Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 139 (02 Dec 2020)
Sequence version 2 (05 Sep 2006)
Previous versions | rss
Add a publicationFeedback
Protein

Endoplasmic reticulum junction formation protein lunapark

Gene

LNPK

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

Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology (PubMed:30032983). Involved in the stabilization of nascent three-way ER tubular junctions within the ER network (PubMed:24223779, PubMed:25404289, PubMed:25548161, PubMed:27619977). May also play a role as a curvature-stabilizing protein within the three-way ER tubular junction network (PubMed:25404289). May be involved in limb development (By similarity). Is involved in central nervous system development (PubMed:30032983).By similarity5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri276 – 301C4-type; plays a role in ER morphology2 PublicationsAdd BLAST26

<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

  • identical protein binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Molecular functionDevelopmental protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q9C0E8

Protein family/group databases

Transport Classification Database

More...
TCDBi
9.B.390.1.1, the tmcc/tex28 (tm-tex) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
Endoplasmic reticulum junction formation protein lunaparkCurated
Alternative name(s):
ER junction formation factor lunaparkImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:LNPKImported
Synonyms:KIAA1715Imported, LNP
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 2

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...
EuPathDBi
HostDB:ENSG00000144320.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:21610, LNPK

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
610236, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9C0E8

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 domaini2 – 45Cytoplasmic1 PublicationAdd BLAST44
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei46 – 66HelicalSequence analysisAdd BLAST21
Topological domaini67 – 77Lumenal1 PublicationAdd BLAST11
Transmembranei78 – 98HelicalSequence analysisAdd BLAST21
Topological domaini99 – 428Cytoplasmic2 PublicationsAdd BLAST330

Keywords - Cellular componenti

Endoplasmic reticulum, 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

Neurodevelopmental disorder with epilepsy and hypoplasia of the corpus callosum (NEDEHCC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by severe psychomotor delay, intellectual disability, hypotonia, epilepsy, and corpus callosum hypoplasia. Some patients show mild cerebellar hypoplasia and atrophy.
Related information in OMIM
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_081176251 – 428Missing in NEDEHCC. 1 PublicationAdd BLAST178

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi2G → A: Abolishes myristoylation. Inhibits three-way ER tubular junction formation. Does not inhibit transmembrane domain 1-induced membrane translocation. 2 Publications1
Mutagenesisi177S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi177S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi179T → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi179T → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi182S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi182S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi194S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi194S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi202S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi202S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi211T → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi211T → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi213T → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi213T → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi218S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231. 1 Publication1
Mutagenesisi218S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231. 1 Publication1
Mutagenesisi227S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231. 1 Publication1
Mutagenesisi227S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231. 1 Publication1
Mutagenesisi231S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227. 1 Publication1
Mutagenesisi231S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227. 1 Publication1
Mutagenesisi276 – 301CQQCF…RCAYC → AQQAFSHNGMALKEEFEYIA FRAAYA: No change in N-myristoylation. Inhibits three-way ER tubular junction formation. 1 PublicationAdd BLAST26

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
80856

MalaCards human disease database

More...
MalaCardsi
LNPK
MIMi618090, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000144320

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134938939

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9C0E8, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
LNPK

Domain mapping of disease mutations (DMDM)

