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Entry version 176 (10 Apr 2019)
Sequence version 3 (02 Mar 2010)
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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

ENPP2

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

Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:15769751, PubMed:26371182, PubMed:27754931). Major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:27754931). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:15769751, PubMed:12176993). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation (PubMed:11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein (PubMed:1733949). May have a role in induction of parturition (PubMed:12176993). Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor (PubMed:1733949, PubMed:11559573).1 Publication7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

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

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (Probable).3 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.5 mM for 16:0-LPC (at pH 8.5)2 Publications
  2. KM=5.5 mM for pNP-TMP (at pH 8.5)2 Publications
  3. KM=11.3 mM for pNppp (isoform 1)2 Publications
  4. KM=5.7 mM for pNppp (isoform 2)2 Publications
  5. KM=19.8 mM for pNppp (isoform 3)2 Publications
  1. Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)2 Publications
  2. Vmax=0.67 nmol/min/µg enzyme with pNppp as substrate (isoform 2)2 Publications
  3. Vmax=1.6 nmol/min/µg enzyme with pNppp as substrate (isoform 3)2 Publications

pH dependencei

Optimum pH is 9.0 (isoform 1), 8.0 (isoform 3). Isoform 1 is less sensitive to pH. Isoform 1, isoform 2 and isoform 3 all retain some activity at pH 9.5.2 Publications

Temperature dependencei

Isoform 1 and isoform 3 are active from 45 to 60 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi172Zinc 1; catalyticCombined sources2 Publications1
<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 sitei210NucleophileBy similarity1
Metal bindingi210Zinc 1; catalyticCombined sources2 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei231SubstrateCombined sources1 Publication1
Binding sitei307SubstrateBy similarity1
Metal bindingi312Zinc 2; catalyticCombined sources1 Publication1
Metal bindingi316Zinc 2; via tele nitrogen; catalyticCombined sources1 Publication1
Metal bindingi359Zinc 1; catalyticCombined sources2 Publications1
Metal bindingi360Zinc 1; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi475Zinc 2; via tele nitrogen; catalyticCombined sources1 Publication1
Metal bindingi740CalciumCombined sources2 Publications1
Metal bindingi742CalciumCombined sources2 Publications1
Metal bindingi744CalciumCombined sources1 Publication1
Metal bindingi746Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi748CalciumCombined sources2 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei853Essential for catalytic activityBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processChemotaxis, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS06258-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.4.39 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-199220 Vitamin B5 (pantothenate) metabolism

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q13822

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000393
SLP:000000641 [Q13822-1]

<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:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (EC:3.1.4.395 Publications)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin2 Publications
Extracellular lysophospholipase D
Short name:
LysoPLD1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ENPP2
Synonyms:ATX2 Publications, PDNP21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000136960.12

Human Gene Nomenclature Database

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HGNCi
HGNC:3357 ENPP2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601060 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q13822

<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 & Seán O’Donoghue; Source: COMPARTMENTS

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi170S → E: Reduces lysophospholipase activity by about 70%. 1
Mutagenesisi210T → A: Loss of lysophospholipase activity. 1 Publication1
Mutagenesisi211F → Y: Reduces lysophospholipase activity by about 70%. 1 Publication1
Mutagenesisi218A → V: Reduces lysophospholipase activity by about 50%. 1 Publication1
Mutagenesisi231N → A: Strongly reduced lysophospholipase activity. 1 Publication1
Mutagenesisi307Y → Q: Reduces lysophospholipase activity by about 70%. 1 Publication1

Keywords - Diseasei

Obesity

Organism-specific databases

DisGeNET

More...
DisGeNETi
5168

Open Targets

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OpenTargetsi
ENSG00000136960

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27792

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3691

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2901

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ENPP2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
290457674

<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 – 27By similarityAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000028164928 – 35Removed by furin2 Publications8
<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_000018856736 – 863Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST828

