UniProtKB - P02763 (A1AG1_HUMAN)
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- BLAST>sp|P02763|A1AG1_HUMAN Alpha-1-acid glycoprotein 1 OS=Homo sapiens OX=9606 GN=ORM1 PE=1 SV=1 MALSWVLTVLSLLPLLEAQIPLCANLVPVPITNATLDQITGKWFYIASAFRNEEYNKSVQ EIQATFFYFTPNKTEDTIFLREYQTRQDQCIYNTTYLNVQRENGTISRYVGGQEHFAHLL ILRDTKTYMLAFDVNDEKNWGLSVYADKPETTKEQLGEFYEALDCLRIPKSDVVYTDWKK DKCEPLEKQHEKERKQEEGES
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Alpha-1-acid glycoprotein 1
ORM1
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>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"Selective binding of imatinib to the genetic variants of human alpha1-acid glycoprotein."
Fitos I., Visy J., Zsila F., Mady G., Simonyi M.
Biochim. Biophys. Acta 1760:1704-1712(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.20"The drug binding site of human alpha1-acid glycoprotein: insight from induced circular dichroism and electronic absorption spectra."
Zsila F., Iwao Y.
Biochim. Biophys. Acta 1770:797-809(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
<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
- acute-phase response 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
- inflammatory response 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
- negative regulation of interleukin-6 production Source: CACAO <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
- negative regulation of tumor necrosis factor production Source: CACAO <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
- neutrophil degranulation Source: Reactome
- platelet degranulation Source: Reactome
- positive regulation of interleukin-1 beta secretion 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
- positive regulation of interleukin-1 secretion 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
- positive regulation of tumor necrosis factor secretion 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
- regulation of immune system process Source: InterPro
<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
| Biological process | Acute phase, Transport |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-114608 Platelet degranulation R-HSA-6798695 Neutrophil degranulation |
<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: Alpha-1-acid glycoprotein 1Short name: AGP 1 Alternative name(s): Orosomucoid-1 Short name: OMD 1 |
| <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:ORM1 Synonyms:AGP1 |
| <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:ENSG00000229314.5 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8498 ORM1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 138600 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P02763 |
<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
Extracellular region or secreted
- blood microparticle Source: UniProtKBInferred from high throughput direct assayi
- collagen-containing extracellular matrix Source: BHF-UCLInferred from high throughput direct assayi
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular region Source: BHF-UCLInferred from high throughput direct assayi
- extracellular space 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
Other locations
- platelet alpha granule lumen Source: Reactome
- specific granule lumen Source: Reactome
- tertiary granule lumen Source: Reactome
<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
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
Organism-specific databases
DisGeNET More...DisGeNETi | 5004 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA260 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4285 |
Drug and drug target database More...DrugBanki | DB05812 Abiraterone DB01418 Acenocoumarol DB01426 Ajmaline DB00802 Alfentanil DB00321 Amitriptyline DB00543 Amoxapine DB01429 Aprindine DB01156 Bupropion DB08907 Canagliflozin DB00482 Celecoxib DB00477 Chlorpromazine DB01151 Desipramine DB00280 Disopyramide DB00590 Doxazosin DB01142 Doxepin DB00530 Erlotinib DB00472 Fluoxetine DB00317 Gefitinib DB00619 Imatinib DB00458 Imipramine DB08820 Ivacaftor DB00934 Maprotiline DB08893 Mirabegron DB00731 Nateglinide DB04821 Nomifensine DB00540 Nortriptyline DB00334 Olanzapine DB00497 Oxycodone DB01359 Penbutolol DB00454 Pethidine DB00946 Phenprocoumon DB08860 Pitavastatin DB00457 Prazosin DB00571 Propranolol DB00908 Quinidine DB08931 Riociguat DB01232 Saquinavir DB00864 Tacrolimus DB00706 Tamsulosin DB05521 Telaprevir DB01041 Thalidomide DB00656 Trazodone DB08867 Ulipristal DB05294 Vandetanib DB08881 Vemurafenib DB08828 Vismodegib DB00682 Warfarin |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ORM1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 112877 |
<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 18 | 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
| 18 | |
| <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_0000017860 | 19 – 201 | Alpha-1-acid glycoprotein 1Add BLAST | 183 |
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 | 19 | Pyrrolidone carboxylic acid1 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":/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 bondi | 23 ↔ 165 | 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
| ||
| <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>Glycosylationi | 33 | N-linked (GlcNAc...) (complex) asparagine8 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 <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>Glycosylationi | 56 | N-linked (GlcNAc...) asparagine4 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 <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>Glycosylationi | 72 | N-linked (GlcNAc...) (complex) asparagine5 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 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 bondi | 90 ↔ 183 | 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
| ||
| <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>Glycosylationi | 93 | N-linked (GlcNAc...) asparagine8 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 <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>GlycosylationiCAR_000170 | 103 | N-linked (GlcNAc...) asparagine4 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 <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
<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.12"Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein."
Treuheit M.J., Costello C.E., Halsall H.B.
