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Q9C0E8

- LNP_HUMAN

UniProt

Q9C0E8 - LNP_HUMAN

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Protein

Protein lunapark

Gene

LNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in tubular endoplasmic reticulum network formation and maintenance. May be involved in limb and central nervous system development.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri276 – 30126C4-type; plays a role in ER morphologyBy similarityAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: Ensembl
  2. embryonic digit morphogenesis Source: Ensembl
  3. embryonic forelimb morphogenesis Source: Ensembl
  4. limb development Source: UniProtKB
  5. regulation of chondrocyte differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lunapark
Gene namesi
Name:LNP
Synonyms:KIAA1715
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:21610. KIAA1715.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Localizes to three-way ER tubule junctions.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 4544CytoplasmicBy similarityAdd
BLAST
Transmembranei46 – 6621HelicalSequence AnalysisAdd
BLAST
Topological domaini67 – 7711LumenalBy similarityAdd
BLAST
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Topological domaini99 – 428330CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: MGI
  2. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134938939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 428427Protein lunaparkPRO_0000248310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine2 Publications
Modified residuei194 – 1941Phosphoserine2 Publications
Modified residuei321 – 3211Phosphoserine1 Publication
Modified residuei414 – 4141PhosphoserineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ9C0E8.
PaxDbiQ9C0E8.
PRIDEiQ9C0E8.

PTM databases

PhosphoSiteiQ9C0E8.

Miscellaneous databases

PMAP-CutDBQ9C0E8.

Expressioni

Gene expression databases

BgeeiQ9C0E8.
CleanExiHS_KIAA1715.
ExpressionAtlasiQ9C0E8. baseline and differential.
GenevestigatoriQ9C0E8.

Organism-specific databases

HPAiHPA014205.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CHMP1AQ9HD421EBI-1047206,EBI-1057156

Protein-protein interaction databases

BioGridi123333. 13 interactions.
STRINGi9606.ENSP00000272748.

Structurei

3D structure databases

ProteinModelPortaliQ9C0E8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili16 – 4126Sequence AnalysisAdd
BLAST
Coiled coili102 – 12827Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi178 – 25073Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the lunapark family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri276 – 30126C4-type; plays a role in ER morphologyBy similarityAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG115207.
GeneTreeiENSGT00390000001859.
HOGENOMiHOG000231891.
HOVERGENiHBG079498.
InParanoidiQ9C0E8.
OrthoDBiEOG7ZSHTN.
PhylomeDBiQ9C0E8.
TreeFamiTF315086.

Family and domain databases

InterProiIPR019273. DUF2296.
[Graphical view]
PfamiPF10058. DUF2296. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9C0E8-1) [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
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
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

Note: No experimental confirmation available.

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.

Note: No experimental confirmation available.

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

Note: No experimental confirmation available.

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

Sequence cautioni

The sequence BAB21806.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621Y → H in BAB71207. (PubMed:14702039)Curated
Sequence conflicti374 – 3741E → G in AAH31530. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 123123Missing in isoform 3. 1 PublicationVSP_020238Add
BLAST
Alternative sequencei1 – 99MGGLFSRWR → MEGK in isoform 2. 1 PublicationVSP_020239
Alternative sequencei235 – 2351M → MEMGLPHIAQAGLEHLSSSD LSTSTSQSAGIT in isoform 4. 1 PublicationVSP_054427

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]
RefSeqiNP_085153.1. NM_030650.1. [Q9C0E8-1]
XP_006712846.1. XM_006712783.1. [Q9C0E8-1]
UniGeneiHs.209561.

Genome annotation databases

EnsembliENST00000272748; ENSP00000272748; ENSG00000144320. [Q9C0E8-1]
ENST00000409660; ENSP00000386237; ENSG00000144320. [Q9C0E8-3]
ENST00000544803; ENSP00000440905; ENSG00000144320. [Q9C0E8-4]
GeneIDi80856.
KEGGihsa:80856.
UCSCiuc002ukc.1. human. [Q9C0E8-1]
uc010fqw.1. human. [Q9C0E8-2]
uc010zer.1. human.

Polymorphism databases

DMDMi114149979.

Keywords - Coding sequence diversityi

Alternative splicing

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 .
CCDSi CCDS33332.1. [Q9C0E8-1 ]
RefSeqi NP_085153.1. NM_030650.1. [Q9C0E8-1 ]
XP_006712846.1. XM_006712783.1. [Q9C0E8-1 ]
UniGenei Hs.209561.

3D structure databases

ProteinModelPortali Q9C0E8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123333. 13 interactions.
STRINGi 9606.ENSP00000272748.

PTM databases

PhosphoSitei Q9C0E8.

Polymorphism databases

DMDMi 114149979.

Proteomic databases

MaxQBi Q9C0E8.
PaxDbi Q9C0E8.
PRIDEi Q9C0E8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000272748 ; ENSP00000272748 ; ENSG00000144320 . [Q9C0E8-1 ]
ENST00000409660 ; ENSP00000386237 ; ENSG00000144320 . [Q9C0E8-3 ]
ENST00000544803 ; ENSP00000440905 ; ENSG00000144320 . [Q9C0E8-4 ]
GeneIDi 80856.
KEGGi hsa:80856.
UCSCi uc002ukc.1. human. [Q9C0E8-1 ]
uc010fqw.1. human. [Q9C0E8-2 ]
uc010zer.1. human.

Organism-specific databases

CTDi 80856.
GeneCardsi GC02M176788.
HGNCi HGNC:21610. KIAA1715.
HPAi HPA014205.
MIMi 610236. gene.
neXtProti NX_Q9C0E8.
PharmGKBi PA134938939.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG115207.
GeneTreei ENSGT00390000001859.
HOGENOMi HOG000231891.
HOVERGENi HBG079498.
InParanoidi Q9C0E8.
OrthoDBi EOG7ZSHTN.
PhylomeDBi Q9C0E8.
TreeFami TF315086.

Miscellaneous databases

ChiTaRSi KIAA1715. human.
GenomeRNAii 80856.
NextBioi 35481258.
PMAP-CutDB Q9C0E8.
PROi Q9C0E8.
SOURCEi Search...

Gene expression databases

Bgeei Q9C0E8.
CleanExi HS_KIAA1715.
ExpressionAtlasi Q9C0E8. baseline and differential.
Genevestigatori Q9C0E8.

Family and domain databases

InterProi IPR019273. DUF2296.
[Graphical view ]
Pfami PF10058. DUF2296. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Adrenal cortex and Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-428.
    Tissue: Stomach.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-194 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p."
    Chen S., Novick P., Ferro-Novick S.
    Nat. Cell Biol. 14:707-716(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLNP_HUMAN
AccessioniPrimary (citable) accession number: Q9C0E8
Secondary accession number(s): B7ZLA8
, Q2M2V8, Q2YD99, Q658W8, Q8N5V9, Q96MS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: November 26, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3