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi54N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi59 ↔ 76PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi63 ↔ 94PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi74 ↔ 87PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi80 ↔ 86PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi103 ↔ 120PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi108 ↔ 138PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi118 ↔ 131PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi124 ↔ 130PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi149 ↔ 195PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi157 ↔ 351PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi367 ↔ 469PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi411N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi414 ↔ 806PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi525N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi567 ↔ 667PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi569 ↔ 652PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi775 ↔ 785PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi807N-linked (GlcNAc...) asparagineSequence analysis1

<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-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13822

PeptideAtlas

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PeptideAtlasi
Q13822

PRoteomics IDEntifications database

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PRIDEi
Q13822

ProteomicsDB human proteome resource

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ProteomicsDBi
59692
59693 [Q13822-2]
59694 [Q13822-3]

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1197

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13822

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

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PhosphoSitePlusi
Q13822

<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

Detected in blood plasma (at protein level) (PubMed:12176993, PubMed:26371182). Predominantly expressed in brain, placenta, ovary, and small intestine. Expressed in a number of carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma and non-small-cell lung cancer. Expressed in body fluids such as plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic fluids. Not detected in leukocytes. Isoform 1 is more highly expressed in peripheral tissues than in the central nervous system (CNS). Adipocytes only express isoform 1. Isoform 3 is more highly expressed in the brain than in peripheral tissues.5 Publications

<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

Up-regulated in massively obese subjects with glucose intolerance, and during adipogenesis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000136960 Expressed in 235 organ(s), highest expression level in pigmented layer of retina

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q13822 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q13822 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA023700
HPA053652

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111194, 3 interactors

Protein interaction database and analysis system

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IntActi
Q13822, 3 interactors

Molecular INTeraction database

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MINTi
Q13822

STRING: functional protein association networks

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STRINGi
9606.ENSP00000259486

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q13822

<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

1863
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZG6X-ray1.80A/B17-863[»]
4ZG7X-ray1.75A55-860[»]
4ZG9X-ray2.95A/B1-863[»]
4ZGAX-ray2.60A1-863[»]
5KXAX-ray2.59A1-863[»]
5M7MX-ray2.70A1-863[»]
5MHPX-ray2.43A1-863[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13822

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

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SMRi
Q13822

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini55 – 98SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini99 – 143SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni211 – 214Substrate bindingBy similarity4
Regioni244 – 255Substrate bindingBy similarityAdd BLAST12
Regioni830 – 851Required for secretionBy similarityAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi127 – 129Cell attachment siteSequence analysis3

<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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155778

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051484

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13822

KEGG Orthology (KO)

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KOi
K01122

Identification of Orthologs from Complete Genome Data

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OMAi
DGLHDTQ

Database of Orthologous Groups

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OrthoDBi
999163at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13822

TreeFam database of animal gene trees

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TreeFami
TF330032

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.720.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR001604 DNA/RNA_non-sp_Endonuclease
IPR029881 ENPP2
IPR020821 Extracellular_endonuc_su_A
IPR002591 Phosphodiest/P_Trfase
IPR036024 Somatomedin_B-like_dom_sf
IPR020436 Somatomedin_B_chordata
IPR001212 Somatomedin_B_dom

The PANTHER Classification System

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PANTHERi
PTHR10151:SF21 PTHR10151:SF21, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01223 Endonuclease_NS, 1 hit
PF01663 Phosphodiest, 1 hit
PF01033 Somatomedin_B, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00022 SOMATOMEDINB

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00892 Endonuclease_NS, 1 hit
SM00477 NUC, 1 hit
SM00201 SO, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53649 SSF53649, 1 hit
SSF90188 SSF90188, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00524 SMB_1, 2 hits
PS50958 SMB_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13822-1) [UniParc]FASTAAdd to basket
Also known as: ATXter, Beta

