HTS_DROME - dbPTM
HTS_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HTS_DROME
UniProt AC Q02645
Protein Name Protein hu-li tai shao
Gene Name hts
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1156
Subcellular Localization Cytoplasm, cytoskeleton. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Required for assembling actin at ring canals in developing egg chambers. Probably interacts with other developmental proteins involved in nurse cell/oocyte transport through the ring canals. Important for normal neuromotor function. [PubMed: 23836506]
Protein Sequence MTEVEQPPQNGIDPTAGEDDDNSKARPADIEQDMREMERRKRVEAIMGSKLFREELERIVDSARDGGAGASGILQQLSDIVGVPVSRVGSVFKSSNCMVPINDIRGVESMGYAKGEKILRCKLAATFRLLDLYGWTQGLGAQITARLKVDQEYFLVNPYGLLYHEITASALNKVDMQGQIVEQGTTNFGGNKSHFVLHSVVHAARPDIRCAIYIGCSPVVAISSLKTGLLPLTKDACVLGEITTHAYTGLFDEEERNRLVRSLGPNSKVILLTNHGALCCGETIEEAFFAACHIVQACETQLKLLPVGLDNLVLIPEESRKAIYEQSRRPPEDLEKKFAAVAAAEDGAATAEKDAAEAVPKVGSPPKWRVGGAEFEALMRMLDNAGYRTGYIYRHPLIKSDPPKPKNDVELPPAVSSLGYLLEEEELFRQGIWKKGDIRKGGDRSRWLNSPNVYQKVEVLETGTPDPKKITKWVAEGSPTHSTPVRIEDPLQFVPAGTNPREFKRVQQLIKDNRRADKISAGPQSHILEGVTWDEASRLKDATVSQAGDHVVMMGAASKGIIQRGFQHNATVYKAPYAKNPFDNVTDDELNEYKRTVERKKKSVHGEYTDTDFSESEAVLQAGTKKYPQSEPETEHQVIEIQTQQAPVPRQAEVVLSDALVSQLAQKYAFLYSPGQYMYACMKMAPLMHKVYVIHKVEPVSKHNYPPVNDGNMSIHHNESGAGFMAQESSVISSTPVRNALASVSLPEERNHSILGLSSTPYRTISHFGFNCPLITSPTILLHPEHRSIWQRVAEQREKVVSFIDLTTLSLDNRKLLNVVTSTHPTQCQSQSQSFISEKHIQLEVTPPKRKQRVYSATISSGLDDSLDELDSLMSGLAINMPRSREQDSGLYRSYTFLPSNHALPKDTDANNRDQTDRERPEAEQEESFHCAGDSGIGDSTGRRPRLATTSNDSSIQEAEAYTQGKHVKLTLSSSPTPTATQSPATIEILINVSLRNAECVQTVQTHEQEFRAKLERVIDEEIHYISQQLAFKQRQAELHEQQTTSRAPIATPSFTTMHPPAPASSSSMVHRSNSAPELCHTYSYVAVGDLSTKQDQASPQLPAEGEPLNDILSSLEKELERLLNSVVTAHMLHNKAIIHECRARFSQLADGIVSS
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------MTEVEQPPQ
------CCCCCCCCC		61.1027794539
86PhosphorylationDIVGVPVSRVGSVFK
HHHCCCHHHHCHHHC		18.3819429919
114AcetylationVESMGYAKGEKILRC
CCCCCCCCCCEEHHH		60.1521791702
117AcetylationMGYAKGEKILRCKLA
CCCCCCCEEHHHHHH		56.5621791702
364PhosphorylationEAVPKVGSPPKWRVG
HHCCCCCCCCCEECC		40.8027626673
450PhosphorylationDRSRWLNSPNVYQKV
CCCCCCCCCCHHHEE		18.7119429919
454PhosphorylationWLNSPNVYQKVEVLE
CCCCCCHHHEEEEEC		14.8419429919
462PhosphorylationQKVEVLETGTPDPKK
HEEEEECCCCCCHHH		42.0429892262
464 (in isoform 3)Phosphorylation-31.7527794539
464PhosphorylationVEVLETGTPDPKKIT
EEEECCCCCCHHHHH		31.7519429919
478PhosphorylationTKWVAEGSPTHSTPV
HHHHHCCCCCCCCCC		20.3821082442
480PhosphorylationWVAEGSPTHSTPVRI
HHHCCCCCCCCCCCC		30.1019429919
482PhosphorylationAEGSPTHSTPVRIED
HCCCCCCCCCCCCCC		36.5629892262
498PhosphorylationLQFVPAGTNPREFKR
CCCCCCCCCHHHHHH		44.1219060867
520PhosphorylationNRRADKISAGPQSHI
CCCHHCCCCCCCHHH		32.6721082442
571PhosphorylationRGFQHNATVYKAPYA
HHHCCCCEEEECCCC		29.6819429919
573PhosphorylationFQHNATVYKAPYAKN
HCCCCEEEECCCCCC		9.3319429919
586PhosphorylationKNPFDNVTDDELNEY
CCCCCCCCHHHHHHH		43.9419429919
593PhosphorylationTDDELNEYKRTVERK
CHHHHHHHHHHHHHH		12.5122668510
596PhosphorylationELNEYKRTVERKKKS
HHHHHHHHHHHHHHH		23.6722668510
603PhosphorylationTVERKKKSVHGEYTD
HHHHHHHHCCCCCCC		28.3819429919
608PhosphorylationKKSVHGEYTDTDFSE
HHHCCCCCCCCCCCH		17.9519429919
609PhosphorylationKSVHGEYTDTDFSES
HHCCCCCCCCCCCHH		28.2819429919
611PhosphorylationVHGEYTDTDFSESEA
CCCCCCCCCCCHHHH		31.0119429919
614PhosphorylationEYTDTDFSESEAVLQ
CCCCCCCCHHHHHHH		42.9219429919
616PhosphorylationTDTDFSESEAVLQAG
CCCCCCHHHHHHHHC		29.6519429919
624PhosphorylationEAVLQAGTKKYPQSE
HHHHHHCCCCCCCCC		27.6419429919
627PhosphorylationLQAGTKKYPQSEPET
HHHCCCCCCCCCCCC		14.2019429919
630PhosphorylationGTKKYPQSEPETEHQ
CCCCCCCCCCCCCEE		51.0919429919
634PhosphorylationYPQSEPETEHQVIEI
CCCCCCCCCEEEEEE		49.8619429919
643PhosphorylationHQVIEIQTQQAPVPR
EEEEEEEECCCCCCC		28.4521082442
657 (in isoform 2)Phosphorylation-14.8218327897
668 (in isoform 2)Phosphorylation-7.1821082442
686 (in isoform 2)Phosphorylation-27.0727794539
687 (in isoform 2)Phosphorylation-4.0029892262
690 (in isoform 2)Phosphorylation-22.6925749252
703 (in isoform 2)Phosphorylation-31.3925749252
705 (in isoform 2)Phosphorylation-14.5028490779
759PhosphorylationHSILGLSSTPYRTIS
CCCCCCCCCCCEECC		38.1428490779
1099PhosphorylationSTKQDQASPQLPAEG
CCCCCCCCCCCCCCC		13.9328490779
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 HTS_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HTS_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 HTS_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS27A_DROMERpS27Aphysical
24292889
DLG1_DROMEdlg1physical
21791202
HTS_DROMEhtsphysical
21128303
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HTS_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-478; THR-480; SER-603;TYR-608; THR-609; THR-611; SER-614; TYR-627 AND SER-630, AND MASSSPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-498, AND MASSSPECTROMETRY.

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