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Protein

Membrane-bound transcription factor site-2 protease

Gene

MBTPS2

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

Involved in regulated intramembrane proteolysis (RIP) that is the cleavage of membrane-spanning regulatory proteins by proteases within the plane of the membrane. It cleaves sterol-regulatory element-binding proteins (SREBPs) within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal fragments shuttle to the nucleus and activate gene transcription (PubMed:9659902, PubMed:27380894). Involved in RIP-mediated regulation of bone formation (PubMed:27380894).2 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

  • Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced. EC:3.4.24.85

<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

Zn2+Note: Binds 1 zinc ion per subunit.

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 bindingi171Zinc; catalytic1
<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 sitei1721
Metal bindingi175Zinc; catalytic1

<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, Metalloprotease, Protease
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.85 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1655829 Regulation of cholesterol biosynthesis by SREBP (SREBF)
R-HSA-381033 ATF6 (ATF6-alpha) activates chaperones
R-HSA-8874211 CREB3 factors activate genes
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes

SIGNOR Signaling Network Open Resource

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SIGNORi
O43462

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M50.001

<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:
Membrane-bound transcription factor site-2 protease (EC:3.4.24.85)
Alternative name(s):
Endopeptidase S2P
Sterol regulatory element-binding proteins intramembrane protease
Short name:
SREBPs intramembrane protease
<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:MBTPS2
Synonyms:S2P
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000012174.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:15455 MBTPS2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
300294 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O43462

<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 – 3Cytoplasmic1 Publication3
<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>Transmembranei4 – 24HelicalSequence analysisAdd BLAST21
Topological domaini25 – 74Lumenal1 PublicationAdd BLAST50
Transmembranei75 – 95HelicalSequence analysisAdd BLAST21
Transmembranei96 – 107HelicalSequence analysisAdd BLAST12
Topological domaini108 – 144Lumenal1 PublicationAdd BLAST37
Transmembranei145 – 169HelicalSequence analysisAdd BLAST25
Transmembranei174 – 186HelicalSequence analysisAdd BLAST13
Transmembranei187 – 209HelicalSequence analysisAdd BLAST23
Transmembranei229 – 251HelicalSequence analysisAdd BLAST23
Topological domaini252 – 446Lumenal1 PublicationAdd BLAST195
Transmembranei447 – 464HelicalSequence analysisAdd BLAST18
Transmembranei465 – 476HelicalSequence analysisAdd BLAST12
Topological domaini477 – 492LumenalSequence analysisAdd BLAST16
Transmembranei493 – 513HelicalSequence analysisAdd BLAST21
Topological domaini514 – 519CytoplasmicSequence analysis6

Keywords - Cellular componenti

Cytoplasm, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

IFAP syndrome with or without BRESHECK syndrome (IFAPS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by a peculiar triad of follicular ichthyosis, total or subtotal atrichia, and photophobia of varying degree. Histopathologically, the epidermal granular layer is generally well-preserved or thickened at the infundibulum. Hair follicles are poorly developed and tend to be surrounded by an inflammatory infiltrate. A subgroup of patients is described with lamellar rather than follicular ichthyosis. Non-consistent features may include growth and psychomotor retardation, aganglionic megacolon, seizures and nail dystrophy.
See also OMIM:308205
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_06305487M → I in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468177EnsemblClinVar.1
Natural variantiVAR_063055226W → L in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468180EnsemblClinVar.1
Natural variantiVAR_063056227H → L in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468176EnsemblClinVar.1
Natural variantiVAR_063057429R → H in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468178EnsemblClinVar.1
Natural variantiVAR_063058475F → S in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468179EnsemblClinVar.1
Olmsted syndrome, X-linked (OLMSX)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare congenital disorder characterized by bilateral mutilating palmoplantar keratoderma and periorificial keratotic plaques with severe itching at all lesions. Diffuse alopecia, constriction of digits, and onychodystrophy have also been reported. Infections and squamous cell carcinomas can arise on the keratotic areas. The digital constriction may progress to autoamputation of fingers and toes.
See also OMIM:300918
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071323464F → S in OLMSX. 1 PublicationCorresponds to variant dbSNP:rs587777306EnsemblClinVar.1
Keratosis follicularis spinulosa decalvans X-linked (KFSDX)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration.
See also OMIM:308800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064409508N → S in KFSDX; sterol responsiveness is reduced by half. 1 PublicationCorresponds to variant dbSNP:rs587776867EnsemblClinVar.1
Osteogenesis imperfecta 19 (OI19)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI19 is characterized by prenatal fractures, short stature, white sclerae, variable scoliosis and pectal deformity, striking tibial anterior angulation and generalized osteopenia.
See also OMIM:301014
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081103459N → S in OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation. 1 Publication1
Natural variantiVAR_081104505L → F in OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation. 1 Publication1

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>Mutagenesisi171H → F: Loss of activity. 1 Publication1
Mutagenesisi172E → A or Q: Loss of activity. 1 Publication1
Mutagenesisi172E → D: Partial loss of activity. 1 Publication1
Mutagenesisi175H → F: Loss of activity. 1 Publication1
Mutagenesisi467D → N: Loss of activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Ichthyosis, Osteogenesis imperfecta, Palmoplantar keratoderma

Organism-specific databases

DisGeNET

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DisGeNETi
51360

MalaCards human disease database

More...
MalaCardsi
MBTPS2
MIMi300918 phenotype
301014 phenotype
308205 phenotype
308800 phenotype

Open Targets

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OpenTargetsi
ENSG00000012174

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
85284 BRESEK syndrome
2273 Ichthyosis follicularis-alopecia-photophobia syndrome
2340 Keratosis follicularis spinulosa decalvans
659 Mutilating palmoplantar keratoderma with periorificial keratotic plaques

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30672

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MBTPS2

<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_00000884821 – 519Membrane-bound transcription factor site-2 proteaseAdd BLAST519

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>Glycosylationi337N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43462

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O43462

MaxQB - The MaxQuant DataBase

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MaxQBi
O43462

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

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PaxDbi
O43462

PeptideAtlas

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PeptideAtlasi
O43462

PRoteomics IDEntifications database

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PRIDEi
O43462

ProteomicsDB human proteome resource

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ProteomicsDBi
48956

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43462

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

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PhosphoSitePlusi
O43462

<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

Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000012174 Expressed in 200 organ(s), highest expression level in endothelial cell

CleanEx database of gene expression profiles

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CleanExi
HS_MBTPS2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O43462 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43462 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009486
HPA005494

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
119495, 54 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368798

<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
O43462

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

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SMRi
O43462

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi109 – 136Poly-SerAdd BLAST28
Compositional biasi285 – 386Cys-richAdd BLAST102
Compositional biasi380 – 384Poly-Ser5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M50A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2921 Eukaryota
COG0750 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000048066

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231255

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006397

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43462

KEGG Orthology (KO)

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KOi
K07765

Identification of Orthologs from Complete Genome Data

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OMAi
HYPYDAF

Database of Orthologous Groups

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OrthoDBi
1012405at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O43462

TreeFam database of animal gene trees

More...
TreeFami
TF314478

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001193 MBTPS2
IPR036034 PDZ_sf
IPR008915 Peptidase_M50

The PANTHER Classification System

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PANTHERi
PTHR13325 PTHR13325, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02163 Peptidase_M50, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01000 SREBPS2PTASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50156 SSF50156, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O43462-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIPVSLVVVV VGGWTVVYLT DLVLKSSVYF KHSYEDWLEN NGLSISPFHI
60 70 80 90 100
RWQTAVFNRA FYSWGRRKAR MLYQWFNFGM VFGVIAMFSS FFLLGKTLMQ
110 120 130 140 150
TLAQMMADSP SSYSSSSSSS SSSSSSSSSS SSSSSSLHNE QVLQVVVPGI
160 170 180 190 200
NLPVNQLTYF FTAVLISGVV HEIGHGIAAI REQVRFNGFG IFLFIIYPGA
210 220 230 240 250
FVDLFTTHLQ LISPVQQLRI FCAGIWHNFV LALLGILALV LLPVILLPFY
260 270 280 290 300
YTGVGVLITE VAEDSPAIGP RGLFVGDLVT HLQDCPVTNV QDWNECLDTI
310 320 330 340 350
AYEPQIGYCI SASTLQQLSF PVRAYKRLDG STECCNNHSL TDVCFSYRNN
360 370 380 390 400
FNKRLHTCLP ARKAVEATQV CRTNKDCKKS SSSSFCIIPS LETHTRLIKV
410 420 430 440 450
KHPPQIDMLY VGHPLHLHYT VSITSFIPRF NFLSIDLPVV VETFVKYLIS
460 470 480 490 500
LSGALAIVNA VPCFALDGQW ILNSFLDATL TSVIGDNDVK DLIGFFILLG
510
GSVLLAANVT LGLWMVTAR
Length:519
Mass (Da):57,444
Last modified:June 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i247D69E0FD7747BD
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B9ZVQ3B9ZVQ3_HUMAN
Membrane-bound transcription factor...
MBTPS2
330Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06305487M → I in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468177EnsemblClinVar.1
Natural variantiVAR_063055226W → L in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468180EnsemblClinVar.1
Natural variantiVAR_063056227H → L in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468176EnsemblClinVar.1
Natural variantiVAR_063057429R → H in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468178EnsemblClinVar.1
Natural variantiVAR_081103459N → S in OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation. 1 Publication1
Natural variantiVAR_071323464F → S in OLMSX. 1 PublicationCorresponds to variant dbSNP:rs587777306EnsemblClinVar.1
Natural variantiVAR_063058475F → S in IFAPS; does not affect subcellular localization; impairs activity. 1 PublicationCorresponds to variant dbSNP:rs122468179EnsemblClinVar.1
Natural variantiVAR_081104505L → F in OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation. 1 Publication1
Natural variantiVAR_064409508N → S in KFSDX; sterol responsiveness is reduced by half. 1 PublicationCorresponds to variant dbSNP:rs587776867EnsemblClinVar.1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF019612 mRNA Translation: AAC51937.1
U73479 Genomic DNA Translation: AAD08632.1
U72788 Genomic DNA Translation: AAD08631.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS14201.1

