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Protein

Transient receptor potential cation channel subfamily M member 2

Gene

TRPM2

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

Isoform 1: Nonselective, voltage-independent cation channel that mediates Na+ and Ca2+ influx, leading to increased cytoplasmic Ca2+ levels (PubMed:11960981, PubMed:12594222, PubMed:11385575, PubMed:11509734, PubMed:11804595, PubMed:15561722, PubMed:16601673, PubMed:19171771, PubMed:20660597, PubMed:27383051, PubMed:27068538). Extracellular calcium passes through the channel and increases channel activity by binding to the cytoplasmic domain and stabilizing the channel in an open conformation (PubMed:19171771). Also contributes to Ca2+ release from intracellular stores in response to ADP-ribose (PubMed:19454650). Plays a role in numerous processes that involve signaling via intracellular Ca2+ levels (Probable). Besides, mediates the release of lysosomal Zn2+ stores in response to reactive oxygen species, leading to increased cytosolic Zn2+ levels (PubMed:25562606, PubMed:27068538). Activated by moderate heat (35 to 40 degrees Celsius) (PubMed:16601673). Activated by intracellular ADP-ribose, beta-NAD (NAD+) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species (PubMed:11960981, PubMed:11385575, PubMed:11509734, PubMed:11804595, PubMed:15561722, PubMed:16601673, PubMed:19171771, PubMed:27383051, PubMed:27068538). The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate (PubMed:20650899, PubMed:25918360). Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius) (PubMed:16601673). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius) (PubMed:22493272). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis. Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca2+ levels (By similarity). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection. Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca2+ levels (By similarity). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its role in increasing cytoplasmic Ca2+ and Zn2+ levels (PubMed:27068538). Confers susceptibility to cell death following oxidative stress (PubMed:12594222, PubMed:25562606).By similarityCurated16 Publications
Isoform 2: Lacks cation channel activity. Does not mediate cation transport in response to oxidative stress or ADP-ribose.1 Publication
Isoform 3: Lacks cation channel activity and negatively regulates the channel activity of isoform 1. Negatively regulates susceptibility to cell death in reposponse to oxidative stress.1 Publication

Caution

The isolated nudix hydrolase domain was shown to have low catalytic activity with ADP-ribose upon heterologous expression (PubMed:11385575). However, a more recent publication demonstrates that the nudix hydrolase domain lacks enzyme activity and suggests that spontaneous degradation of the substrate underlies the previously reported low activity (PubMed:27383051).2 Publications

<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

Inactivated by exposure to extracellular pH between 4.0 and 6.5; irreversibly inactivated when open channels are exposed to extracellular pH between 4.0 and 6.5, while pre-exposure of closed channels to extracellular pH 5.5 gives rise to currents that rapidly inactivate, but protects against irreversible inactivation (PubMed:20660597). Inactivated by intracellular ATP (PubMed:11509734). Activated by arachidonic acid (PubMed:11804595).3 Publications

<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

  • calcium channel activity Source: Reactome
  • calcium ion binding Source: UniProtKB
  • calcium-release channel activity Source: UniProtKB
  • cation channel activity Source: UniProtKB
  • ligand-gated calcium channel activity Source: UniProtKB
  • sodium channel activity Source: UniProtKB-KW

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 functionCalcium channel, Ion channel, Sodium channel
Biological processCalcium transport, Ion transport, Sodium transport, Transport
LigandCalcium, Sodium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3295583 TRP channels
R-HSA-6798695 Neutrophil degranulation

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.4.5.5 the transient receptor potential ca(2+) channel (trp-cc) family

<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:
Transient receptor potential cation channel subfamily M member 2
Alternative name(s):
Estrogen-responsive element-associated gene 1 protein1 Publication
Long transient receptor potential channel 21 Publication
Short name:
LTrpC-2
Short name:
LTrpC21 Publication
Transient receptor potential channel 71 Publication
Short name:
TrpC71 Publication
Transient receptor potential melastatin 21 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:TRPM2
Synonyms:EREG11 Publication, KNP3, LTRPC21 Publication, TRPC71 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 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000142185.16

Human Gene Nomenclature Database

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HGNCi
HGNC:12339 TRPM2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603749 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O94759

