COS_DROME - dbPTM
COS_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COS_DROME
UniProt AC O16844
Protein Name Kinesin-like protein costa
Gene Name cos
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1201
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation, which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh signaling inhibits ci phosphorylation by interfering with the cos-ci-kinases complex formation. Negatively regulates hh-signaling pathways during various processes, including photoreceptor differentiation. [PubMed: 25639794]
Protein Sequence MEIPIQVAVRIFPHRELKDLLRSFGPTEPKKDAQAVDEGADSKDSEAQVPAAEKDNPSISETDPNGNAEQDSAADSKTIPDANGNDSGQKDYPDSAYCVQAIPISASALGLPSALPGGDPMDSIAAGLIQVGPHTVPVTHALPSSSSQEQVYHQTVFPLITLFLEGFDASVVTYGQRGQGKSYTLYGNVQDPTLTDSTEGVVQLCVRDIFSHISLHPERTYAINVGFVEICGGDVCDLLGMGNIHCTNVDAVFHWLQVGLSARQSLPAHTLFTLTLEQQWVSKEGLLQHRLSTASFSDLCGTERCGDQPPGRPLDAGLCMLEQVISTLTDPGLMYGVNGNIPYGQTTLTTLLKDSFGGRAQTLVILCVSPLEEHLPETLGNLQFAFKVQCVRNFVIMNTYSDDNTMIVQPAEPVPESNSSAGPLSQAGPGDNFGLQFAASQWSKLVTNAEGLFSKLIDSKLITEVEKEQIEEWLFLKQECEECLSSTEAMRQQKQLVPILEAEEPEDVNSEAANSESPNSDNENDTDNESHRPDLDDKIESLMEEFRDKTDALILEKHAEYLSKHPKAVMQSQDREIEAQPPEENGDDRKVSIGSRRRSVQPGASLSTAELAMLNRVASQQPPPPIDPESVVDPLESSSGEGIRQAALAAAAATAPIEQLQKKLRKLVAEIEGKQRQLREIEETIQVKQNIIAELVKNSDTRSHAKQRFHKKRAKLEAECDKAKKQLGKALVQGRDQSEIERWTTIIGHLERRLEDLSSMKHIAGESGQKVKKLQQSVGESRKQADDLQKKLRKECKLRCQMEAELAKLRESRETGKELVKAQGSPEQQGRQLKAVQARITHLNHILREKSDNLEEQPGPEQQETLRHEIRNLRGTRDLLLEERCHLDRKLKRDKVLTQKEERKLLECDEAIEAIDAAIEFKNEMITGHRSIDTSDRIQREKGEQMLMARLNRLSTEEMRTLLYKYFTKVIDLRDSSRKLELQLVQLERERDAWEWKERVLSNAVRQARLEGERNAVLLQRQHEMKLTLMLRHMAEETSASSASYGERALAPACVAPPVQASSDFDYDHFYKGGGNPSKALIKAPKPMPTGSALDKYKDKEQRSGRNIFAKFHVLTRYASAAAAGSSGSTAEESTALIESTTTATATTTSTTTTGAVGKVKDKALVSFRPEQLKRLMPAPTATKVTRQKNKIIIQDASRRN
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
572PhosphorylationHPKAVMQSQDREIEA
CCHHHHHCCCCCCCC
18.8911934882
592PhosphorylationNGDDRKVSIGSRRRS
CCCCCCEECCCCCCC
25.0229892262
599PhosphorylationSIGSRRRSVQPGASL
ECCCCCCCCCCCCCC
24.2422817900
605PhosphorylationRSVQPGASLSTAELA
CCCCCCCCCCHHHHH
28.8622817900
608PhosphorylationQPGASLSTAELAMLN
CCCCCCCHHHHHHHH
29.4622817900
825PhosphorylationELVKAQGSPEQQGRQ
HHHHHCCCHHHHHHH
17.1225749252
931PhosphorylationEMITGHRSIDTSDRI
CHHHCCCCCCCCHHH
21.1011934882

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
572SPhosphorylationKinaseFUP23647
GPS
931SPhosphorylationKinaseFUP23647
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COS_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 COS_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CI_DROMEciphysical
9244298
CI_DROMEciphysical
10825151
FUSED_DROMEfuphysical
10825151
FUSED_DROMEfuphysical
11495917
FUSED_DROMEfuphysical
11839821
CI_DROMEciphysical
15710747
DICH_DROMEDphysical
15710747
DPOLA_DROMEDNApol-alpha180physical
15710747
KDC2_DROMEPka-C3physical
15710747
FUSED_DROMEfuphysical
22036573
SMO_DROMEsmogenetic
16423832
CI_DROMEcigenetic
22677792
SGG_DROMEsggphysical
21852395
KC1A_DROMECkIalphaphysical
21852395
FUSED_DROMEfuphysical
14636583
FUSED_DROMEfuphysical
14523402
FUSED_DROMEfuphysical
14614827
FUSED_DROMEfuphysical
18987629
FUSED_DROMEfuphysical
25289679
FUSED_DROMEfuphysical
26271100
FUSED_DROMEfuphysical
9244297
FUSED_DROMEfuphysical
15063184
SMO_DROMEsmophysical
14523402
SMO_DROMEsmophysical
14614827
SMO_DROMEsmophysical
14636583
SMO_DROMEsmophysical
17284519
SMO_DROMEsmophysical
25289679
KAPC_DROMEPka-C1physical
25289679
COS_DROMEcosphysical
21844892
PTC_DROMEptcphysical
17284519
SXL_DROMESxlphysical
17284519
GNAI_DROMEGalphaiphysical
18987629
CI_DROMEciphysical
14636583
CI_DROMEciphysical
14523402
CI_DROMEciphysical
21852395
CI_DROMEciphysical
26271100
CI_DROMEciphysical
9244297
CI_DROMEciphysical
11090136
CI_DROMEciphysical
15063184
PP4C_DROMEPp4-19Cphysical
19088085

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COS_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-599 AND SER-605, ANDMASS SPECTROMETRY.

TOP