BBP_SCHPO - dbPTM
BBP_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BBP_SCHPO
UniProt AC O74555
Protein Name Branchpoint-bridging protein
Gene Name bpb1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 587
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Necessary for the splicing of pre-mRNA. The BPB1(SF1)-u2af59-u2af23 complex has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns..
Protein Sequence MLNSRSVGSTGSNNTPLGRRRFDEKPDSLPPLPDANGMSNGYRDSYKSNSRMDHRPDGYHDGRGRRAYRKHYWGHPTPIEEMLPSQMELETAVKSCMTMEQLELYSLNVRLEEITQKLRTGDVVPHHRERSPSPPPQYDNHGRRLNTREIRYKKKLEDERHRIIERAMKMVPGFRAPSDYRRPAKTQEKVYVPVKDYPEINFIGLLIGPRGHTLKDMEAKSGAKIAIRGKGSVKEGKGRSDPSVRGNMEEDLHCLVTADSEDKINHAIKLIDNVIQTAASVPEGQNDLKRNQLRQLATLNGTLRDDENQVCQNCGNVGHRRFDCPERINHTMNIVCRHCGSIGHIARDCPVRDQQPPMADSTADREYQSLMQELGGGSAISNGNGEPQKSIEFSESGAASPQAGHPPPWAAASTSVSSSTSSPAPWAKPASSAAPSNPAPWQQPAAPQSAPALSMNPSSLPPWQQPTQQSAVQPSNLVPSQNAPFIPGTSAPLPPTTFAPPGVPLPPIPGAPGMPNLNMSQPPMVPPGMALPPGMPAPFPGYPAVPAMPGIPGATAPPGAPGSYNTSESSNLNAPPGVSMPNGYSNR
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
6Phosphorylation--MLNSRSVGSTGSN
--CCCCCCCCCCCCC
30.5629996109
9PhosphorylationLNSRSVGSTGSNNTP
CCCCCCCCCCCCCCC
27.6929996109
10PhosphorylationNSRSVGSTGSNNTPL
CCCCCCCCCCCCCCC
38.4129996109
12PhosphorylationRSVGSTGSNNTPLGR
CCCCCCCCCCCCCCC
27.3129996109
15PhosphorylationGSTGSNNTPLGRRRF
CCCCCCCCCCCCCCC
24.9229996109
131PhosphorylationVPHHRERSPSPPPQY
CCCCCCCCCCCCCCC
25.6128889911
133PhosphorylationHHRERSPSPPPQYDN
CCCCCCCCCCCCCCC
51.8128889911
138PhosphorylationSPSPPPQYDNHGRRL
CCCCCCCCCCCCCCC
25.2029996109
390PhosphorylationGNGEPQKSIEFSESG
CCCCCCCEEEECCCC
23.3121712547
394PhosphorylationPQKSIEFSESGAASP
CCCEEEECCCCCCCC
20.3327738172
396PhosphorylationKSIEFSESGAASPQA
CEEEECCCCCCCCCC
32.3127738172
400PhosphorylationFSESGAASPQAGHPP
ECCCCCCCCCCCCCC
19.6021712547
419PhosphorylationASTSVSSSTSSPAPW
HCCCCCCCCCCCCCC
25.4621712547

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 BBP_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BBP_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 BBP_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U2AF2_SCHPOprp2physical
10923022
YC93_SCHPOSPCC584.03cgenetic
22681890
GET1_SCHPOget1genetic
22681890
SRP2_SCHPOsrp2genetic
26302002

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

loading...

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-131 AND SER-133, ANDMASS SPECTROMETRY.

TOP