SGG_DROME - dbPTM
SGG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGG_DROME
UniProt AC P18431
Protein Name Protein kinase shaggy
Gene Name sgg
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 514
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cell cortex. Cell junction, synapse. Cell projection, axon. In syncytial embryos, detected at the centrosomes throughout the cell cycle, and in the mit
Protein Description Required for several developmental events such as syncytial blastoderm formation and embryonic segmentation. Is involved in transcriptional regulation. Required for arm phosphorylation. Wg signaling operates by inactivating the sgg repression of en autoactivation. Negatively controls the neuromuscular junction (NMJ) growth in presynaptic motoneurons. Plays a role in the regulation of microtubule dynamics and actin cytoskeleton during embryogenesis. Required for phosphorylation of sra in activated eggs. Essential for completion of meiosis, possibly by triggering calcineurin activation via sra phosphorylation. Phosphorylates microtubule-associated protein futsch in axons..
Protein Sequence MSGRPRTSSFAEGNKQSPSLVLGGVKTCSRDGSKITTVVATPGQGTDRVQEVSYTDTKVIGNGSFGVVFQAKLCDTGELVAIKKVLQDRRFKNRELQIMRKLEHCNIVKLLYFFYSSGEKRDEVFLNLVLEYIPETVYKVARQYAKTKQTIPINFIRLYMYQLFRSLAYIHSLGICHRDIKPQNLLLDPETAVLKLCDFGSAKQLLHGEPNVSYICSRYYRAPELIFGAINYTTKIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEVIKVLGTPTREQIREMNPNYTEFKFPQIKSHPWQKVFRIRTPTEAINLVSLLLEYTPSARITPLKACAHPFFDELRMEGNHTLPNGRDMPPLFNFTEHELSIQPSLVPQLLPKHLQNASGPGGNRPSAGGAASIAASGSTSVSSTGSGASVEGSAQPQSQGTAAAAGSGSGGATAGTGGASAGGPGSGNNSSSGGASGAPSAVAAGGANAAVAGGAGGGGGAGAATAAATATGAIGATNAGGANVTDS
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
2Phosphorylation------MSGRPRTSS
------CCCCCCCCC		25.5927794539
7 (in isoform 4)Phosphorylation-17.6119429919
7Phosphorylation-MSGRPRTSSFAEGN
-CCCCCCCCCCCCCC		17.6119429919
8PhosphorylationMSGRPRTSSFAEGNK
CCCCCCCCCCCCCCC		31.0019429919
9PhosphorylationSGRPRTSSFAEGNKQ
CCCCCCCCCCCCCCC		32.6619429919
17PhosphorylationFAEGNKQSPSLVLGG
CCCCCCCCCCEEECC		41.4628490779
93 (in isoform 1)Phosphorylation-34.3321082442
94 (in isoform 1)Phosphorylation-39.7421082442
95 (in isoform 1)Phosphorylation-33.3821082442
124 (in isoform 1)Phosphorylation-33.7521082442
213PhosphorylationLHGEPNVSYICSRYY
HCCCCCHHHHHCCCC		45.5819429919
214PhosphorylationHGEPNVSYICSRYYR
CCCCCHHHHHCCCCC		14.0621082442
214 (in isoform 1)Phosphorylation-14.068382613
216 (in isoform 1)Phosphorylation-29.7219429919
217PhosphorylationPNVSYICSRYYRAPE
CCHHHHHCCCCCCCH		29.0919429919
219 (in isoform 1)Phosphorylation-28.4419429919
329 (in isoform 1)Phosphorylation-25.5921082442
372 (in isoform 1)Phosphorylation-24.9619429919
566 (in isoform 1)Phosphorylation-18.8421082442
766Phosphorylation-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		18.5418327897
767Phosphorylation--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		11.1518327897
770Phosphorylation-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		17.4818327897
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 SGG_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGG_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 SGG_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMRCD_DROMEEtl1physical
21447707
POE_DROMEpoephysical
21447707
HEAT1_DROMEl(2)k09022physical
21447707
EIF3A_DROMEeIF3-S10physical
21447707
DDX1_DROMEDdx1physical
21447707
OR69B_DROMEOr69aphysical
21447707
OR69A_DROMEOr69aphysical
21447707
U520_DROMEl(3)72Abphysical
21447707
ROGDI_DROMErogdiphysical
21447707
Y4230_DROMECG14230physical
21447707
EIF3C_DROMEeIF3-S8physical
21447707
CADN_DROMECadNphysical
21447707
PH4H_DROMEHnphysical
21447707
TNNT_DROMEupphysical
21447707
SRR55_DROMEB52physical
21447707
FAT_DROMEftphysical
21447707
MYSP1_DROMEPrmphysical
21447707
MYSP2_DROMEPrmphysical
21447707
TNNI_DROMEwupAphysical
21447707
RSSA_DROMEstaphysical
21447707
TAF1_DROMETaf1physical
21447707
GSK3H_DROMEgsktphysical
21447707
GELS_DROMEGelphysical
21447707
GCY3E_DROMEGyc32Ephysical
21447707
SOG_DROMEsogphysical
21447707
MYSN_DROMEzipphysical
21447707
MARS_DROMEmarsphysical
21447707
DOA_DROMEDoaphysical
21447707
TRA1_DROMENipped-Aphysical
21447707
LVA_DROMElvaphysical
21447707
CEG1A_DROMECenG1Aphysical
21447707
E2AK3_DROMEPEKphysical
21447707
APLP_DROMERfabgphysical
21447707
TNKS_DROMETnksphysical
21447707
NEMF_DROMEClbnphysical
21447707
ARM_DROMEarmgenetic
12636921
ARM_DROMEarmgenetic
21483653
WNTG_DROMEwggenetic
11124806
CP310_DROMECyp310a1genetic
16414040
RHO1_DROMERho1genetic
26234154
5HT2B_DROME5-HT1Bgenetic
15996552
BRM_DROMEbrmgenetic
11124806
OSA_DROMEosagenetic
11124806
CRY1_DROMEcrygenetic
17418796
AXN_DROMEAxngenetic
11124806
AXN_DROMEAxngenetic
19124571
PANG1_DROMEpangenetic
12730381
PANG2_DROMEpangenetic
12730381
JNK_DROMEbskgenetic
18832361
2ABA_DROMEtwsgenetic
14973271
GSK3H_DROMEgsktgenetic
17179138
FOSLD_DROMEkaygenetic
18832361
FOSLA_DROMEkaygenetic
18832361
FUTSC_DROMEfutschgenetic
15269269
ARM_DROMEarmphysical
11927557
ARM_DROMEarmphysical
14966281
HYD_DROMEhydphysical
26334301
AXN_DROMEAxnphysical
22174071
AXN_DROMEAxnphysical
19850033
FUTSC_DROMEfutschphysical
16949836
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGG_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-766; TYR-767 ANDSER-770, AND MASS SPECTROMETRY.
"Modulation of the glycogen synthase kinase-3 family by tyrosinephosphorylation.";
Hughes K., Nikolakaki E., Plyte S.E., Totty N.F., Woodgett J.R.;
EMBO J. 12:803-808(1993).
Cited for: PHOSPHORYLATION AT TYR-767.

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