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Protein

Apolipoprotein(a)

Gene

LPA

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

Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330.1 Publication

Miscellaneous

Apo(a) is known to be proteolytically cleaved, leading to the formation of the so-called mini-Lp(a). Apo(a) fragments accumulate in atherosclerotic lesions, where they may promote thrombogenesis. O-glycosylation may limit the extent of proteolytic fragmentation. Homology with plasminogen kringles IV and V is thought to underlie the atherogenicity of the protein, because the fragments are competing with plasminogen for fibrin(ogen) binding.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei4369Charge relay system1
Active sitei4412Charge relay system1
Active sitei4498Charge relay system1

<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

  • apolipoprotein binding Source: BHF-UCL
  • endopeptidase inhibitor activity Source: ProtInc
  • fibronectin binding Source: BHF-UCL
  • heparin binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL

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, Protease, Serine protease
Biological processLipid transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8964041 LDL remodeling

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.999

<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:
Apolipoprotein(a) (EC:3.4.21.-)
Short name:
Apo(a)
Short name:
Lp(a)
<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:LPA
<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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000198670.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:6667 LPA

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
152200 gene+phenotype

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P08519

<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

<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

Keywords - Diseasei

Atherosclerosis

Organism-specific databases

DisGeNET

More...
DisGeNETi
4018
MIMi152200 gene+phenotype

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30432

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00513 Aminocaproic Acid

Polymorphism and mutation databases

Domain mapping of disease mutations (DMDM)

More...
DMDMi
114062

<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 – 19Add BLAST19
<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_000002809720 – 4548Apolipoprotein(a)Add BLAST4529

