ACT_SCHPO - dbPTM
ACT_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACT_SCHPO
UniProt AC P10989
Protein Name Actin
Gene Name act1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 375
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells..
Protein Sequence MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPCLLTEAPLNPKSNREKMTQIIFETFNAPAFYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAIMRLDLAGRDLTDYLMKILMERGYTFSTTAEREIVRDIKEKLCYVALDFEQELQTAAQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSALGLENAGIHEATYNSIMKCDVDIRKDLYGNVVMSGGTTMYPGIADRMQKEIQALAPSSMKVKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVYRKCF
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
33PhosphorylationAPRAVFPSIVGRPRH
CCHHHCHHHCCCCCC		20.5925720772
60PhosphorylationYVGDEAQSKRGILTL
CCCCHHHCCCCEEEE		31.2225720772
68SumoylationKRGILTLKYPIEHGI
CCCEEEEECEEHHCC		43.69-
202PhosphorylationERGYTFSTTAEREIV
HCCCCCCCCHHHHHH		26.3228889911
239PhosphorylationQSSSLEKSYELPDGQ
HHCCCCCEEECCCCC		17.9225720772
240PhosphorylationSSSLEKSYELPDGQV
HCCCCCEEECCCCCE		32.3325720772
284SumoylationATYNSIMKCDVDIRK
HHHHHHHCCCCCCCH		26.13-
323PhosphorylationEIQALAPSSMKVKIV
HHHHHCCCCCEEEEE		37.1428889911
324PhosphorylationIQALAPSSMKVKIVA
HHHHCCCCCEEEEEC		22.8928889911
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 ACT_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACT_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 ACT_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPOD2_SCHPOcdc1genetic
8292390
TBA1_SCHPOnda2genetic
8292390
TPM_SCHPOcdc8genetic
10371213
SSP1_SCHPOssp1physical
7628434
ACT_SCHPOact1physical
21148484
COFI_SCHPOadf1physical
21148484
COFI_SCHPOadf1physical
21723825
PROF_SCHPOcdc3genetic
10371213
MPIP_SCHPOcdc25genetic
8292390
ACT_SCHPOact1physical
23695164
PROF_SCHPOcdc3genetic
23589458
TPM_SCHPOcdc8genetic
23589458
MYO2_SCHPOmyo2genetic
23589458
MLR4_SCHPOcdc4genetic
23589458
CDC12_SCHPOcdc12genetic
23589458
TPM_SCHPOcdc8physical
24167549
CAP_SCHPOcap1physical
26542710
ACT_SCHPOact1physical
26771498
PROF_SCHPOcdc3genetic
25543282
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACT_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-202 AND SER-324, ANDMASS SPECTROMETRY.

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