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

« Hide
        10         20         30         40         50
MARRSSFQSC QIISLFTFAV GVNICLGFTA HRIKRAEGWE EGPPTVLSDS
60 70 80 90 100
PWTNISGSCK GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG
110 120 130 140 150
WECTKDRCGE VRNEENACHC SEDCLARGDC CTNYQVVCKG ESHWVDDDCE
160 170 180 190 200
EIKAAECPAG FVRPPLIIFS VDGFRASYMK KGSKVMPNIE KLRSCGTHSP
210 220 230 240 250
YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA TFHLRGREKF
260 270 280 290 300
NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDHER
310 320 330 340 350
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR EIDKIVGQLM DGLKQLKLHR
360 370 380 390 400
CVNVIFVGDH GMEDVTCDRT EFLSNYLTNV DDITLVPGTL GRIRSKFSNN
410 420 430 440 450
AKYDPKAIIA NLTCKKPDQH FKPYLKQHLP KRLHYANNRR IEDIHLLVER
460 470 480 490 500
RWHVARKPLD VYKKPSGKCF FQGDHGFDNK VNSMQTVFVG YGSTFKYKTK
510 520 530 540 550
VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF RPTMPEEVTR
560 570 580 590 600
PNYPGIMYLQ SDFDLGCTCD DKVEPKNKLD ELNKRLHTKG STEERHLLYG
610 620 630 640 650
RPAVLYRTRY DILYHTDFES GYSEIFLMPL WTSYTVSKQA EVSSVPDHLT
660 670 680 690 700
SCVRPDVRVS PSFSQNCLAY KNDKQMSYGF LFPPYLSSSP EAKYDAFLVT
710 720 730 740 750
NMVPMYPAFK RVWNYFQRVL VKKYASERNG VNVISGPIFD YDYDGLHDTE
760 770 780 790 800
DKIKQYVEGS SIPVPTHYYS IITSCLDFTQ PADKCDGPLS VSSFILPHRP
810 820 830 840 850
DNEESCNSSE DESKWVEELM KMHTARVRDI EHLTSLDFFR KTSRSYPEIL
860
TLKTYLHTYE SEI
Length:863
Mass (Da):98,994
Last modified:March 2, 2010 - v3
<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:i94A7A2B3701F0993
GO
Isoform 2 (identifier: Q13822-2) [UniParc]FASTAAdd to basket
Also known as: ATXmel, Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     324-324: E → EESSYGSPFTPAKRPKRKVAPKRRQERPVAPPKKRRRKIHRMDHYAAETRQDK

Show »
Length:915
Mass (Da):105,201
Checksum:i30C7CB1E60101B75
GO
Isoform 3 (identifier: Q13822-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     593-593: E → EAETRKFRGSRNENKENINGNFEPRK

Show »
Length:888
Mass (Da):101,968
Checksum:i17A8986783028C4D
GO

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

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RIB9E5RIB9_HUMAN
Ectonucleotide pyrophosphatase/phos...
ENPP2
162Annotation score:

Annotation score:2 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>
E5RJ49E5RJ49_HUMAN
Ectonucleotide pyrophosphatase/phos...
ENPP2
245Annotation score:

Annotation score:2 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>
E7EUF1E7EUF1_HUMAN
Ectonucleotide pyrophosphatase/phos...
ENPP2
884Annotation score:

Annotation score:2 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>
E5RIA2E5RIA2_HUMAN
Ectonucleotide pyrophosphatase/phos...
ENPP2
498Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti23N → S in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti23N → S in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti73D → H in BAA08260 (PubMed:8586446).Curated1
Sequence conflicti100G → A in AAB00855 (PubMed:8579579).Curated1
Sequence conflicti291Q → R in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti291Q → R in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti349H → R in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti349H → R in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti457K → P AA sequence (PubMed:1733949).Curated1
Sequence conflicti501V → S AA sequence (PubMed:1733949).Curated1
Sequence conflicti508E → N AA sequence (PubMed:1733949).Curated1
Sequence conflicti554P → L AA sequence (PubMed:1733949).Curated1
Sequence conflicti629P → L in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti629P → L in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti644S → R in BAA08260 (PubMed:8586446).Curated1
Sequence conflicti703V → A in BAA08260 (PubMed:8586446).Curated1
Sequence conflicti769Y → H in BAA08260 (PubMed:8586446).Curated1
Isoform 3 (identifier: Q13822-3)
Sequence conflicti23N → S in ABW38316 (PubMed:18175805).1
Sequence conflicti291Q → R in ABW38316 (PubMed:18175805).1
Sequence conflicti349H → R in ABW38316 (PubMed:18175805).1
Sequence conflicti493S → P in ABW38316 (PubMed:18175805).1
Sequence conflicti599F → Y in ABW38316 (PubMed:18175805).1
Sequence conflicti602S → T in ABW38316 (PubMed:18175805).1
Sequence conflicti654P → L in ABW38316 (PubMed:18175805).1

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_060469493S → P7 PublicationsCorresponds to variant dbSNP:rs10283100Ensembl.1
Natural variantiVAR_057472577N → S. Corresponds to variant dbSNP:rs2289886Ensembl.1
Natural variantiVAR_057473726S → L. Corresponds to variant dbSNP:rs16892767Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006750324E → EESSYGSPFTPAKRPKRKVA PKRRQERPVAPPKKRRRKIH RMDHYAAETRQDK in isoform 2. 2 Publications1
Alternative sequenceiVSP_036398593E → EAETRKFRGSRNENKENING NFEPRK in isoform 3. 1 Publication1

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
L35594 mRNA Translation: AAA64785.1
D45421 mRNA Translation: BAA08260.1
D45914 Genomic DNA Translation: BAA08342.1
L46720 mRNA Translation: AAB00855.1
EU131011 mRNA Translation: ABW38316.2
AC099818 Genomic DNA No translation available.
AC107960 Genomic DNA No translation available.
BC034961 mRNA Translation: AAH34961.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34936.1 [Q13822-1]
CCDS47914.1 [Q13822-3]
CCDS6329.1 [Q13822-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A55144

NCBI Reference Sequences

More...
RefSeqi
NP_001035181.1, NM_001040092.2 [Q13822-1]
NP_001124335.1, NM_001130863.2 [Q13822-3]
NP_006200.3, NM_006209.4 [Q13822-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.190977

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000075322; ENSP00000075322; ENSG00000136960 [Q13822-1]
ENST00000259486; ENSP00000259486; ENSG00000136960 [Q13822-2]
ENST00000522826; ENSP00000428291; ENSG00000136960 [Q13822-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5168

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5168

UCSC genome browser

More...
UCSCi
uc003yos.3 human [Q13822-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35594 mRNA Translation: AAA64785.1
D45421 mRNA Translation: BAA08260.1
D45914 Genomic DNA Translation: BAA08342.1
L46720 mRNA Translation: AAB00855.1
EU131011 mRNA Translation: ABW38316.2
AC099818 Genomic DNA No translation available.
AC107960 Genomic DNA No translation available.
BC034961 mRNA Translation: AAH34961.1
CCDSiCCDS34936.1 [Q13822-1]
CCDS47914.1 [Q13822-3]
CCDS6329.1 [Q13822-2]
PIRiA55144
RefSeqiNP_001035181.1, NM_001040092.2 [Q13822-1]
NP_001124335.1, NM_001130863.2 [Q13822-3]
NP_006200.3, NM_006209.4 [Q13822-2]
UniGeneiHs.190977

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZG6X-ray1.80A/B17-863[»]
4ZG7X-ray1.75A55-860[»]
4ZG9X-ray2.95A/B1-863[»]
4ZGAX-ray2.60A1-863[»]
5KXAX-ray2.59A1-863[»]
5M7MX-ray2.70A1-863[»]
5MHPX-ray2.43A1-863[»]
ProteinModelPortaliQ13822
SMRiQ13822
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111194, 3 interactors
IntActiQ13822, 3 interactors
MINTiQ13822
STRINGi9606.ENSP00000259486

Chemistry databases

BindingDBiQ13822
ChEMBLiCHEMBL3691
GuidetoPHARMACOLOGYi2901
SwissLipidsiSLP:000000393
SLP:000000641 [Q13822-1]

PTM databases

GlyConnecti1197
iPTMnetiQ13822
PhosphoSitePlusiQ13822

Polymorphism and mutation databases

BioMutaiENPP2
DMDMi290457674

Proteomic databases

jPOSTiQ13822
PeptideAtlasiQ13822
PRIDEiQ13822
ProteomicsDBi59692
59693 [Q13822-2]
59694 [Q13822-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5168
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000075322; ENSP00000075322; ENSG00000136960 [Q13822-1]
ENST00000259486; ENSP00000259486; ENSG00000136960 [Q13822-2]
ENST00000522826; ENSP00000428291; ENSG00000136960 [Q13822-3]
GeneIDi5168
KEGGihsa:5168
UCSCiuc003yos.3 human [Q13822-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5168
DisGeNETi5168
EuPathDBiHostDB:ENSG00000136960.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ENPP2

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0025550
HGNCiHGNC:3357 ENPP2
HPAiHPA023700
HPA053652
MIMi601060 gene
neXtProtiNX_Q13822
OpenTargetsiENSG00000136960
PharmGKBiPA27792

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

GeneTreeiENSGT00940000155778
HOVERGENiHBG051484
InParanoidiQ13822
KOiK01122
OMAiDGLHDTQ
OrthoDBi999163at2759
PhylomeDBiQ13822
TreeFamiTF330032

Enzyme and pathway databases

BioCyciMetaCyc:HS06258-MONOMER
BRENDAi3.1.4.39 2681
ReactomeiR-HSA-199220 Vitamin B5 (pantothenate) metabolism
SABIO-RKiQ13822

Miscellaneous databases

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

More...
ChiTaRSi
ENPP2 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Autotaxin

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

More...
GenomeRNAii
5168

Protein Ontology

More...
PROi
PR:Q13822

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136960 Expressed in 235 organ(s), highest expression level in pigmented layer of retina
ExpressionAtlasiQ13822 baseline and differential
GenevisibleiQ13822 HS

Family and domain databases

Gene3Di3.40.720.10, 1 hit
InterProiView protein in InterPro
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR001604 DNA/RNA_non-sp_Endonuclease
IPR029881 ENPP2
IPR020821 Extracellular_endonuc_su_A
IPR002591 Phosphodiest/P_Trfase
IPR036024 Somatomedin_B-like_dom_sf
IPR020436 Somatomedin_B_chordata
IPR001212 Somatomedin_B_dom
PANTHERiPTHR10151:SF21 PTHR10151:SF21, 1 hit
PfamiView protein in Pfam
PF01223 Endonuclease_NS, 1 hit
PF01663 Phosphodiest, 1 hit
PF01033 Somatomedin_B, 2 hits
PRINTSiPR00022 SOMATOMEDINB
SMARTiView protein in SMART
SM00892 Endonuclease_NS, 1 hit
SM00477 NUC, 1 hit
SM00201 SO, 2 hits
SUPFAMiSSF53649 SSF53649, 1 hit
SSF90188 SSF90188, 2 hits
PROSITEiView protein in PROSITE
PS00524 SMB_1, 2 hits
PS50958 SMB_2, 2 hits

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 nameiENPP2_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: Q13822
Secondary accession number(s): A8UHA1
, E9PHP7, Q13827, Q14555, Q15117, Q9UCQ8, Q9UCR0, Q9UCR1, Q9UCR2, Q9UCR3, Q9UCR4
<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: September 19, 2002
Last sequence update: March 2, 2010
Last modified: April 10, 2019
This is version 176 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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