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 bondi28 ↔ 105By similarity
Disulfide bondi49 ↔ 88By similarity
<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>Glycosylationi61N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi77 ↔ 100By similarity
Glycosylationi101N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi142 ↔ 219By similarity
Disulfide bondi163 ↔ 202By similarity
Disulfide bondi191 ↔ 214By similarity
Glycosylationi215N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi256 ↔ 333By similarity
Disulfide bondi277 ↔ 316By similarity
Disulfide bondi305 ↔ 328By similarity
Glycosylationi329N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi370 ↔ 447By similarity
Disulfide bondi391 ↔ 430By similarity
Disulfide bondi419 ↔ 442By similarity
Glycosylationi443N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi484 ↔ 561By similarity
Disulfide bondi505 ↔ 544By similarity
Disulfide bondi533 ↔ 556By similarity
Glycosylationi557N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi598 ↔ 675By similarity
Disulfide bondi619 ↔ 658By similarity
Disulfide bondi647 ↔ 670By similarity
Glycosylationi671N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi712 ↔ 789By similarity
Disulfide bondi733 ↔ 772By similarity
Disulfide bondi761 ↔ 784By similarity
Glycosylationi785N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi826 ↔ 903By similarity
Disulfide bondi847 ↔ 886By similarity
Disulfide bondi875 ↔ 898By similarity
Glycosylationi899N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi940 ↔ 1017By similarity
Disulfide bondi961 ↔ 1000By similarity
Disulfide bondi989 ↔ 1012By similarity
Glycosylationi1013N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1054 ↔ 1131By similarity
Disulfide bondi1075 ↔ 1114By similarity
Disulfide bondi1103 ↔ 1126By similarity
Glycosylationi1127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1168 ↔ 1245By similarity
Disulfide bondi1189 ↔ 1228By similarity
Disulfide bondi1217 ↔ 1240By similarity
Glycosylationi1241N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1282 ↔ 1359By similarity
Disulfide bondi1303 ↔ 1342By similarity
Disulfide bondi1331 ↔ 1354By similarity
Glycosylationi1355N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1396 ↔ 1473By similarity
Disulfide bondi1417 ↔ 1456By similarity
Disulfide bondi1445 ↔ 1468By similarity
Glycosylationi1469N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1510 ↔ 1587By similarity
Disulfide bondi1531 ↔ 1570By similarity
Disulfide bondi1559 ↔ 1582By similarity
Glycosylationi1583N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1624 ↔ 1701By similarity
Disulfide bondi1645 ↔ 1684By similarity
Disulfide bondi1673 ↔ 1696By similarity
Glycosylationi1697N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1738 ↔ 1815By similarity
Disulfide bondi1759 ↔ 1798By similarity
Disulfide bondi1787 ↔ 1810By similarity
Glycosylationi1811N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1852 ↔ 1929By similarity
Disulfide bondi1873 ↔ 1912By similarity
Disulfide bondi1901 ↔ 1924By similarity
Glycosylationi1925N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1966 ↔ 2043By similarity
Disulfide bondi1987 ↔ 2026By similarity
Disulfide bondi2015 ↔ 2038By similarity
Glycosylationi2039N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2080 ↔ 2157By similarity
Disulfide bondi2101 ↔ 2140By similarity
Disulfide bondi2129 ↔ 2152By similarity
Glycosylationi2153N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2194 ↔ 2271By similarity
Disulfide bondi2215 ↔ 2254By similarity
Disulfide bondi2243 ↔ 2266By similarity
Glycosylationi2267N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2308 ↔ 2385By similarity
Disulfide bondi2329 ↔ 2368By similarity
Disulfide bondi2357 ↔ 2380By similarity
Glycosylationi2381N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2422 ↔ 2499By similarity
Disulfide bondi2443 ↔ 2482By similarity
Disulfide bondi2471 ↔ 2494By similarity
Glycosylationi2495N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2536 ↔ 2613By similarity
Disulfide bondi2557 ↔ 2596By similarity
Disulfide bondi2585 ↔ 2608By similarity
Glycosylationi2609N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2650 ↔ 2727By similarity
Disulfide bondi2671 ↔ 2710By similarity
Disulfide bondi2699 ↔ 2722By similarity
Glycosylationi2723N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2764 ↔ 2841By similarity
Disulfide bondi2785 ↔ 2824By similarity
Disulfide bondi2813 ↔ 2836By similarity
Glycosylationi2837N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2878 ↔ 2955By similarity
Disulfide bondi2899 ↔ 2938By similarity
Disulfide bondi2927 ↔ 2950By similarity
Glycosylationi2951N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2992 ↔ 3069By similarity
Disulfide bondi3013 ↔ 3052By similarity
Disulfide bondi3041 ↔ 3064By similarity
Glycosylationi3065N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3106 ↔ 3183By similarity
Disulfide bondi3127 ↔ 3166By similarity
Disulfide bondi3155 ↔ 3178By similarity
Glycosylationi3179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3220 ↔ 3297By similarity
Disulfide bondi3241 ↔ 3280By similarity
Disulfide bondi3269 ↔ 3292By similarity
Glycosylationi3293N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3334 ↔ 3411By similarity
Disulfide bondi3355 ↔ 3394By similarity
Disulfide bondi3383 ↔ 3406By similarity
Glycosylationi3407N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3448 ↔ 3525By similarity
Disulfide bondi3469 ↔ 3508By similarity
Disulfide bondi3497 ↔ 3520By similarity
Glycosylationi3521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3562 ↔ 3639By similarity
Disulfide bondi3583 ↔ 3622By similarity
Disulfide bondi3611 ↔ 3634By similarity
Glycosylationi3635N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3676 ↔ 3753
Disulfide bondi3697 ↔ 3736
Disulfide bondi3725 ↔ 3748
Glycosylationi3749N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3782 ↔ 3859
Disulfide bondi3803 ↔ 3842
Disulfide bondi3831 ↔ 3854
Glycosylationi3855N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3889N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3896 ↔ 3973By similarity
Disulfide bondi3917 ↔ 3956By similarity
Disulfide bondi3945 ↔ 3968By similarity
Glycosylationi3969N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4010 ↔ 4087By similarity
Disulfide bondi4031 ↔ 4070By similarity
Disulfide bondi4059 ↔ 4082By similarity
Glycosylationi4083N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4124 ↔ 4201By similarity
Disulfide bondi4145 ↔ 4184By similarity
Disulfide bondi4173 ↔ 4196By similarity
Glycosylationi4197N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4228 ↔ 4307By similarity
Disulfide bondi4249 ↔ 4290By similarity
Disulfide bondi4278 ↔ 4302By similarity
Disulfide bondi4354 ↔ 4370By similarity
Disulfide bondi4446 ↔ 4504By similarity
Disulfide bondi4476 ↔ 4483By similarity
Disulfide bondi4494 ↔ 4522By similarity

