ACTB_RAT - dbPTM
ACTB_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTB_RAT
UniProt AC P60711
Protein Name Actin, cytoplasmic 1
Gene Name Actb
Organism Rattus norvegicus (Rat).
Sequence Length 375
Subcellular Localization Cytoplasm, cytoskeleton. Localized in cytoplasmic mRNP granules containing untranslated mRNAs..
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 MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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
1Acetylation-------MDDDIAAL
-------CCCCCEEE
13.23-
2Acetylation------MDDDIAALV
------CCCCCEEEE
63.39-
14PhosphorylationALVVDNGSGMCKAGF
EEEEECCCCCEECCC
29.6123984901
33PhosphorylationAPRAVFPSIVGRPRH
CCCCCCHHHCCCCCC
20.595130775
44OxidationRPRHQGVMVGMGQKD
CCCCCCEEEECCCCC
2.49-
47OxidationHQGVMVGMGQKDSYV
CCCEEEECCCCCCCC
3.32-
50UbiquitinationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.80-
50AcetylationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.8022902405
52PhosphorylationVGMGQKDSYVGDEAQ
EECCCCCCCCCCHHH
28.8425403869
53PhosphorylationGMGQKDSYVGDEAQS
ECCCCCCCCCCHHHC
20.704817623
60PhosphorylationYVGDEAQSKRGILTL
CCCCHHHCCCCEEEE
31.2229779826
61UbiquitinationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43-
61AcetylationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.4325786129
66PhosphorylationQSKRGILTLKYPIEH
HCCCCEEEEECEECC
21.2028826663
68AcetylationKRGILTLKYPIEHGI
CCCEEEEECEECCCC
43.6922902405
73MethylationTLKYPIEHGIVTNWD
EEECEECCCCCCCHH
31.8130526847
84MethylationTNWDDMEKIWHHTFY
CCHHHHHHHHHHHHH
44.45-
84AcetylationTNWDDMEKIWHHTFY
CCHHHHHHHHHHHHH
44.4522902405
89PhosphorylationMEKIWHHTFYNELRV
HHHHHHHHHHCCCCC
18.229548383
91PhosphorylationKIWHHTFYNELRVAP
HHHHHHHHCCCCCCC
14.64174691
113AcetylationTEAPLNPKANREKMT
EECCCCCCCCHHHHH
58.1622902405
113UbiquitinationTEAPLNPKANREKMT
EECCCCCCCCHHHHH
58.16-
166PhosphorylationVTHTVPIYEGYALPH
CEEEEEEECCCCCCH
9.38174693
169PhosphorylationTVPIYEGYALPHAIL
EEEEECCCCCCHHHH
7.94174695
186PhosphorylationDLAGRDLTDYLMKIL
HHCCCCHHHHHHHHH
27.2122673903
188PhosphorylationAGRDLTDYLMKILTE
CCCCHHHHHHHHHHH
11.9418876225
191UbiquitinationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.78-
191AcetylationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.7825786129
198PhosphorylationKILTERGYSFTTTAE
HHHHHCCCCCCCCHH
13.56174687
199PhosphorylationILTERGYSFTTTAER
HHHHCCCCCCCCHHH
20.9527097102
199O-linked_GlycosylationILTERGYSFTTTAER
HHHHCCCCCCCCHHH
20.9521933451
201PhosphorylationTERGYSFTTTAEREI
HHCCCCCCCCHHHHH
19.8027097102
202PhosphorylationERGYSFTTTAEREIV
HCCCCCCCCHHHHHH
23.2327097102
203PhosphorylationRGYSFTTTAEREIVR
CCCCCCCCHHHHHHH
24.3827097102
213AcetylationREIVRDIKEKLCYVA
HHHHHHHHHHHHEEE
53.7522902405
215AcetylationIVRDIKEKLCYVALD
HHHHHHHHHHEEECC
38.5625786129
215UbiquitinationIVRDIKEKLCYVALD
HHHHHHHHHHEEECC
38.56-
218PhosphorylationDIKEKLCYVALDFEQ
HHHHHHHEEECCHHH
10.1325532521
229PhosphorylationDFEQEMATAASSSSL
CHHHHHHHHHCCCCC
22.8028551015
232PhosphorylationQEMATAASSSSLEKS
HHHHHHHCCCCCCCC
28.4327097102
233PhosphorylationEMATAASSSSLEKSY
HHHHHHCCCCCCCCE
21.1527097102
234PhosphorylationMATAASSSSLEKSYE
HHHHHCCCCCCCCEE
36.1327097102
235PhosphorylationATAASSSSLEKSYEL
HHHHCCCCCCCCEEC
42.3627097102
239PhosphorylationSSSSLEKSYELPDGQ
CCCCCCCCEECCCCC
17.9228689409
240PhosphorylationSSSLEKSYELPDGQV
CCCCCCCEECCCCCE
32.3322108457
249PhosphorylationLPDGQVITIGNERFR
CCCCCEEEECCCEEC
24.7946314633
291UbiquitinationKCDVDIRKDLYANTV
CCCCCCCCHHHCCCE
53.04-
291AcetylationKCDVDIRKDLYANTV
CCCCCCCCHHHCCCE
53.0416212439
294PhosphorylationVDIRKDLYANTVLSG
CCCCCHHHCCCEECC
14.13174707
297PhosphorylationRKDLYANTVLSGGTT
CCHHHCCCEECCCCC
18.0425532521
300PhosphorylationLYANTVLSGGTTMYP
HHCCCEECCCCCCCC
30.7322108457
304PhosphorylationTVLSGGTTMYPGIAD
CEECCCCCCCCCHHH
20.2722108457
306PhosphorylationLSGGTTMYPGIADRM
ECCCCCCCCCHHHHH
9.01-
315AcetylationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.5622902405
315UbiquitinationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.56-
318PhosphorylationDRMQKEITALAPSTM
HHHHHHHHHHCCCCE
19.403973057
323PhosphorylationEITALAPSTMKIKII
HHHHHCCCCEEEEEE
35.219423901
324PhosphorylationITALAPSTMKIKIIA
HHHHCCCCEEEEEEC
22.7927097102
326UbiquitinationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.72-
326AcetylationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.7225786129
328UbiquitinationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.65-
328AcetylationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.6525786129
338PhosphorylationAPPERKYSVWIGGSI
CCCCCCEEEEECHHH
17.6330417516
362PhosphorylationMWISKQEYDESGPSI
HHHHCCCCCCCCCCC
23.632081829
365PhosphorylationSKQEYDESGPSIVHR
HCCCCCCCCCCCCCC
53.7829764405
368PhosphorylationEYDESGPSIVHRKCF
CCCCCCCCCCCCCCC
40.5422673903

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
33SPhosphorylationKinasePRKACAP00517
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
44MOxidation

-
47MOxidation

-
73HMethylation

30526847
73HMethylation

30526847
84KMethylation

-

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 ACTB_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESPN_RATEspnphysical
12598619

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

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Related Literatures of Post-Translational Modification

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