Biochem. J. 283:105-112(1992) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. - Ref.13"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-33. - Ref.14"A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation."
Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.
J. Proteome Res. 3:556-566(2004) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.15"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93. - Ref.16"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. - Ref.17"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. - Ref.19"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93. - Ref.21"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93 AND ASN-103. - Ref.22"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-72, STRUCTURE OF CARBOHYDRATES. - Ref.23"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 11:1-17(2012) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
<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
Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acidProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P02763 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P02763 |
PeptideAtlas More...PeptideAtlasi | P02763 |
PRoteomics IDEntifications database More...PRIDEi | P02763 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51584 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P02763 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P02763 |
GlyConnect protein glycosylation platform More...GlyConnecti | 14 718 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P02763 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P02763 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P02763 |
<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
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000229314 |
CleanEx database of gene expression profiles More...CleanExi | HS_ORM1 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P02763 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB006265 HPA046438 HPA047725 HPA057726 |
<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%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| SERPINE1 | P05121 | 4 | EBI-976767,EBI-953978 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111046, 16 interactors |
Protein interaction database and analysis system More...IntActi | P02763, 7 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000259396 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P02763 |
<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 | 24 – 26 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 33 – 39 | 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 | 41 – 52 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 53 – 59 | 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 | 62 – 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 | 11 | |
| <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 | 73 – 76 | 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 – 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 | 10 | |
| <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 | 89 – 100 | 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 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 | 101 – 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 | 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 | 105 – 110 | 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 | 113 – 121 | 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 | 9 | |
| <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 | 127 – 132 | 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 | 137 – 139 | 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 | 141 – 149 | 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 | 9 | |
| <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 | 153 – 156 | 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 | 157 – 166 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 170 – 172 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 178 – 180 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 184 – 192 | 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 | 9 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P02763 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P02763 |
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 | P02763 |
<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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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.24"The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin."
Schonfeld D.L., Ravelli R.B., Mueller U., Skerra A.
J. Mol. Biol. 384:393-405(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-201, DOMAIN, DISULFIDE BONDS.
<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
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IWZI Eukaryota ENOG4111C49 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000125170 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000035 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P02763 |
KEGG Orthology (KO) More...KOi | K17308 |
Database of Orthologous Groups More...OrthoDBi | EOG091G0NAQ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P02763 |
TreeFam database of animal gene trees More...TreeFami | TF343791 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.128.20, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001500 A1A_glycop IPR012674 Calycin IPR000566 Lipocln_cytosolic_FA-bd_dom |
The PANTHER Classification System More...PANTHERi | PTHR11967 PTHR11967, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00061 Lipocalin, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF036899 AGP, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00708 A1AGLPROTEIN |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50814 SSF50814, 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>Sequencei
<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.
10 20 30 40 50
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF
60 70 80 90 100
RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ
110 120 130 140 150
RENGTISRYV GGQEHFAHLL ILRDTKTYML AFDVNDEKNW GLSVYADKPE
160 170 180 190 200
TTKEQLGEFY EALDCLRIPK SDVVYTDWKK DKCEPLEKQH EKERKQEEGE
S
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 170 | K → R in AAI43315 (PubMed:15489334).Curated | 1 | |
| <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 conflicti | 182 | Missing AA sequence (PubMed:4561179).Curated | 1 | |
| <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 conflicti | 193 | Missing AA sequence (PubMed:4561179).Curated | 1 |
<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
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_013840 | 38 | Q → R in allele ORM1*S. 4 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_056166 | 167 | R → C1 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_013841 | 174 | V → M in allele ORM1*F2. 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 |
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 | X02544 mRNA Translation: CAA26397.1 M13692 mRNA Translation: AAA35515.1 X05779 , X05780, X05781, X05782, X05783, X05784 Genomic DNA Translation: CAA29229.1 Sequence problems. X06676 Genomic DNA No translation available. X06680 Genomic DNA No translation available. BT019790 mRNA Translation: AAV38593.1 AK312035 mRNA Translation: BAG34972.1 AL356796 Genomic DNA No translation available. CH471090 Genomic DNA Translation: EAW87416.1 BC104818 mRNA Translation: AAI04819.1 BC104820 mRNA Translation: AAI04821.1 BC143313 mRNA Translation: AAI43314.1 BC143314 mRNA Translation: AAI43315.1 BC026238 mRNA Translation: AAH26238.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6803.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A28346 OMHU1 |
