CLASP_DROME - dbPTM
CLASP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLASP_DROME
UniProt AC Q9NBD7
Protein Name CLIP-associating protein
Gene Name chb
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1491
Subcellular Localization Cytoplasm, cytoskeleton. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cell projection, growth cone. Cleavage furrow. Localizes to punctate cytoplasmic foci in interphase. Concentrates
Protein Description Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Required for several aspects of mitotic spindle formation including the formation of the overlapping central spindle microtubules and kinetochore attachment. Required for the incorporation of tubulin subunits at the plus ends of kinetochore microtubules during poleward microtubule flux. Acts antagonistically to Klp10A and Klp67A to maintain metaphase spindle length. Also required for guidance of CNS axons downstream of Abl. May function to identify a subset of microtubules that probe the peripheral growth cone domain, where guidance signals exert their influence on cytoskeletal organization. Also required during oogenesis for the organization of the polarized microtubule network inside the 16-cell cyst that ensures oocyte differentiation..
Protein Sequence MAYRKPSDLDGFIQQMPKADMRVKVQLAEDLVTFLSDDTNSIVCTDMGFLIDGLMPWLTGSHFKIAQKSLEAFSELIKRLGSDFNAYTATVLPHVIDRLGDSRDTVREKAQLLLRDLMEHRVLPPQALIDKLATSCFKHKNAKVREEFLQTIVNALHEYGTQQLSVRVYIPPVCALLGDPTVNVREAAIQTLVEIYKHVGDRLRPDLRRMDDVPASKLAMLEQKFDQVKQEGLLLPSALKNTNGNGVGLDEADNIGLRERPTRMIKRPLHSAVSSSLRPKPNVNDVTGDAGAVTMESFESSFEVVPQLNIFHAKDMDDIYKQVLVIISDKNADWEKRVDALKKIRALLILSYHTQPQFVAVQLKELSLSFVDILKEELRSQVIREACITIAYMSKTLRNKLDAFCWSILEHLINLIQNSAKVIASASTIALKYIIKYTHAPKLLKIYTDTLNQSKSKDIRSTLCELMVLLFEEWQTKALERNATVLRDTLKKSIGDADCDARRHSRYAYWAFRRHFPELADQIYGTLDIAAQRALEREREGGGGGGTGTGTGTAPETRRTVSRIGRTPGTLQKPTPSMRSISAVDTAAAQRAKVRAQYTLYSRQRKPLGPNNSNQASMTGAAASGSLPRPRLNSNSGGTPATTPGSVTPRPRGRAGVSQSQPGSRSTSPSTKLRDQYGGIGNYYRGATGAIPKKASGIPRSTASSRETSPTRSGGGLMKRSMYSTGAGSRRTPERNNPVRPSAAARLLAQSREAEHTLGVGDDGQPDYVSGDYMRSGGMRMGRKLMGRDESDDIDSEASSVCSERSFDSSYTRGNKSNYSLSGSHTRLDWSTQRAPFDDIETIIQFCASTHWSERKDGLISLTQYLADGKELTQQQLKCVLDMFRKMFMDTHTKVYSLFLDTVTELILVHANELHEWLFILLTRLFNKLGTDLLNSMHSKIWKTLQVVHEYFPTQLQLKELFRIISDSTQTPTTKTRIAILRFLTDLANTYCKSSDFPSDQSQACERTVLKLAQLAADQKSMELRSQARSCLVALYNLNTPQMTLLLADLPKVYQDSARSCIHSHMRRQSQSCNSGANSPSSSPLSSSSPKPLQSPSVGPFASLQSHHHQLSISSTSPRSRQSSVEQELLFSSELDIQHNIQKTSEEIRHCFGGQYQTALAPNGFNGHLQYHDQGQQDSCASLSSNSKTQSSANTTQSNTPESATMRLDNLERERTTQNAKSPTDDAKVITVSINMAENGELILASNLMESEVVRVALTLTKDQPVELLQTSLTNLGICIKGGNCELPNKHFRSIMRMLLNILEAEHTDVVIAGLHVLSKIMRSNKMRHNWMHFLELILLKIIQCYQHSKEALRDIDSMIPRIAPSLPLDLSINIVNPVIATGEFPTNLCAIKILLEVTEHHGSEITDAHLDIVFPNLARSADDTQSMVRKAAVFCIVKLYFVLGEEKVKPKLSVLNPSKVRLLNVYIEKQRNCISGGGSSTKNSSAASSS
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
570PhosphorylationRIGRTPGTLQKPTPS
HCCCCCCCCCCCCCC		27.5021082442
580PhosphorylationKPTPSMRSISAVDTA
CCCCCCHHHHHHHHH		16.5619429919
582PhosphorylationTPSMRSISAVDTAAA
CCCCHHHHHHHHHHH		24.4019429919
586PhosphorylationRSISAVDTAAAQRAK
HHHHHHHHHHHHHHH		16.1729892262
624PhosphorylationSMTGAAASGSLPRPR
HHCCCCCCCCCCCCC		24.9621082442
626PhosphorylationTGAAASGSLPRPRLN
CCCCCCCCCCCCCCC		32.4819060867
634PhosphorylationLPRPRLNSNSGGTPA
CCCCCCCCCCCCCCC		36.6419429919
636PhosphorylationRPRLNSNSGGTPATT