More...
DMDMi
114149979

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002483102 – 428Endoplasmic reticulum junction formation protein lunaparkAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine2 Publications1
<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 residuei114Phosphoserine1 Publication1
Modified residuei153Phosphoserine1 Publication1
Modified residuei177PhosphoserineCombined sources1 Publication1
Modified residuei182PhosphoserineCombined sources1 Publication1
Modified residuei194PhosphoserineCombined sources1 Publication1
Modified residuei211Phosphothreonine1 Publication1
Modified residuei213PhosphothreonineCombined sources1
Modified residuei217PhosphoserineCombined sources1 Publication1
Modified residuei227Phosphoserine1 Publication1
Modified residuei321PhosphoserineCombined sources1 Publication1
Modified residuei353Phosphoserine1 Publication1
Modified residuei384PhosphoserineCombined sources1 Publication1
Modified residuei414PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Myristoylated; myristoylation is necessary for the endoplasmic reticulum (ER) three-way ER tubular junction formation, but is not required neither for membrane translocation, membrane topology formation, nor for the specific localization to ER membranes (PubMed:24223779).1 Publication
Phosphorylated. Phosphorylation occurs at Ser-177, Ser-182, Ser-217, Ser-227, Ser-321 and Ser-384 during interphase (PubMed:27619977). Phosphorylation occurs at Ser-114, Ser-153, Ser-194, Thr-211 and Ser-353 during mitosis; these phosphorylations reduce both its homodimerization and the ER three-way tubular junction formation (PubMed:27619977).1 Publication
Subject to proteasomal degradation following phosphorylation during mitosis (PubMed:27619977).1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-1616

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9C0E8

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9C0E8

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q9C0E8

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9C0E8

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

More...
PaxDbi
Q9C0E8

PeptideAtlas

More...
PeptideAtlasi
Q9C0E8

PRoteomics IDEntifications database

More...
PRIDEi
Q9C0E8

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
7218
80023 [Q9C0E8-1]
80024 [Q9C0E8-2]
80025 [Q9C0E8-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9C0E8

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

More...
PhosphoSitePlusi
Q9C0E8

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9C0E8

<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 neural precursor cells, where it is detected at the growth-cone-like structure and branching sites of neurite-like processes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000144320, Expressed in calcaneal tendon and 216 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9C0E8, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9C0E8, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000144320, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; homodimerization requires the C4-type zinc finger motif and decreases during mitosis in a phosphorylation-dependent manner (PubMed:27619977).

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
123333, 72 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q9C0E8

Protein interaction database and analysis system

More...
IntActi
Q9C0E8, 44 interactors

Molecular INTeraction database

More...
MINTi
Q9C0E8

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000272748

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9C0E8, protein

<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

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

More...
SMRi
Q9C0E8

Database of comparative protein structure models

More...
ModBasei
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

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili16 – 41Sequence analysisAdd BLAST26
Coiled coili102 – 128Sequence analysisAdd BLAST27

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 biasi178 – 250Pro-richAdd BLAST73

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

The transmembrane domain 1 and 2 function as a signal-anchor and stop-transfer sequence, respectively, generating a double-spanning integral membrane protein with a N- and C-terminal cytoplasmic orientation (PubMed:24223779). Transmembrane domain 1 and 2 are probably sufficient to mediate membrane translocation and topology formation in a N-myristoylation-independent manner (PubMed:24223779). Transmembrane domain 2 is sufficient to block the protein secretion pathway (PubMed:24223779). The two coiled-coil domains are necessary for its endoplasmic reticulum (ER) three-way tubular junction localization (PubMed:27619977). The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation (PubMed:24223779, PubMed:27619977).2 Publications

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

Belongs to the lunapark family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri276 – 301C4-type; plays a role in ER morphology2 PublicationsAdd BLAST26

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2846, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000001859

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_036951_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9C0E8

Identification of Orthologs from Complete Genome Data

More...
OMAi
TAPKNRI

Database of Orthologous Groups

More...
OrthoDBi
1595535at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9C0E8

TreeFam database of animal gene trees

More...
TreeFami
TF315086

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR040115, Lnp
IPR019273, Lunapark_dom

