ACTS_RAT - dbPTM
ACTS_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTS_RAT
UniProt AC P68136
Protein Name Actin, alpha skeletal muscle
Gene Name Acta1
Organism Rattus norvegicus (Rat).
Sequence Length 377
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 MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
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
2Acetylation------MCDEDETTA
------CCCCCCCEE
8.68-
3Acetylation-----MCDEDETTAL
-----CCCCCCCEEE
66.15-
35PhosphorylationAPRAVFPSIVGRPRH
CCCCCCHHHCCCCCC
20.595130775
46OxidationRPRHQGVMVGMGQKD
CCCCCCEEEECCCCC
2.49-
49OxidationHQGVMVGMGQKDSYV
CCCEEEECCCCCCCC
3.32-
52AcetylationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.80174327
52UbiquitinationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.80-
54PhosphorylationVGMGQKDSYVGDEAQ
EECCCCCCCCCCHHH
28.8425403869
54O-linked_GlycosylationVGMGQKDSYVGDEAQ
EECCCCCCCCCCHHH
28.849548347
55PhosphorylationGMGQKDSYVGDEAQS
ECCCCCCCCCCHHHC
20.704817623
62PhosphorylationYVGDEAQSKRGILTL
CCCCHHHCCCCEEEE
31.2229779826
63AcetylationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43174317
63N6-malonyllysineVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43-
63MalonylationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43-
63UbiquitinationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43-
68PhosphorylationQSKRGILTLKYPIEH
HCCCCEEEEECEECC
21.2028826663
70AcetylationKRGILTLKYPIEHGI
CCCEEEEECEECCCC
43.69174315
71PhosphorylationRGILTLKYPIEHGII
CCEEEEECEECCCCC
16.7422673903
75MethylationTLKYPIEHGIITNWD
EEECEECCCCCCCHH
33.21-
79PhosphorylationPIEHGIITNWDDMEK
EECCCCCCCHHHHHH
28.4736748793
86AcetylationTNWDDMEKIWHHTFY
CCHHHHHHHHHHHHH
44.45174323
86MethylationTNWDDMEKIWHHTFY
CCHHHHHHHHHHHHH
44.45-
86UbiquitinationTNWDDMEKIWHHTFY
CCHHHHHHHHHHHHH
44.45-
91PhosphorylationMEKIWHHTFYNELRV
HHHHHHHHHHCCCCC
18.229548383
93PhosphorylationKIWHHTFYNELRVAP
HHHHHHHHCCCCCCC
14.64174691
115AcetylationTEAPLNPKANREKMT
CCCCCCCCCCHHHHH
58.1630595959
128PhosphorylationMTQIMFETFNVPAMY
HHHHHHHHCCHHHHH
14.8321630457
135PhosphorylationTFNVPAMYVAIQAVL
HCCHHHHHHHHHHHH
6.7121630457
150PhosphorylationSLYASGRTTGIVLDS
HHHHCCCCEEEEEEC
32.6622673903
151PhosphorylationLYASGRTTGIVLDSG
HHHCCCCEEEEEECC
24.4522673903
157O-linked_GlycosylationTTGIVLDSGDGVTHN
CEEEEEECCCCCCCC
34.3210632789
157PhosphorylationTTGIVLDSGDGVTHN
CEEEEEECCCCCCCC
34.32-
168PhosphorylationVTHNVPIYEGYALPH
CCCCCCEECCCCHHH
9.383840507
171PhosphorylationNVPIYEGYALPHAIM
CCCEECCCCHHHHHH
7.9415569651
188PhosphorylationDLAGRDLTDYLMKIL
HCCCCCHHHHHHHHH
27.2122673903
190PhosphorylationAGRDLTDYLMKILTE
CCCCHHHHHHHHHHH
11.9418876225
193UbiquitinationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.78-
193AcetylationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.7822646669
200PhosphorylationKILTERGYSFVTTAE
HHHHHCCCCCEEHHC
12.73174795
201O-linked_GlycosylationILTERGYSFVTTAER
HHHHCCCCCEEHHCH
18.965130783
201PhosphorylationILTERGYSFVTTAER
HHHHCCCCCEEHHCH
18.965130783
204PhosphorylationERGYSFVTTAEREIV
HCCCCCEEHHCHHHH
20.4822673903
205PhosphorylationRGYSFVTTAEREIVR
CCCCCEEHHCHHHHH
22.639548407
215AcetylationREIVRDIKEKLCYVA
HHHHHHHHHHHCEEE
53.758276005
220PhosphorylationDIKEKLCYVALDFEN
HHHHHHCEEEEECCH
10.13174797
234O-linked_GlycosylationNEMATAASSSSLEKS
HHHHHHCCCCCCCHH
28.4310633201
234PhosphorylationNEMATAASSSSLEKS
HHHHHHCCCCCCCHH
28.4328551015
235PhosphorylationEMATAASSSSLEKSY
HHHHHCCCCCCCHHE
21.1528551015
236PhosphorylationMATAASSSSLEKSYE
HHHHCCCCCCCHHEE
36.1328551015
237PhosphorylationATAASSSSLEKSYEL
HHHCCCCCCCHHEEC
42.3628551015
241PhosphorylationSSSSLEKSYELPDGQ
CCCCCCHHEECCCCC
17.9228689409
242PhosphorylationSSSLEKSYELPDGQV
CCCCCHHEECCCCCE
32.3322108457
251PhosphorylationLPDGQVITIGNERFR
CCCCCEEEECCCEEC
24.7946314633
296PhosphorylationIDIRKDLYANNVMSG
CEECHHHHHCCCCCC
19.88174185
317UbiquitinationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.56-
317AcetylationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.56174321
320PhosphorylationDRMQKEITALAPSTM
HHHHHHHHHHCCCCE
19.403972893
325PhosphorylationEITALAPSTMKIKII
HHHHHCCCCEEEEEE
35.219423901
325O-linked_GlycosylationEITALAPSTMKIKII
HHHHHCCCCEEEEEE
35.219548443
326PhosphorylationITALAPSTMKIKIIA
HHHHCCCCEEEEEEC
22.7927097102
328UbiquitinationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.72-
328AcetylationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.72174325
330UbiquitinationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.65-
330AcetylationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.657629333
364PhosphorylationMWITKQEYDEAGPSI
HCCHHHHHCCCCCCC
19.317330141
370O-linked_GlycosylationEYDEAGPSIVHRKCF
HHCCCCCCCCCCCCC
36.0010633213
370PhosphorylationEYDEAGPSIVHRKCF
HHCCCCCCCCCCCCC
36.0022673903

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
35SPhosphorylationKinasePRKACAP00517
GPS
201SPhosphorylationKinasePRKACAP00517
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
46MOxidation

-
49MOxidation

-
75HMethylation

-
86KMethylation

-

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 ACTS_RAT !!

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

Oops, there are no PPI records of ACTS_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTS_RAT

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Related Literatures of Post-Translational Modification

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