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Protein

Myelin protein P0

Gene

MPZ

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

Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.2 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

  • structural molecule activity Source: ProtInc

GO - Biological processi

  • cell aggregation Source: UniProtKB
  • cell-cell adhesion via plasma-membrane adhesion molecules Source: UniProtKB
  • chemical synaptic transmission Source: ProtInc
  • myelination Source: UniProtKB
  • negative regulation of apoptotic process Source: Ensembl

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

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SIGNORi
P25189

<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:
Myelin protein P0
Alternative name(s):
Myelin peripheral protein
Short name:
MPP
Myelin protein zero
<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:MPZ
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000158887.15

Human Gene Nomenclature Database

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HGNCi
HGNC:7225 MPZ

Online Mendelian Inheritance in Man (OMIM)

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MIMi
159440 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P25189

<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 domaini30 – 153ExtracellularSequence analysisAdd BLAST124
<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>Transmembranei154 – 179HelicalSequence analysisAdd BLAST26
Topological domaini180 – 248CytoplasmicSequence analysisAdd BLAST69

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

Cell membrane, 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

Charcot-Marie-Tooth disease 1B (CMT1B)40 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet.
See also OMIM:118200
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_00450030I → M in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs770546306EnsemblClinVar.1
Natural variantiVAR_00450132V → F in CMT1B; severe. 1 Publication1
Natural variantiVAR_00450234T → I in CMT1B. 1 Publication1
Natural variantiVAR_05439339H → P in CMT1B; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane. 2 PublicationsCorresponds to variant dbSNP:rs371856018EnsemblClinVar.1
Natural variantiVAR_05439450Missing in CMT1B. 1 Publication1
Natural variantiVAR_05439551 – 57Missing in CMT1B; affects targeting to the cell membrane; reduces intercellular adhesion. 1 Publication7
Natural variantiVAR_02997151S → F in CMT1B. 1 Publication1
Natural variantiVAR_00450454S → C in CMT1B; severe. 1
Natural variantiVAR_00450554S → P in CMT1B. 1 Publication1
Natural variantiVAR_00450658V → F in CMT1B; moderate. 1 Publication1
Natural variantiVAR_01597262I → F in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913602EnsemblClinVar.1
Natural variantiVAR_00450963S → F in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913585EnsemblClinVar.1
Natural variantiVAR_00450763Missing in CMT1B. 3 Publications1
Natural variantiVAR_03188665T → A in CMT1B. 1 Publication1
Natural variantiVAR_02997465T → I in CMT1B. 1 Publication1
Natural variantiVAR_00451168Y → C in CMT1B; severe/mild. 4 Publications1
Natural variantiVAR_00451278S → L in CMT1B; severe. 8 PublicationsCorresponds to variant dbSNP:rs121913601EnsemblClinVar.1
Natural variantiVAR_03188778S → W in CMT1B. 1 Publication1
Natural variantiVAR_00451590D → E in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913584EnsemblClinVar.1
Natural variantiVAR_00451693G → E in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs1060503418Ensembl.1
Natural variantiVAR_00451796K → E in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913583EnsemblClinVar.1
Natural variantiVAR_00451998R → H in CMT1B. 6 PublicationsCorresponds to variant dbSNP:rs121913589EnsemblClinVar.1
Natural variantiVAR_00452098R → P in CMT1B. Corresponds to variant dbSNP:rs121913589EnsemblClinVar.1
Natural variantiVAR_00452198R → S in CMT1B. 1 Publication1
Natural variantiVAR_00452299I → T in CMT1B. 1
Natural variantiVAR_004523101W → C in CMT1B. 1 Publication1
Natural variantiVAR_015976103G → E in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913600EnsemblClinVar.1
Natural variantiVAR_031889109D → N in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs1060503420Ensembl.1
Natural variantiVAR_004524112I → T in CMT1B; severe. 1 Publication1
Natural variantiVAR_004528122N → S in CMT1B; loss of glycosylation site. 1 Publication1
Natural variantiVAR_004529124T → M in CMT1B, CMT2I and CMT2J; CMTJ2 patients present Adie pupil; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane; affects glycosylation. 11 PublicationsCorresponds to variant dbSNP:rs121913595EnsemblClinVar.1
Natural variantiVAR_004532128D → E in CMT1B. 1
Natural variantiVAR_004534130K → R in CMT1B, CMT2I and DSS. 4 PublicationsCorresponds to variant dbSNP:rs281865127EnsemblClinVar.1
Natural variantiVAR_004535132P → L in CMT1B; moderate. 1 Publication1
Natural variantiVAR_004536134D → E in CMT1B. 2 Publications1
Natural variantiVAR_029979134D → G in CMT1B. 1 Publication1
Natural variantiVAR_004537134D → N in CMT1B. 1 Publication1
Natural variantiVAR_004539135I → T in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913587EnsemblClinVar.1
Natural variantiVAR_004540137G → S in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913588EnsemblClinVar.1
Natural variantiVAR_029980138K → N in CMT1B. 1 Publication1
Natural variantiVAR_029981139T → N in CMT1B. 1 Publication1