The PANTHER Classification System

More...
PANTHERi
PTHR22166, PTHR22166, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10058, zinc_ribbon_10, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 4 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: Q9C0E8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS
60 70 80 90 100
SVLYLFTCLI VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK
110 120 130 140 150
RTERNNEALD DLKSQRKKIL EEVMEKETYK TAKLILERFD PDSKKAKECE
160 170 180 190 200
PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP ASPNQGPPPQ VPVSPGPPKD
210 220 230 240 250
SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP GPPLARPILP
260 270 280 290 300
RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY
310 320 330 340 350
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN
360 370 380 390 400
EESLEHDVLD DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA
410 420
SVIETNSTVP GADSIPDPEL SGESLTAE
Length:428
Mass (Da):47,740
Last modified:September 5, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF5BBA4186C2691BF
GO
Isoform 2 (identifier: Q9C0E8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MGGLFSRWR → MEGK

Show »
Length:423
Mass (Da):47,094
Checksum:iCAF46E3EB956B8BC
GO
Isoform 3 (identifier: Q9C0E8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Show »
Length:305
Mass (Da):33,001
Checksum:i2FDFED2CFE7C83EC
GO
Isoform 4 (identifier: Q9C0E8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     235-235: M → MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT

Show »
Length:459
Mass (Da):50,848
Checksum:i367198608E69DDF1
GO

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

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JL94C9JL94_HUMAN
Endoplasmic reticulum junction form...
LNPK
114Annotation 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>
C9JM95C9JM95_HUMAN
Endoplasmic reticulum junction form...
LNPK
83Annotation 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>
H7BZA1H7BZA1_HUMAN
Endoplasmic reticulum junction form...
LNPK
69Annotation 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 BAB21806 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti262Y → H in BAB71207 (PubMed:14702039).Curated1
Sequence conflicti374E → G in AAH31530 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081176251 – 428Missing in NEDEHCC. 1 PublicationAdd BLAST178

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0202381 – 123Missing in isoform 3. 1 PublicationAdd BLAST123
Alternative sequenceiVSP_0202391 – 9MGGLFSRWR → MEGK in isoform 2. 1 Publication9
Alternative sequenceiVSP_054427235M → MEMGLPHIAQAGLEHLSSSD LSTSTSQSAGIT in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB051502 mRNA Translation: BAB21806.1 Different initiation.
AK056532 mRNA Translation: BAB71207.1
AC016751 Genomic DNA No translation available.
AC016915 Genomic DNA No translation available.
BC031530 mRNA Translation: AAH31530.1
BC105132 mRNA Translation: AAI05133.1
BC105134 mRNA Translation: AAI05135.1
BC110329 mRNA Translation: AAI10330.1
BC143681 mRNA Translation: AAI43682.1
AL832947 mRNA Translation: CAH56306.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS33332.1 [Q9C0E8-1]
CCDS77488.1 [Q9C0E8-3]
CCDS77489.1 [Q9C0E8-4]

NCBI Reference Sequences

More...
RefSeqi
NP_001291937.1, NM_001305008.1
NP_001291938.1, NM_001305009.1 [Q9C0E8-4]
NP_001291940.1, NM_001305011.1 [Q9C0E8-3]
NP_085153.1, NM_030650.2 [Q9C0E8-1]
XP_006712846.1, XM_006712783.2 [Q9C0E8-1]
XP_016860544.1, XM_017005055.1 [Q9C0E8-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000272748; ENSP00000272748; ENSG00000144320 [Q9C0E8-1]
ENST00000409660; ENSP00000386237; ENSG00000144320 [Q9C0E8-3]
ENST00000544803; ENSP00000440905; ENSG00000144320 [Q9C0E8-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
80856

