 250 | R → P in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000576 | 267 | T → I in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000577 | 270 | A → P in HOGA. Corresponds to variant dbSNP:rs121965041EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000578 | 271 | R → K in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071927 | 318 | E → K in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000579 | 319 | H → Y in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000580 | 332 | V → M in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000581 | 353 | G → D in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000582 | 375 | G → A in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000583 | 394 | C → R in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071928 | 394 | C → Y in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000584 | 402 | L → P in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000585 | 417 | P → L in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071929 | 436 | I → N in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000586 | 437 | L → F in HOGA; no effect on activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 4942 |
MalaCards human disease database More...MalaCardsi | OAT |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 258870 phenotype |
Open Targets More...OpenTargetsi | ENSG00000065154 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 414 Gyrate atrophy of choroid and retina |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31880 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5954 |
Drug and drug target database More...DrugBanki | DB02821 Canaline DB02054 Gabaculine DB00129 L-Ornithine DB00114 Pyridoxal Phosphate |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | OAT |
Domain mapping of disease mutations (DMDM) More...DMDMi | 129018 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei | 1 – 35 | Mitochondrion; in renal form1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 35 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei | 1 – 25 | Mitochondrion; in hepatic formAdd BLAST | 25 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000001262 | 26 – 439 | Ornithine aminotransferase, hepatic formAdd BLAST | 414 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000001263 | 36 – 439 | Ornithine aminotransferase, renal formAdd BLAST | 404 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 49 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 66 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 102 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 107 | N6-acetyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 107 | N6-succinyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 292 | N6-(pyridoxal phosphate)lysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 362 | N6-acetyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 362 | N6-succinyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 386 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 392 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 405 | N6-acetyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 405 | N6-succinyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 421 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
AcetylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P04181 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P04181 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P04181 |
PeptideAtlas More...PeptideAtlasi | P04181 |
PRoteomics IDEntifications database More...PRIDEi | P04181 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51672 51673 [P04181-2] |
2D gel databases
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00022334 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P04181 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P04181 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P04181 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P04181 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000065154 |
CleanEx database of gene expression profiles More...CleanExi | HS_OAT |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P04181 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P04181 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB033576 HPA040098 HPA064742 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Functional analysis of missense mutations of OAT, causing gyrate atrophy of choroid and retina."
Doimo M., Desbats M.A., Baldoin M.C., Lenzini E., Basso G., Murphy E., Graziano C., Seri M., Burlina A., Sartori G., Trevisson E., Salviati L.
Hum. Mutat. 34:229-236(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOGA ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417; ASN-436 AND PHE-437, CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226; LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437, SUBUNIT, SUBCELLULAR LOCATION.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110996, 44 interactors |
Protein interaction database and analysis system More...IntActi | P04181, 27 interactors |
Molecular INTeraction database More...MINTi | P04181 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000357838 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P04181 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 40 – 50 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 61 – 67 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 69 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 77 – 82 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 83 – 86 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 87 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 95 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 105 – 107 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 115 – 119 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 120 – 131 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 134 – 141 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 142 – 159 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 169 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 182 – 186 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 191 – 194 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 204 – 207 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 212 – 218 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 224 – 229 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 231 – 233 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 234 – 237 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 245 – 255 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 259 – 263 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 265 – 272 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 273 – 276 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 277 – 281 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 286 – 290 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 292 – 295 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 302 – 306 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 308 – 311 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 327 – 342 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 345 – 360 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 365 – 367 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 368 – 374 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 377 – 382 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 390 – 399 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 408 – 410 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 411 – 414 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 422 – 437 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P04181 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P04181 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P04181 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transit peptidePhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1402 Eukaryota COG4992 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00630000089895 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000020206 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000434 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P04181 |
KEGG Orthology (KO) More...KOi | K00819 |
Identification of Orthologs from Complete Genome Data More...OMAi | RTAWDLC |
Database of Orthologous Groups More...OrthoDBi | EOG091G06WM |
Database for complete collections of gene phylogenies More...PhylomeDBi | P04181 |
TreeFam database of animal gene trees More...TreeFami | TF105720 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00610 OAT_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005814 Aminotrans_3 IPR010164 Orn_aminotrans IPR034758 Orn_aminotrans_mito IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major |
The PANTHER Classification System More...PANTHERi | PTHR11986:SF18 PTHR11986:SF18, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00202 Aminotran_3, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53383 SSF53383, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01885 Orn_aminotrans, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00600 AA_TRANSFER_CLASS_3, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded 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.
