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Protein

Acyloxyacyl hydrolase

Gene

AOAH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (PubMed:1883828, PubMed:8089145, PubMed:29343645). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (By similarity). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (By similarity).By similarity3 Publications

<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. a chemical reaction that the enzyme catalyzes.<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

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit. The calcium ions probably have a structural role.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by EDTA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi184Calcium 11 Publication1
Metal bindingi186Calcium 11 Publication1
Metal bindingi186Calcium 21 Publication1
Metal bindingi188Calcium 11 Publication1
Metal bindingi188Calcium 21 Publication1
Metal bindingi190Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi205Calcium 11 Publication1
Metal bindingi205Calcium 21 Publication1
Metal bindingi207Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi208Calcium 11 Publication1
Metal bindingi210Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi213Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi223Calcium 31 Publication1
Metal bindingi227Calcium 31 Publication1
Metal bindingi229Calcium 31 Publication1
Metal bindingi231Calcium 31 Publication1
Metal bindingi233Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi245Calcium 31 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2632 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei345LipopolysaccharideBy similarity1

<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

  • acyloxyacyl hydrolase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB

GO - Biological processi

<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 functionHydrolase
Biological processLipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.77 2681

<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:
Acyloxyacyl hydrolase1 Publication (EC:3.1.1.773 Publications)
Cleaved into the following 2 chains:
Acyloxyacyl hydrolase small subunit1 Publication
Acyloxyacyl hydrolase large subunit1 Publication
<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:AOAH1 Publication
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000136250.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:548 AOAH

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
102593 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P28039

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasmic vesicle, Secreted

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi61T → A: Loss of glycosylation. No effect on enzyme activity or localization to cytoplasmic vesicles. 1 Publication1
Mutagenesisi173K → E: No effect on enzyme activity. 1 Publication1
Mutagenesisi263S → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi263S → L: Nearly abolishes catalytic activity. 1 Publication1
Mutagenesisi345R → E: No effect on enzyme activity; when associated with E-379. 1 Publication1
Mutagenesisi372G → M: Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate. 1 Publication1
Mutagenesisi379K → E: No effect on enzyme activity; when associated with E-345. 1 Publication1
Mutagenesisi419P → M: Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
313

Open Targets

More...
OpenTargetsi
ENSG00000136250

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24838

Chemistry databases

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2873

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AOAH

Domain mapping of disease mutations (DMDM)

More...
DMDMi
113976

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 231 PublicationAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002073924 – 341 PublicationAdd BLAST11
<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_000002074035 – 156Acyloxyacyl hydrolase small subunit1 PublicationAdd BLAST122
ChainiPRO_0000020741157 – 575Acyloxyacyl hydrolase large subunit1 PublicationAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi41 ↔ 114PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi44 ↔ 108PROSITE-ProRule annotationCombined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi59N-linked (GlcNAc...) asparagineCombined sources1 Publication1 Publication1
Disulfide bondi70 ↔ 83PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi123 ↔ 453Interchain (between small and large subunit)Combined sources1 Publication
Disulfide bondi160 ↔ 169Combined sources1 Publication
Disulfide bondi206 ↔ 230Combined sources1 Publication
Glycosylationi207N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi249 ↔ 329Combined sources1 Publication
Disulfide bondi376 ↔ 459Combined sources1 Publication
Glycosylationi466N-linked (GlcNAc...) asparagineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Cleaved into a large and a small subunit.3 Publications
The small subunit is N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P28039

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P28039

PeptideAtlas

More...
PeptideAtlasi
P28039

PRoteomics IDEntifications database

More...
PRIDEi
P28039

ProteomicsDB human proteome resource

More...
ProteomicsDBi
54435
54436 [P28039-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P28039

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P28039

<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
ENSG00000136250 Expressed in 176 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

More...
CleanExi
HS_AOAH

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P28039 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P28039 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA021666
HPA026716

<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

Heterodimer of the large and small subunits; disulfide-linked.3 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P28039, 2 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000258749

<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

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P28039

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P28039

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini37 – 118Saposin B-typePROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni38 – 70Important for enzyme activity, localization to cytoplasmic vesicles, and protein stability1 PublicationAdd BLAST33
Regioni173 – 177Lipopolysaccharide bindingBy similarity5

