CPSF6_DROME - dbPTM
CPSF6_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF6_DROME
UniProt AC Q9VSH4
Protein Name Cleavage and polyadenylation specificity factor subunit CG7185
Gene Name CG7185
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 652
Subcellular Localization Nucleus.
Protein Description May play a role in pre-mRNA 3'-processing..
Protein Sequence MADVVLDLYAEDLDKDFAGQAQDEFGGDGVDLYDDIGGPTESAASGGGGGGTPSADGAAGPGSGEPGERNSGGPNGVYHQSSGSLTPTMNRRYQLYVGNLTWWTTDQDIANSLRDIGVSDLQEVKFFENRANGQSKGFSVISLGSESSLRAVLDQLPKKEMHGQAPVVTYPSKQALTQFESLQKTRPVPPPQQNGPPRGPAPPSMGGGPMPTGHPGGPQGGGPPGHPPRGMNSIMQPGQYRPQHMSQVPQVGGPNSGPPRMQPPMHPQGGLMGNQQPPPRYPSAQGQWPGQRPGGPRPGPPNGPPQRPMFQGGPMGMPVRGPAGPDWRRPPMHGGFPPQGPPRGLPPAPGPGGPHGAPAPHVNPAFFNQPGGPAQHPGMGGPPHGAPGPQPGMNMPPQQGMNMTPQHGPPPQFAQHGPRGPWPPPQGKPPGPFPDPQQMGPQLTEVEFEEVMSRNRTVSSSAIARAVSDAAAGEYSSAIETLVTAISLIKQSKVAHDERCKILISSLQDTLHGIEAKSYNRRERSRSRERSHRSRQRRERSTSRYRERSRERERDRDRERERDGGSYRERSRSRERERQAPDHYRDDSRSVRPRKSPEPVVAEAAEAPSSKRYYEDRERYRSSDRERRDRDRDRDRERERDRDRREEHRSRH
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
45PhosphorylationGPTESAASGGGGGGT
CCCCCCCCCCCCCCC
37.3719429919
52PhosphorylationSGGGGGGTPSADGAA
CCCCCCCCCCCCCCC
19.8319429919
54PhosphorylationGGGGGTPSADGAAGP
CCCCCCCCCCCCCCC
38.5419429919
84PhosphorylationVYHQSSGSLTPTMNR
CCCCCCCCCCCCCCC
30.9019429919
86PhosphorylationHQSSGSLTPTMNRRY
CCCCCCCCCCCCCEE
20.5719429919
88PhosphorylationSSGSLTPTMNRRYQL
CCCCCCCCCCCEEEE
23.1119429919
468PhosphorylationSAIARAVSDAAAGEY
HHHHHHHHHHHHCCH
22.1323607784
475PhosphorylationSDAAAGEYSSAIETL
HHHHHCCHHHHHHHH
13.6523607784
476PhosphorylationDAAAGEYSSAIETLV
HHHHCCHHHHHHHHH
14.7023607784
477PhosphorylationAAAGEYSSAIETLVT
HHHCCHHHHHHHHHH
32.1523607784
481PhosphorylationEYSSAIETLVTAISL
CHHHHHHHHHHHHHH
22.0323607784
484PhosphorylationSAIETLVTAISLIKQ
HHHHHHHHHHHHHHH
22.7623607784
487PhosphorylationETLVTAISLIKQSKV
HHHHHHHHHHHHHHC
22.9023607784
492PhosphorylationAISLIKQSKVAHDER
HHHHHHHHHCCCHHH
24.8923607784
541PhosphorylationSRQRRERSTSRYRER
HHHHHHHHHHHHHHH
26.4425749252
542PhosphorylationRQRRERSTSRYRERS
HHHHHHHHHHHHHHH
24.3625749252
543PhosphorylationQRRERSTSRYRERSR
HHHHHHHHHHHHHHH
28.6725749252
596PhosphorylationRSVRPRKSPEPVVAE
CCCCCCCCCCCHHHH
35.4621082442
622PhosphorylationEDRERYRSSDRERRD
HHHHHHHHCHHHHHH
27.8822817900
623PhosphorylationDRERYRSSDRERRDR
HHHHHHHCHHHHHHH
31.5225749252

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 CPSF6_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPSF6_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 CPSF6_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED17_DROMEMED17physical
22036573
MED11_DROMEMED11physical
22036573
MED10_DROMEMED10physical
22036573
MED27_DROMEMED27physical
22036573
MED7_DROMEMED7physical
22036573
MED25_DROMEMED25physical
22036573
YAP1_DROMEykiphysical
24114784

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPSF6_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-596, AND MASSSPECTROMETRY.

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