<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

N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O-glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Proteomic databases

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

More...
PaxDbi
P08519

PeptideAtlas

More...
PeptideAtlasi
P08519

PRoteomics IDEntifications database

More...
PRIDEi
P08519

ProteomicsDB human proteome resource

More...
ProteomicsDBi
52116

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
56

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P08519

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

More...
PhosphoSitePlusi
P08519

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P08519

<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
ENSG00000198670 Expressed in 59 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_LPA

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P08519 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P08519 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB016072
HPA060604

<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

Disulfide-linked to apo-B100. Binds to fibronectin and decorin.

<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

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P08519, 2 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000321334

<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

14548
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
P08519

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

More...
SMRi
P08519

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
P08519

<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>Domaini20 – 130Kringle 1PROSITE-ProRule annotationAdd BLAST111
Domaini131 – 244Kringle 2PROSITE-ProRule annotationAdd BLAST114
Domaini245 – 358Kringle 3PROSITE-ProRule annotationAdd BLAST114
Domaini359 – 472Kringle 4PROSITE-ProRule annotationAdd BLAST114
Domaini473 – 586Kringle 5PROSITE-ProRule annotationAdd BLAST114
Domaini587 – 700Kringle 6PROSITE-ProRule annotationAdd BLAST114
Domaini701 – 814Kringle 7PROSITE-ProRule annotationAdd BLAST114
Domaini815 – 928Kringle 8PROSITE-ProRule annotationAdd BLAST114
Domaini929 – 1042Kringle 9PROSITE-ProRule annotationAdd BLAST114
Domaini1043 – 1156Kringle 10PROSITE-ProRule annotationAdd BLAST114
Domaini1157 – 1270Kringle 11PROSITE-ProRule annotationAdd BLAST114
Domaini1271 – 1384Kringle 12PROSITE-ProRule annotationAdd BLAST114
Domaini1385 – 1498Kringle 13PROSITE-ProRule annotationAdd BLAST114
Domaini1499 – 1612Kringle 14PROSITE-ProRule annotationAdd BLAST114
Domaini1613 – 1726Kringle 15PROSITE-ProRule annotationAdd BLAST114
Domaini1727 – 1840Kringle 16PROSITE-ProRule annotationAdd BLAST114
Domaini1841 – 1954Kringle 17PROSITE-ProRule annotationAdd BLAST114
Domaini1955 – 2068Kringle 18PROSITE-ProRule annotationAdd BLAST114
Domaini2069 – 2182Kringle 19PROSITE-ProRule annotationAdd BLAST114
Domaini2183 – 2296Kringle 20PROSITE-ProRule annotationAdd BLAST114
Domaini2297 – 2410Kringle 21PROSITE-ProRule annotationAdd BLAST114
Domaini2411 – 2524Kringle 22PROSITE-ProRule annotationAdd BLAST114
Domaini2525 – 2638Kringle 23PROSITE-ProRule annotationAdd BLAST114
Domaini2639 – 2752Kringle 24PROSITE-ProRule annotationAdd BLAST114
Domaini2753 – 2866Kringle 25PROSITE-ProRule annotationAdd BLAST114
Domaini2867 – 2980Kringle 26PROSITE-ProRule annotationAdd BLAST114
Domaini2981 – 3094Kringle 27PROSITE-ProRule annotationAdd BLAST114
Domaini3095 – 3208Kringle 28PROSITE-ProRule annotationAdd BLAST114
Domaini3209 – 3322Kringle 29PROSITE-ProRule annotationAdd BLAST114
Domaini3323 – 3436Kringle 30PROSITE-ProRule annotationAdd BLAST114
Domaini3437 – 3550Kringle 31PROSITE-ProRule annotationAdd BLAST114
Domaini3551 – 3664Kringle 32PROSITE-ProRule annotationAdd BLAST114
Domaini3665 – 3770Kringle 33PROSITE-ProRule annotationAdd BLAST106
Domaini3771 – 3884Kringle 34PROSITE-ProRule annotationAdd BLAST114
Domaini3885 – 3998Kringle 35PROSITE-ProRule annotationAdd BLAST114
Domaini3999 – 4112Kringle 36PROSITE-ProRule annotationAdd BLAST114
Domaini4113 – 4226Kringle 37PROSITE-ProRule annotationAdd BLAST114
Domaini4227 – 4327Kringle 38PROSITE-ProRule annotationAdd BLAST101
Domaini4328 – 4546Peptidase S1PROSITE-ProRule annotationAdd BLAST219

