RHP23_SCHPO - dbPTM
RHP23_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHP23_SCHPO
UniProt AC O74803
Protein Name UV excision repair protein rhp23
Gene Name rhp23
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 368
Subcellular Localization Nucleus .
Protein Description Involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA.; Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation..
Protein Sequence MNLTFKNLQQQKFVISDVSADTKISELKEKIQTQQNYEVERQKLIYSGRILADDKTVGEYNIKEQDFIVCMVSRPKTSTSTPKSAASPAPNPPASVPEKKVEAPSSTVAESTSTTQTVAAAAPSNPDTTATSEAPIDANTLAVGAQRNVAVENMVEMGYERSEVERAMRAAFNNPDRAVEYLLTGIPEDILNRQREESAAALAAQQQQSEALAPTSTGQPANLFEQAALSENENQEQPSNTVGDDPLGFLRSIPQFQQLRQIVQQNPQMLETILQQIGQGDPALAQAITQNPEAFLQLLAEGAEGESALPSGGIQIQITQEESESIDRLCQLGFDRNIVIQAYLACDKNEELAANYLFEHGHESEDEP
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
79PhosphorylationVSRPKTSTSTPKSAA
EECCCCCCCCCCCCC
41.6825720772
80PhosphorylationSRPKTSTSTPKSAAS
ECCCCCCCCCCCCCC
42.3425720772
81PhosphorylationRPKTSTSTPKSAASP
CCCCCCCCCCCCCCC
34.5225720772
84PhosphorylationTSTSTPKSAASPAPN
CCCCCCCCCCCCCCC
30.2128889911
87PhosphorylationSTPKSAASPAPNPPA
CCCCCCCCCCCCCCC
22.7028889911
95PhosphorylationPAPNPPASVPEKKVE
CCCCCCCCCCHHHCC
43.9327738172
356PhosphorylationNEELAANYLFEHGHE
CHHHHHHHHHHCCCC
14.1921712547
364PhosphorylationLFEHGHESEDEP---
HHHCCCCCCCCC---
44.6828889911

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 RHP23_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHP23_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 RHP23_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPN1_SCHPOmts4physical
12615927
CUT9_SCHPOcut9physical
12615927
RL401_SCHPOubi1physical
11788722
RL402_SCHPOubi1physical
11788722
RS27A_SCHPOubi3physical
11788722
DSK2_SCHPOdph1physical
11788722
ATF1_SCHPOatf1physical
11584278
RPN1_SCHPOmts4physical
11584278
UBI4P_SCHPOubi4physical
17211518
RPN1_SCHPOmts4physical
20614012
ATL1_SCHPOatl1genetic
22658721
UBI4P_SCHPOubi4physical
23038266
PUS1_SCHPOpus1genetic
23038266
UBI4P_SCHPOubi4physical
25306921

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHP23_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-87 AND SER-364,AND MASS SPECTROMETRY.

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