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 752CytoplasmicSequence analysisAdd BLAST752
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei753 – 773HelicalSequence analysisAdd BLAST21
Topological domaini774 – 795ExtracellularSequence analysisAdd BLAST22
Transmembranei796 – 816HelicalSequence analysisAdd BLAST21
Topological domaini817 – 872CytoplasmicSequence analysisAdd BLAST56
Transmembranei873 – 893HelicalSequence analysisAdd BLAST21
Topological domaini894 – 896ExtracellularSequence analysis3
Transmembranei897 – 917HelicalSequence analysisAdd BLAST21
Topological domaini918 – 936CytoplasmicSequence analysisAdd BLAST19
Transmembranei937 – 957HelicalSequence analysisAdd BLAST21
Topological domaini958 – 1025ExtracellularSequence analysisAdd BLAST68
Transmembranei1026 – 1046HelicalSequence analysisAdd BLAST21
Topological domaini1047 – 1503CytoplasmicSequence analysisAdd BLAST457

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasmic vesicle, Lysosome, Membrane

<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>Mutagenesisi215M → A: Abolishes lowering of temperature threshold for activation in response to reactive oxygen species. 1 Publication1
Mutagenesisi952K → A: Strongly reduces channel activity at ph 7.3. Increased residual channel activity after exposure to pH 5.5. 1 Publication1
Mutagenesisi958H → A: No effect on channel activity. 1 Publication1
Mutagenesisi961R → A: Mildly decreases channel activity. 1 Publication1
Mutagenesisi962R → A: Abolishes channel activity. 1 Publication1
Mutagenesisi968R → A: Abolishes channel activity. 1 Publication1
Mutagenesisi973H → A: No effect on channel activity. 1 Publication1
Mutagenesisi995H → A: Moderately decreases channel activity. 1 Publication1
Mutagenesisi1002D → A: Strongly increased residual channel activity after exposure to pH 5.5. 1 Publication1
Mutagenesisi1005K → A: Decreases channel activity. 1 Publication1
Mutagenesisi1007K → A: Nearly abolishes channel activity. 1 Publication1
Mutagenesisi1397M → I: Only slight effect on activity. 1 Publication1
Mutagenesisi1404R → Q: Abolishes channel activity. 1 Publication1
Mutagenesisi1405 – 1408ILRQ → EFRE: Decreased channel activity in response to ADP-ribose. 1 Publication4
Mutagenesisi1408 – 1409QE → KK: Expected to abolish the initially proposed hydrolase activity. Does not abolish channel activity in response to ADP-ribose. 1 Publication2
Mutagenesisi1408Q → E: Decreased channel activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
7226

Open Targets

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OpenTargetsi
ENSG00000142185

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37012

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1250402

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
494

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TRPM2

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002153261 – 1503Transient receptor potential cation channel subfamily M member 2Add BLAST1503

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O94759

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

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PaxDbi
O94759

PeptideAtlas

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PeptideAtlasi
O94759

PRoteomics IDEntifications database

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PRIDEi
O94759

ProteomicsDB human proteome resource

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ProteomicsDBi
50419
50420 [O94759-2]
50421 [O94759-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O94759

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

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PhosphoSitePlusi
O94759

<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

Highly expressed in brain and peripheral blood cells, such as neutrophils. Also detected in bone marrow, spleen, heart, liver and lung. Isoform 2 is found in neutrophil granulocytes.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000142185 Expressed in 112 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_TRPC7
HS_TRPM2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O94759 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O94759 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA030976
HPA035260

<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

Isoform 1 can interact with isoform 3. This interaction decreases calcium influx through isoform 1 and suppresses susceptibility to oxidative stress-induced cell death.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113077, 2 interactors

Protein interaction database and analysis system

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IntActi
O94759, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000300482

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O94759

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O94759

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

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SMRi
O94759

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>Domaini1354 – 1498Nudix hydrolasePROSITE-ProRule annotationAdd BLAST145

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>Motifi1390 – 1411Nudix boxPROSITE-ProRule annotationAdd BLAST22

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The cytosolic nudix box binds ADP-ribose and is required for channel activation by ADP-ribose (PubMed:15561722, PubMed:16601673).2 Publications

<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

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3614 Eukaryota
KOG4195 Eukaryota
ENOG410XR5B LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156404

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000236350

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG055825

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O94759

KEGG Orthology (KO)

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KOi
K04977

Database of Orthologous Groups

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OrthoDBi
738147at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O94759