Natural variantiVAR_029982140S → T in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs572010627EnsemblClinVar.1
Natural variantiVAR_004541143T → M in CMT1B. Corresponds to variant dbSNP:rs750724650EnsemblClinVar.1
Natural variantiVAR_029983145Y → S in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913603EnsemblClinVar.1
Natural variantiVAR_029984146V → F in CMT1B. 1 Publication1
Natural variantiVAR_004542163G → R in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs281865128EnsemblClinVar.1
Natural variantiVAR_029985170L → R in CMT1B. 1 Publication1
Natural variantiVAR_029986216T → ER in CMT1B; referred to as 'T216ER'. 1
Natural variantiVAR_054397224D → Y in CMT1B; also in two asymptomatic individuals from the same family. 1 PublicationCorresponds to variant dbSNP:rs267607247EnsemblClinVar.1
Natural variantiVAR_054398227R → S in CMT1B. 1 Publication1
Natural variantiVAR_029987236Missing in CMT1B. 1 Publication1
Charcot-Marie-Tooth disease 2I (CMT2I)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
See also OMIM:607677
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02997260D → H in CMT2I. 1 PublicationCorresponds to variant dbSNP:rs121913604EnsemblClinVar.1
Natural variantiVAR_02997362I → M in CMT2I. 1 PublicationCorresponds to variant dbSNP:rs121913605EnsemblClinVar.1
Natural variantiVAR_01597489I → N in CMT2I; patient carrying also Met-92 and Met-162. 1 PublicationCorresponds to variant dbSNP:rs267607244EnsemblClinVar.1
Natural variantiVAR_01597592V → M in CMT2I; patient carrying also Asn-89 and Met-162. 1 PublicationCorresponds to variant dbSNP:rs267607245EnsemblClinVar.1
Natural variantiVAR_021609118D → N in CMT2I. 1 Publication1
Natural variantiVAR_015980162I → M in CMT2I; patient carrying also Asn-89 and Met-92. 1 PublicationCorresponds to variant dbSNP:rs267607246EnsemblClinVar.1
Natural variantiVAR_021610236K → E in CMT2I. 1 Publication1
Charcot-Marie-Tooth disease 2J (CMT2J)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Charcot-Marie-Tooth disease type 2J is characterized by the association of axonal peripheral neuropathy with hearing loss and pupillary abnormalities such as Adie pupil.
See also OMIM:607736
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02997597E → V in CMT2J. 1 PublicationCorresponds to variant dbSNP:rs121913606EnsemblClinVar.1
Adie pupil (ADIEP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA stationary, benign disorder characterized by tonic, sluggishly reacting pupil and hypoactive or absent tendon reflexes. Adie pupil is a characteristic of Charcot-Marie-Tooth disease type 2J.
See also OMIM:103100
Charcot-Marie-Tooth disease, dominant, intermediate type, D (CMTDID)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type D is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.
See also OMIM:607791
Dejerine-Sottas syndrome (DSS)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome.
See also OMIM:145900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03188442Missing in DSS. 1 Publication1
Natural variantiVAR_00450863S → C in DSS. 1 PublicationCorresponds to variant dbSNP:rs121913585EnsemblClinVar.1
Natural variantiVAR_029976110G → D in DSS. 1 Publication1
Natural variantiVAR_004525114I → T in DSS; associated on the same allele as His-116 and Asn-128 in one patient. 1 PublicationCorresponds to variant dbSNP:rs267607241EnsemblClinVar.1
Natural variantiVAR_004526116N → H in DSS; associated on the same allele as Thr-114 and Asn-128 in one patient. 1 PublicationCorresponds to variant dbSNP:rs267607242EnsemblClinVar.1
Natural variantiVAR_004527118D → DFY in DSS. 1 Publication1
Natural variantiVAR_004530124 – 125Missing in DSS. 2 Publications2
Natural variantiVAR_004531127C → Y in DSS. 1
Natural variantiVAR_004533128D → N in DSS; associated on the same allele as Thr-114 and His-116 in one patient. 1 PublicationCorresponds to variant dbSNP:rs267607243EnsemblClinVar.1
Natural variantiVAR_015979136V → E in DSS. 1 Publication1
Natural variantiVAR_031892221A → T in DSS. 1 Publication1
Neuropathy, congenital hypomyelinating or amyelinating (CHN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe degenerating neuropathy that results from a congenital impairment in myelin formation. It is clinically characterized by early onset of hypotonia, areflexia, distal muscle weakness, and very slow nerve conduction velocities (as low as 3m/s). Some patients manifest nearly complete absence of spontaneous limb movements, respiratory distress at birth, and complete absence of myelin shown by electron microscopy of peripheral nerves. Inheritance can be autosomal dominant or recessive.
See also OMIM:605253
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029978124T → K in CHN. 1 PublicationCorresponds to variant dbSNP:rs121913595EnsemblClinVar.1
Roussy-Levy syndrome (ROULS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disorder that resembles Charcot-Marie-Tooth disease type 1 in that it presents with foot deformity, weakness and atrophy of distal limb muscles, especially the peronei, and absent tendon reflexes. The phenotype differs, however, in that it includes static tremor of the upper limbs and gait ataxia.
See also OMIM:180800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015978131N → K in ROULS. 1 PublicationCorresponds to variant dbSNP:rs121913599EnsemblClinVar.1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Deafness, Dejerine-Sottas syndrome, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