NCBI Reference Sequences

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RefSeqi
NP_056968.1, NM_015884.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.443490

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000379484; ENSP00000368798; ENSG00000012174

Database of genes from NCBI RefSeq genomes

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GeneIDi
51360

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:51360

UCSC genome browser

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UCSCi
uc004dae.4 human

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019612 mRNA Translation: AAC51937.1
U73479 Genomic DNA Translation: AAD08632.1
U72788 Genomic DNA Translation: AAD08631.1
CCDSiCCDS14201.1
RefSeqiNP_056968.1, NM_015884.3
UniGeneiHs.443490

3D structure databases

ProteinModelPortaliO43462
SMRiO43462
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119495, 54 interactors
STRINGi9606.ENSP00000368798

Protein family/group databases

MEROPSiM50.001

PTM databases

iPTMnetiO43462
PhosphoSitePlusiO43462

Polymorphism and mutation databases

BioMutaiMBTPS2

Proteomic databases

EPDiO43462
jPOSTiO43462
MaxQBiO43462
PaxDbiO43462
PeptideAtlasiO43462
PRIDEiO43462
ProteomicsDBi48956

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379484; ENSP00000368798; ENSG00000012174
GeneIDi51360
KEGGihsa:51360
UCSCiuc004dae.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
51360
DisGeNETi51360
EuPathDBiHostDB:ENSG00000012174.11

GeneCards: human genes, protein and diseases

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GeneCardsi
MBTPS2
HGNCiHGNC:15455 MBTPS2
HPAiCAB009486
HPA005494
MalaCardsiMBTPS2
MIMi300294 gene
300918 phenotype
301014 phenotype
308205 phenotype
308800 phenotype
neXtProtiNX_O43462
OpenTargetsiENSG00000012174
Orphaneti85284 BRESEK syndrome
2273 Ichthyosis follicularis-alopecia-photophobia syndrome
2340 Keratosis follicularis spinulosa decalvans
659 Mutilating palmoplantar keratoderma with periorificial keratotic plaques
PharmGKBiPA30672

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG2921 Eukaryota
COG0750 LUCA
GeneTreeiENSGT00510000048066
HOGENOMiHOG000231255
HOVERGENiHBG006397
InParanoidiO43462
KOiK07765
OMAiHYPYDAF
OrthoDBi1012405at2759
PhylomeDBiO43462
TreeFamiTF314478

Enzyme and pathway databases

BRENDAi3.4.24.85 2681
ReactomeiR-HSA-1655829 Regulation of cholesterol biosynthesis by SREBP (SREBF)
R-HSA-381033 ATF6 (ATF6-alpha) activates chaperones
R-HSA-8874211 CREB3 factors activate genes
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
SIGNORiO43462

Miscellaneous databases

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

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ChiTaRSi
MBTPS2 human

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

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GenomeRNAii
51360

Protein Ontology

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PROi
PR:O43462

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000012174 Expressed in 200 organ(s), highest expression level in endothelial cell
CleanExiHS_MBTPS2
ExpressionAtlasiO43462 baseline and differential
GenevisibleiO43462 HS

Family and domain databases

InterProiView protein in InterPro
IPR001193 MBTPS2
IPR036034 PDZ_sf
IPR008915 Peptidase_M50
PANTHERiPTHR13325 PTHR13325, 1 hit
PfamiView protein in Pfam
PF02163 Peptidase_M50, 1 hit
PRINTSiPR01000 SREBPS2PTASE
SUPFAMiSSF50156 SSF50156, 1 hit
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiMBTP2_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: O43462
Secondary accession number(s): Q9UM70, Q9UMD3
<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: July 15, 1999
Last sequence update: June 1, 1998
Last modified: January 16, 2019
This is version 167 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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