HRS_DROME - dbPTM
HRS_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HRS_DROME
UniProt AC Q960X8
Protein Name Hepatocyte growth factor-regulated tyrosine kinase substrate
Gene Name Hrs
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 760
Subcellular Localization Cytoplasm, cell cortex . Cytoplasm, perinuclear region . Locates to vesicles present in the perinuclear regions of muscle cells and in the periphery of Garland cells of third-instar larvae.
Protein Description Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Required during gastrulation and appears to regulate early embryonic signaling pathways. Inhibits tyrosine kinase receptor signaling by promoting degradation of the tyrosine-phosphorylated, active receptor, potentially by sorting activated receptors into MVBs. The MVBs are then trafficked to the lysosome where their contents are degraded..
Protein Sequence MFRSSFDKNLENATSHLRLEPDWPSILLICDEINQKDVTPKNAFAAIKKKMNSPNPHSSCYSLLVLESIVKNCGAPVHEEVFTKENCEMFSSFLESTPHENVRQKMLELVQTWAYAFRSSDKYQAIKDTMTILKAKGHTFPELREADAMFTADTAPNWADGRVCHRCRVEFTFTNRKHHCRNCGQVFCGQCTAKQCPLPKYGIEKEVRVCDGCFAALQRPTSGSGGAKSGPRPADSELPAEYLNSTLAQQVQTPARKTEQELKEEEELQLALALSQSEAEQQKPKLQSLPPAAYRMQQRSPSPEAPPEPKEYHQQPEEATNPELAKYLNRSYWEQRKISESSSMASPSAPSPMPPTPQPQQIMPLQVKSADEVQIDEFAANMRTQVEIFVNRMKSNSSRGRSISNDSSVQTLFMTLTSLHSQQLSYIKEMDDKRMWYEQLQDKLTQIKDSRAALDQLRQEHVEKLRRIAEEQERQRQMQMAQKLDIMRKKKQEYLQYQRQLALQRIQEQEREMQLRQEQQKAQYLMGQSAPPFPYMPPSAVPQHGSPSHQLNNVYNPYAAGVPGYLPQGPAPAPNGHGQFQAIPPGMYNPAIQQPMPPNLQPGGLMQQPAPPGNPQMMPPMPENQFANNPAAILQLPQQHSIAQPPQIPFQPQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPVQQPQPQPQMGHVMLQQHQAPPAAQAPPVTEIANNQVQAVAAAPAPPQNEPGPAPVKAEEPATAELISFD
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
4Phosphorylation----MFRSSFDKNLE
----CCCCHHHHCHH		24.8821082442
5Phosphorylation---MFRSSFDKNLEN
---CCCCHHHHCHHH		32.9622668510
221PhosphorylationFAALQRPTSGSGGAK
EEHHCCCCCCCCCCC		48.1621082442
222PhosphorylationAALQRPTSGSGGAKS
EHHCCCCCCCCCCCC		33.3721082442
224PhosphorylationLQRPTSGSGGAKSGP
HCCCCCCCCCCCCCC		33.5421082442
242PhosphorylationDSELPAEYLNSTLAQ
CCCCCHHHHHHHHHH		17.1818281928
246PhosphorylationPAEYLNSTLAQQVQT
CHHHHHHHHHHHCCC		25.6621082442
253PhosphorylationTLAQQVQTPARKTEQ
HHHHHCCCCCHHCHH		21.7621082442
294PhosphorylationQSLPPAAYRMQQRSP
HCCCHHHHHHHHCCC		14.5527794539
300PhosphorylationAYRMQQRSPSPEAPP
HHHHHHCCCCCCCCC		25.9521082442
302PhosphorylationRMQQRSPSPEAPPEP
HHHHCCCCCCCCCCC		36.3021082442
312PhosphorylationAPPEPKEYHQQPEEA
CCCCCHHHCCCHHHC		15.8518281928
320PhosphorylationHQQPEEATNPELAKY
CCCHHHCCCHHHHHH		55.3619429919
327PhosphorylationTNPELAKYLNRSYWE
CCHHHHHHHCHHHHH		12.0018281928
332PhosphorylationAKYLNRSYWEQRKIS
HHHHCHHHHHHHCCC		15.1018281928
339PhosphorylationYWEQRKISESSSMAS
HHHHHCCCCCCCCCC		34.1721082442
356PhosphorylationAPSPMPPTPQPQQIM
CCCCCCCCCCCCCCC		28.7821082442
758PhosphorylationPATAELISFD-----
CCEEECCCCC-----		35.6721082442
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 HRS_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HRS_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 HRS_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COG7_DROMECog7physical
14605208
VA0D1_DROMEVhaAC39-1physical
14605208
CTBP_DROMECtBPphysical
14605208
FLNA_DROMEcherphysical
15710747
DIA_DROMEdiaphysical
15710747
TFP11_DROMEsip1physical
15710747
ACTN_DROMEActnphysical
15710747
ANX11_DROMEAnxB11physical
15710747
SPTCB_DROMEbeta-Specphysical
15710747
CACT_DROMEcactphysical
15710747
HEAT1_DROMEl(2)k09022physical
15710747
DTBP1_DROMEDysbphysical
15710747
CLH_DROMEChcphysical
15710747
FOJO_DROMEfjphysical
15710747
MED12_DROMEktophysical
15710747
UGDH_DROMEsglphysical
15710747
SNAP_DROMEalphaSnapphysical
15710747
SRYA_DROMESry-alphaphysical
15710747
DCUP_DROMEUpdophysical
15710747
UBIQP_DROMEUbi-p63Ephysical
24574010
RBF_DROMERbfgenetic
27056762
RSSA_DROMEstagenetic
22160599
DSH_DROMEdshgenetic
16606693
AFF4_DROMElilligenetic
17110483
WNTG_DROMEwggenetic
16606693
FRIZ_DROMEfzgenetic
16606693
FAT_DROMEftphysical
24114784
TOLL_DROMETlphysical
20404143
VPS28_DROMEVps28physical
26490120
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HRS_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-300 AND SER-302, ANDMASS SPECTROMETRY.

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