CCCCCCCCCCCCCCC		38.1219429919
648PhosphorylationATTPGSVTPRPRGRA
CCCCCCCCCCCCCCC		18.4422817900
658PhosphorylationPRGRAGVSQSQPGSR
CCCCCCCCCCCCCCC		24.1729892262
660PhosphorylationGRAGVSQSQPGSRST
CCCCCCCCCCCCCCC		30.7325749252
664PhosphorylationVSQSQPGSRSTSPST
CCCCCCCCCCCCCCC		29.7319429919
666PhosphorylationQSQPGSRSTSPSTKL
CCCCCCCCCCCCCHH		34.6325749252
677PhosphorylationSTKLRDQYGGIGNYY
CCHHHHHCCCCCCCC		22.9319429919
701PhosphorylationKASGIPRSTASSRET
CCCCCCCCCCCCCCC		23.9925749252
708PhosphorylationSTASSRETSPTRSGG
CCCCCCCCCCCCCCC		38.6130478224
709PhosphorylationTASSRETSPTRSGGG
CCCCCCCCCCCCCCC		21.3730478224
713PhosphorylationRETSPTRSGGGLMKR
CCCCCCCCCCCCCCC		44.2430478224
742PhosphorylationRNNPVRPSAAARLLA
CCCCCCHHHHHHHHH		21.7019429919
751PhosphorylationAARLLAQSREAEHTL
HHHHHHHHCCHHHCC		26.8725749252
757PhosphorylationQSREAEHTLGVGDDG
HHCCHHHCCCCCCCC		19.4019429919
768PhosphorylationGDDGQPDYVSGDYMR
CCCCCCCCCCCCCHH		11.8219429919
770PhosphorylationDGQPDYVSGDYMRSG
CCCCCCCCCCCHHCC		21.5122668510
773PhosphorylationPDYVSGDYMRSGGMR
CCCCCCCCHHCCCCC		9.6519429919
800PhosphorylationDIDSEASSVCSERSF
CCCHHHHHHHCCCCC		33.9029892262
803PhosphorylationSEASSVCSERSFDSS
HHHHHHHCCCCCCCC		33.6129892262
806PhosphorylationSSVCSERSFDSSYTR
HHHHCCCCCCCCCCC		29.3819429919
809PhosphorylationCSERSFDSSYTRGNK
HCCCCCCCCCCCCCC		24.1919429919
817PhosphorylationSYTRGNKSNYSLSGS
CCCCCCCCCCCCCCC		45.0319429919
820PhosphorylationRGNKSNYSLSGSHTR
CCCCCCCCCCCCCCC		21.9519429919
822PhosphorylationNKSNYSLSGSHTRLD
CCCCCCCCCCCCCCC		32.1019429919
824PhosphorylationSNYSLSGSHTRLDWS
CCCCCCCCCCCCCCC		20.5019429919
826PhosphorylationYSLSGSHTRLDWSTQ
CCCCCCCCCCCCCCC		34.3219429919
1095PhosphorylationSSPKPLQSPSVGPFA
CCCCCCCCCCCCCCC		27.1619429919
1097PhosphorylationPKPLQSPSVGPFASL
CCCCCCCCCCCCCHH		44.9819429919
1120PhosphorylationISSTSPRSRQSSVEQ
CCCCCCCCCCCHHHH		37.7522817900
1123PhosphorylationTSPRSRQSSVEQELL
CCCCCCCCHHHHHHH		34.9322817900
1124PhosphorylationSPRSRQSSVEQELLF
CCCCCCCHHHHHHHH		22.7222817900
1200PhosphorylationANTTQSNTPESATMR
CCCCCCCCCCCHHHH		33.4130478224
1222PhosphorylationRTTQNAKSPTDDAKV
HHCCCCCCCCCCCCE		30.5327626673
1224PhosphorylationTQNAKSPTDDAKVIT
CCCCCCCCCCCCEEE		54.3121082442
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 CLASP_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLASP_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 CLASP_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FD3_DROMEfd59Aphysical
14605208
NPC2_DROMENpc2agenetic
20498300
SUDX_DROMESu(dx)genetic
20498300
POK_DROMEaopgenetic
20498300
CAPU_DROMEcapugenetic
20498300
SWET1_DROMEslvgenetic
20498300
PNUT_DROMEpnutgenetic
20498300
CALM_DROMECamgenetic
20498300
SUZ2_DROMESu(z)2genetic
20498300
TRA2_DROMEtra2genetic
20498300
MYSN_DROMEzipgenetic
20498300
DAB_DROMEDabgenetic
20498300
NU301_DROMEE(bx)genetic
20498300
ABL_DROMEAblgenetic
15207236
EIF1A_DROMECG31957genetic
20498300
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CLASP_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-634; THR-648; SER-806;SER-817; SER-820; SER-822; SER-824; SER-1120; SER-1123 AND SER-1124,AND MASS SPECTROMETRY.
"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-582; SER-626; SER-1120AND SER-1123, AND MASS SPECTROMETRY.

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