DisGeNET

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DisGeNETi
4359

MalaCards human disease database

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MalaCardsi
MPZ
MIMi103100 phenotype
118200 phenotype
145900 phenotype
180800 phenotype
605253 phenotype
607677 phenotype
607736 phenotype
607791 phenotype

Open Targets

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OpenTargetsi
ENSG00000158887

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

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Orphaneti
99942 Autosomal dominant Charcot-Marie-Tooth disease type 2I
99943 Autosomal dominant Charcot-Marie-Tooth disease type 2J
100046 Autosomal dominant intermediate Charcot-Marie-Tooth disease type D
324585 Autosomal dominant intermediate Charcot-Marie-Tooth disease with neuropathic pain
101082 Charcot-Marie-Tooth disease type 1B
64748 Dejerine-Sottas syndrome
3115 Roussy-Levy syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30930

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MPZ

Domain mapping of disease mutations (DMDM)

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DMDMi
127721

<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 – 29Add BLAST29
<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_000001930030 – 248Myelin protein P0Add BLAST219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi50 ↔ 127PROSITE-ProRule annotation1 Publication
<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>Glycosylationi122N-linked (GlcNAc...) (complex) asparagineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei210Phosphoserine; by PKCBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei228PhosphoserineBy similarity1
Modified residuei233Phosphoserine; by PKCBy similarity1
Modified residuei243Phosphoserine; by PKCBy similarity1