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
The sequence of this isoform differs from the canonical sequence as follows:
1-138: Missing.
10 20 30 40 50
MNTGVEAGET ACKLARKWGY TVKGIQKYKA KIVFAAGNFW GRTLSAISSS
60 70 80 90 100
TDPTSYDGFG PFMPGFDIIP YNDLPALERA LQDPNVAAFM VEPIQGEAGV
110 120 130 140 150
VVPDPGYLMG VRELCTRHQV LFIADEIQTG LARTGRWLAV DYENVRPDIV
160 170 180 190 200
LLGKALSGGL YPVSAVLCDD DIMLTIKPGE HGSTYGGNPL GCRVAIAALE
210 220 230 240 250
VLEEENLAEN ADKLGIILRN ELMKLPSDVV TAVRGKGLLN AIVIKETKDW
260 270 280 290 300
DAWKVCLRLR DNGLLAKPTH GDIIRFAPPL VIKEDELRES IEIINKTILS
F
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071924 | 51 | G → D in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000565 | 54 | N → K in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000566 | 55 | Y → H in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000567 | 89 | N → K in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_015648 | 90 | Q → E in HOGA; mistargeted, accumulates in cytoplasm. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000568 | 93 | C → F in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071925 | 104 | Q → R in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000569 | 154 | R → L in HOGA; complete loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000570 | 180 | R → T in HOGA; complete loss of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000571 | 184 | Missing in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071926 | 199 | P → Q in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000572 | 226 | A → V in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000573 | 241 | P → L in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000574 | 245 | Y → C in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000575 | 250 | R → P in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000576 | 267 | T → I in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000577 | 270 | A → P in HOGA. Corresponds to variant dbSNP:rs121965041EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000578 | 271 | R → K in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071927 | 318 | E → K in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000579 | 319 | H → Y in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000580 | 332 | V → M in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000581 | 353 | G → D in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000582 | 375 | G → A in HOGA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000583 | 394 | C → R in HOGA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071928 | 394 | C → Y in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000584 | 402 | L → P in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000585 | 417 | P → L in HOGA; loss of activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071929 | 436 | I → N in HOGA; loss of activity and protein stability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000586 | 437 | L → F in HOGA; no effect on activity and protein stability. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 No translation available. 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS53586.1 [P04181-2] CCDS7639.1 [P04181-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A30806 XNHUO I55360 |
NCBI Reference Sequences More...RefSeqi | NP_000265.1, NM_000274.3 [P04181-1] NP_001165285.1, NM_001171814.1 [P04181-2] NP_001309894.1, NM_001322965.1 [P04181-1] NP_001309895.1, NM_001322966.1 [P04181-1] NP_001309896.1, NM_001322967.1 [P04181-1] NP_001309897.1, NM_001322968.1 [P04181-1] NP_001309898.1, NM_001322969.1 [P04181-1] NP_001309899.1, NM_001322970.1 [P04181-1] NP_001309900.1, NM_001322971.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.523332 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000368845; ENSP00000357838; ENSG00000065154 [P04181-1] ENST00000539214; ENSP00000439042; ENSG00000065154 [P04181-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4942 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4942 |
UCSC genome browser More...UCSCi | uc001lhp.4 human [P04181-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P04181 | Testicular tissue protein Li 130 | 439 | |||
| OAT isoform 2 | 439 | ||||
| Ornithine aminotransferase | 439 | ||||
| OAT isoform 1 | 301 | ||||
| P04181-2 | 301 | ||||
| +3 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P04181 | Testicular tissue protein Li 130 | 439 | |||
| OAT isoform 2 | 439 | ||||
| Ornithine aminotransferase | 439 | ||||
| UPI0005FB0E49 | 494 | ||||
| UPI0005FB4216 | 494 | ||||
| +79 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P04181 | Testicular tissue protein Li 130 | 439 | |||
| OAT isoform 2 | 439 | ||||
| Ornithine aminotransferase | 439 | ||||
| UPI0005FB0E49 | 494 | ||||
| UPI0005FB4216 | 494 | ||||
| +244 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 No translation available. 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS53586.1 [P04181-2] CCDS7639.1 [P04181-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A30806 XNHUO I55360 |
NCBI Reference Sequences More...RefSeqi | NP_000265.1, NM_000274.3 [P04181-1] NP_001165285.1, NM_001171814.1 [P04181-2] NP_001309894.1, NM_001322965.1 [P04181-1] NP_001309895.1, NM_001322966.1 [P04181-1] NP_001309896.1, NM_001322967.1 [P04181-1] NP_001309897.1, NM_001322968.1 [P04181-1] NP_001309898.1, NM_001322969.1 [P04181-1] NP_001309899.1, NM_001322970.1 [P04181-1] NP_001309900.1, NM_001322971.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.523332 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB 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 | [»] | |
