CPSF2_DROME - dbPTM
CPSF2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF2_DROME
UniProt AC Q9V3D6
Protein Name Probable cleavage and polyadenylation specificity factor subunit 2
Gene Name Cpsf100
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 756
Subcellular Localization Nucleus .
Protein Description Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Required for the cotranscriptional processing of 3'-ends of polyadenylated and histone pre-mRNA..
Protein Sequence MTSIIKLHTISGAMDESPPCYILQIDDVRILLDCGWDEKFDANFIKELKRQVHTLDAVLLSHPDAYHLGALPYLVGKLGLNCPIYATIPVFKMGQMFMYDLYMSHFNMGDFDLFSLDDVDTAFEKITQLKYNQTVSLKDKGYGISITPLNAGHMIGGTIWKIVKVGEEDIVYATDFNHKKERHLSGCELDRLQRPSLLITDAYNAQYQQARRRARDEKLMTNILQTVRNNGNVLIAVDTAGRVLELAHMLDQLWKNKESGLMAYSLALLNNVSYNVIEFAKSQIEWMSDKLTKAFEGARNNPFQFKHIQLCHSLADVYKLPAGPKVVLASTPDLESGFTRDLFVQWASNANNSIILTTRTSPGTLAMELVENCAPGKQIELDVRRRVDLEGAELEEYLRTQGEKLNPLIVKPDVEEESSSESEDDIEMSVITGKHDIVVRPEGRHHSGFFKSNKRHHVMFPYHEEKVKCDEYGEIINLDDYRIADATGYEFVPMEEQNKENVKKEEPGIGAEQQANGGIVDNDVQLLEKPTKLISQRKTIEVNAQVQRIDFEGRSDGESMLKILSQLRPRRVIVIHGTAEGTQVVARHCEQNVGARVFTPQKGEIIDVTSEIHIYQVRLTEGLVSQLQFQKGKDAEVAWVDGRLGMRVKAIEAPMDVTVEQDASVQEGKTLTLETLADDEIPIHNSVLINELKLSDFKQTLMRNNINSEFSGGVLWCSNGTLALRRVDAGKVAMEGCLSEEYYKIRELLYEQYAIV
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
221PhosphorylationARDEKLMTNILQTVR
HHHHHHHHHHHHHHH
29.5522817900
226PhosphorylationLMTNILQTVRNNGNV
HHHHHHHHHHHCCCE
20.2822817900
418PhosphorylationKPDVEEESSSESEDD
CCCCCCCCCCCCCCC
42.3019429919
419PhosphorylationPDVEEESSSESEDDI
CCCCCCCCCCCCCCE
41.2119429919
420PhosphorylationDVEEESSSESEDDIE
CCCCCCCCCCCCCEE
55.1919429919
422PhosphorylationEEESSSESEDDIEMS
CCCCCCCCCCCEEEE
48.5519429919

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 CPSF2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPSF2_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 CPSF2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYMPK_DROMESymphysical
26081560
CPSF3_DROMECpsf73physical
26081560

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPSF2_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 THR-221 AND THR-226, ANDMASS SPECTROMETRY.

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