<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

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IDXR Eukaryota
COG5640 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000170962

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004270

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0AH5

TreeFam database of animal gene trees

More...
TreeFami
TF329901

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00108 KR, 38 hits
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.20.10, 38 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00051 Kringle, 38 hits
PF00089 Trypsin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00722 CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00130 KR, 38 hits
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 38 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00021 KRINGLE_1, 38 hits
PS50070 KRINGLE_2, 38 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P08519-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEHKEVVLLL LLFLKSAAPE QSHVVQDCYH GDGQSYRGTY STTVTGRTCQ
60 70 80 90 100
AWSSMTPHQH NRTTENYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC
110 120 130 140 150
NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
160 170 180 190 200
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP
210 220 230 240 250
YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR
260 270 280 290 300
PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
310 320 330 340 350
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP
360 370 380 390 400
SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH
410 420 430 440 450
SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
460 470 480 490 500
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV
510 520 530 540 550
TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG
560 570 580 590 600
VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH
610 620 630 640 650
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP
660 670 680 690 700
DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ
710 720 730 740 750
APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY
760 770 780 790 800
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP
810 820 830 840 850
TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW
860 870 880 890 900
SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL
910 920 930 940 950
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG
960 970 980 990 1000
TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC
1010 1020 1030 1040 1050
YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG
1060 1070 1080 1090 1100
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM
1110 1120 1130 1140 1150
NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL
1160 1170 1180 1190 1200
EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH
1210 1220 1230 1240 1250
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG
1260 1270 1280 1290 1300
TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG
1310 1320 1330 1340 1350
RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR
1360 1370 1380 1390 1400
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN
1410 1420 1430 1440 1450
GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA
1460 1470 1480 1490 1500
VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP
1510 1520 1530 1540 1550
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP
1560 1570 1580 1590 1600
NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV
1610 1620 1630 1640 1650
TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS
1660 1670 1680 1690 1700
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ
1710 1720 1730 1740 1750
CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY
1760 1770 1780 1790 1800
STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT
1810 1820 1830 1840 1850
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ
1860 1870 1880 1890 1900
ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY
1910 1920 1930 1940 1950
CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA
1960 1970 1980 1990 2000
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR
2010 2020 2030 2040 2050
TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA
2060 2070 2080 2090 2100
VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT
2110 2120 2130 2140 2150
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE
2160 2170 2180 2190 2200
YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ
2210 2220 2230 2240 2250
SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA
2260 2270 2280 2290 2300
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE
2310 2320 2330 2340 2350
QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA
2360 2370 2380 2390 2400
GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP
2410 2420 2430 2440 2450
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT
2460 2470 2480 2490 2500
PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS
2510 2520 2530 2540 2550
DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST
2560 2570 2580 2590 2600
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD
2610 2620 2630 2640 2650
PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC
2660 2670 2680 2690 2700
YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR
2710 2720 2730 2740 2750
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS
2760 2770 2780 2790 2800
EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP
2810 2820 2830 2840 2850
EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA
2860 2870 2880 2890 2900
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ
2910 2920 2930 2940 2950
AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC
2960 2970 2980 2990 3000
NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
3010 3020 3030 3040 3050
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP
3060 3070 3080 3090 3100
YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR
3110 3120 3130 3140 3150
PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
3160 3170 3180 3190 3200
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP
3210 3220 3230 3240 3250
SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH
3260 3270 3280 3290 3300
SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
3310 3320 3330 3340 3350
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV
3360 3370 3380 3390 3400
TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDPVA APYCYTRDPS
3410 3420 3430 3440 3450
VRWEYCNLTQ CSDAEGTAVA PPTITPIPSL EAPSEQAPTE QRPGVQECYH
3460 3470 3480 3490 3500
GNGQSYQGTY FITVTGRTCQ AWSSMTPHSH SRTPAYYPNA GLIKNYCRNP
3510 3520 3530 3540 3550
DPVAAPWCYT TDPSVRWEYC NLTRCSDAEW TAFVPPNVIL APSLEAFFEQ
3560 3570 3580 3590 3600
ALTEETPGVQ DCYYHYGQSY RGTYSTTVTG RTCQAWSSMT PHQHSRTPEN
3610 3620 3630 3640 3650
YPNAGLTRNY CRNPDAEIRP WCYTMDPSVR WEYCNLTQCL VTESSVLATL
3660 3670 3680 3690 3700
TVVPDPSTEA SSEEAPTEQS PGVQDCYHGD GQSYRGSFST TVTGRTCQSW
3710 3720 3730 3740 3750
SSMTPHWHQR TTEYYPNGGL TRNYCRNPDA EISPWCYTMD PNVRWEYCNL
3760 3770 3780 3790 3800
TQCPVTESSV LATSTAVSEQ APTEQSPTVQ DCYHGDGQSY RGSFSTTVTG
3810 3820 3830 3840 3850
RTCQSWSSMT PHWHQRTTEY YPNGGLTRNY CRNPDAEIRP WCYTMDPSVR
3860 3870 3880 3890 3900
WEYCNLTQCP VMESTLLTTP TVVPVPSTEL PSEEAPTENS TGVQDCYRGD
3910 3920 3930 3940 3950
GQSYRGTLST TITGRTCQSW SSMTPHWHRR IPLYYPNAGL TRNYCRNPDA
3960 3970 3980 3990 4000
EIRPWCYTMD PSVRWEYCNL TRCPVTESSV LTTPTVAPVP STEAPSEQAP
4010 4020 4030 4040 4050
PEKSPVVQDC YHGDGRSYRG ISSTTVTGRT CQSWSSMIPH WHQRTPENYP
4060 4070 4080 4090 4100
NAGLTENYCR NPDSGKQPWC YTTDPCVRWE YCNLTQCSET ESGVLETPTV
4110 4120 4130 4140 4150
VPVPSMEAHS EAAPTEQTPV VRQCYHGNGQ SYRGTFSTTV TGRTCQSWSS
4160 4170 4180 4190 4200
MTPHRHQRTP ENYPNDGLTM NYCRNPDADT GPWCFTMDPS IRWEYCNLTR
4210 4220 4230 4240 4250
CSDTEGTVVA PPTVIQVPSL GPPSEQDCMF GNGKGYRGKK ATTVTGTPCQ
4260 4270 4280 4290 4300
EWAAQEPHRH STFIPGTNKW AGLEKNYCRN PDGDINGPWC YTMNPRKLFD
4310 4320 4330 4340 4350
YCDIPLCASS SFDCGKPQVE PKKCPGSIVG GCVAHPHSWP WQVSLRTRFG
4360 4370 4380 4390 4400
KHFCGGTLIS PEWVLTAAHC LKKSSRPSSY KVILGAHQEV NLESHVQEIE
4410 4420 4430 4440 4450
VSRLFLEPTQ ADIALLKLSR PAVITDKVMP ACLPSPDYMV TARTECYITG
4460 4470 4480 4490 4500
WGETQGTFGT GLLKEAQLLV IENEVCNHYK YICAEHLARG TDSCQGDSGG
4510 4520 4530 4540
PLVCFEKDKY ILQGVTSWGL GCARPNKPGV YARVSRFVTW IEGMMRNN
Length:4,548
Mass (Da):501,319
Last modified:August 1, 1988 - 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:i96921BE96A465C5F
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WWY0A0A087WWY0_HUMAN
Apolipoprotein(a)
LPA
571Annotation 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>