TreeFam database of animal gene trees

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TreeFami
TF314204

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR005821 Ion_trans_dom
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR000086 NUDIX_hydrolase_dom
IPR029594 TRPM2

The PANTHER Classification System

More...
PANTHERi
PTHR13800:SF2 PTHR13800:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00520 Ion_trans, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55811 SSF55811, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51462 NUDIX, 1 hit

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

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 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O94759-1) [UniParc]FASTAAdd to basket
Also known as: TRPM2-L

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
MEPSALRKAG SEQEEGFEGL PRRVTDLGMV SNLRRSNSSL FKSWRLQCPF
60 70 80 90 100
GNNDKQESLS SWIPENIKKK ECVYFVESSK LSDAGKVVCQ CGYTHEQHLE
110 120 130 140 150
EATKPHTFQG TQWDPKKHVQ EMPTDAFGDI VFTGLSQKVK KYVRVSQDTP
160 170 180 190 200
SSVIYHLMTQ HWGLDVPNLL ISVTGGAKNF NMKPRLKSIF RRGLVKVAQT
210 220 230 240 250
TGAWIITGGS HTGVMKQVGE AVRDFSLSSS YKEGELITIG VATWGTVHRR
260 270 280 290 300
EGLIHPTGSF PAEYILDEDG QGNLTCLDSN HSHFILVDDG THGQYGVEIP
310 320 330 340 350
LRTRLEKFIS EQTKERGGVA IKIPIVCVVL EGGPGTLHTI DNATTNGTPC
360 370 380 390 400
VVVEGSGRVA DVIAQVANLP VSDITISLIQ QKLSVFFQEM FETFTESRIV
410 420 430 440 450
EWTKKIQDIV RRRQLLTVFR EGKDGQQDVD VAILQALLKA SRSQDHFGHE
460 470 480 490 500
NWDHQLKLAV AWNRVDIARS EIFMDEWQWK PSDLHPTMTA ALISNKPEFV
510 520 530 540 550
KLFLENGVQL KEFVTWDTLL YLYENLDPSC LFHSKLQKVL VEDPERPACA
560 570 580 590 600
PAAPRLQMHH VAQVLRELLG DFTQPLYPRP RHNDRLRLLL PVPHVKLNVQ
610 620 630 640 650
GVSLRSLYKR SSGHVTFTMD PIRDLLIWAI VQNRRELAGI IWAQSQDCIA
660 670 680 690 700
AALACSKILK ELSKEEEDTD SSEEMLALAE EYEHRAIGVF TECYRKDEER
710 720 730 740 750
AQKLLTRVSE AWGKTTCLQL ALEAKDMKFV SHGGIQAFLT KVWWGQLSVD
760 770 780 790 800
NGLWRVTLCM LAFPLLLTGL ISFREKRLQD VGTPAARARA FFTAPVVVFH
810 820 830 840 850
LNILSYFAFL CLFAYVLMVD FQPVPSWCEC AIYLWLFSLV CEEMRQLFYD
860 870 880 890 900
PDECGLMKKA ALYFSDFWNK LDVGAILLFV AGLTCRLIPA TLYPGRVILS
910 920 930 940 950
LDFILFCLRL MHIFTISKTL GPKIIIVKRM MKDVFFFLFL LAVWVVSFGV
960 970 980 990 1000
AKQAILIHNE RRVDWLFRGA VYHSYLTIFG QIPGYIDGVN FNPEHCSPNG
1010 1020 1030 1040 1050
TDPYKPKCPE SDATQQRPAF PEWLTVLLLC LYLLFTNILL LNLLIAMFNY
1060 1070 1080 1090 1100
TFQQVQEHTD QIWKFQRHDL IEEYHGRPAA PPPFILLSHL QLFIKRVVLK
1110 1120 1130 1140 1150
TPAKRHKQLK NKLEKNEEAA LLSWEIYLKE NYLQNRQFQQ KQRPEQKIED
1160 1170 1180 1190 1200
ISNKVDAMVD LLDLDPLKRS GSMEQRLASL EEQVAQTAQA LHWIVRTLRA
1210 1220 1230 1240 1250
SGFSSEADVP TLASQKAAEE PDAEPGGRKK TEEPGDSYHV NARHLLYPNC
1260 1270 1280 1290 1300
PVTRFPVPNE KVPWETEFLI YDPPFYTAER KDAAAMDPMG DTLEPLSTIQ
1310 1320 1330 1340 1350
YNVVDGLRDR RSFHGPYTVQ AGLPLNPMGR TGLRGRGSLS CFGPNHTLYP
1360 1370 1380 1390 1400
MVTRWRRNED GAICRKSIKK MLEVLVVKLP LSEHWALPGG SREPGEMLPR
1410 1420 1430 1440 1450
KLKRILRQEH WPSFENLLKC GMEVYKGYMD DPRNTDNAWI ETVAVSVHFQ
1460 1470 1480 1490 1500
DQNDVELNRL NSNLHACDSG ASIRWQVVDR RIPLYANHKT LLQKAAAEFG

