ASP_DROME - dbPTM
ASP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASP_DROME
UniProt AC Q9VC45
Protein Name Protein abnormal spindle
Gene Name asp {ECO:0000312|EMBL:AAF56330.3}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1954
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. During interphase in syncytial embryos distribution is cytoplasmic. On entering mitosis, moves to polar regions of the spindle immediately surrounding the centrosome. At telophase, migrates to mic
Protein Description Required to maintain the structure of the centrosomal microtubule organizing center (MTOC) during mitosis. May have a preferential role in regulating neurogenesis. Required for germ cell mitosis and oocyte differentiation..
Protein Sequence MSAFEITVTPSRLKQKKRAEGREPAVVVMAPFSAKAIVQFEDVPITKTARRQVRVLNPSDDDIEVKVMKAIREEHNLSLEWMEHTVPARDEVSMELVWSPVLEVACKETLQLIDNRNFRKEVMIILKSKSNQPVKNPRKFPTVGKTLQLKSPTGAGKTMKSVVSAAVQQKKRMSAAAAPPSKQTWRVTAPSRPAAWAHPPPQAPLVEKNVYKTPQEEPVYISPQPRSLKENLSPMTPGNLLDVIDNLRFTPLTETRGKGQATIFPDNLAAWPTPTLKGNVKSCANDMRPRRITPDDLEDQPATNKTFDVKHSETINISLDTLDCSRIDGQPHTPLNKTTTIVHATHTRALACIHEEEGPSPPRTPTKSAIHDLKRDIKLVGSPLRKYSESMKDLSLLSPQTKYAIQGSMPNLNEMKIRSIEQNRYYQEQQIQIKAKDLNSSSSSEASLAGQQEFLFNHSEILAQSSRFNLHEVGRKSVKGSPVKNPHKRRSHELSFSDAPSNESLYRNETVAISPPKKQRVEDTTLPRSAAPANASARSSSAHAWPHAQSKKFKLAQTMSLMKKPATPRKVRDTSIQPSVKLYDSELYMQTCINPDPFAATTTIDPFLASTMYLDEQAVDRHQADFKKWLNALVSIPADLDADLNNKIDVGKLFNEVRNKELVVAPTKEEQSMNYLTKYRLETLRKAAVELFFSEQMRLPCSKVAVYVNKQALRIRSDRNLHLDVVMQRTILELLLCFNPLWLRLGLEVVFGEKIQMQSNRDIVGLSTFILNRLFRNKCEEQRYSKAYTLTEEYAETIKKHSLQKILFLLLFLDQAKQKRIVKHNPCLFVKKSPHKETKDILLRFSSELLANIGDITRELRRLGYVLQHRQTFLDEFDYAFNNLAVDLRDGVRLTRVMEVILLRDDLTRQLRVPAISRLQRIFNVKLALGALGEANFQLGGDIAAQDIVDGHREKTLSLLWQLIYKFRSPKFHAAATVLQKWWRRHWLHVVIQRRIRHKELMRRHRAATVIQAVFRGHQMRKYVKLFKTERTQAAIILQKFTRRYLAQKQLYQSYHSIITIQRWWRAQQLGRQHRQRFVELREAAIFLQRIWRRRLFAKKLLAAAETARLQRSQKQQAAASYIQMQWRSYQLGRIQRQQFLRQRDLIMFVQRRMRSKWSMLEQRKEFQQLKRAAINIQQRWRAKLSMRKCNADYLALRSSVLKVQAYRKATIQMRIDRNHYYSLRKNVICLQQRLRAIMKMREQRENYLRLRNASILVQKRYRMRQQMIQDRNAYLRTRKCIINVQRRWRATLQMRRERKNYLHLQTTTKRIQIKFRAKREMKKQRAEFLQLKKVTLVVQKRRRALLQMRKERQEYLHLREVTIKLQRRFHAQKSMRFMRAKYRGTQAAVSCLQMHWRNHLLRKRERNSFLQLRQAAITLQRRYRARLNMIKQLKSYAQLKQAAITIQTRYRAKKAMQKQVVLYQKQREAIIKVQRRYRGNLEMRKQIEVYQKQRQAVIRLQKWWRSIRDMRLCKAGYRRIRLSSLSIQRKWRATVQARRQREIFLSTIRKVRLMQAFIRATLLMRQQRREFEMKRRAAVVIQRRFRARCAMLKARQDYQLIQSSVILVQRKFRANRSMKQARQEFVQLRTIAVHLQQKFRGKRLMIEQRNCFQLLRCSMPGFQARARGFMARKRFQALMTPEMMDLIRQKRAAKVIQRYWRGYLIRRRQKHQGLLDIRKRIAQLRQEAKAVNSVRCKVQEAVRFLRGRFIASDALAVLSRLDRLSRTVPHLLMWCSEFMSTFCYGIMAQAIRSEVDKQLIERCSRIILNLARYNSTTVNTFQEGGLVTIAQMLLRWCDKDSEIFNTLCTLIWVFAHCPKKRKIIHDYMTNPEAIYMVRETKKLVARKEKMKQNARKPPPMTSGRYKSQKINFTPCSLPSLEPDFGIIRYSPYTFISSVYAFDTILCKLQIDMF
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
9PhosphorylationSAFEITVTPSRLKQK
CCCEEEECHHHHHHH		13.5928490779
151PhosphorylationGKTLQLKSPTGAGKT
CCEEEECCCCCCCHH		35.9622817900
174PhosphorylationVQQKKRMSAAAAPPS
HHHHHHHCCCCCCCC		20.8421082442
220PhosphorylationTPQEEPVYISPQPRS
CCCCCCEEECCCCCC		13.3428490779
222PhosphorylationQEEPVYISPQPRSLK
CCCCEEECCCCCCHH		10.3728490779
227PhosphorylationYISPQPRSLKENLSP
EECCCCCCHHHCCCC		50.9430478224
233PhosphorylationRSLKENLSPMTPGNL
CCHHHCCCCCCCCCH		24.9819429919
236PhosphorylationKENLSPMTPGNLLDV
HHCCCCCCCCCHHHH		31.2819429919
360PhosphorylationIHEEEGPSPPRTPTK
CCCCCCCCCCCCCCH		59.3928490779
364PhosphorylationEGPSPPRTPTKSAIH
CCCCCCCCCCHHHHH		40.8728490779
366PhosphorylationPSPPRTPTKSAIHDL
CCCCCCCCHHHHHHH		36.7028490779
382PhosphorylationRDIKLVGSPLRKYSE
HHHHHHCCHHHHHCH		17.1827626673
387PhosphorylationVGSPLRKYSESMKDL
HCCHHHHHCHHHCHH		15.9621082442
388PhosphorylationGSPLRKYSESMKDLS
CCHHHHHCHHHCHHH		26.6522817900
390PhosphorylationPLRKYSESMKDLSLL
HHHHHCHHHCHHHHC		25.7822817900
395PhosphorylationSESMKDLSLLSPQTK
CHHHCHHHHCCHHHH		37.0818327897
398PhosphorylationMKDLSLLSPQTKYAI
HCHHHHCCHHHHHHH		21.9119429919
401PhosphorylationLSLLSPQTKYAIQGS
HHHCCHHHHHHHCCC		29.4319429919
408PhosphorylationTKYAIQGSMPNLNEM
HHHHHCCCCCCCCHH		18.0725749252
477PhosphorylationLHEVGRKSVKGSPVK
HHHCCCCCCCCCCCC		27.9225749252
481PhosphorylationGRKSVKGSPVKNPHK
CCCCCCCCCCCCCCC		22.3222817900
491PhosphorylationKNPHKRRSHELSFSD
CCCCCCCCCCCCCCC		25.9122817900
495PhosphorylationKRRSHELSFSDAPSN
CCCCCCCCCCCCCCC		21.5122817900
497PhosphorylationRSHELSFSDAPSNES
CCCCCCCCCCCCCCC		29.5022817900
501PhosphorylationLSFSDAPSNESLYRN
CCCCCCCCCCCCCCC		55.7522817900
504PhosphorylationSDAPSNESLYRNETV
CCCCCCCCCCCCCEE		34.6418327897
514PhosphorylationRNETVAISPPKKQRV
CCCEEEECCCCCCCC		25.9728490779
567PhosphorylationSLMKKPATPRKVRDT
HHHCCCCCCCCCCCC		31.9627626673
785PhosphorylationKCEEQRYSKAYTLTE
CCHHHHCCHHHCCCH		17.0122817900
1524PhosphorylationGYRRIRLSSLSIQRK
CCCEEEHHHHCHHHH		21.2719429919
1525PhosphorylationYRRIRLSSLSIQRKW
CCEEEHHHHCHHHHH		30.6319429919
1527PhosphorylationRIRLSSLSIQRKWRA
EEEHHHHCHHHHHHH		20.7219429919
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 ASP_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASP_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 ASP_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALM_DROMECamphysical
14605208
SQH_DROMEsqhgenetic
24142104
DSOR1_DROMEDsor1genetic
9648737
ZW10_DROMEZw10genetic
11146659
ERKA_DROMErlgenetic
9648737
CALM_DROMECamphysical
26620907
MYSN_DROMEzipphysical
24142104
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASP_DROME

loading...

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-151; SER-360; THR-364;SER-388; SER-390; SER-395; SER-398; SER-491; SER-495; SER-497;SER-501; SER-504 AND SER-514, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory