Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Endoplasmic reticulum junction formation protein lunapark (ER junction formation factor lunapark)

 LNP_HUMAN               Reviewed;         428 AA.
Q9C0E8; B7ZLA8; Q2M2V8; Q2YD99; Q658W8; Q8N5V9; Q96MS5;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000305};
AltName: Full=ER junction formation factor lunapark {ECO:0000312|HGNC:HGNC:21610};
Name=LNPK {ECO:0000312|HGNC:HGNC:21610};
Synonyms=KIAA1715 {ECO:0000312|HGNC:HGNC:21610}, LNP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Adrenal cortex, and Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-428.
TISSUE=Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-194 AND
SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
MYRISTOYLATION AT GLY-2.
PubMed=20213681; DOI=10.1002/pmic.200900783;
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
Tsunasawa S., Utsumi T.;
"Strategy for comprehensive identification of human N-myristoylated
proteins using an insect cell-free protein synthesis system.";
Proteomics 10:1780-1793(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182 AND
SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
SUBCELLULAR LOCATION.
PubMed=22729086; DOI=10.1038/ncb2523;
Chen S., Novick P., Ferro-Novick S.;
"ER network formation requires a balance of the dynamin-like GTPase
Sey1p and the Lunapark family member Lnp1p.";
Nat. Cell Biol. 14:707-716(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; THR-213 AND
SER-217, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MYRISTOYLATION AT GLY-2,
CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY,
MUTAGENESIS OF GLY-2 AND 276-CYS--CYS-301, AND MEMBRANE INTEGRATION
TARGETING SEQUENCE.
PubMed=24223779; DOI=10.1371/journal.pone.0078235;
Moriya K., Nagatoshi K., Noriyasu Y., Okamura T., Takamitsu E.,
Suzuki T., Utsumi T.;
"Protein N-myristoylation plays a critical role in the endoplasmic
reticulum morphological change induced by overexpression of protein
Lunapark, an integral membrane protein of the endoplasmic reticulum.";
PLoS ONE 8:E78235-E78235(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-217 AND
SER-384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25404289; DOI=10.1073/pnas.1419997111;
Shemesh T., Klemm R.W., Romano F.B., Wang S., Vaughan J., Zhuang X.,
Tukachinsky H., Kozlov M.M., Rapoport T.A.;
"A model for the generation and interconversion of ER morphologies.";
Proc. Natl. Acad. Sci. U.S.A. 111:E5243-E5251(2014).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=25548161; DOI=10.1073/pnas.1423026112;
Chen S., Desai T., McNew J.A., Gerard P., Novick P.J.,
Ferro-Novick S.;
"Lunapark stabilizes nascent three-way junctions in the endoplasmic
reticulum.";
Proc. Natl. Acad. Sci. U.S.A. 112:418-423(2015).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-114; SER-153; SER-177;
SER-182; SER-194; THR-211; SER-217; SER-227; SER-321; SER-353 AND
SER-384, PROTEASOMAL DEGRADATION, MUTAGENESIS OF GLY-2; SER-177;
THR-179; SER-182; SER-194; SER-202; THR-211; THR-213; SER-218; SER-227
AND SER-231, DOMAIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=27619977; DOI=10.7554/eLife.18605;
Wang S., Tukachinsky H., Romano F.B., Rapoport T.A.;
"Cooperation of the ER-shaping proteins atlastin, lunapark, and
reticulons to generate a tubular membrane network.";
Elife 5:0-0(2016).
-!- FUNCTION: Endoplasmic reticulum (ER)-shaping membrane protein that
plays a role in determining ER morphology. 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 and central nervous
system development (By similarity). {ECO:0000250|UniProtKB:Q7TQ95,
ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289,
ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977}.
-!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc
finger motif and decreases during mitosis in a phosphorylation-
dependent manner (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
-!- INTERACTION:
Q53G59:KLHL12; NbExp=4; IntAct=EBI-11024283, EBI-740929;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9C0E8-1; Sequence=Displayed;
Name=2;
IsoId=Q9C0E8-2; Sequence=VSP_020239;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9C0E8-3; Sequence=VSP_020238;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9C0E8-4; Sequence=VSP_054427;
Note=No experimental confirmation available.;
-!- DOMAIN: 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). {ECO:0000269|PubMed:24223779,
ECO:0000269|PubMed:27619977}.
-!- 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}.
-!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB21806.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB051502; BAB21806.1; ALT_INIT; mRNA.
EMBL; AK056532; BAB71207.1; -; mRNA.
EMBL; AC016751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031530; AAH31530.1; -; mRNA.
EMBL; BC105132; AAI05133.1; -; mRNA.
EMBL; BC105134; AAI05135.1; -; mRNA.
EMBL; BC110329; AAI10330.1; -; mRNA.
EMBL; BC143681; AAI43682.1; -; mRNA.
EMBL; AL832947; CAH56306.1; -; mRNA.
