PTC_DROME - dbPTM
PTC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTC_DROME
UniProt AC P18502
Protein Name Protein patched
Gene Name ptc
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1286
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Segmentation polarity protein. Acts as a receptor for the hedgehog protein (HH). Associates with the smoothened protein (SMO) to transduce the hedgehog signal leading to the activation of wingless, decapentaplegic and patched itself. Participates in cell interactions that establish pattern within the segment and the imaginal disks during development. In the absence of HH, represses the constitutive signaling activity of smo through fused (FU)..
Protein Sequence MDRDSLPRVPDTHGDVVDEKLFSDLYIRTSWVDAQVALDQIDKGKARGSRTAIYLRSVFQSHLETLGSSVQKHAGKVLFVAILVLSTFCVGLKSAQIHSKVHQLWIQEGGRLEAELAYTQKTIGEDESATHQLLIQTTHDPNASVLHPQALLAHLEVLVKATAVKVHLYDTEWGLRDMCNMPSTPSFEGIYYIEQILRHLIPCSIITPLDCFWEGSQLLGPESAVVIPGLNQRLLWTTLNPASVMQYMKQKMSEEKISFDFETVEQYMKRAAIGSGYMEKPCLNPLNPNCPDTAPNKNSTQPPDVGAILSGGCYGYAAKHMHWPEELIVGGAKRNRSGHLRKAQALQSVVQLMTEKEMYDQWQDNYKVHHLGWTQEKAAEVLNAWQRNFSREVEQLLRKQSRIATNYDIYVFSSAALDDILAKFSHPSALSIVIGVAVTVLYAFCTLLRWRDPVRGQSSVGVAGVLLMCFSTAAGLGLSALLGIVFNAASTQVVPFLALGLGVDHIFMLTAAYAESNRREQTKLILKKVGPSILFSACSTAGSFFAAAFIPVPALKVFCLQAAIVMCSNLAAALLVFPAMISLDLRRRTAGRADIFCCCFPVWKEQPKVAPPVLPLNNNNGRGARHPKSCNNNRVPLPAQNPLLEQRADIPGSSHSLASFSLATFAFQHYTPFLMRSWVKFLTVMGFLAALISSLYASTRLQDGLDIIDLVPKDSNEHKFLDAQTRLFGFYSMYAVTQGNFEYPTQQQLLRDYHDSFVRVPHVIKNDNGGLPDFWLLLFSEWLGNLQKIFDEEYRDGRLTKECWFPNASSDAILAYKLIVQTGHVDNPVDKELVLTNRLVNSDGIINQRAFYNYLSAWATNDVFAYGASQGKLYPEPRQYFHQPNEYDLKIPKSLPLVYAQMPFYLHGLTDTSQIKTLIGHIRDLSVKYEGFGLPNYPSGIPFIFWEQYMTLRSSLAMILACVLLAALVLVSLLLLSVWAAVLVILSVLASLAQIFGAMTLLGIKLSAIPAVILILSVGMMLCFNVLISLGFMTSVGNRQRRVQLSMQMSLGPLVHGMLTSGVAVFMLSTSPFEFVIRHFCWLLLVVLCVGACNSLLVFPILLSMVGPEAELVPLEHPDRISTPSPLPVRSSKRSGKSYVVQGSRSSRGSCQKSHHHHHKDLNDPSLTTITEEPQSWKSSNSSIQMPNDWTYQPREQRPASYAAPPPAYHKAAAQQHHQHQGPPTTPPPPFPTAYPPELQSIVVQPEVTVETTHSDSNTTKVTATANIKVELAMPGRAVRSYNFTS
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
142N-linked_GlycosylationIQTTHDPNASVLHPQ
EEECCCCCCCCCCHH
51.40-
298N-linked_GlycosylationPDTAPNKNSTQPPDV
CCCCCCCCCCCCCCC
57.86-
335N-linked_GlycosylationIVGGAKRNRSGHLRK
HCCCCCCCCCCHHHH
41.59-
388N-linked_GlycosylationVLNAWQRNFSREVEQ
HHHHHHHHHHHHHHH
24.93-
536PhosphorylationVGPSILFSACSTAGS
HCHHHHHHHHCCCCC
25.5622817900
807N-linked_GlycosylationTKECWFPNASSDAIL
EECCCCCCCCCHHHH
42.87-
1122PhosphorylationLEHPDRISTPSPLPV
CCCCCCCCCCCCCCC
34.8519429919
1123PhosphorylationEHPDRISTPSPLPVR
CCCCCCCCCCCCCCC
25.9719429919
1125PhosphorylationPDRISTPSPLPVRSS
CCCCCCCCCCCCCCC
38.8719429919

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 PTC_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTC_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 PTC_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD51_DROMEspn-Aphysical
15575970
CEG1A_DROMECenG1Aphysical
15575970
LIP3_DROMELip3physical
15575970
NPL4_DROMENpl4physical
15575970
ECR_DROMEEcRphysical
15575970
TID_DROMEl(2)tidphysical
12783860
MOEH_DROMEMoephysical
15710747
ZN330_DROMENoa36physical
15710747
ABRU_DROMEabphysical
15710747
BTKL_DROMEBtk29Aphysical
15710747
DCLK_DROMECG17528physical
15710747
FLNA_DROMEcherphysical
15710747
HIW_DROMEhiwphysical
15710747
PPN_DROMEPpnphysical
15710747
FRIZ2_DROMEfz2physical
15710747
MLP2_DROMEMlp84Bphysical
15710747
HRD1_DROMEsip3physical
15710747
GALT6_DROMEpgant6physical
15710747
CYHR1_DROMECG32486physical
15710747
NU160_DROMENup160physical
15710747
TONSL_DROMECG7457physical
15710747
CHD1_DROMEChd1physical
15710747
LACH_DROMELacphysical
15710747
LAMA_DROMELanAphysical
15710747
ITBX_DROMEmysphysical
15710747
NCD_DROMEncdphysical
15710747
NEDD4_DROMENedd4physical
15710747
POF_DROMEPofphysical
15710747
PTC_DROMEptcphysical
15710747
DGK2_DROMErdgAphysical
15710747
RG190_DROMERhoGAPp190physical
15710747
RL22_DROMERpL22physical
15710747
SAS_DROMEsasphysical
15710747
ITA3_DROMEscbphysical
15710747
KCNAB_DROMEShabphysical
15710747
SINA_DROMEsinaphysical
15710747
SNAI_DROMEsnaphysical
15710747
TF2B_DROMETfIIBphysical
15710747
FUSED_DROMEfugenetic
9874371
FUSED_DROMEfugenetic
11820817
FUSED_DROMEfugenetic
8861096
SMO_DROMEsmogenetic
11934850
SMO_DROMEsmogenetic
9598354
SMO_DROMEsmogenetic
11112325
SMO_DROMEsmogenetic
15754211
SMO_DROMEsmogenetic
19635474
DECA_DROMEdppgenetic
8306973
DECA_DROMEdppgenetic
9102309
DECA_DROMEdppgenetic
11112325
HMEN_DROMEengenetic
26575288
YAP1_DROMEykigenetic
22705500
VEIN_DROMEvngenetic
10588875
HH_DROMEhhgenetic
8575316
HH_DROMEhhgenetic
11112325
CI_DROMEcigenetic
8575316
CI_DROMEcigenetic
8861096
CI_DROMEcigenetic
11171398
HHAT_DROMEraspgenetic
16459296
COLL_DROMEkngenetic
9383063
SMO_DROMEsmophysical
17284519
SUDX_DROMESu(dx)physical
24302888
IHOG_DROMEihogphysical
20501592
PTC_DROMEptcphysical
10983992
PTC_DROMEptcphysical
16980583
PTC_DROMEptcphysical
17284519
SMUF1_DROMElackphysical
24302888
SXL_DROMESxlphysical
17284519
NEDD4_DROMENedd4physical
16980583
NEDD4_DROMENedd4physical
24302888
HH_DROMEhhphysical
12783860
HH_DROMEhhphysical
16980583
HH_DROMEhhphysical
20048000
APLP_DROMERfabgphysical
18198278

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTC_DROME

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Related Literatures of Post-Translational Modification

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