SMO_DROME - dbPTM
SMO_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMO_DROME
UniProt AC P91682
Protein Name Protein smoothened
Gene Name smo
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1036
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Segment polarity protein required for correct patterning of every segment. G protein-coupled receptor that associates with the patched protein (ptc) to transduce the hedgehog (hh) signal through the activation of an inhibitory G-protein. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. [PubMed: 25639794]
Protein Sequence MQYLNFPRMPNIMMFLEVAILCLWVVADASASSAKFGSTTPASAQQSDVELEPINGTLNYRLYAKKGRDDKPWFDGLDSRHIQCVRRARCYPTSNATNTCFGSKLPYELSSLDLTDFHTEKELNDKLNDYYALKHVPKCWAAIQPFLCAVFKPKCEKINGEDMVYLPSYEMCRITMEPCRILYNTTFFPKFLRCNETLFPTKCTNGARGMKFNGTGQCLSPLVPTDTSASYYPGIEGCGVRCKDPLYTDDEHRQIHKLIGWAGSICLLSNLFVVSTFFIDWKNANKYPAVIVFYINLCFLIACVGWLLQFTSGSREDIVCRKDGTLRHSEPTAGENLSCIVIFVLVYYFLTAGMVWFVFLTYAWHWRAMGHVQDRIDKKGSYFHLVAWSLPLVLTITTMAFSEVDGNSIVGICFVGYINHSMRAGLLLGPLCGVILIGGYFITRGMVMLFGLKHFANDIKSTSASNKIHLIIMRMGVCALLTLVFILVAIACHVTEFRHADEWAQSFRQFIICKISSVFEEKSSCRIENRPSVGVLQLHLLCLFSSGIVMSTWCWTPSSIETWKRYIRKKCGKEVVEEVKMPKHKVIAQTWAKRKDFEDKGRLSITLYNTHTDPVGLNFDVNDLNSSETNDISSTWAAYLPQCVKRRMALTGAATGNSSSHGPRKNSLDSEISVSVRHVSVESRRNSVDSQVSVKIAEMKTKVASRSRGKHGGSSSNRRTQRRRDYIAAATGKSSRRRESSTSVESQVIALKKTTYPNASHKVGVFAHHSSKKQHNYTSSMKRRTANAGLDPSILNEFLQKNGDFIFPFLQNQDMSSSSEEDNSRASQKIQDLNVVVKQQEISEDDHDGIKIEELPNSKQVALENFLKNIKKSNESNSNRHSRNSARSQSKKSQKRHLKNPAADLDFRKDCVKYRSNDSLSCSSEELDVALDVGSLLNSSFSGISMGKPHSRNSKTSCDVGIQANPFELVPSYGEDELQQAMRLLNAASRQRTEAANEDFGGTELQGLLGHSHRHQREPTFMSESDKLKMLLLPSK
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
55N-linked_GlycosylationDVELEPINGTLNYRL
CCEEEECCCEEEEEE		48.38-
95N-linked_GlycosylationARCYPTSNATNTCFG
CCEECCCCCCCCCCC		53.94-
184N-linked_GlycosylationEPCRILYNTTFFPKF
CCCCCEEECCCCHHH		29.24-
195N-linked_GlycosylationFPKFLRCNETLFPTK
CHHHCCCCCCCCCCC		38.56-
213N-linked_GlycosylationGARGMKFNGTGQCLS
CCCCCEECCCCCCCC		41.41-
336N-linked_GlycosylationSEPTAGENLSCIVIF
CCCCCCCCHHHHHHH		36.01-
419N-linked_GlycosylationICFVGYINHSMRAGL
EEEHHHCCHHHHHHH		16.82-
658PhosphorylationTGAATGNSSSHGPRK
HCCCCCCCCCCCCCC		34.2622817900
659PhosphorylationGAATGNSSSHGPRKN
CCCCCCCCCCCCCCC		30.2922817900
660PhosphorylationAATGNSSSHGPRKNS
CCCCCCCCCCCCCCC		32.0822817900
667PhosphorylationSHGPRKNSLDSEISV
CCCCCCCCCCCEEEE		36.2722817900
670PhosphorylationPRKNSLDSEISVSVR
CCCCCCCCEEEEEEE		41.9722817900
673PhosphorylationNSLDSEISVSVRHVS
CCCCCEEEEEEEEEE		12.3222817900
687PhosphorylationSVESRRNSVDSQVSV
EEHHHCCCCCCHHHH		26.0319429919
690PhosphorylationSRRNSVDSQVSVKIA
HHCCCCCCHHHHHHH		30.2619429919
693PhosphorylationNSVDSQVSVKIAEMK
CCCCCHHHHHHHHHH		15.2825749252
843PhosphorylationVVKQQEISEDDHDGI
EEEECCCCCCCCCCC		33.9319429919
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 SMO_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMO_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 SMO_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS21_DROMERpS21physical
14605208
DYL1_DROMEctpphysical
14605208
COS_DROMEcosphysical
14614827
FUSED_DROMEfuphysical
14597665
COS_DROMEcosphysical
14597665
RS27A_DROMERpS27Aphysical
24244405
HRS_DROMEHrsphysical
24244405
FUSED_DROMEfugenetic
12874118
FUSED_DROMEfugenetic
17182028
HRS_DROMEHrsgenetic
24244405
MAD_DROMEMadgenetic
12954721
WNTG_DROMEwggenetic
9598354
COS_DROMEcosgenetic
16423832
COS_DROMEcosgenetic
12874118
PTC_DROMEptcgenetic
12874118
PTC_DROMEptcgenetic
15744048
PTC_DROMEptcgenetic
18245841
TPPC2_DROMETrs20genetic
15744048
ERF1_DROMEeRF1genetic
15744048
HH_DROMEhhgenetic
18245841
CI_DROMEcigenetic
12954721
PP2A_DROMEmtsgenetic
18245841
CSK2A_DROMECkIIalphagenetic
20876583
GPRK2_DROMEGprk2genetic
20844016
GPRK2_DROMEGprk2genetic
27280464
FUSED_DROMEfuphysical
14636583
FUSED_DROMEfuphysical
14523402
FUSED_DROMEfuphysical
14614827
FUSED_DROMEfuphysical
25289679
SMO_DROMEsmophysical
17284519
SMO_DROMEsmophysical
17960137
SMO_DROMEsmophysical
20844016
SMO_DROMEsmophysical
22537496
KAPC_DROMEPka-C1physical
25289679
COS_DROMEcosphysical
14636583
COS_DROMEcosphysical
14523402
COS_DROMEcosphysical
17671093
COS_DROMEcosphysical
22537496
COS_DROMEcosphysical
25289679
COS_DROMEcosphysical
21844892
COS_DROMEcosphysical
21852395
PTC_DROMEptcphysical
10983992
PTC_DROMEptcphysical
17284519
SMUF1_DROMElackphysical
24302888
SXL_DROMESxlphysical
17284519
UBIQP_DROMEUbi-p63Ephysical
23843610
VPS36_DROMEVps36physical
23843610
CI_DROMEciphysical
14636583
CI_DROMEciphysical
14523402
PP4C_DROMEPp4-19Cphysical
19088085
GPRK2_DROMEGprk2physical
20844016
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMO_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-658; SER-659; SER-667;SER-670; SER-673; SER-687; SER-690 AND SER-693, AND MASS SPECTROMETRY.

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