SEY1_SCHPO - dbPTM
SEY1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEY1_SCHPO
UniProt AC Q9UTE0
Protein Name Protein sey1 {ECO:0000255|HAMAP-Rule:MF_03109}
Gene Name sey1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 762
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Enriched in the cortical ER. Concentrated in punctae along the ER tubules.
Protein Description Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization..
Protein Sequence MSTASNRVSTQIVDEHKQFNNELPKFMQSVGLLDAGFNYHVVAVLGSQSTGKSTLLNNLFGTSFSVMDASKRQQTTKGIWLSKANNSPILVMDVEGTDGRERGEDQDFERKSALFSISTSEVIIVNMWENQVGLYQGSNMALLKTVLEVNLQLFHNKKERCLLQFVIRDFLGNTSMENLADTIMTDLNNIWASLSKPEGFENSVINDFFDVGFTGLPHKILCSDAFSEAVDSLRERFVDNNNSDYIFNVSYHKKIPADGFSLYTREIWDTIENNKDLDLPTQQQLLAQYRCDEIITEVMEPFSTACTILQKEFLPGNLCKDLPTKLLNMFETVIEAYDRQASRYNVHIYQKKKQELIASVDSHLYVFFQAQLNALHKELIKSFFDASNEFPSDTPFKESSSIKINELVNKMREEGESLSLPHVHWDVDPFILKLSEELTQNSETLCKEKLKEKLEELFTGFEFEVSEAVEVAFQKLSHNVWDTLLNEFLAAQNTTIEKIKNIVPFYVDIDDTKTTEEYIINFKKNSWLFFRKKIDSEMSEVLLQQRLRVYFEELFRYDSDGMPKLWKKSGTIDRDYRESLTKTLDLINVLASIKVSDGNYPDLNVDIKTLEPEYTSPASFFTILNRRRVSDISVNFKRSADLIFMDCKRSVINTTTRIPPYFWVLLIVLGWNEFMAILRNPFVFMILMFGGTVVYGLYISGLIWPAKMVLERATNNLVDLATDRFSNTYQEQVQQRAMQRTEKSGSPVASADDAEAEKTALS
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------MSTASNRVS
------CCCCCCCCC		32.4524763107
744PhosphorylationAMQRTEKSGSPVASA
HHHHHHHCCCCCCCC		37.9725720772
746PhosphorylationQRTEKSGSPVASADD
HHHHHCCCCCCCCCH		24.2428889911
750PhosphorylationKSGSPVASADDAEAE
HCCCCCCCCCHHHHH		32.2521712547
762PhosphorylationEAEKTALS-------
HHHHHHCC-------		35.3925720772
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 SEY1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEY1_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 SEY1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_SCHPOddb1genetic
22681890
RIK1_SCHPOrik1genetic
22681890
YBX5_SCHPOSPBC17D1.05genetic
22681890
YG58_SCHPOSPBC56F2.08cgenetic
22681890
NU132_SCHPOnup132genetic
22681890
BDC1_SCHPObdc1genetic
22681890
PFD5_SCHPObob1genetic
22681890
DBR1_SCHPOdbr1genetic
22681890
CCQ1_SCHPOccq1genetic
22681890
YE04_SCHPOSPAC17H9.04cgenetic
22681890
CSN1_SCHPOcsn1genetic
22681890
MUG80_SCHPOmug80genetic
22681890
ARP42_SCHPOarp42genetic
22681890
ASH2_SCHPOash2genetic
22681890
NOT3_SCHPOnot3genetic
22681890
NSK1_SCHPOnsk1genetic
22681890
FKBP4_SCHPOfkbp39genetic
22681890
CIP2_SCHPOcip2genetic
22681890
RL16B_SCHPOrpl1601genetic
22681890
DGK1_SCHPOptp4genetic
22681890
YG42_SCHPOrrp2genetic
22681890
FFT3_SCHPOfft3genetic
22681890
SUM2_SCHPOsum2genetic
22681890
YHZ3_SCHPOath1genetic
22681890
TBA2_SCHPOatb2genetic
22681890
MCL1_SCHPOmcl1genetic
22681890
ASE1_SCHPOase1genetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEY1_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-746, AND MASSSPECTROMETRY.

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