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFCC Eukaryota
ENOG410XTCS LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008427

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000008100

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004254

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P28039

KEGG Orthology (KO)

More...
KOi
K01065

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P28039

TreeFam database of animal gene trees

More...
TreeFami
TF329246

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039676 AOAH
IPR001087 GDSL
IPR008138 SapB_2
IPR011001 Saposin-like
IPR008139 SaposinB_dom

The PANTHER Classification System

More...
PANTHERi
PTHR15010 PTHR15010, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00657 Lipase_GDSL, 1 hit
PF03489 SapB_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00741 SapB, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47862 SSF47862, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50015 SAP_B, 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 basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P28039-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MQSPWKILTV APLFLLLSLQ SSASPANDDQ SRPSLSNGHT CVGCVLVVSV
60 70 80 90 100
IEQLAQVHNS TVQASMERLC SYLPEKLFLK TTCYLVIDKF GSDIIKLLSA
110 120 130 140 150
DMNADVVCHT LEFCKQNTGQ PLCHLYPLPK ETWKFTLQKA RQIVKKSPIL
160 170 180 190 200
KYSRSGSDIC SLPVLAKICQ KIKLAMEQSV PFKDVDSDKY SVFPTLRGYH
210 220 230 240 250
WRGRDCNDSD ESVYPGRRPN NWDVHQDSNC NGIWGVDPKD GVPYEKKFCE
260 270 280 290 300
GSQPRGIILL GDSAGAHFHI SPEWITASQM SLNSFINLPT ALTNELDWPQ
310 320 330 340 350
LSGATGFLDS TVGIKEKSIY LRLWKRNHCN HRDYQNISRN GASSRNLKKF
360 370 380 390 400
IESLSRNKVL DYPAIVIYAM IGNDVCSGKS DPVPAMTTPE KLYSNVMQTL
410 420 430 440 450
KHLNSHLPNG SHVILYGLPD GTFLWDNLHN RYHPLGQLNK DMTYAQLYSF
460 470 480 490 500
LNCLQVSPCH GWMSSNKTLR TLTSERAEQL SNTLKKIAAS EKFTNFNLFY
510 520 530 540 550
MDFAFHEIIQ EWQKRGGQPW QLIEPVDGFH PNEVALLLLA DHFWKKVQLQ
560 570
WPQILGKENP FNPQIKQVFG DQGGH
Length:575
Mass (Da):65,105
Last modified:August 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE3B3853DBD308AF7
GO
Isoform 2 (identifier: P28039-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-74: Missing.

Note: No experimental confirmation available.
Show »
Length:543
Mass (Da):61,647
Checksum:iBE14624794189A57
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WVT3A0A087WVT3_HUMAN
Acyloxyacyl hydrolase
AOAH
688Annotation score:

Annotation score:1 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>
C9JJA7C9JJA7_HUMAN
Acyloxyacyl hydrolase
AOAH
108Annotation score:

Annotation score:1 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>
F8WCP9F8WCP9_HUMAN
Acyloxyacyl hydrolase
AOAH
52Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti222W → C in BAD97196 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_05066328D → N2 PublicationsCorresponds to variant dbSNP:rs2228410Ensembl.1
Natural variantiVAR_020133166A → T. Corresponds to variant dbSNP:rs3735384Ensembl.1
Natural variantiVAR_033513266A → G. Corresponds to variant dbSNP:rs3735386Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_04257143 – 74Missing in isoform 2. 1 PublicationAdd BLAST32

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M62840 mRNA Translation: AAA35506.1
AK297016 mRNA Translation: BAH12476.1
AK223476 mRNA Translation: BAD97196.1
AC083876 Genomic DNA No translation available.
AC087069 Genomic DNA No translation available.
CH236951 Genomic DNA Translation: EAL23977.1
CH471073 Genomic DNA Translation: EAW94073.1
BC025698 mRNA Translation: AAH25698.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS5448.1 [P28039-1]
CCDS55102.1 [P28039-2]

Protein sequence database of the Protein Information Resource

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PIRi
A40292

NCBI Reference Sequences

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RefSeqi
NP_001170977.1, NM_001177506.1
NP_001170978.1, NM_001177507.1 [P28039-2]
NP_001628.1, NM_001637.3 [P28039-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.488007
Hs.689297

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000612871; ENSP00000484305; ENSG00000136250 [P28039-2]
ENST00000617537; ENSP00000483783; ENSG00000136250 [P28039-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
313

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:313

UCSC genome browser

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UCSCi
uc032zjw.2 human [P28039-1]

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

<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:
EMBLi
GenBanki
DDBJi
Links Updated
M62840 mRNA Translation: AAA35506.1
AK297016 mRNA Translation: BAH12476.1
AK223476 mRNA Translation: BAD97196.1
AC083876 Genomic DNA No translation available.
AC087069 Genomic DNA No translation available.
CH236951 Genomic DNA Translation: EAL23977.1
CH471073 Genomic DNA Translation: EAW94073.1
BC025698 mRNA Translation: AAH25698.1
CCDSiCCDS5448.1 [P28039-1]
CCDS55102.1 [P28039-2]
PIRiA40292
RefSeqiNP_001170977.1, NM_001177506.1
NP_001170978.1, NM_001177507.1 [P28039-2]
NP_001628.1, NM_001637.3 [P28039-1]
UniGeneiHs.488007
Hs.689297

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5W78X-ray2.27A24-152[»]
B153-575[»]
5W7CX-ray2.23A/B24-152[»]
C/D153-575[»]
ProteinModelPortaliP28039
SMRiP28039
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28039, 2 interactors
STRINGi9606.ENSP00000258749

Chemistry databases

GuidetoPHARMACOLOGYi2873

PTM databases

iPTMnetiP28039
PhosphoSitePlusiP28039

Polymorphism and mutation databases

BioMutaiAOAH
DMDMi113976

Proteomic databases

EPDiP28039
PaxDbiP28039
PeptideAtlasiP28039
PRIDEiP28039
ProteomicsDBi54435
54436 [P28039-2]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
313
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000612871; ENSP00000484305; ENSG00000136250 [P28039-2]
ENST00000617537; ENSP00000483783; ENSG00000136250 [P28039-1]
GeneIDi313
KEGGihsa:313
UCSCiuc032zjw.2 human [P28039-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
313
DisGeNETi313
EuPathDBiHostDB:ENSG00000136250.11

GeneCards: human genes, protein and diseases

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GeneCardsi
AOAH
HGNCiHGNC:548 AOAH
HPAiHPA021666
HPA026716
MIMi102593 gene
neXtProtiNX_P28039
OpenTargetsiENSG00000136250
PharmGKBiPA24838

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IFCC Eukaryota
ENOG410XTCS LUCA
GeneTreeiENSGT00390000008427
HOGENOMiHOG000008100
HOVERGENiHBG004254
InParanoidiP28039
KOiK01065
PhylomeDBiP28039
TreeFamiTF329246

Enzyme and pathway databases

BRENDAi3.1.1.77 2681

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
AOAH human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
AOAH

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
313

Protein Ontology

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PROi
PR:P28039

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136250 Expressed in 176 organ(s), highest expression level in blood
CleanExiHS_AOAH
ExpressionAtlasiP28039 baseline and differential
GenevisibleiP28039 HS

Family and domain databases

InterProiView protein in InterPro
IPR039676 AOAH
IPR001087 GDSL
IPR008138 SapB_2
IPR011001 Saposin-like
IPR008139 SaposinB_dom
PANTHERiPTHR15010 PTHR15010, 1 hit
PfamiView protein in Pfam
PF00657 Lipase_GDSL, 1 hit
PF03489 SapB_2, 1 hit
SMARTiView protein in SMART
SM00741 SapB, 1 hit
SUPFAMiSSF47862 SSF47862, 1 hit
PROSITEiView protein in PROSITE
PS50015 SAP_B, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiAOAH_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>AccessioniPrimary (citable) accession number: P28039
Secondary accession number(s): A4D1Y5, B7Z490, Q53F13
<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 historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: December 5, 2018
This is version 158 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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