ACTA_HUMAN - dbPTM
ACTA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTA_HUMAN
UniProt AC P62736
Protein Name Actin, aortic smooth muscle
Gene Name ACTA2
Organism Homo sapiens (Human).
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 MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
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------MCEEEDSTA
------CCCCCCCCE
10.166725286
3Acetylation-----MCEEEDSTAL
-----CCCCCCCCEE
64.2222223895
35PhosphorylationAPRAVFPSIVGRPRH
CCCCCCHHHCCCCCC
20.5930266825
46OxidationRPRHQGVMVGMGQKD
CCCCCCEEEECCCCC
2.49-
49OxidationHQGVMVGMGQKDSYV
CCCEEEECCCCCCCC
3.32-
52AcetylationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.807213953
52MethylationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.80-
52UbiquitinationVMVGMGQKDSYVGDE
EEEECCCCCCCCCCH
42.8021890473
54PhosphorylationVGMGQKDSYVGDEAQ
EECCCCCCCCCCHHH
28.8423401153
55PhosphorylationGMGQKDSYVGDEAQS
ECCCCCCCCCCHHHC
20.7027273156
62PhosphorylationYVGDEAQSKRGILTL
CCCCHHHCCCCEEEE
31.2223401153
63SumoylationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43-
63AcetylationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.437215567
63SumoylationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.43-
63UbiquitinationVGDEAQSKRGILTLK
CCCHHHCCCCEEEEE
42.4321890473
68PhosphorylationQSKRGILTLKYPIEH
HCCCCEEEEECEECC
21.2022617229
70AcetylationKRGILTLKYPIEHGI
CCCEEEEECEECCCC
43.6925825284
70MethylationKRGILTLKYPIEHGI
CCCEEEEECEECCCC
43.69-
70UbiquitinationKRGILTLKYPIEHGI
CCCEEEEECEECCCC
43.6921890473
71PhosphorylationRGILTLKYPIEHGII
CCEEEEECEECCCCC
16.7418180459
75MethylationTLKYPIEHGIITNWD
EEECEECCCCCCCHH
33.2130626964
79PhosphorylationPIEHGIITNWDDMEK
EECCCCCCCHHHHHH
28.4736012735
84SulfoxidationIITNWDDMEKIWHHS
CCCCHHHHHHHHHHH
5.3930846556
86AcetylationTNWDDMEKIWHHSFY
CCHHHHHHHHHHHHH
44.4523236377
86MethylationTNWDDMEKIWHHSFY
CCHHHHHHHHHHHHH
44.45-
91PhosphorylationMEKIWHHSFYNELRV
HHHHHHHHHHHCCCC
19.2826657352
93PhosphorylationKIWHHSFYNELRVAP
HHHHHHHHHCCCCCC
15.6727259358
97MethylationHSFYNELRVAPEEHP
HHHHHCCCCCCCCCC
19.17-
105PhosphorylationVAPEEHPTLLTEAPL
CCCCCCCCCCCCCCC
35.9926437602
108PhosphorylationEEHPTLLTEAPLNPK
CCCCCCCCCCCCCCC
32.9621406692
115AcetylationTEAPLNPKANREKMT
CCCCCCCCCCHHHHH
58.1630585401
115UbiquitinationTEAPLNPKANREKMT
CCCCCCCCCCHHHHH
58.1621890473
122PhosphorylationKANREKMTQIMFETF
CCCHHHHHHHHHHHC
26.47-
128PhosphorylationMTQIMFETFNVPAMY
HHHHHHHHCCHHHHH
14.83-
145PhosphorylationIQAVLSLYASGRTTG
HHHHHHHHHCCCCEE
8.7130803931
150PhosphorylationSLYASGRTTGIVLDS
HHHHCCCCEEEEEEC
32.6626657352
151PhosphorylationLYASGRTTGIVLDSG
HHHCCCCEEEEEECC
24.4526437602
157PhosphorylationTTGIVLDSGDGVTHN
CEEEEEECCCCCCCC
34.3210632791
162PhosphorylationLDSGDGVTHNVPIYE
EECCCCCCCCCCEEC
17.1726437602
168PhosphorylationVTHNVPIYEGYALPH
CCCCCCEECCCCHHH
9.387561247
171PhosphorylationNVPIYEGYALPHAIM
CCCEECCCCHHHHHH
7.947330091
178SulfoxidationYALPHAIMRLDLAGR
CCHHHHHHHHHCCCC
3.4530846556
188PhosphorylationDLAGRDLTDYLMKIL
HCCCCCHHHHHHHHH
27.2128152594
190PhosphorylationAGRDLTDYLMKILTE
CCCCHHHHHHHHHHH
11.9426846344
192SulfoxidationRDLTDYLMKILTERG
CCHHHHHHHHHHHCC
1.7531801345
193AcetylationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.7822646677
193MethylationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.78-
193UbiquitinationDLTDYLMKILTERGY
CHHHHHHHHHHHCCC
31.7821890473
196PhosphorylationDYLMKILTERGYSFV
HHHHHHHHHCCCCCE
27.4046158449
198MethylationLMKILTERGYSFVTT
HHHHHHHCCCCCEEH
44.08-
200PhosphorylationKILTERGYSFVTTAE
HHHHHCCCCCEEHHC
12.7354893
201PhosphorylationILTERGYSFVTTAER
HHHHCCCCCEEHHCH
18.9636642193
204PhosphorylationERGYSFVTTAEREIV
HCCCCCEEHHCHHHH
20.4826657352
205PhosphorylationRGYSFVTTAEREIVR
CCCCCEEHHCHHHHH
22.6328857561
215AcetylationREIVRDIKEKLCYVA
HHHHHHHHHHHCEEE
53.7511921171
215UbiquitinationREIVRDIKEKLCYVA
HHHHHHHHHHHCEEE
53.7521890473
217AcetylationIVRDIKEKLCYVALD
HHHHHHHHHCEEEEE
38.567910615
217MethylationIVRDIKEKLCYVALD
HHHHHHHHHCEEEEE
38.56-
219S-nitrosocysteineRDIKEKLCYVALDFE
HHHHHHHCEEEEECC
3.68-
219GlutathionylationRDIKEKLCYVALDFE
HHHHHHHCEEEEECC
3.6822555962
219S-nitrosylationRDIKEKLCYVALDFE
HHHHHHHCEEEEECC
3.6821278135
220PhosphorylationDIKEKLCYVALDFEN
HHHHHHCEEEEECCH
10.1329396449
231PhosphorylationDFENEMATAASSSSL
ECCHHHHHHCCCCCC
22.8026657352
234PhosphorylationNEMATAASSSSLEKS
HHHHHHCCCCCCCHH
28.4326657352
235PhosphorylationEMATAASSSSLEKSY
HHHHHCCCCCCCHHE
21.1535096073
236PhosphorylationMATAASSSSLEKSYE
HHHHCCCCCCCHHEE
36.1326657352
237PhosphorylationATAASSSSLEKSYEL
HHHCCCCCCCHHEEC
42.3629396449
240UbiquitinationASSSSLEKSYELPDG
CCCCCCCHHEECCCC
64.73-
241PhosphorylationSSSSLEKSYELPDGQ
CCCCCCHHEECCCCC
17.9229255136
242PhosphorylationSSSLEKSYELPDGQV
CCCCCHHEECCCCCE
32.3329255136
251PhosphorylationLPDGQVITIGNERFR
CCCCCEEEECCCEEC
24.7926846344
259S-nitrosocysteineIGNERFRCPETLFQP
ECCCEECCCCHHCCC
3.08-
259S-nitrosylationIGNERFRCPETLFQP
ECCCEECCCCHHCCC
3.0821278135
262PhosphorylationERFRCPETLFQPSFI
CEECCCCHHCCCCCC
20.29-
267PhosphorylationPETLFQPSFIGMESA
CCHHCCCCCCCHHCC
20.7946158533
273PhosphorylationPSFIGMESAGIHETT
CCCCCHHCCCCCCCC
23.9322210691
280PhosphorylationSAGIHETTYNSIMKC
CCCCCCCCCHHHHCC
20.09-
281PhosphorylationAGIHETTYNSIMKCD
CCCCCCCCHHHHCCC
17.843828983
283PhosphorylationIHETTYNSIMKCDID
CCCCCCHHHHCCCCE
17.41-
287S-nitrosocysteineTYNSIMKCDIDIRKD
CCHHHHCCCCEECHH
2.83-
287S-nitrosylationTYNSIMKCDIDIRKD
