SEC8_SCHPO - dbPTM
SEC8_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC8_SCHPO
UniProt AC O74562
Protein Name Exocyst complex component sec8
Gene Name sec8
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1073
Subcellular Localization Cytoplasm . Cell tip . Cell septum . Cytoplasmic vesicle . Associated with the actinomyosin ring at the division site and at the cell tips.
Protein Description Component of the exocyst complex involved in the delivery of secretory vesicles to the plasma membrane. Also required for polarized cell growth and division septum assembly. The exocyst complex plays an important role in the targeting of rho3, as well as the two main hydrolases required for cell separation, eng1 and agn1, to the cell wall surrounding the septum before cell separation begins..
Protein Sequence MDTRGYSETKKGRYPVGKKSLESPNGYSNYGTSMDNELSSEYASRGMHIGDLENLVNEIEDEWKDLGREDYQPISTALELLDDSSFGRDYKSFLNVYDRISAALQTIAHTHKDDFTRGISAYGEIMEGIQKCNSRIIALKQSLEASQECIGNTNSKELQQTLARSSQYKKVISVLKELNEANQLFDNFHTLVDSKQYYHASDLIRRVWDELSRSDFDGILVVEQFKSRMTGLLSHLEDILSEELVSITFLKDAVAYPIVSYCSPNPLRETSNPYFLRDFLKNNANTSTLGQSEQLRYLEEALSLKLSDCLKMDYGRDSLRDIRIVLESLNLLGKLPNAISSLKSRTSAEMFTTVDSTSRAIVNKYSLGNNVSTVNPFSKSLYDIGLHAETDREHTMISEFLTNLFTKLRCVLMHYRGISEFMTKLETKTPKHASSSHKSSIMSVNSDPTSPKVSKFDTSDSTFPFDTLLQAFESEIRLMLKDYLISKEEYIENSGNFVVGTEMSIYNLPGENEEDKLFDVTNEIAVENKSNAFYARINELVNEKAPELILNKSNASVSTIELFSGSSKEIVRLAGHVVFVGPSVFHASSVLPQTVFFLEDSVSILKNPNIPPQFAVNFMKEFLRGSYIPQLYKFMSSHFDTIMKDVGAFQLHRDWKIYSKIPIFKCHVAIVQYFHDLQDYLPIVALNLVEFYELLHTLLVRFRNHCSDYLSDLCRTAVLKEYKHVNEDTEDVDDTVRVKLLHDDVTYPQFIKFLKQKNPSLEGLNELCRMENKRLLQYEDRAITSEVKLPVSVLSKDSDLVNSVSYLHNSMEWFLQRCFSRFMNGSRRMNVLQQNQANFGGDFLPIDNLLGNNSDLMKGAYKEVFDSLQRLQFDALLLIRMEVRLQYIHSINQSVNLPDYVVEYRGRPDASIMALNSTIVTTNLKLETCLNEWERRFVFQGLSELVDSSLYSIFYKIESMNRGSCLQMLKNMSAMIQILKTVKEIHGDVEFPKSSRVFGIYQNGAKKIIEHFIAAPKKELLPDVKQMVRIYYQRLMKDAKRNGRDDLYRQYQKKIGSVLTQFDNTVGGARKNP
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
20PhosphorylationRYPVGKKSLESPNGY
CCCCCCCCCCCCCCC
40.6325720772
443PhosphorylationSHKSSIMSVNSDPTS
CCCCCCEECCCCCCC
19.2429996109
446PhosphorylationSSIMSVNSDPTSPKV
CCCEECCCCCCCCCC
42.6924763107
449PhosphorylationMSVNSDPTSPKVSKF
EECCCCCCCCCCCCC
63.7528889911
450PhosphorylationSVNSDPTSPKVSKFD
ECCCCCCCCCCCCCC
28.2828889911
760PhosphorylationFLKQKNPSLEGLNEL
HHHHHCCCCHHHHHH
48.7428889911

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 SEC8_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC8_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 SEC8_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC6_SCHPOsec6physical
11854409
SEC10_SCHPOsec10physical
11854409
EXO70_SCHPOexo70physical
11854409
CDC42_SCHPOcdc42genetic
21899677
YD6C_SCHPOsec3physical
22891673
RHO3_SCHPOrho3genetic
21652630
EXO70_SCHPOexo70genetic
21652630
FOR3_SCHPOfor3genetic
21652630
MYO52_SCHPOmyo52genetic
21652630
FOR3_SCHPOfor3genetic
21401840
RHO4_SCHPOrho4genetic
25724972

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEC8_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 THR-449 AND SER-450, ANDMASS SPECTROMETRY.

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