O75608 (LYPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acyl-protein thioesterase 1 Short name=APT-1 Short name=hAPT1 EC=3.1.2.- Alternative name(s): Lysophospholipase 1 Lysophospholipase I Short name=LPL-I Short name=LysoPLA I | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 230 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity and also low lysophospholipase activity. Ref.6 |
| Catalytic activity | Palmitoyl-protein + H2O = palmitate + protein. |
| Enzyme regulation | Inhibited by palmostatin-B, leading to impair depalmitoylating of Ras. Ref.6 |
| Subunit structure | Homodimer. Ref.2 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the AB hydrolase superfamily. AB hydrolase 2 family. |
| Sequence caution | The sequence AAB88180.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nitric oxide metabolic processTraceable author statement. Source: Reactome regulation of nitric-oxide synthase activityTraceable author statement. Source: Reactome small molecule metabolic processTraceable author statement. Source: Reactome |
| Cellular_component | cytosol Traceable author statement. Source: Reactome mitochondrionInferred from electronic annotation. Source: Compara |
| Molecular_function | lysophospholipase activity Traceable author statement PubMed 10064899. Source: ProtInc palmitoyl-(protein) hydrolase activityInferred from mutant phenotype Ref.6. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O75608-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: O75608-2) The sequence of this isoform differs from the canonical sequence as follows: 57-72: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 230 | 230 | Acyl-protein thioesterase 1 | PRO_0000102267 | |||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 119 | 1 | Charge relay system | ||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 174 | 1 | Charge relay system | ||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 208 | 1 | Charge relay system | ||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 57 – 72 | 16 | Missing in isoform 2. | VSP_009196 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 153 | 1 | P → S. Corresponds to variant rs11549448 [ dbSNP | Ensembl ]. | VAR_060991 | |||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 127 – 131 | 5 | YTALT → SLIRG in AAB88180. Ref.5 | ||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 12 – 14 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 21 – 27 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 30 – 32 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 34 – 42 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 49 – 53 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 58 – 60 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 64 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 70 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 86 – 105 | 20 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 110 – 112 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 118 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 120 – 129 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 137 – 143 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 149 – 151 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 160 – 163 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 171 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 175 – 177 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 179 – 192 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 195 – 197 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 198 – 203 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 212 – 225 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Hu G. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A." Devedjiev Y., Dauter Z., Kuznetsov S.R., Jones T.L.Z., Derewenda Z.S. Structure 8:1137-1146(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 6-230, SUBUNIT. Tissue: Testis. |
| [3] | "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. Chen Z.Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Umbilical cord blood. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow and Eye. |
| [5] | Yu W., Sarginson J., Gibbs R.A. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-230 (ISOFORM 1). Tissue: Brain. |
| [6] | "Small-molecule inhibition of APT1 affects Ras localization and signaling." Dekker F.J., Rocks O., Vartak N., Menninger S., Hedberg C., Balamurugan R., Wetzel S., Renner S., Gerauer M., Scholermann B., Rusch M., Kramer J.W., Rauh D., Coates G.W., Brunsveld L., Bastiaens P.I., Waldmann H. Nat. Chem. Biol. 6:449-456(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, FUNCTION. |
| [7] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF081281 mRNA. Translation: AAC31610.1. AF291053 mRNA. Translation: AAG10063.1. AF077198 mRNA. Translation: AAD26993.1. AF077199 mRNA. Translation: AAD26994.1. BC008652 mRNA. Translation: AAH08652.1. BC010397 mRNA. Translation: AAH10397.1. AF035293 mRNA. Translation: AAB88180.1. Different initiation. | ||||||||||||
| IPI | IPI00007321. IPI00398727. | ||||||||||||
| RefSeq | NP_006321.1. NM_006330.2. | ||||||||||||
| UniGene | Hs.435850. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O75608. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | O75608. 2 interactions. | ||||||||||||
| STRING | 9606.ENSP00000320043. | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | S09.026. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | O75608. | ||||||||||||
2D gel databases | |||||||||||||
| OGP | O75608. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | O75608. | ||||||||||||
| PeptideAtlas | O75608. | ||||||||||||
| PRIDE | O75608. | ||||||||||||
Protocols and materials databases | |||||||||||||
| DNASU | 10434. | ||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000316963; ENSP00000320043; ENSG00000120992. ENST00000343231; ENSP00000344477; ENSG00000120992. | ||||||||||||
| GeneID | 10434. | ||||||||||||
| KEGG | hsa:10434. | ||||||||||||
| UCSC | uc003xry.3. human. uc003xrz.3. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 10434. | ||||||||||||
| GeneCards | GC08M055008. | ||||||||||||
| HGNC | HGNC:6737. LYPLA1. | ||||||||||||
| HPA | HPA050941. | ||||||||||||
| MIM | 605599. gene. | ||||||||||||
| neXtProt | NX_O75608. | ||||||||||||
| PharmGKB | PA30499. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0400. | ||||||||||||
| HOGENOM | HOG000260139. | ||||||||||||
| HOVERGEN | HBG052378. | ||||||||||||
| InParanoid | O75608. | ||||||||||||
| KO | K06128. | ||||||||||||
| OMA | GYIMRAW. | ||||||||||||
| OrthoDB | EOG4320ZX. | ||||||||||||
| PhylomeDB | O75608. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Reactome | REACT_111217. Metabolism. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | O75608. | ||||||||||||
| Bgee | O75608. | ||||||||||||
| CleanEx | HS_LYPLA1. | ||||||||||||
| Genevestigator | O75608. | ||||||||||||
| GermOnline | ENSG00000120992. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003140. PLipase/COase/thioEstase. [Graphical view] | ||||||||||||
| Pfam | PF02230. Abhydrolase_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| BindingDB | O75608. | ||||||||||||
| ChEMBL | CHEMBL1681631. | ||||||||||||
| ChiTaRS | LYPLA1. human. | ||||||||||||
| EvolutionaryTrace | O75608. | ||||||||||||
| GenomeRNAi | 10434. | ||||||||||||
| NextBio | 39546. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | LYPA1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O75608 Secondary accession number(s): O43202, Q9UQF9 | ||||||||
| Entry history |
| ||||||||
| Entry status | 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. | ||||||||
Relevant documents
| Human chromosome 8 Human chromosome 8: 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
