YBPC_SCHPO - dbPTM
YBPC_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YBPC_SCHPO
UniProt AC O42947
Protein Name Uncharacterized protein C16H5.12c
Gene Name SPBC16H5.12c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 737
Subcellular Localization
Protein Description
Protein Sequence MSVDTAKSDIQAEPSTGTLENKSSKTYSDSENNSTLDVSAQVLTLDNKSRILCIADVRGELSLINSLVEETNASCVIHTGDFGFFERSSLPSISERTLRHIVQFSPLIKKLPRSKNFDYYPSNPIGDLKNSIASHPDCLLSELPQFLSQEKKFSVPVYVVWGACEDVHVLEKFRSGEYSIPNLNIVDELHSYLLQIGDMKIRLLGLGGPYVPFKLFDNGDGKGTIAGGQGTMWTTILQMGELIETAKSLLDREEARIFITHHPIGREGVLSQLATACQADLTLSAGLHFRYGASYNEFCVNHSPEHYLQKLSAARAQFMEVYDTVKAEVEKMVTPEQHHLINNVVRLVSRMPDATNSYAMNNMLPGTAFKNLWNFNLLDASFGWTVFVVENGHVQVESKSHGFNLGYRRMASRRNENYASHIPRSTSENTGTYYYANNRLVESQAQFTKNREATATPTEEEQIEGYDQEHTDELGMSRANTTEESAETHEVIEEKSGPPAAEEEPISGVAEKPSPNEEEQPAIGGKEEVDVEEVTKGTGNLELGETTTEVTILEQENAANVTRSQAQEGRRTDMQKGNDREFRQYSGEQRYERCGFHITPCNSEEEARSYFKDGTDSLITNIQIRTSLNRYKSPQAPQNVNPTNYAYVFVENQNAVSKALGSIKVPEGVRVNIMRDDSYYRQNRGWYRNNRMEGHGTGMRTNRGRGRGGRMNRMQHPRPLQSGGSVNKQSAEPTTHG
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
2Phosphorylation------MSVDTAKSD
------CCCCCCHHH
28.8024763107
5Phosphorylation---MSVDTAKSDIQA
---CCCCCCHHHCCC
33.5529996109
8PhosphorylationMSVDTAKSDIQAEPS
CCCCCCHHHCCCCCC
37.1729996109
15PhosphorylationSDIQAEPSTGTLENK
HHCCCCCCCCCCCCC
30.8629996109
16PhosphorylationDIQAEPSTGTLENKS
HCCCCCCCCCCCCCC
44.9224763107
26PhosphorylationLENKSSKTYSDSENN
CCCCCCCCCCCCCCC
30.1524763107
27PhosphorylationENKSSKTYSDSENNS
CCCCCCCCCCCCCCC
17.7625720772
28PhosphorylationNKSSKTYSDSENNST
CCCCCCCCCCCCCCE
39.6325720772
30PhosphorylationSSKTYSDSENNSTLD
CCCCCCCCCCCCEEE
35.9629996109
34PhosphorylationYSDSENNSTLDVSAQ
CCCCCCCCEEEEEEE
41.7625720772
35PhosphorylationSDSENNSTLDVSAQV
CCCCCCCEEEEEEEE
29.1525720772
105PhosphorylationLRHIVQFSPLIKKLP
HHHHHHHHHHHHHCC
11.1621712547
426PhosphorylationASHIPRSTSENTGTY
HHCCCCCCCCCCCCE
41.1425720772
427PhosphorylationSHIPRSTSENTGTYY
HCCCCCCCCCCCCEE
30.0525720772
454PhosphorylationFTKNREATATPTEEE
HHCCCCCCCCCCHHH
26.7225720772
456PhosphorylationKNREATATPTEEEQI
CCCCCCCCCCHHHHH
26.7928889911
458PhosphorylationREATATPTEEEQIEG
CCCCCCCCHHHHHCC
52.2328889911
466PhosphorylationEEEQIEGYDQEHTDE
HHHHHCCCCHHHHHH
11.1529996109
471PhosphorylationEGYDQEHTDELGMSR
CCCCHHHHHHHCCCC
30.3429996109
477PhosphorylationHTDELGMSRANTTEE
HHHHHCCCCCCCCHH
26.8329996109
481PhosphorylationLGMSRANTTEESAET
HCCCCCCCCHHHHHH
34.3029996109
482PhosphorylationGMSRANTTEESAETH
CCCCCCCCHHHHHHH
37.2525720772
485PhosphorylationRANTTEESAETHEVI
CCCCCHHHHHHHHHH
25.7725720772
514PhosphorylationSGVAEKPSPNEEEQP
CCCCCCCCCCCCCCC
51.9624763107

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 YBPC_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YBPC_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 YBPC_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATF21_SCHPOatf21physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YBPC_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 THR-456 AND THR-458, ANDMASS SPECTROMETRY.

TOP