LBR_DROME - dbPTM
LBR_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LBR_DROME
UniProt AC Q8MLV1
Protein Name Lamin-B receptor
Gene Name LBR {ECO:0000312|FlyBase:FBgn0034657}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 741
Subcellular Localization Nucleus inner membrane
Multi-pass membrane protein
Nucleoplasmic side .
Protein Description Anchors the lamina and the heterochromatin to the inner nuclear membrane..
Protein Sequence MQHSPSTTTDHIHFAARFFDRNSYTMDRRLRRPRRTEDVSSGPLLAQSKQPSLLPVTRRTGSVTAAGATATATATAGPATRTRASPSRNKVVAPPSPDLGPRTRRSSRPRSSVGPLTGSGSGSSLPIKAAIKARTPIPEVSEVSSPIRLSTSNLPMTLTTNTSSGAPNKAFNTSSVNSGNSFSRTTTSSTTTTTERIEIRAEGDGEVDTDSIRKRITERLRRSVSKTISNLAGTPVTNTEEGSRYSRSVSRSVYDDEKSSKRSYSTGEEDIDEEDELEEDQFRSFNVTRKSATPAEISCRQLKAPREFGGWLGAFLFLLLLPTAVYYLTWSCTARNACQFKHLNLGILLDVNYLTRQVFQPRVVGAFAAYQVVVFLLVALLPGRRVHLTRETYKFNCLAVSLTLLIASGVAEYLKYPVVTFVLRHYLRFCIFGLVGAFVAAAWSYWLVDTAKYNVLRQTLTNDYGRTGSFVVDFALGRQLNPKWLGRVDWKQFQYRLSLVTTLIYATCYIYQTLVWPQKPQLGEQEGYLYQAKYYWNNVNYDPATLFSASCLLFYVLDAIIFEHHLSSSFELQHEGYGCLLLLRYAATPYLLTAVTKYFYEQRVPISCWYAPLAVAALLSLGLLVKRFSCAYKYKYRLNSQSPIFANIETIHTYQGSRLLLSGMWGWVRQPNYLGDIVALLALAAPMALRPAWPPVLGLSLIILLLLHRATRANARNQARYHSSWQRYSTQVRSYILPRVY
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
82PhosphorylationTAGPATRTRASPSRN
ECCCCCCCCCCCCCC		26.6625749252
96PhosphorylationNKVVAPPSPDLGPRT
CCCCCCCCCCCCCCC		29.9519429919
106PhosphorylationLGPRTRRSSRPRSSV
CCCCCCCCCCCCCCC		27.6625749252
107PhosphorylationGPRTRRSSRPRSSVG
CCCCCCCCCCCCCCC		44.4825749252
111PhosphorylationRRSSRPRSSVGPLTG
CCCCCCCCCCCCCCC		31.8719060867
112PhosphorylationRSSRPRSSVGPLTGS
CCCCCCCCCCCCCCC		32.1622817900
135PhosphorylationKAAIKARTPIPEVSE
HHHHHCCCCCCCHHC		30.3519429919
141PhosphorylationRTPIPEVSEVSSPIR
CCCCCCHHCCCCCEE		30.5328490779
144PhosphorylationIPEVSEVSSPIRLST
CCCHHCCCCCEEEEC		26.7522817900
145PhosphorylationPEVSEVSSPIRLSTS
CCHHCCCCCEEEECC		29.5322817900
181PhosphorylationSSVNSGNSFSRTTTS
CCCCCCCCCCCEECC		28.2919429919
183PhosphorylationVNSGNSFSRTTTSST
CCCCCCCCCEECCCC		28.6519429919
185PhosphorylationSGNSFSRTTTSSTTT
CCCCCCCEECCCCCC		32.9727626673
211PhosphorylationDGEVDTDSIRKRITE
CCCCCHHHHHHHHHH		26.7820450229
223PhosphorylationITERLRRSVSKTISN
HHHHHHHHHHHHHHH		25.0623607784
225PhosphorylationERLRRSVSKTISNLA
HHHHHHHHHHHHHHC		25.9023607784
227PhosphorylationLRRSVSKTISNLAGT
HHHHHHHHHHHHCCC		23.3319429919
229PhosphorylationRSVSKTISNLAGTPV
HHHHHHHHHHCCCCC		30.9019429919
234PhosphorylationTISNLAGTPVTNTEE
HHHHHCCCCCCCCCC		14.6919429919
237PhosphorylationNLAGTPVTNTEEGSR
HHCCCCCCCCCCCCC		37.3119429919
239PhosphorylationAGTPVTNTEEGSRYS
CCCCCCCCCCCCCCC		26.5019429919
243PhosphorylationVTNTEEGSRYSRSVS
CCCCCCCCCCCCCCC		31.1819429919
245PhosphorylationNTEEGSRYSRSVSRS
CCCCCCCCCCCCCCC		15.3319429919
246PhosphorylationTEEGSRYSRSVSRSV
CCCCCCCCCCCCCCC		19.5719429919
248PhosphorylationEGSRYSRSVSRSVYD
CCCCCCCCCCCCCCC		20.6419429919
250PhosphorylationSRYSRSVSRSVYDDE
CCCCCCCCCCCCCCC		21.7819429919
252PhosphorylationYSRSVSRSVYDDEKS
CCCCCCCCCCCCCCC		19.9519429919
259PhosphorylationSVYDDEKSSKRSYST
CCCCCCCCCCCCCCC		38.7619429919
260PhosphorylationVYDDEKSSKRSYSTG
CCCCCCCCCCCCCCC		43.0619429919
263PhosphorylationDEKSSKRSYSTGEED
CCCCCCCCCCCCCCC		27.4619429919
264PhosphorylationEKSSKRSYSTGEEDI
CCCCCCCCCCCCCCC		17.8119429919
265PhosphorylationKSSKRSYSTGEEDID
CCCCCCCCCCCCCCC		31.0519429919
266PhosphorylationSSKRSYSTGEEDIDE
CCCCCCCCCCCCCCC		40.1419429919
284PhosphorylationLEEDQFRSFNVTRKS
CCHHHHHHCCCCCCC		23.5919429919
288PhosphorylationQFRSFNVTRKSATPA
HHHHCCCCCCCCCCC		33.2222817900
291PhosphorylationSFNVTRKSATPAEIS
HCCCCCCCCCCCCCC		33.8019429919
293PhosphorylationNVTRKSATPAEISCR
CCCCCCCCCCCCCHH		30.0719429919
298PhosphorylationSATPAEISCRQLKAP
CCCCCCCCHHHCCCC		8.5125749252
640PhosphorylationKYKYRLNSQSPIFAN
HEEEECCCCCCEEEE		36.3122817900
642PhosphorylationKYRLNSQSPIFANIE
EEECCCCCCEEEEEE		21.5622817900
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

Oops, there are no upstream regulatory protein records of LBR_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LBR_DROME !!
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 LBR_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATNA_DROMEAtpalphaphysical
14605208
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LBR_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; THR-135; SER-144;SER-223; SER-225; THR-234; THR-237; SER-243; SER-246; SER-248;SER-250; SER-263; THR-266; SER-284; THR-288; SER-291; THR-293;SER-298; SER-640 AND SER-642, AND MASS SPECTROMETRY.

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