<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

The reference genome sequence encodes a variant that contains 16 Kringle domains and that lack residues 533 to 3040. Depending on the individual, the encoded protein contains 2-43 copies of kringle-type domains. The allele represented here contains 38 copies of the kringle-type repeats.1 Publication

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_0472933498R → Q. Corresponds to variant dbSNP:rs41259144Ensembl.1
Natural variantiVAR_0472943866L → V. Corresponds to variant dbSNP:rs7765803Ensembl.1
Natural variantiVAR_0472953880L → V. Corresponds to variant dbSNP:rs7765781Ensembl.1
Natural variantiVAR_0472963907T → P. Corresponds to variant dbSNP:rs41272110Ensembl.1
Natural variantiVAR_0472973929R → Q. Corresponds to variant dbSNP:rs41272112Ensembl.1
Natural variantiVAR_0472984106M → T. Corresponds to variant dbSNP:rs41264308Ensembl.1
Natural variantiVAR_0472994187M → T. Corresponds to variant dbSNP:rs1801693Ensembl.1
Natural variantiVAR_0066334193W → R Loss of lysine-sepharose binding. 1 Publication1
Natural variantiVAR_0473004330G → A. Corresponds to variant dbSNP:rs41265936Ensembl.1
Natural variantiVAR_0473014399I → M. Corresponds to variant dbSNP:rs3798220Ensembl.1
Natural variantiVAR_0473024524R → C. Corresponds to variant dbSNP:rs3124784Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X06290 mRNA Translation: CAA29618.1
AL109933 Genomic DNA No translation available.
AL596089 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
S00657

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.520120

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000316300; ENSP00000321334; ENSG00000198670
ENST00000447678; ENSP00000395608; ENSG00000198670

UCSC genome browser

More...
UCSCi
uc063sqy.1 human

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

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06290 mRNA Translation: CAA29618.1
AL109933 Genomic DNA No translation available.
AL596089 Genomic DNA No translation available.
PIRiS00657
UniGeneiHs.520120

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I71X-ray1.45A3781-3863[»]
1JFNNMR-A3665-3770[»]
1KIVX-ray2.10A4124-4201[»]
2FEBNMR-A3885-3980[»]
3KIVX-ray1.80A4123-4201[»]
4BV5X-ray2.10A/B4123-4201[»]
4BV7X-ray1.70A4123-4201[»]
4BVCX-ray1.60A4123-4201[»]
4BVDX-ray1.68A4123-4201[»]
4BVVX-ray1.80A4227-4307[»]
4BVWX-ray2.00A/B3781-3859[»]
4KIVX-ray2.20A4123-4201[»]
ProteinModelPortaliP08519
SMRiP08519
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08519, 2 interactors
STRINGi9606.ENSP00000321334

Chemistry databases

DrugBankiDB00513 Aminocaproic Acid

Protein family/group databases

MEROPSiS01.999

PTM databases

GlyConnecti56
iPTMnetiP08519
PhosphoSitePlusiP08519
UniCarbKBiP08519

Polymorphism and mutation databases

DMDMi114062

Proteomic databases

PaxDbiP08519
PeptideAtlasiP08519
PRIDEiP08519
ProteomicsDBi52116

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316300; ENSP00000321334; ENSG00000198670
ENST00000447678; ENSP00000395608; ENSG00000198670
UCSCiuc063sqy.1 human

Organism-specific databases

DisGeNETi4018
EuPathDBiHostDB:ENSG00000198670.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
LPA

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0057735
HGNCiHGNC:6667 LPA
HPAiCAB016072
HPA060604
MIMi152200 gene+phenotype
neXtProtiNX_P08519
PharmGKBiPA30432

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IDXR Eukaryota
COG5640 LUCA
HOGENOMiHOG000170962
HOVERGENiHBG004270
OrthoDBiEOG091G0AH5
TreeFamiTF329901

Enzyme and pathway databases

ReactomeiR-HSA-8964041 LDL remodeling

Miscellaneous databases

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

More...
ChiTaRSi
LPA human
EvolutionaryTraceiP08519

Protein Ontology

More...
PROi
PR:P08519

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000198670 Expressed in 59 organ(s), highest expression level in liver
CleanExiHS_LPA
ExpressionAtlasiP08519 baseline and differential
GenevisibleiP08519 HS

Family and domain databases

CDDicd00108 KR, 38 hits
cd00190 Tryp_SPc, 1 hit
Gene3Di2.40.20.10, 38 hits
InterProiView protein in InterPro
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00051 Kringle, 38 hits
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00130 KR, 38 hits
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 38 hits
PROSITEiView protein in PROSITE
PS00021 KRINGLE_1, 38 hits
PS50070 KRINGLE_2, 38 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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 nameiAPOA_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: P08519
Secondary accession number(s): Q5VTD7, Q9UD88
<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, 1988
Last sequence update: August 1, 1988
Last modified: September 12, 2018
This is version 174 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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