LNPK
entrez
80856
canonical
uniprot
Q9C0E8
canonical
ensembl
ENSG00000144320
resolver
ensp
ENSP00000272748
resolver
ensp
ENSP00000386237
resolver
ensp
ENSP00000440905
resolver
ensp
ENSP00000644527
resolver
genesymbol
LNPK
resolver
genesymbol_syn
KIAA1715
resolver
genesymbol_syn
LNP
resolver
hgnc
HGNC:21610
resolver
uniprot
B7Z829
resolver
uniprot
B7ZLA8
resolver
uniprot
Q2M2V8
resolver
uniprot
Q2YD99
resolver
uniprot
Q658W8
resolver
uniprot
Q8N5V9
resolver
uniprot
Q96MS5
resolver
uniprot_entry
B7Z829_HUMAN
resolver
uniprot_entry
LNP_HUMAN
resolver
uniprot_sec
B7ZLA8
resolver
uniprot_sec
Q2M2V8
resolver
uniprot_sec
Q2YD99
resolver
uniprot_sec
Q658W8
resolver
uniprot_sec
Q8N5V9
resolver
uniprot_sec
Q96MS5
resolver
amino_acid_sequence
MGGLFSRWRTKPSTVEVLESIDKEIQALEEFREKNQRLQKLWVGRLILYSSVLYLFTCLIVYLWYLPDEFTARLAMTLPFFAFPLIIWSIRTVIIFFFSKRTERNNEALDDLKSQRKKILEEVMEKETYKTAKLILERFDPDSKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTPASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPPGPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAYCFFLNPARKTRPQAPRLPEFSFEKRQVVEGSSSVGPLPSGSVLSSDNQFNEESLEHDVLDDNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPELSGESLTAE
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with epilepsy and hypoplasia of the corpus callosum (NEDEHCC) [MIM:618090]: An autosomal recessive disorder characterized by severe psychomotor delay, intellectual disability, hypotonia, epilepsy, and corpus callosum hypoplasia. Some patients show mild cerebellar hypoplasia and atrophy. {ECO:0000269|PubMed:30032983}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:Q7TQ95, ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977, ECO:0000269|PubMed:30032983}.
uniprot
proteins
mass_dalton
47740
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Abolishes myristoylation. Inhibits three-way ER tubular junction formation. Does not inhibit transmembrane domain 1-induced membrane translocation."; /evidence="ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:27619977"; MUTAGEN 177; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 177; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 179; /note="T->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 179; /note="T->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 182; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 182; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 194; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 194; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 202; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 202; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 211; /note="T->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 211; /note="T->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 213; /note="T->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 213; /note="T->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 218; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 218; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 227; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 227; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 231; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 231; /note="S->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."; /evidence="ECO:0000269|PubMed:27619977"; MUTAGEN 276..301; /note="CQQCFSHNGMALKEEFEYIAFRCAYC->AQQAFSHNGMALKEEFEYIAFRAAYA: No change in N-myristoylation. Inhibits three-way ER tubular junction formation."; /evidence="ECO:0000269|PubMed:24223779
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000269|PubMed:24223779}.; PTM: 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). {ECO:0000269|PubMed:27619977}.; PTM: Subject to proteasomal degradation following phosphorylation during mitosis (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
uniprot
proteins
protein_family
Lunapark family
uniprot
proteins
pubmed
11214970
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20213681
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22729086
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24223779
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25404289
uniprot
proteins
pubmed
25548161
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27619977
uniprot
proteins
pubmed
30032983
uniprot
proteins
sequence_length
428
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977}; Multi-pass membrane protein {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779}; Cytoplasmic side {ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25548161}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network (PubMed:22729086, PubMed:24223779, PubMed:25404289, PubMed:25548161, PubMed:27619977). {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977}.
uniprot
proteins
transmembrane_region
TRANSMEM 46..66; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 78..98; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins