LASP1_DROME - dbPTM
LASP1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LASP1_DROME
UniProt AC Q8I7C3
Protein Name LIM and SH3 domain protein Lasp
Gene Name Lasp {ECO:0000312|FlyBase:FBgn0063485}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 657
Subcellular Localization
Protein Description
Protein Sequence MNKTCARCQKVVYPIEELKCLDKTWHKTCFKCTECGMTLNMKTYKGYNKMPYCEAHIPKAKATAIADTPELKRIAENTKIQSNVKYHADFEKAKGKFTQVADDPETLRIKQNTKHISNVAYHGDLEKKAAMEKQRGSAEVSDSSNESEYFSEQLAAEQFSQYAPTASPIPPAATTLHQQQQQLQHQQQQQYQQHQQQLQQQQHQHQHYLQQQQQTLPPPPIQHQQYNTAAITPTYQQLQQQQQQQQQQRAQQQQLHDPYAHYQQPQALRQQQQQQQQQQQQLLQQQAIKQASHLYPTATSQQQQMPPPQSPANPQQQALNSYNEMRSAILQNSHHPSGNSVDQYDQPQQQQHQPQQQSTNPTLVAAQQQQSHHSLLNNNASNGGISHSHHSNINNNGHGSQNQMLPPQMRRSAASVVAYDGNSKQQVAAGPGAAQNHLQQLYASPNYAAVTPSENSINVKQHASNGHMPNQQQQHVAGGSNIGKIADYDPLTDGPRVVPNAGRSSTTLVYSSEPRGNQGGNSVYPKRIGSVSDIDPANGIYGSLTAAEQAHQQQKHQQYYQQVQMMQQQEHPPQQQQMRQQPSYSSLQEKQSRQSTAMRVYRAIYDYEAQDVDEVSFREGDVIFEVESIDSGWMTGRVERTGKTGMLPANYVEQAVI
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
68PhosphorylationKATAIADTPELKRIA
HHHHCCCCHHHHHHH		15.0527626673
86PhosphorylationKIQSNVKYHADFEKA
CCCCCCEEEECHHHH		9.6518281928
117PhosphorylationKQNTKHISNVAYHGD
ECCCCCCCCEECCCC		25.6019429919
121PhosphorylationKHISNVAYHGDLEKK
CCCCCEECCCCHHHH		11.3119429919
259PhosphorylationQQQLHDPYAHYQQPQ
HHHHHCHHHHHHHHH		16.4519429919
262PhosphorylationLHDPYAHYQQPQALR
HHCHHHHHHHHHHHH		10.7319429919
310PhosphorylationQQMPPPQSPANPQQQ
CCCCCCCCCCCHHHH		31.5821082442
412PhosphorylationLPPQMRRSAASVVAY
CCHHHHHCCCEEEEE		20.1619429919
415PhosphorylationQMRRSAASVVAYDGN
HHHHCCCEEEEECCC		19.4819429919
419PhosphorylationSAASVVAYDGNSKQQ
CCCEEEEECCCCHHH		16.8718281928
442PhosphorylationQNHLQQLYASPNYAA
HHHHHHHHHCCCEEE		10.7418281928
444PhosphorylationHLQQLYASPNYAAVT
HHHHHHHCCCEEEEC		10.5018281928
447PhosphorylationQLYASPNYAAVTPSE
HHHHCCCEEEECCCC		10.1818281928
451PhosphorylationSPNYAAVTPSENSIN
CCCEEEECCCCCCCC		19.1721082442
456PhosphorylationAVTPSENSINVKQHA
EECCCCCCCCCHHHH		16.1021082442
464PhosphorylationINVKQHASNGHMPNQ
CCCHHHHHCCCCCCH		41.0221082442
488PhosphorylationNIGKIADYDPLTDGP
CCHHCCCCCCCCCCC		15.5018281928
504PhosphorylationVVPNAGRSSTTLVYS
ECCCCCCCCCEEEEE		30.9919429919
505PhosphorylationVPNAGRSSTTLVYSS
CCCCCCCCCEEEEEC		24.8519429919
506PhosphorylationPNAGRSSTTLVYSSE
CCCCCCCCEEEEECC		25.9519429919
507PhosphorylationNAGRSSTTLVYSSEP
CCCCCCCEEEEECCC		19.0419429919
510PhosphorylationRSSTTLVYSSEPRGN
CCCCEEEEECCCCCC		15.0219429919
524PhosphorylationNQGGNSVYPKRIGSV
CCCCCCCCCCCCCCC		11.6718281928
530PhosphorylationVYPKRIGSVSDIDPA
CCCCCCCCCCCCCCC		18.9719429919
532PhosphorylationPKRIGSVSDIDPANG
CCCCCCCCCCCCCCC		30.4619429919
541PhosphorylationIDPANGIYGSLTAAE
CCCCCCCHHHHHHHH		11.3219429919
543PhosphorylationPANGIYGSLTAAEQA
CCCCCHHHHHHHHHH		12.9419429919
545PhosphorylationNGIYGSLTAAEQAHQ
CCCHHHHHHHHHHHH		26.0619429919
559PhosphorylationQQQKHQQYYQQVQMM
HHHHHHHHHHHHHHH		9.1819429919
560PhosphorylationQQKHQQYYQQVQMMQ
HHHHHHHHHHHHHHH		6.5319429919
583PhosphorylationQQMRQQPSYSSLQEK
HHHHHCCCHHHHHHH		33.0521082442
584PhosphorylationQMRQQPSYSSLQEKQ
HHHHCCCHHHHHHHH		14.6819060867
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 LASP1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LASP1_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 LASP1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OSKA_DROMEoskgenetic
19036801
ACTN_DROMEActnphysical
25113030
ACT1_DROMEAct5Cphysical
25113030
TNNT_DROMEupphysical
25113030
TNNI_DROMEwupAphysical
25113030
MYSA_DROMEMhcphysical
25113030
ACT2_DROMEAct42Aphysical
25113030
ACT3_DROMEAct57Bphysical
25113030
ACT4_DROMEAct79Bphysical
25113030
OSKA_DROMEoskphysical
19036801
ACT6_DROMEAct88Fphysical
25113030
TITIN_DROMEslsphysical
25113030
ACT5_DROMEAct87Ephysical
25113030
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LASP1_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-530, 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 SER-505 AND SER-530, ANDMASS SPECTROMETRY.

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