LNP_HUMAN - dbPTM
LNP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LNP_HUMAN
UniProt AC Q9C0E8
Protein Name Endoplasmic reticulum junction formation protein lunapark {ECO:0000305}
Gene Name LNPK {ECO:0000312|HGNC:HGNC:21610}
Organism Homo sapiens (Human).
Sequence Length 428
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein
Cytoplasmic side . Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network (PubMed:22729086, Pu
Protein Description 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]
Protein Sequence MGGLFSRWRTKPSTVEVLESIDKEIQALEEFREKNQRLQKLWVGRLILYSSVLYLFTCLIVYLWYLPDEFTARLAMTLPFFAFPLIIWSIRTVIIFFFSKRTERNNEALDDLKSQRKKILEEVMEKETYKTAKLILERFDPDSKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTPASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPPGPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAYCFFLNPARKTRPQAPRLPEFSFEKRQVVEGSSSVGPLPSGSVLSSDNQFNEESLEHDVLDDNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPELSGESLTAE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2N-myristoyl glycine------MGGLFSRWR
------CCCCCCCCC		41.32-
2Myristoylation------MGGLFSRWR
------CCCCCCCCC		41.3224223779
10PhosphorylationGLFSRWRTKPSTVEV
CCCCCCCCCCCHHHH		40.1123312004
13PhosphorylationSRWRTKPSTVEVLES
CCCCCCCCHHHHHHH		46.7923312004
14PhosphorylationRWRTKPSTVEVLESI
CCCCCCCHHHHHHHH		29.2523312004
113UbiquitinationNEALDDLKSQRKKIL
HHHHHHHHHHHHHHH		52.08-
114PhosphorylationEALDDLKSQRKKILE
HHHHHHHHHHHHHHH		42.3827619977
118UbiquitinationDLKSQRKKILEEVME
HHHHHHHHHHHHHHH		55.50-
126UbiquitinationILEEVMEKETYKTAK
HHHHHHHHCHHHHHH		36.94-
129PhosphorylationEVMEKETYKTAKLIL
HHHHHCHHHHHHHHH		13.8730631047
130UbiquitinationVMEKETYKTAKLILE
HHHHCHHHHHHHHHH		49.80-
133UbiquitinationKETYKTAKLILERFD
HCHHHHHHHHHHHHC		41.09-
144AcetylationERFDPDSKKAKECEP
HHHCCCCCCHHCCCC		65.227697099
145AcetylationRFDPDSKKAKECEPP
HHCCCCCCHHCCCCC		69.517697109
147MalonylationDPDSKKAKECEPPSA
CCCCCCHHCCCCCCC		72.3132601280
147AcetylationDPDSKKAKECEPPSA
CCCCCCHHCCCCCCC		72.317697119
147UbiquitinationDPDSKKAKECEPPSA
CCCCCCHHCCCCCCC		72.31-
153PhosphorylationAKECEPPSAGAAVTA
HHCCCCCCCCCCEEC		50.4828555341
159PhosphorylationPSAGAAVTARPGQEI
CCCCCCEECCCCHHH		16.5422210691
177PhosphorylationTAAQRNLSPTPASPN
HHHHHCCCCCCCCCC		30.2129255136
179PhosphorylationAQRNLSPTPASPNQG
HHHCCCCCCCCCCCC		28.2829255136
182PhosphorylationNLSPTPASPNQGPPP
CCCCCCCCCCCCCCC		26.1129255136
194PhosphorylationPPPQVPVSPGPPKDS
CCCCCCCCCCCCCCC		20.3329255136
201 (in isoform 3)Ubiquitination-34.2321890473
201PhosphorylationSPGPPKDSSAPGGPP
CCCCCCCCCCCCCCC		34.2329978859
202PhosphorylationPGPPKDSSAPGGPPE
CCCCCCCCCCCCCCC		48.9229978859
211PhosphorylationPGGPPERTVTPALSS
CCCCCCCCCCHHHCC		27.3730266825
213PhosphorylationGPPERTVTPALSSNV
CCCCCCCCHHHCCCC		11.3930266825
217PhosphorylationRTVTPALSSNVLPRH
CCCCHHHCCCCCCCC		23.2128555341
218PhosphorylationTVTPALSSNVLPRHL
CCCHHHCCCCCCCCC		31.6329396449
227PhosphorylationVLPRHLGSPATSVPG
CCCCCCCCCCCCCCC		20.0929255136
230PhosphorylationRHLGSPATSVPGMGL
CCCCCCCCCCCCCCC		33.3729255136
231PhosphorylationHLGSPATSVPGMGLH
CCCCCCCCCCCCCCC		28.5529255136
262PhosphorylationALDRIVEYLVGDGPQ
HHHHHHHHHHCCCCC		8.8727642862
293PhosphorylationALKEEFEYIAFRCAY
HHHHHHHHHHHHHHH		11.67-
310PhosphorylationFLNPARKTRPQAPRL
HHCCCCCCCCCCCCC		41.87-
319 (in isoform 2)Ubiquitination-59.5221890473
321PhosphorylationAPRLPEFSFEKRQVV
CCCCCCCCCCCCEEE		30.7325159151
324UbiquitinationLPEFSFEKRQVVEGS
CCCCCCCCCEEEECC		46.232189047
324 (in isoform 1)Ubiquitination-46.2321890473
353PhosphorylationDNQFNEESLEHDVLD
CCCCCHHHHHCCCCC		32.6427619977
373PhosphorylationTDDKIPATEQTNQVI
CCCCCCCHHHHHHHH		24.2223927012
376PhosphorylationKIPATEQTNQVIEKA
CCCCHHHHHHHHHHH		22.7623927012
384PhosphorylationNQVIEKASDSEEPEE
HHHHHHHCCCCCHHH		53.3829255136
386PhosphorylationVIEKASDSEEPEEKQ
HHHHHCCCCCHHHHH		41.1729255136
414PhosphorylationSTVPGADSIPDPELS
CCCCCCCCCCCHHHC		35.17-
421PhosphorylationSIPDPELSGESLTAE
CCCCHHHCCCCCCCC		38.5620068231
424PhosphorylationDPELSGESLTAE---
CHHHCCCCCCCC---		34.2520068231
426PhosphorylationELSGESLTAE-----
HHCCCCCCCC-----		37.7120068231
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseKLHL12Q53G59
PMID:32433973
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
114SPhosphorylation

27619977
153SPhosphorylation

27619977
177SPhosphorylation

20068231
182SPhosphorylation

18691976
194SPhosphorylation

18691976
211TPhosphorylation

27619977
217SPhosphorylation

23186163
227SPhosphorylation

27619977
321SPhosphorylation

18691976
353SPhosphorylation

27619977
384SPhosphorylation

24275569
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LNP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TT30B_HUMANTTC30Bphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LNP_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins 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).
Cited for: MYRISTOYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182; SER-194;THR-213 AND SER-321, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-424, ANDMASS SPECTROMETRY.

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