RBA50_SCHPO - dbPTM
RBA50_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBA50_SCHPO
UniProt AC O43088
Protein Name RNA polymerase II-associated protein rba50
Gene Name rba50
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 452
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation..
Protein Sequence MENHRSVFSNVIGDIVEKPPKQLVEVKRSVQRHARGFPAVSRTLPKRESKSMSAYKEKMLRKNKESPGLEGKGNLDDQGIDEENRVRLERMNDLEIEGAQEEIRATIRDDLLEMLKKRAFKKKAERELAQRKDRSSQVNTPDLSQRPSDDSFLSNEKLRSSEKLNRNLQSVLSSEAVDSSSGSPSPPMALSQAEIRSRQTKRVMFPDKAEELTKIFSLPTLAPIKGNEEDDASEDAKHSPKKHSPALSDGTTSNDGAPLEFDTTHLPEKQVTLDPNDPSFYEQLHDKYFPNLPVDEKQMQWLHDPSPAENSYHPSVESLHAHEIRFGFKGEIITPSQSQTIPVNEGLHHHGDAPFSAGYTLVELAHLLRSSFPTQRCIAIQTIGRIIYRLNSGEFREVLSPELHTLVEDAHIYELLAAAASDQVKHLTVRSLAIEALWLCSQSQHGSSRSAV
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
66PhosphorylationMLRKNKESPGLEGKG
HHHHCCCCCCCCCCC
26.3624763107
135PhosphorylationLAQRKDRSSQVNTPD
HHHHHCCCCCCCCCC
34.9424763107
136PhosphorylationAQRKDRSSQVNTPDL
HHHHCCCCCCCCCCH
38.7621712547
140PhosphorylationDRSSQVNTPDLSQRP
CCCCCCCCCCHHHCC
21.2324763107
151PhosphorylationSQRPSDDSFLSNEKL
HHCCCCCCCCCHHHH
32.8321712547
183PhosphorylationAVDSSSGSPSPPMAL
HHCCCCCCCCCCCCC
24.9325720772
185PhosphorylationDSSSGSPSPPMALSQ
CCCCCCCCCCCCCCH
43.2529996109
217PhosphorylationEELTKIFSLPTLAPI
HHHHHHHCCCCCCCC
36.5927738172
233PhosphorylationGNEEDDASEDAKHSP
CCCCCCCCCHHCCCC
42.9021712547
239PhosphorylationASEDAKHSPKKHSPA
CCCHHCCCCCCCCCC
37.3921712547
244PhosphorylationKHSPKKHSPALSDGT
CCCCCCCCCCCCCCC
22.2828889911
248PhosphorylationKKHSPALSDGTTSND
CCCCCCCCCCCCCCC
35.7821712547
251PhosphorylationSPALSDGTTSNDGAP
CCCCCCCCCCCCCCC
31.8521712547
252PhosphorylationPALSDGTTSNDGAPL
CCCCCCCCCCCCCCC
30.9421712547
392PhosphorylationRIIYRLNSGEFREVL
HHHHHCCCCCHHHHH
44.2728889911
413PhosphorylationLVEDAHIYELLAAAA
HHCHHHHHHHHHHHC
7.2328889911
421PhosphorylationELLAAAASDQVKHLT
HHHHHHCCHHCCCHH
24.6928889911

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 RBA50_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBA50_SCHPO !!

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 RBA50_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RBA50_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBA50_SCHPO

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Related Literatures of Post-Translational Modification

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