AHY
Length:1,503
Mass (Da):171,198
Last modified:October 23, 2007 - v2
<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:i02338437501ABFAB
GO
Isoform 2 (identifier: O94759-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     538-557: Missing.
     1291-1325: DTLEPLSTIQYNVVDGLRDRRSFHGPYTVQAGLPL → E

Show »
Length:1,449
Mass (Da):165,273
Checksum:iCFFA7E256DABB60B
GO
Isoform 3 (identifier: O94759-3) [UniParc]FASTAAdd to basket
Also known as: TRPM2-S

The sequence of this isoform differs from the canonical sequence as follows:
     847-1503: Missing.

Show »
Length:846
Mass (Da):95,699
Checksum:i70B0B29CADE26939
GO

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

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PGK7E9PGK7_HUMAN
Transient receptor potential cation...
TRPM2
1,553Annotation score:

Annotation score:3 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>
A0A087WT16A0A087WT16_HUMAN
Transient receptor potential cation...
TRPM2
247Annotation 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>
C9JZQ8C9JZQ8_HUMAN
Transient receptor potential cation...
TRPM2
143Annotation 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 reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAB64300 differs from that shown. Reason: Frameshift at positions 1227 and 1237.Curated

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 conflicti1088S → N in CAD01139 (PubMed:11960981).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02521652N → K1 PublicationCorresponds to variant dbSNP:rs45625933Ensembl.1
Natural variantiVAR_025217166V → I1 PublicationCorresponds to variant dbSNP:rs45544142Ensembl.1
Natural variantiVAR_025218385V → M1 PublicationCorresponds to variant dbSNP:rs45485992Ensembl.1
Natural variantiVAR_020032543D → E1 PublicationCorresponds to variant dbSNP:rs1556314Ensembl.1
Natural variantiVAR_025219780D → E1 PublicationCorresponds to variant dbSNP:rs9974927Ensembl.1
Natural variantiVAR_0252201189Q → R5 PublicationsCorresponds to variant dbSNP:rs9978351Ensembl.1
Natural variantiVAR_0252211199R → W1 PublicationCorresponds to variant dbSNP:rs45611537Ensembl.1
Natural variantiVAR_0252221201S → G1 PublicationCorresponds to variant dbSNP:rs45519835Ensembl.1
Natural variantiVAR_0252231249N → S1 PublicationCorresponds to variant dbSNP:rs45513700Ensembl.1
Natural variantiVAR_0252241347T → M1 PublicationCorresponds to variant dbSNP:rs45589233Ensembl.1
Natural variantiVAR_0252251359E → K1 PublicationCorresponds to variant dbSNP:rs45570639Ensembl.1
Natural variantiVAR_0252261368I → M1 PublicationCorresponds to variant dbSNP:rs45613636Ensembl.1
Natural variantiVAR_0252271438A → S1 PublicationCorresponds to variant dbSNP:rs45578242Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006574538 – 557Missing in isoform 2. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_013018847 – 1503Missing in isoform 3. 1 PublicationAdd BLAST657
Alternative sequenceiVSP_0065751291 – 1325DTLEP…AGLPL → E in isoform 2. 1 PublicationAdd BLAST35

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
AB001535 mRNA Translation: BAA34700.1
AJ417076 mRNA Translation: CAD01139.1
AY603182 mRNA Translation: AAT12288.1
AB166745 mRNA Translation: BAD83705.1
AJ878416 mRNA Translation: CAI47593.1
DQ012935 Genomic DNA Translation: AAY22174.1
AP001754 Genomic DNA Translation: BAA95563.1
CH471079 Genomic DNA Translation: EAX09426.1
CH471079 Genomic DNA Translation: EAX09427.1
AB017549 mRNA Translation: BAB64300.1 Frameshift.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13710.1 [O94759-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001307279.1, NM_001320350.1
NP_001307280.1, NM_001320351.1
NP_003298.1, NM_003307.3
XP_005261228.1, XM_005261171.3 [O94759-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.369759