CCDS; CCDS33332.1; -. [Q9C0E8-1]
CCDS; CCDS77488.1; -. [Q9C0E8-3]
CCDS; CCDS77489.1; -. [Q9C0E8-4]
RefSeq; NP_001291937.1; NM_001305008.1.
RefSeq; NP_001291938.1; NM_001305009.1. [Q9C0E8-4]
RefSeq; NP_001291940.1; NM_001305011.1. [Q9C0E8-3]
RefSeq; NP_085153.1; NM_030650.2. [Q9C0E8-1]
RefSeq; XP_006712846.1; XM_006712783.2. [Q9C0E8-1]
RefSeq; XP_016860544.1; XM_017005055.1. [Q9C0E8-3]
UniGene; Hs.209561; -.
ProteinModelPortal; Q9C0E8; -.
SMR; Q9C0E8; -.
BioGrid; 123333; 39.
ELM; Q9C0E8; -.
IntAct; Q9C0E8; 19.
STRING; 9606.ENSP00000272748; -.
iPTMnet; Q9C0E8; -.
PhosphoSitePlus; Q9C0E8; -.
BioMuta; LNP; -.
DMDM; 114149979; -.
EPD; Q9C0E8; -.
MaxQB; Q9C0E8; -.
PaxDb; Q9C0E8; -.
PeptideAtlas; Q9C0E8; -.
PRIDE; Q9C0E8; -.
Ensembl; ENST00000272748; ENSP00000272748; ENSG00000144320. [Q9C0E8-1]
Ensembl; ENST00000409660; ENSP00000386237; ENSG00000144320. [Q9C0E8-3]
Ensembl; ENST00000544803; ENSP00000440905; ENSG00000144320. [Q9C0E8-4]
GeneID; 80856; -.
KEGG; hsa:80856; -.
UCSC; uc002ukc.2; human. [Q9C0E8-1]
CTD; 80856; -.
DisGeNET; 80856; -.
EuPathDB; HostDB:ENSG00000144320.13; -.
GeneCards; LNPK; -.
HGNC; HGNC:21610; LNPK.
HPA; HPA014205; -.
MIM; 610236; gene.
neXtProt; NX_Q9C0E8; -.
OpenTargets; ENSG00000144320; -.
PharmGKB; PA134938939; -.
eggNOG; KOG2846; Eukaryota.
eggNOG; ENOG4111I2R; LUCA.
GeneTree; ENSGT00390000001859; -.
HOGENOM; HOG000231891; -.
HOVERGEN; HBG079498; -.
InParanoid; Q9C0E8; -.
OMA; KECEPPS; -.
OrthoDB; EOG091G0IRW; -.
PhylomeDB; Q9C0E8; -.
TreeFam; TF315086; -.
ChiTaRS; KIAA1715; human.
GenomeRNAi; 80856; -.
PMAP-CutDB; Q9C0E8; -.
PRO; PR:Q9C0E8; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000144320; -.
CleanEx; HS_KIAA1715; -.
ExpressionAtlas; Q9C0E8; baseline and differential.
Genevisible; Q9C0E8; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IDA:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; IMP:UniProtKB.
GO; GO:0060173; P:limb development; NAS:UniProtKB.
GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; IMP:UniProtKB.
GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
InterPro; IPR019273; Lunapark_dom.
Pfam; PF10058; zinc_ribbon_10; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Developmental protein; Endoplasmic reticulum; Lipoprotein; Membrane;
Metal-binding; Myristate; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20213681,
ECO:0000269|PubMed:24223779}.
CHAIN 2 428 Endoplasmic reticulum junction formation
protein lunapark.
/FTId=PRO_0000248310.
TOPO_DOM 2 45 Cytoplasmic.
{ECO:0000269|PubMed:24223779}.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TOPO_DOM 67 77 Lumenal. {ECO:0000269|PubMed:24223779}.
TRANSMEM 78 98 Helical. {ECO:0000255}.
TOPO_DOM 99 428 Cytoplasmic.
{ECO:0000269|PubMed:24223779,
ECO:0000269|PubMed:25548161}.
ZN_FING 276 301 C4-type; plays a role in ER morphology.
{ECO:0000269|PubMed:24223779,
ECO:0000269|PubMed:27619977}.
COILED 16 41 {ECO:0000255}.
COILED 102 128 {ECO:0000255}.
COMPBIAS 178 250 Pro-rich.
MOD_RES 114 114 Phosphoserine.
{ECO:0000269|PubMed:27619977}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000269|PubMed:27619977}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:27619977}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:27619977}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:27619977}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000269|PubMed:27619977}.
MOD_RES 213 213 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:27619977}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000269|PubMed:27619977}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:27619977}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000269|PubMed:27619977}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:27619977}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:20213681,
ECO:0000269|PubMed:24223779}.
VAR_SEQ 1 123 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020238.
VAR_SEQ 1 9 MGGLFSRWR -> MEGK (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_020239.
VAR_SEQ 235 235 M -> MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054427.
MUTAGEN 2 2 G->A: Abolishes myristoylation. Inhibits
three-way ER tubular junction formation.