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:80856

UCSC genome browser

More...
UCSCi
uc002ukc.2, human [Q9C0E8-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AB051502 mRNA Translation: BAB21806.1 Different initiation.
AK056532 mRNA Translation: BAB71207.1
AC016751 Genomic DNA No translation available.
AC016915 Genomic DNA No translation available.
BC031530 mRNA Translation: AAH31530.1
BC105132 mRNA Translation: AAI05133.1
BC105134 mRNA Translation: AAI05135.1
BC110329 mRNA Translation: AAI10330.1
BC143681 mRNA Translation: AAI43682.1
AL832947 mRNA Translation: CAH56306.1
CCDSiCCDS33332.1 [Q9C0E8-1]
CCDS77488.1 [Q9C0E8-3]
CCDS77489.1 [Q9C0E8-4]
RefSeqiNP_001291937.1, NM_001305008.1
NP_001291938.1, NM_001305009.1 [Q9C0E8-4]
NP_001291940.1, NM_001305011.1 [Q9C0E8-3]
NP_085153.1, NM_030650.2 [Q9C0E8-1]
XP_006712846.1, XM_006712783.2 [Q9C0E8-1]
XP_016860544.1, XM_017005055.1 [Q9C0E8-3]

3D structure databases

SMRiQ9C0E8
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi123333, 72 interactors
ELMiQ9C0E8
IntActiQ9C0E8, 44 interactors
MINTiQ9C0E8
STRINGi9606.ENSP00000272748

Protein family/group databases

TCDBi9.B.390.1.1, the tmcc/tex28 (tm-tex) family

PTM databases

iPTMnetiQ9C0E8
PhosphoSitePlusiQ9C0E8
SwissPalmiQ9C0E8

Polymorphism and mutation databases

BioMutaiLNPK
DMDMi114149979

Proteomic databases

CPTACiCPTAC-1616
EPDiQ9C0E8
jPOSTiQ9C0E8
MassIVEiQ9C0E8
MaxQBiQ9C0E8
PaxDbiQ9C0E8
PeptideAtlasiQ9C0E8
PRIDEiQ9C0E8
ProteomicsDBi7218
80023 [Q9C0E8-1]
80024 [Q9C0E8-2]
80025 [Q9C0E8-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3018, 17 antibodies

Genome annotation databases

EnsembliENST00000272748; ENSP00000272748; ENSG00000144320 [Q9C0E8-1]
ENST00000409660; ENSP00000386237; ENSG00000144320 [Q9C0E8-3]
ENST00000544803; ENSP00000440905; ENSG00000144320 [Q9C0E8-4]
GeneIDi80856
KEGGihsa:80856
UCSCiuc002ukc.2, human [Q9C0E8-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
80856
DisGeNETi80856
EuPathDBiHostDB:ENSG00000144320.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
LNPK
HGNCiHGNC:21610, LNPK
HPAiENSG00000144320, Low tissue specificity
MalaCardsiLNPK
MIMi610236, gene
618090, phenotype
neXtProtiNX_Q9C0E8
OpenTargetsiENSG00000144320
PharmGKBiPA134938939

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2846, Eukaryota
GeneTreeiENSGT00390000001859
HOGENOMiCLU_036951_0_0_1
InParanoidiQ9C0E8
OMAiTAPKNRI
OrthoDBi1595535at2759
PhylomeDBiQ9C0E8
TreeFamiTF315086

Enzyme and pathway databases

PathwayCommonsiQ9C0E8

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
80856, 4 hits in 845 CRISPR screens

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

More...
ChiTaRSi
LNPK, human

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

More...
GenomeRNAii
80856
PharosiQ9C0E8, Tbio

Protein Ontology

More...
PROi
PR:Q9C0E8
RNActiQ9C0E8, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000144320, Expressed in calcaneal tendon and 216 other tissues
ExpressionAtlasiQ9C0E8, baseline and differential
GenevisibleiQ9C0E8, HS

Family and domain databases

InterProiView protein in InterPro
IPR040115, Lnp
IPR019273, Lunapark_dom
PANTHERiPTHR22166, PTHR22166, 1 hit
PfamiView protein in Pfam
PF10058, zinc_ribbon_10, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLNP_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: Q9C0E8
Secondary accession number(s): B7ZLA8
, Q2M2V8, Q2YD99, Q658W8, Q8N5V9, Q96MS5
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: December 2, 2020
This is version 139 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Reference proteome

Documents

  1. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 2
    Human chromosome 2: 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again