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000300481; ENSP00000300481; ENSG00000142185 [O94759-2]
ENST00000300482; ENSP00000300482; ENSG00000142185 [O94759-1]
ENST00000397928; ENSP00000381023; ENSG00000142185 [O94759-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7226

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7226

UCSC genome browser

More...
UCSCi
uc002zet.1 human [O94759-1]

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001535 mRNA Translation: BAA34700.1
AJ417076 mRNA Translation: CAD01139.1
AY603182 mRNA Translation: AAT12288.1
AB166745 mRNA Translation: BAD83705.1
AJ878416 mRNA Translation: CAI47593.1
DQ012935 Genomic DNA Translation: AAY22174.1
AP001754 Genomic DNA Translation: BAA95563.1
CH471079 Genomic DNA Translation: EAX09426.1
CH471079 Genomic DNA Translation: EAX09427.1
AB017549 mRNA Translation: BAB64300.1 Frameshift.
CCDSiCCDS13710.1 [O94759-1]
RefSeqiNP_001307279.1, NM_001320350.1
NP_001307280.1, NM_001320351.1
NP_003298.1, NM_003307.3
XP_005261228.1, XM_005261171.3 [O94759-1]
UniGeneiHs.369759

3D structure databases

ProteinModelPortaliO94759
SMRiO94759
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113077, 2 interactors
IntActiO94759, 1 interactor
STRINGi9606.ENSP00000300482

Chemistry databases

BindingDBiO94759
ChEMBLiCHEMBL1250402
GuidetoPHARMACOLOGYi494

Protein family/group databases

TCDBi1.A.4.5.5 the transient receptor potential ca(2+) channel (trp-cc) family

PTM databases

iPTMnetiO94759
PhosphoSitePlusiO94759

Polymorphism and mutation databases

BioMutaiTRPM2

Proteomic databases

jPOSTiO94759
PaxDbiO94759
PeptideAtlasiO94759
PRIDEiO94759
ProteomicsDBi50419
50420 [O94759-2]
50421 [O94759-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300481; ENSP00000300481; ENSG00000142185 [O94759-2]
ENST00000300482; ENSP00000300482; ENSG00000142185 [O94759-1]
ENST00000397928; ENSP00000381023; ENSG00000142185 [O94759-1]
GeneIDi7226
KEGGihsa:7226
UCSCiuc002zet.1 human [O94759-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7226
DisGeNETi7226
EuPathDBiHostDB:ENSG00000142185.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TRPM2
HGNCiHGNC:12339 TRPM2
HPAiHPA030976
HPA035260
MIMi603749 gene
neXtProtiNX_O94759
OpenTargetsiENSG00000142185
PharmGKBiPA37012

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3614 Eukaryota
KOG4195 Eukaryota
ENOG410XR5B LUCA
GeneTreeiENSGT00940000156404
HOGENOMiHOG000236350
HOVERGENiHBG055825
InParanoidiO94759
KOiK04977
OrthoDBi738147at2759
PhylomeDBiO94759
TreeFamiTF314204

Enzyme and pathway databases

ReactomeiR-HSA-3295583 TRP channels
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TRPM2

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

More...
GenomeRNAii
7226

Protein Ontology

More...
PROi
PR:O94759

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000142185 Expressed in 112 organ(s), highest expression level in blood
CleanExiHS_TRPC7
HS_TRPM2
ExpressionAtlasiO94759 baseline and differential
GenevisibleiO94759 HS

Family and domain databases

InterProiView protein in InterPro
IPR005821 Ion_trans_dom
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR000086 NUDIX_hydrolase_dom
IPR029594 TRPM2
PANTHERiPTHR13800:SF2 PTHR13800:SF2, 1 hit
PfamiView protein in Pfam
PF00520 Ion_trans, 1 hit
SUPFAMiSSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462 NUDIX, 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 nameiTRPM2_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: O94759
Secondary accession number(s): D3DSL6
, Q5KTC2, Q6J3P5, Q96KN6, Q96Q93
<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: May 30, 2000
Last sequence update: October 23, 2007
Last modified: January 16, 2019
This is version 175 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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