NCBI Reference Sequences More...RefSeqi | NP_000598.2, NM_000607.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.522356 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000259396; ENSP00000259396; ENSG00000229314 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5004 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5004 |
UCSC genome browser More...UCSCi | uc004bik.5 human |
<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
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 |
|---|
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P02763 | Alpha-1-acid glycoprotein | 201 | |||
| UPI00062A6E20 | 202 | ||||
| Alpha-1-acid glycoprotein | 201 | ||||
| Alpha-1-acid glycoprotein | 201 | ||||
| Alpha-1-acid glycoprotein | 201 | ||||
| +8 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P02763 | Alpha-1-acid glycoprotein | 201 | |||
| UPI00062A6E20 | 202 | ||||
| Alpha-1-acid glycoprotein | 201 | ||||
| Alpha-1-acid glycoprotein | 201 | ||||
| Alpha-1-acid glycoprotein | 201 | ||||
| +18 | |||||
<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 | X02544 mRNA Translation: CAA26397.1 M13692 mRNA Translation: AAA35515.1 X05779 , X05780, X05781, X05782, X05783, X05784 Genomic DNA Translation: CAA29229.1 Sequence problems. X06676 Genomic DNA No translation available. X06680 Genomic DNA No translation available. BT019790 mRNA Translation: AAV38593.1 AK312035 mRNA Translation: BAG34972.1 AL356796 Genomic DNA No translation available. CH471090 Genomic DNA Translation: EAW87416.1 BC104818 mRNA Translation: AAI04819.1 BC104820 mRNA Translation: AAI04821.1 BC143313 mRNA Translation: AAI43314.1 BC143314 mRNA Translation: AAI43315.1 BC026238 mRNA Translation: AAH26238.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6803.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A28346 OMHU1 |
NCBI Reference Sequences More...RefSeqi | NP_000598.2, NM_000607.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.522356 |
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 |
| 3KQ0 | X-ray | 1.80 | A | 19-201 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P02763 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P02763 | |||||
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 | 111046, 16 interactors |
Protein interaction database and analysis system More...IntActi | P02763, 7 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000259396 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P02763 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4285 |
Drug and drug target database More...DrugBanki | DB05812 Abiraterone DB01418 Acenocoumarol DB01426 Ajmaline DB00802 Alfentanil DB00321 Amitriptyline DB00543 Amoxapine DB01429 Aprindine DB01156 Bupropion DB08907 Canagliflozin DB00482 Celecoxib DB00477 Chlorpromazine DB01151 Desipramine DB00280 Disopyramide DB00590 Doxazosin DB01142 Doxepin DB00530 Erlotinib DB00472 Fluoxetine DB00317 Gefitinib DB00619 Imatinib DB00458 Imipramine DB08820 Ivacaftor DB00934 Maprotiline DB08893 Mirabegron DB00731 Nateglinide DB04821 Nomifensine DB00540 Nortriptyline DB00334 Olanzapine DB00497 Oxycodone DB01359 Penbutolol DB00454 Pethidine DB00946 Phenprocoumon DB08860 Pitavastatin DB00457 Prazosin DB00571 Propranolol DB00908 Quinidine DB08931 Riociguat DB01232 Saquinavir DB00864 Tacrolimus DB00706 Tamsulosin DB05521 Telaprevir DB01041 Thalidomide DB00656 Trazodone DB08867 Ulipristal DB05294 Vandetanib DB08881 Vemurafenib DB08828 Vismodegib DB00682 Warfarin |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P02763 |
GlyConnect protein glycosylation platform More...GlyConnecti | 14 718 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P02763 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P02763 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P02763 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ORM1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 112877 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P02763 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P02763 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P02763 |
PeptideAtlas More...PeptideAtlasi | P02763 |
PRoteomics IDEntifications database More...PRIDEi | P02763 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51584 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5004 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000259396; ENSP00000259396; ENSG00000229314 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5004 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5004 |
UCSC genome browser More...UCSCi | uc004bik.5 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5004 |
DisGeNET More...DisGeNETi | 5004 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000229314.5 |
GeneCards: human genes, protein and diseases More...GeneCardsi | ORM1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8498 ORM1 |
Human Protein Atlas More...HPAi | CAB006265 HPA046438 HPA047725 HPA057726 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 138600 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P02763 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA260 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IWZI Eukaryota ENOG4111C49 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000125170 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000035 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P02763 |
KEGG Orthology (KO) More...KOi | K17308 |
Database of Orthologous Groups More...OrthoDBi | EOG091G0NAQ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P02763 |
TreeFam database of animal gene trees More...TreeFami | TF343791 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-114608 Platelet degranulation R-HSA-6798695 Neutrophil degranulation |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | ORM1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P02763 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | ORM1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5004 |
Protein Ontology More...PROi | PR:P02763 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000229314 |
CleanEx database of gene expression profiles More...CleanExi | HS_ORM1 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P02763 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.128.20, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001500 A1A_glycop IPR012674 Calycin IPR000566 Lipocln_cytosolic_FA-bd_dom |
The PANTHER Classification System More...PANTHERi | PTHR11967 PTHR11967, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00061 Lipocalin, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF036899 AGP, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00708 A1AGLPROTEIN |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50814 SSF50814, 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 | A1AG1_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 | P02763Primary (citable) accession number: P02763 Secondary accession number(s): B7ZKQ5 , Q5T539, Q5U067, Q8TC16 | |
| <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: | July 21, 1986 |
| Last sequence update: | January 1, 1988 | |
| Last modified: | July 18, 2018 | |
| This is version 198 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 9
Human chromosome 9: 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