Does not inhibit transmembrane domain 1-
induced membrane translocation.
{ECO:0000269|PubMed:24223779,
ECO:0000269|PubMed:27619977}.
MUTAGEN 177 177 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 177 177 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 179 179 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 179 179 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 182 182 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 182 182 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 194 194 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 194 194 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 202 202 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 202 202 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 211 211 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 211 211 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 213 213 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 213 213 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 218 218 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 218 218 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 227 227 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 227 227 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 231 231 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.
{ECO:0000269|PubMed:27619977}.
MUTAGEN 231 231 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. {ECO:0000269|PubMed:27619977}.
MUTAGEN 276 301 CQQCFSHNGMALKEEFEYIAFRCAYC->AQQAFSHNGMALK
EEFEYIAFRAAYA: No change in N-
myristoylation. Inhibits three-way ER
tubular junction formation.
{ECO:0000269|PubMed:24223779}.
CONFLICT 262 262 Y -> H (in Ref. 2; BAB71207).
{ECO:0000305}.
CONFLICT 374 374 E -> G (in Ref. 4; AAH31530).
{ECO:0000305}.
SEQUENCE 428 AA; 47740 MW; F5BBA4186C2691BF CRC64;
MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS SVLYLFTCLI
VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK RTERNNEALD DLKSQRKKIL
EEVMEKETYK TAKLILERFD PDSKKAKECE PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP
ASPNQGPPPQ VPVSPGPPKD SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP
GPPLARPILP RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN EESLEHDVLD
DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA SVIETNSTVP GADSIPDPEL
SGESLTAE


Related products :

Catalog number Product name Quantity
29-815 OCLN is an integral membrane protein which is located at tight junctions. This protein may be involved in the formation and maintenance of the tight junction. The possibility of several alternatively 0.1 mg
26-765 MPP7 acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. MPP7 is involved in the assembly of protein complexes at sites of c 0.05 mg
26-631 Protein disulfide isomerases, such as PDIA6, are endoplasmic reticulum (ER) resident proteins that catalyze formation, reduction, and isomerization of disulfide bonds in proteins and are thought to pl 0.05 mg
25-373 Connexins, such as GJA9, are involved in the formation of gap junctions, intercellular conduits that directly connect the cytoplasms of contacting cells. Each gap junction channel is formed by docking 0.05 mg
EIAAB10183 Connexin-31.9,Cx31.9,Gap junction alpha-11 protein,Gap junction chi-1 protein,Gap junction delta-3 protein,GJA11,GJC1,GJD3,Homo sapiens,Human
EIAAB10182 Connexin-30.2,Cx30.2,Gap junction alpha-11 protein,Gap junction chi-1 protein,Gap junction delta-3 protein,Gja11,Gjc1,Gjd3,Mouse,Mus musculus
G3625 Protein lunapark (KIAA1715), Human, ELISA Kit 96T
CSB-EL012283HU Human Protein lunapark(KIAA1715) ELISA kit 96T
CSB-EL012283HU Human Protein lunapark(KIAA1715) ELISA kit SpeciesHuman 96T
LNP_HUMAN ELISA Kit FOR Protein lunapark; organism: Human; gene name: LNP 96T
LNP_MOUSE ELISA Kit FOR Protein lunapark; organism: Mouse; gene name: Lnp 96T
26-827 MLF1 is involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. It interferes with erythopoietin-induced erythroid termina 0.05 mg
E4864h Human Lunapark ELISA Kit 96T
EIAAB10198 Connexin-47,Cx47,Gap junction alpha-12 protein,Gap junction gamma-2 protein,Gja12,Gjc2,Mouse,Mus musculus
EIAAB10178 Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,Gja9,Gjd2,Rat,Rattus norvegicus
EIAAB10195 Connexin-47,Cx47,Gap junction alpha-12 protein,Gap junction gamma-2 protein,Gja12,Gjc2,Rat,Rattus norvegicus
EIAAB10179 Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,Gja9,Gjd2,Mouse,Mus musculus
EIAAB10181 Bos taurus,Bovine,Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,GJA9,GJD2
EIAAB10188 Connexin-45,Cx45,Cxn-45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,Gja7,Gjc1,Mouse,Mus musculus
EIAAB10189 Connexin-45,Cx45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,Gja7,Gjc1,Rat,Rattus norvegicus
EIAAB10191 Connexin-45,Cx45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,GJA7,GJC1,Homo sapiens,Human
EIAAB10109 Connexin-43,Cx43,Gap junction 43 kDa heart protein,Gap junction alpha-1 protein,GJA1,GJAL,Homo sapiens,Human
EIAAB10180 Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,GJA9,GJD2,Homo sapiens,Human
EIAAB10190 Connexin-45,Cx45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,GJA7,GJC1,Pig,Sus scrofa
EIAAB10113 Connexin-43,Cx43,Cxn-43,Gap junction 43 kDa heart protein,Gap junction alpha-1 protein,Gja1,Rat,Rattus norvegicus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur