ZASP_DROME - dbPTM
ZASP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZASP_DROME
UniProt AC A1ZA47
Protein Name PDZ and LIM domain protein Zasp
Gene Name Zasp52
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2194
Subcellular Localization Cytoplasm, cytoskeleton . Regulates or strengthens the link of integrins to the actin cytoskeleton.
Protein Description Regulator of cell matrix adhesion having two related functions, one upstream of Actn organizing the Z line and the other downstream of integrins regulating assembly of integrin adhesion sites. Also required for the formation of myotendinous junctions in muscles..
Protein Sequence MAQPQLLQIKLSRFDAQPWGFRLQGGTDFAQPLLVQKVNAGSLSEQAGLQPGDAVVKINDVDVFNLRHKDAQDIVVRSGNNFVITVQRGGSTWRPHVTPTGNVPQPNSPYLQTVTKTSLAHKQQDSQHIGCGYNNAARPFSNGGDGGVKSIVNKQYNTPVGIYSDESIAETLSAQAEVLAGGVLGVNFKKNEKEYQGDRSEVLKFLREEETGQSTPAFGNSHYEHDAPQQLQQPQQQYNQHQQHYHQQQQQQQSSTTRHVSAPVNSPKPPSTGGLPTGQNICTECERLITGVFVRIKDKNLHVECFKCATCGTSLKNQGYYNFNNKLYCDIHAKQAAINNPPTGTEGYVPVPIKPNTKLSASTISSALNSHGYGGHSNGYSNGNSTPAPAPVASSQATATVATVAPSAATAATAAATPQAATATDSPAATASSSDNMSAYVADEPSSIYGQISAESVALAPPPPQPPTAGGGDQPFEYVTLTGNVIRSVQAPGKGACPSYKVNQGYARPFGAAAPKSPVSYPPQQQQQSPRPAPGGQNPYATLPRSNVGQQGGEAVEELQPEFEEEDCYEMDIEVALAASRQSQRGSSFTWPPPQDDSHLAPTAAPLYIPPPETQHVVVSNPVQQVPPLPPGGATARLDPQPVVGTSANGAPQWQSYSAPQLTTASARQLAEQESSSDSYTSTSTTTTTTSEEYQRMYAAQVQAYQMQEQSGSEFDYQVDYASTQDSVQDYPSGRRSAQECVDSLAVPLSTYKLVDMVREVTPSPVTTPTQTPAPAAPTTRRVVFNDEPEIKELPQLPAELETIPEASEAVEDREGLVIEQRCQILESERKFQPTPEIKIEIAPVRQIPPTKIPNPMPKEWINPMIRVLTTAPEVPFHLVECPFPRPCGDDFEAEAAAAEAAKTQEVPEPLPPQVSAAPPATVSVEPSPAPLRESPPRGSRLSQAMVTAPEFELKFAPPADQGIPLPEETEPYMPPPIDTKPYLREDYRPKSPFVSALTTAPDRPFEGHFDKDVPIHMIDLPTPKEHLSMCDALCTAPERGYTPLNPENAMHRVDEEQKQQELKKREFQVLDHEEELGIRPEPPQSVEYYETRRDQPRKSSAFAAMQAFQPSREPLSSNTVSNAGSVADTPRASIVSALKEETDLEYQKYLKAQQRNQKRLDYFHQKEEELSGLQGQQLTQLQRELSNQQQNLLSQQQLQQSKLLQLQQCVQSQELQQQVQHLTQKSQQQPPQANQQQQQQQQQRGTQQQQHSQVTQRTQQQQQQVPQQVTQQQQQEHSLLSQTTLAETQTLQANAQSQSSASYSSKATACSNSSSTVPPANTSTAFAPAPAPAPTSIPVRPSAIAVQSSYCSSQFDVHELIEETAEELEHSEVLFPPPSPLSHLTKQGKAVQSGLHKADSIPKYQRNWTVLPTQSPIRTPEPQELRENVPLAFVDAPKAPVTSDSSTVHRPIAQVAAPTTVVAPSREREKERRPQLSVPIIVEDRSGPVTMAFQPLDELVRPDQALTPTRPYTPSLTNKPAPIVPFYQTEEKLVFEECSATHARNYNELNASPFPDRTRSPAPGPPPNPLNAIRAPRMKEPETKSNILSVSGGPRLQTGSITTGQSYQGQLLAHSEQSSQSASQSYNQQPERITEQRVGNLNIQQREQSSQLQQQAQSQTQSQTRSQVGNTQIERRRKVTEEFERTQSAKTIEIRTGSQSVSQSKAQSQSISQAQTQAQSQSQNQSDTERRSSYGKTGFVASQAKRLSCMEEEISSLTSQSQAISARASALGEGCFPNLRSPTFDSKFPLKPAPAESIVPGYATVPAATKMLTAPPPGFLQQQQQQQQRSAFSGYQATTSSVQQSSFASSSKATTSSLSSSSASASASASVARSSQSLTQASAITTTTNNQATTAYRSSNGSITKPNLASRPSIASITAPGSASAPAPVPSAAPTKATAPFKAPIVPKSVIANAVNAAAPPAPAVFPPDLSDLNLNSNVDNSPGAGGKSAGAFGATSAPKRGRGILNKAAGPGVRIPLCNSCNVQIRGPFITALGRIWCPDHFICVNGNCRRPLQDIGFVEEKGDLYCEYCFEKYLAPTCSKCAGKIKGDCLNAIGKHFHPECFTCGQCGKIFGNRPFFLEDGNAYCEADWNELFTTKCFACGFPVEAGDRWVEALNHNYHSQCFNCTFCKQNLEGQSFYNKGGRPFCKNHAR
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
141PhosphorylationNNAARPFSNGGDGGV
CCCCCCCCCCCCCCH		36.9319429919
239 (in isoform 5)Phosphorylation-28.6428490779
239 (in isoform 4)Phosphorylation-28.6428490779
348PhosphorylationPPTGTEGYVPVPIKP
CCCCCCCEEECCCCC		8.7118281928
490 (in isoform 3)Phosphorylation-42.9819429919
494 (in isoform 3)Phosphorylation-42.1319429919
557 (in isoform 3)Phosphorylation-61.1019429919
737PhosphorylationDYPSGRRSAQECVDS
CCCCCCCCHHHHHHH		32.7028490779
744PhosphorylationSAQECVDSLAVPLST
CHHHHHHHCCCCHHH		9.6128490779
762PhosphorylationVDMVREVTPSPVTTP
HHCCCCCCCCCCCCC		17.1928490779
764PhosphorylationMVREVTPSPVTTPTQ
CCCCCCCCCCCCCCC		23.7228490779
767PhosphorylationEVTPSPVTTPTQTPA
CCCCCCCCCCCCCCC		30.3728490779
924PhosphorylationAAPPATVSVEPSPAP
CCCCCEEEECCCCCC		19.1928490779
928PhosphorylationATVSVEPSPAPLRES
CEEEECCCCCCCCCC		21.8628490779
935PhosphorylationSPAPLRESPPRGSRL
CCCCCCCCCCCCCCC		33.5028490779
992PhosphorylationREDYRPKSPFVSALT
CCCCCCCCCCCCHHC		26.6727794539
1023PhosphorylationIHMIDLPTPKEHLSM
CEEEECCCCHHHHHH		55.0527794539
1134PhosphorylationVADTPRASIVSALKE
CCCCCCHHHHHHHHH		25.4628490779
1137PhosphorylationTPRASIVSALKEETD
CCCHHHHHHHHHHHC		26.6428490779
1401PhosphorylationSGLHKADSIPKYQRN
CCCCCCCCCCCCCCC		45.7227794539
1416PhosphorylationWTVLPTQSPIRTPEP
CEECCCCCCCCCCCH		25.4428490779
1420PhosphorylationPTQSPIRTPEPQELR
CCCCCCCCCCHHHHH		32.4928490779
1559PhosphorylationASPFPDRTRSPAPGP
CCCCCCCCCCCCCCC		42.7628490779
1561PhosphorylationPFPDRTRSPAPGPPP
CCCCCCCCCCCCCCC		25.4628490779
1689PhosphorylationEEFERTQSAKTIEIR
HHHHHHHCCEEEEEE		30.9927794539
1697PhosphorylationAKTIEIRTGSQSVSQ
CEEEEEECCCCCCCH		47.0127794539
1699PhosphorylationTIEIRTGSQSVSQSK
EEEEECCCCCCCHHH		20.7627794539
1701PhosphorylationEIRTGSQSVSQSKAQ
EEECCCCCCCHHHHH		25.9827794539
1782PhosphorylationGCFPNLRSPTFDSKF
CCCCCCCCCCCCCCC		31.3028490779
1784PhosphorylationFPNLRSPTFDSKFPL
CCCCCCCCCCCCCCC		41.1228490779
1787PhosphorylationLRSPTFDSKFPLKPA
CCCCCCCCCCCCCCC		31.8228490779
1983PhosphorylationLNSNVDNSPGAGGKS
CCCCCCCCCCCCCCC		21.9027794539
1990PhosphorylationSPGAGGKSAGAFGAT
CCCCCCCCCCCCCCC		34.9027794539
1998PhosphorylationAGAFGATSAPKRGRG
CCCCCCCCCCCCCCC		41.8827794539
2179PhosphorylationKQNLEGQSFYNKGGR
CCHHCCCCCCCCCCC		40.3227794539
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 ZASP_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZASP_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 ZASP_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EI3D2_DROMECG4810physical
14605208
CEG1A_DROMECenG1Aphysical
14605208
MTND_DROMECG32068physical
14605208
MMD4_DROMEmod(mdg4)physical
14605208
ACTN_DROMEActnphysical
14605208
RS3_DROMERpS3physical
14605208
MAL2_DROMEMal-A2physical
14605208
ACTN_DROMEActnphysical
18166658
ACTN_DROMEActnphysical
23505387
ACTN_DROMEActnphysical
27783625
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZASP_DROME

loading...

Related Literatures of Post-Translational Modification

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