<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-glycosylated; contains sulfate-substituted glycan.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P25189

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

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PaxDbi
P25189

PeptideAtlas

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PeptideAtlasi
P25189

PRoteomics IDEntifications database

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PRIDEi
P25189

ProteomicsDB human proteome resource

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ProteomicsDBi
54264

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1526

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P25189

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

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PhosphoSitePlusi
P25189

<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

Found only in peripheral nervous system Schwann cells.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000158887 Expressed in 126 organ(s), highest expression level in tibial nerve

CleanEx database of gene expression profiles

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CleanExi
HS_MPZ

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P25189 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P25189 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA068925

<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

Homodimer and homotetramer.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110499, 2 interactors

Protein interaction database and analysis system

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IntActi
P25189, 3 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000431538

<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

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P25189

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

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SMRi
P25189

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>Domaini30 – 143Ig-like V-typeAdd BLAST114

<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 myelin P0 protein family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJG4 Eukaryota
ENOG4111R0Y LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00900000140913

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000232144

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG096384

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P25189

KEGG Orthology (KO)

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KOi
K06770

Identification of Orthologs from Complete Genome Data

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OMAi
YLIRYCW

Database of Orthologous Groups

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OrthoDBi
EOG091G0H91

Database for complete collections of gene phylogenies

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PhylomeDBi
P25189

TreeFam database of animal gene trees

More...
TreeFami
TF331728

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR013106 Ig_V-set
IPR019566 Myelin-PO_C
IPR000920 Myelin_P0-rel
IPR019738 Myelin_P0_CS
IPR029869 P0

The PANTHER Classification System

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PANTHERi
PTHR13869 PTHR13869, 1 hit
PTHR13869:SF7 PTHR13869:SF7, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF10570 Myelin-PO_C, 1 hit
PF07686 V-set, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00213 MYELINP0

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 1 hit
SM00406 IGv, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00568 MYELIN_P0, 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 (2+)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 2 <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 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P25189-1) [UniParc]FASTAAdd to basket

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
MAPGAPSSSP SPILAVLLFS SLVLSPAQAI VVYTDREVHG AVGSRVTLHC
60 70 80 90 100
SFWSSEWVSD DISFTWRYQP EGGRDAISIF HYAKGQPYID EVGTFKERIQ
110 120 130 140 150
WVGDPRWKDG SIVIHNLDYS DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV
160 170 180 190 200
PTRYGVVLGA VIGGVLGVVL LLLLLFYVVR YCWLRRQAAL QRRLSAMEKG
210 220 230 240
KLHKPGKDAS KRGRQTPVLY AMLDHSRSTK AVSEKKAKGL GESRKDKK
Length:248
Mass (Da):27,555
Last modified:May 1, 1992 - 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:iA93F4744DACB0D5E
GO
Isoform L-MPZ (identifier: P25189-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     248-248: K → KRLAGRAGDRGLGVESAKGPKVMVIEMELRKDEQSPELRPAVKSPSRTSLKNALKNMMGLNSDK

Note: Based on a naturally occurring readthrough transcript. Highly antigenic.
Show »
Length:311
Mass (Da):34,387
Checksum:i04FA6B8C665820CB
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0J9YWT2A0A0J9YWT2_HUMAN
Myelin protein P0
MPZ
136Annotation 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>
E9PL80E9PL80_HUMAN
Myelin protein P0
MPZ
52Annotation 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 AAH06491 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAP35411 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA03540 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAG36330 differs from that shown. Reason: Erroneous initiation.Curated
The sequence EAW52606 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00450030I → M in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs770546306EnsemblClinVar.1
Natural variantiVAR_00450132V → F in CMT1B; severe. 1 Publication1
Natural variantiVAR_00450234T → I in CMT1B. 1 Publication1
Natural variantiVAR_01597135D → Y in CMT1B and CMTDID. 2 PublicationsCorresponds to variant dbSNP:rs121913596EnsemblClinVar.1
Natural variantiVAR_05439339H → P in CMT1B; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane. 2 PublicationsCorresponds to variant dbSNP:rs371856018EnsemblClinVar.1
Natural variantiVAR_03188442Missing in DSS. 1 Publication1
Natural variantiVAR_00450344S → F in CMT2I and CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913598EnsemblClinVar.1
Natural variantiVAR_05439450Missing in CMT1B. 1 Publication1
Natural variantiVAR_05439551 – 57Missing in CMT1B; affects targeting to the cell membrane; reduces intercellular adhesion. 1 Publication7
Natural variantiVAR_02997151S → F in CMT1B. 1 Publication1
Natural variantiVAR_00450454S → C in CMT1B; severe. 1
Natural variantiVAR_00450554S → P in CMT1B. 1 Publication1
Natural variantiVAR_05439656E → K in CMT2. 1 Publication1
Natural variantiVAR_00450658V → F in CMT1B; moderate. 1 Publication1
Natural variantiVAR_02997260D → H in CMT2I. 1 PublicationCorresponds to variant dbSNP:rs121913604EnsemblClinVar.1
Natural variantiVAR_03188561D → G in CMT2; unclassified. 1 PublicationCorresponds to variant dbSNP:rs786204119EnsemblClinVar.1
Natural variantiVAR_01597262I → F in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913602EnsemblClinVar.1
Natural variantiVAR_02997362I → M in CMT2I. 1 PublicationCorresponds to variant dbSNP:rs121913605EnsemblClinVar.1
Natural variantiVAR_00450863S → C in DSS. 1 PublicationCorresponds to variant dbSNP:rs121913585EnsemblClinVar.1
Natural variantiVAR_00450963S → F in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913585EnsemblClinVar.1
Natural variantiVAR_00450763Missing in CMT1B. 3 Publications1
Natural variantiVAR_00451064Missing in CMT1B and DSS. 1 Publication1
Natural variantiVAR_03188665T → A in CMT1B. 1 Publication1
Natural variantiVAR_02997465T → I in CMT1B. 1 Publication1
Natural variantiVAR_00451168Y → C in CMT1B; severe/mild. 4 Publications1
Natural variantiVAR_01597375D → V in CMT2J and CMT2I. 3 PublicationsCorresponds to variant dbSNP:rs121913597EnsemblClinVar.1
Natural variantiVAR_00451278S → L in CMT1B; severe. 8 PublicationsCorresponds to variant dbSNP:rs121913601EnsemblClinVar.1
Natural variantiVAR_03188778S → W in CMT1B. 1 Publication1
Natural variantiVAR_00451381H → R in CMT1B and CMT2I; severe; reduces intercellular adhesion; does not affect targeting to the cell membrane. 3 PublicationsCorresponds to variant dbSNP:rs121913594EnsemblClinVar.1
Natural variantiVAR_03188881H → Y in CMT; associated with F-113. 1 PublicationCorresponds to variant dbSNP:rs281865123EnsemblClinVar.1
Natural variantiVAR_00451482Y → C in CMT1B and DSS. 4 Publications1
Natural variantiVAR_01597489I → N in CMT2I; patient carrying also Met-92 and Met-162. 1 PublicationCorresponds to variant dbSNP:rs267607244EnsemblClinVar.1
Natural variantiVAR_00451590D → E in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913584EnsemblClinVar.1
Natural variantiVAR_01597592V → M in CMT2I; patient carrying also Asn-89 and Met-162. 1 PublicationCorresponds to variant dbSNP:rs267607245EnsemblClinVar.1
Natural variantiVAR_00451693G → E in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs1060503418Ensembl.1
Natural variantiVAR_00451796K → E in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913583EnsemblClinVar.1
Natural variantiVAR_02997597E → V in CMT2J. 1 PublicationCorresponds to variant dbSNP:rs121913606EnsemblClinVar.1
Natural variantiVAR_00451898R → C in CMT1B and DSS; severe. 5 PublicationsCorresponds to variant dbSNP:rs121913590EnsemblClinVar.1
Natural variantiVAR_00451998R → H in CMT1B. 6 PublicationsCorresponds to variant dbSNP:rs121913589EnsemblClinVar.1
Natural variantiVAR_00452098R → P in CMT1B. Corresponds to variant dbSNP:rs121913589EnsemblClinVar.1
Natural variantiVAR_00452198R → S in CMT1B. 1 Publication1
Natural variantiVAR_00452299I → T in CMT1B. 1
Natural variantiVAR_004523101W → C in CMT1B. 1 Publication1
Natural variantiVAR_015976103G → E in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913600EnsemblClinVar.1
Natural variantiVAR_031889109D → N in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs1060503420Ensembl.1
Natural variantiVAR_029976110G → D in DSS. 1 Publication1
Natural variantiVAR_004524112I → T in CMT1B; severe. 1 Publication1
Natural variantiVAR_031890113V → F in CMT; unclassified; associated with Y-81. 1 PublicationCorresponds to variant dbSNP:rs281865126EnsemblClinVar.1
Natural variantiVAR_029977113V → I in CMT2. 1 Publication1
Natural variantiVAR_004525114I → T in DSS; associated on the same allele as His-116 and Asn-128 in one patient. 1 PublicationCorresponds to variant dbSNP:rs267607241EnsemblClinVar.1
Natural variantiVAR_004526116N → H in DSS; associated on the same allele as Thr-114 and Asn-128 in one patient. 1 PublicationCorresponds to variant dbSNP:rs267607242EnsemblClinVar.1
Natural variantiVAR_004527118D → DFY in DSS. 1 Publication1
Natural variantiVAR_021609118D → N in CMT2I. 1 Publication1
Natural variantiVAR_031891119Y → C in CMT2; unclassified. 1 PublicationCorresponds to variant dbSNP:rs879254038EnsemblClinVar.1
Natural variantiVAR_004528122N → S in CMT1B; loss of glycosylation site. 1 Publication1
Natural variantiVAR_015977123G → C in DSS and CMT1B. 2 Publications1
Natural variantiVAR_004530124 – 125Missing in DSS. 2 Publications2
Natural variantiVAR_029978124T → K in CHN. 1 PublicationCorresponds to variant dbSNP:rs121913595EnsemblClinVar.1