| 5VWO | X-ray | 1.77 | A/B/C | 36-439 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P04181 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P04181 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110996, 44 interactors |
Protein interaction database and analysis system More...IntActi | P04181, 27 interactors |
Molecular INTeraction database More...MINTi | P04181 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000357838 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P04181 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5954 |
Drug and drug target database More...DrugBanki | DB02821 Canaline DB02054 Gabaculine DB00129 L-Ornithine DB00114 Pyridoxal Phosphate |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P04181 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P04181 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P04181 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P04181 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | OAT |
Domain mapping of disease mutations (DMDM) More...DMDMi | 129018 |
2D gel databases
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00022334 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P04181 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P04181 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P04181 |
PeptideAtlas More...PeptideAtlasi | P04181 |
PRoteomics IDEntifications database More...PRIDEi | P04181 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51672 51673 [P04181-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4942 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000368845; ENSP00000357838; ENSG00000065154 [P04181-1] ENST00000539214; ENSP00000439042; ENSG00000065154 [P04181-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4942 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4942 |
UCSC genome browser More...UCSCi | uc001lhp.4 human [P04181-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4942 |
DisGeNET More...DisGeNETi | 4942 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000065154.11 |
GeneCards: human genes, protein and diseases More...GeneCardsi | OAT |
Human Gene Nomenclature Database More...HGNCi | HGNC:8091 OAT |
Human Protein Atlas More...HPAi | CAB033576 HPA040098 HPA064742 |
MalaCards human disease database More...MalaCardsi | OAT |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 258870 phenotype 613349 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P04181 |
Open Targets More...OpenTargetsi | ENSG00000065154 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 414 Gyrate atrophy of choroid and retina |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31880 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1402 Eukaryota COG4992 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00630000089895 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000020206 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000434 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P04181 |
KEGG Orthology (KO) More...KOi | K00819 |
Identification of Orthologs from Complete Genome Data More...OMAi | RTAWDLC |
Database of Orthologous Groups More...OrthoDBi | EOG091G06WM |
Database for complete collections of gene phylogenies More...PhylomeDBi | P04181 |
TreeFam database of animal gene trees More...TreeFami | TF105720 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00098; UER00358 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS00832-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.6.1.13 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-70614 Amino acid synthesis and interconversion (transamination) |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P04181 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | OAT human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P04181 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4942 |
Protein Ontology More...PROi | PR:P04181 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000065154 |
CleanEx database of gene expression profiles More...CleanExi | HS_OAT |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P04181 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P04181 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00610 OAT_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005814 Aminotrans_3 IPR010164 Orn_aminotrans IPR034758 Orn_aminotrans_mito IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major |
The PANTHER Classification System More...PANTHERi | PTHR11986:SF18 PTHR11986:SF18, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00202 Aminotran_3, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53383 SSF53383, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01885 Orn_aminotrans, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00600 AA_TRANSFER_CLASS_3, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | OAT_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P04181Primary (citable) accession number: P04181 Secondary accession number(s): D3DRF0 , Q16068, Q16069, Q68CS0, Q6IAV9, Q9UD03 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 20, 1987 |
| Last sequence update: | March 20, 1987 | |
| Last modified: | July 18, 2018 | |
| This is version 209 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
