YJQ1_SCHPO - dbPTM
YJQ1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YJQ1_SCHPO
UniProt AC Q9USH9
Protein Name Uncharacterized ABC transporter ATP-binding protein C825.01
Gene Name SPCC825.01
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 822
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MARGKRSTQRDADLELESLQSEIESESPQPVTKSKAKKNKKKLNKASAFNSDNDSNYDLKPEDDEVDEEVVPVKKKPSKKSKKAKANAFEAFADEQSVEEEEEEDSEKPVRKNKKSSKKASPKNAFDALADDMDDLSLDEEESESSEKSKKKKKKSKSKDDGSEALDDGDIESSEKDKKKKKKSKENDDAPKKDRKTRKKEEKARKLASMLESENKDNDANAAPLNKTDAFKDGLPSGRLIFAYASGQKVAPDGSNPADGITVTGNLLSPPNSRDLQVEKLSVSAWGKLLIKDSELNLINGRRYGLIAPNGSGKSTLLHAIACGLIPTPSSLDFYLLDREYIPNELTCVEAVLDINEQERKHLEAMMEDLLDDPDKNAVELDTIQTRLTDLETENSDHRVYKILRGLQFTDEMIAKRTNELSGGWRMRIALARILFIKPTLMMLDEPTNHLDLEAVAWLEEYLTHEMEGHTLLITCHTQDTLNEVCTDIIHLYHQKLDYYSGNYDTFLKVRAERDVQLAKKARQQEKDMAKLQNKLNMTGSEQQKKAKAKVKAMNKKLEKDKQSGKVLDEEIIQEKQLVIRFEDCGGGIPSPAIKFQDVSFNYPGGPTIFSKLNFGLDLKSRVALVGPNGAGKTTLIKLILEKVQPSTGSVVRHHGLRLALFNQHMGDQLDMRLSAVEWLRTKFGNKPEGEMRRIVGRYGLTGKSQVIPMGQLSDGQRRRVLFAFLGMTQPHILLLDEPTNALDIDTIDALADALNNFDGGVVFITHDFRLIDQVAEEIWIVQNGTVKEFDGEIRDYKMMLKQQIAKEREEERRIELEKQKK
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
7Phosphorylation-MARGKRSTQRDADL
-CCCCCCCCHHHHHH
32.1721712547
8PhosphorylationMARGKRSTQRDADLE
CCCCCCCCHHHHHHH
31.4921712547
18PhosphorylationDADLELESLQSEIES
HHHHHHHHHHHHHHC
44.3121712547
21PhosphorylationLELESLQSEIESESP
HHHHHHHHHHHCCCC
45.9224763107
25PhosphorylationSLQSEIESESPQPVT
HHHHHHHCCCCCCCC
49.3821712547
27PhosphorylationQSEIESESPQPVTKS
HHHHHCCCCCCCCHH
37.8128889911
32PhosphorylationSESPQPVTKSKAKKN
CCCCCCCCHHHHHHC
35.9625720772
47PhosphorylationKKKLNKASAFNSDND
HHHCCHHHHCCCCCC
34.6928889911
51PhosphorylationNKASAFNSDNDSNYD
CHHHHCCCCCCCCCC
31.1928889911
55PhosphorylationAFNSDNDSNYDLKPE
HCCCCCCCCCCCCCC
43.4728889911
57PhosphorylationNSDNDSNYDLKPEDD
CCCCCCCCCCCCCCC
26.9728889911
97PhosphorylationEAFADEQSVEEEEEE
HHHHCCCCCHHHHHC
29.4628889911
106PhosphorylationEEEEEEDSEKPVRKN
HHHHHCCCCCCCHHC
51.2921712547
137PhosphorylationADDMDDLSLDEEESE
HHCCCCCCCCHHHHH
40.5428889911
143PhosphorylationLSLDEEESESSEKSK
CCCCHHHHHCHHHHH
46.1624763107
146PhosphorylationDEEESESSEKSKKKK
CHHHHHCHHHHHHHH
45.0221712547
149PhosphorylationESESSEKSKKKKKKS
HHHCHHHHHHHHHCC
45.7325720772
158PhosphorylationKKKKKSKSKDDGSEA
HHHHCCCCCCCCCCC
48.7024763107
163PhosphorylationSKSKDDGSEALDDGD
CCCCCCCCCCCCCCC
27.0428889911
173PhosphorylationLDDGDIESSEKDKKK
CCCCCCCCCHHHHHH
44.1025720772

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 YJQ1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YJQ1_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 YJQ1_SCHPO !!

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

Oops, there are no PPI records of YJQ1_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YJQ1_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-27; SER-47; SER-51;SER-55; TYR-57; SER-97; SER-137 AND SER-163, AND MASS SPECTROMETRY.

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