Natural variantiVAR_004529124T → M in CMT1B, CMT2I and CMT2J; CMTJ2 patients present Adie pupil; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane; affects glycosylation. 11 PublicationsCorresponds to variant dbSNP:rs121913595EnsemblClinVar.1
Natural variantiVAR_004531127C → Y in DSS. 1
Natural variantiVAR_004532128D → E in CMT1B. 1
Natural variantiVAR_004533128D → N in DSS; associated on the same allele as Thr-114 and His-116 in one patient. 1 PublicationCorresponds to variant dbSNP:rs267607243EnsemblClinVar.1
Natural variantiVAR_004534130K → R in CMT1B, CMT2I and DSS. 4 PublicationsCorresponds to variant dbSNP:rs281865127EnsemblClinVar.1
Natural variantiVAR_015978131N → K in ROULS. 1 PublicationCorresponds to variant dbSNP:rs121913599EnsemblClinVar.1
Natural variantiVAR_004535132P → L in CMT1B; moderate. 1 Publication1
Natural variantiVAR_004536134D → E in CMT1B. 2 Publications1
Natural variantiVAR_029979134D → G in CMT1B. 1 Publication1
Natural variantiVAR_004537134D → N in CMT1B. 1 Publication1
Natural variantiVAR_004538135I → L in CMT1B and DSS. 1 PublicationCorresponds to variant dbSNP:rs879253858EnsemblClinVar.1
Natural variantiVAR_004539135I → T in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs121913587EnsemblClinVar.1
Natural variantiVAR_015979136V → E in DSS. 1 Publication1
Natural variantiVAR_004540137G → S in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913588EnsemblClinVar.1
Natural variantiVAR_029980138K → N in CMT1B. 1 Publication1
Natural variantiVAR_029981139T → N in CMT1B. 1 Publication1
Natural variantiVAR_029982140S → T in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs572010627EnsemblClinVar.1
Natural variantiVAR_004541143T → M in CMT1B. Corresponds to variant dbSNP:rs750724650EnsemblClinVar.1
Natural variantiVAR_029983145Y → S in CMT1B. 1 PublicationCorresponds to variant dbSNP:rs121913603EnsemblClinVar.1
Natural variantiVAR_029984146V → F in CMT1B. 1 Publication1
Natural variantiVAR_015980162I → M in CMT2I; patient carrying also Asn-89 and Met-92. 1 PublicationCorresponds to variant dbSNP:rs267607246EnsemblClinVar.1
Natural variantiVAR_004542163G → R in CMT1B. 2 PublicationsCorresponds to variant dbSNP:rs281865128EnsemblClinVar.1
Natural variantiVAR_004543167G → A in CMT1B and DSS; severe. 1 Publication1
Natural variantiVAR_004544167G → R in CMT2I and DSS. 2 PublicationsCorresponds to variant dbSNP:rs121913586EnsemblClinVar.1
Natural variantiVAR_029985170L → R in CMT1B. 1 Publication1
Natural variantiVAR_029986216T → ER in CMT1B; referred to as 'T216ER'. 1
Natural variantiVAR_031892221A → T in DSS. 1 Publication1
Natural variantiVAR_054397224D → Y in CMT1B; also in two asymptomatic individuals from the same family. 1 PublicationCorresponds to variant dbSNP:rs267607247EnsemblClinVar.1
Natural variantiVAR_054398227R → S in CMT1B. 1 Publication1
Natural variantiVAR_021610236K → E in CMT2I. 1 Publication1
Natural variantiVAR_029987236Missing in CMT1B. 1 Publication1
Natural variantiVAR_004545244R → L. Corresponds to variant dbSNP:rs749722729EnsemblClinVar.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_045844248K → KRLAGRAGDRGLGVESAKGP KVMVIEMELRKDEQSPELRP AVKSPSRTSLKNALKNMMGL NSDK in isoform L-MPZ. Curated1

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
D10537 mRNA Translation: BAA01395.1
D14720 Genomic DNA Translation: BAA03540.1 Different initiation.
L24893, L24894 Genomic DNA Translation: AAA20656.1
AK313555 mRNA Translation: BAG36330.1 Different initiation.
BT006765 mRNA Translation: AAP35411.1 Different initiation.
AL592295 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW52606.1 Different initiation.
BC006491 mRNA Translation: AAH06491.1 Different initiation.
S66705 mRNA Translation: AAB28708.1
U10018, U10017 Genomic DNA Translation: AAA18981.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1229.2 [P25189-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JH0252

NCBI Reference Sequences

More...
RefSeqi
NP_000521.2, NM_000530.7 [P25189-1]
NP_001302420.1, NM_001315491.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.591486

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000463290; ENSP00000431538; ENSG00000158887 [P25189-1]
ENST00000533357; ENSP00000432943; ENSG00000158887 [P25189-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4359

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4359

UCSC genome browser

More...
UCSCi
uc001gaf.4 human [P25189-1]

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

Inherited peripheral neuropathies mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10537 mRNA Translation: BAA01395.1
D14720 Genomic DNA Translation: BAA03540.1 Different initiation.
L24893, L24894 Genomic DNA Translation: AAA20656.1
AK313555 mRNA Translation: BAG36330.1 Different initiation.
BT006765 mRNA Translation: AAP35411.1 Different initiation.
AL592295 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW52606.1 Different initiation.
BC006491 mRNA Translation: AAH06491.1 Different initiation.
S66705 mRNA Translation: AAB28708.1
U10018, U10017 Genomic DNA Translation: AAA18981.1
CCDSiCCDS1229.2 [P25189-1]
PIRiJH0252
RefSeqiNP_000521.2, NM_000530.7 [P25189-1]
NP_001302420.1, NM_001315491.1
UniGeneiHs.591486

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N2Pmodel-A1-248[»]
3OAIX-ray2.10A/B30-150[»]
ProteinModelPortaliP25189
SMRiP25189
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110499, 2 interactors
IntActiP25189, 3 interactors
STRINGi9606.ENSP00000431538

PTM databases

GlyConnecti1526
iPTMnetiP25189
PhosphoSitePlusiP25189

Polymorphism and mutation databases

BioMutaiMPZ
DMDMi127721

Proteomic databases

MaxQBiP25189
PaxDbiP25189
PeptideAtlasiP25189
PRIDEiP25189
ProteomicsDBi54264

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4359
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000463290; ENSP00000431538; ENSG00000158887 [P25189-1]
ENST00000533357; ENSP00000432943; ENSG00000158887 [P25189-1]
GeneIDi4359
KEGGihsa:4359
UCSCiuc001gaf.4 human [P25189-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4359
DisGeNETi4359
EuPathDBiHostDB:ENSG00000158887.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MPZ
HGNCiHGNC:7225 MPZ
HPAiHPA068925
MalaCardsiMPZ
MIMi103100 phenotype
118200 phenotype
145900 phenotype
159440 gene
180800 phenotype
605253 phenotype
607677 phenotype
607736 phenotype
607791 phenotype
neXtProtiNX_P25189
OpenTargetsiENSG00000158887
Orphaneti99942 Autosomal dominant Charcot-Marie-Tooth disease type 2I
99943 Autosomal dominant Charcot-Marie-Tooth disease type 2J
100046 Autosomal dominant intermediate Charcot-Marie-Tooth disease type D
324585 Autosomal dominant intermediate Charcot-Marie-Tooth disease with neuropathic pain
101082 Charcot-Marie-Tooth disease type 1B
64748 Dejerine-Sottas syndrome
3115 Roussy-Levy syndrome
PharmGKBiPA30930

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IJG4 Eukaryota
ENOG4111R0Y LUCA
GeneTreeiENSGT00900000140913
HOGENOMiHOG000232144
HOVERGENiHBG096384
InParanoidiP25189
KOiK06770
OMAiYLIRYCW
OrthoDBiEOG091G0H91
PhylomeDBiP25189
TreeFamiTF331728

Enzyme and pathway databases

SIGNORiP25189

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Myelin_protein_zero

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

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GenomeRNAii
4359

Protein Ontology

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PROi
PR:P25189

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000158887 Expressed in 126 organ(s), highest expression level in tibial nerve
CleanExiHS_MPZ
ExpressionAtlasiP25189 baseline and differential
GenevisibleiP25189 HS

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR013106 Ig_V-set
IPR019566 Myelin-PO_C
IPR000920 Myelin_P0-rel
IPR019738 Myelin_P0_CS
IPR029869 P0
PANTHERiPTHR13869 PTHR13869, 1 hit
PTHR13869:SF7 PTHR13869:SF7, 1 hit
PfamiView protein in Pfam
PF10570 Myelin-PO_C, 1 hit
PF07686 V-set, 1 hit
PRINTSiPR00213 MYELINP0
SMARTiView protein in SMART
SM00409 IG, 1 hit
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00568 MYELIN_P0, 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 nameiMYP0_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: P25189
Secondary accession number(s): Q16072
, Q5VTH4, Q92677, Q9BR67
<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 1, 1992
Last sequence update: May 1, 1992
Last modified: December 5, 2018
This is version 208 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

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

Documents

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