CCHHHHCCCCEECHH
2.8321278135
293MalonylationKCDIDIRKDLYANNV
CCCCEECHHHHHCCC
53.0426320211
293UbiquitinationKCDIDIRKDLYANNV
CCCCEECHHHHHCCC
53.04-
296Nitrated tyrosineIDIRKDLYANNVLSG
CEECHHHHHCCCCCC
19.88-
296PhosphorylationIDIRKDLYANNVLSG
CEECHHHHHCCCCCC
19.8820563989
302PhosphorylationLYANNVLSGGTTMYP
HHHCCCCCCCCCCCC
30.7821406692
305PhosphorylationNNVLSGGTTMYPGIA
CCCCCCCCCCCCCHH
16.3521406692
306PhosphorylationNVLSGGTTMYPGIAD
CCCCCCCCCCCCHHH
20.2721406692
307SulfoxidationVLSGGTTMYPGIADR
CCCCCCCCCCCHHHH
3.6930846556
308PhosphorylationLSGGTTMYPGIADRM
CCCCCCCCCCHHHHH
9.0120563997
317SumoylationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.56-
317AcetylationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.567221445
317SumoylationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.56-
317UbiquitinationGIADRMQKEITALAP
CHHHHHHHHHHHHCC
41.5621890473
320PhosphorylationDRMQKEITALAPSTM
HHHHHHHHHHCCCCE
19.4030266825
325PhosphorylationEITALAPSTMKIKII
HHHHHCCCCEEEEEE
35.2123401153
326PhosphorylationITALAPSTMKIKIIA
HHHHCCCCEEEEEEC
22.7946158473
328SumoylationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.72-
328AcetylationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.727215575
328MethylationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.72-
328SumoylationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.72-
328UbiquitinationALAPSTMKIKIIAPP
HHCCCCEEEEEECCC
40.7221890473
330SumoylationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.65-
330AcetylationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.657692061
330SumoylationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.65-
330UbiquitinationAPSTMKIKIIAPPER
CCCCEEEEEECCCCC
23.6521890473
338SumoylationIIAPPERKYSVWIGG
EECCCCCCEEEEECH
39.97-
350PhosphorylationIGGSILASLSTFQQM
ECHHHHHHHHHHHHH
21.29-
364PhosphorylationMWISKQEYDEAGPSI
HHHCHHHHCCCCCCC
19.3120068231
370O-linked_GlycosylationEYDEAGPSIVHRKCF
HHCCCCCCCCCCCCC
36.0029351928
370PhosphorylationEYDEAGPSIVHRKCF
HHCCCCCCCCCCCCC
36.0026657352
375UbiquitinationGPSIVHRKCF-----
CCCCCCCCCC-----
25.72-
376S-nitrosocysteinePSIVHRKCF------
CCCCCCCCC------
5.02-
376S-nitrosylationPSIVHRKCF------
CCCCCCCCC------
5.0221278135

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 ACTA_HUMAN !!

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

-
49MOxidation

-
75HMethylation

30626964
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 ACTA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPD_HUMANCCT4physical
11580270
PCY1B_HUMANPCYT1Bphysical
11580270
TCPE_HUMANCCT5physical
11580270
MYH9_HUMANMYH9physical
22939629
MYH11_HUMANMYH11physical
22939629
RL10A_HUMANRPL10Aphysical
22939629
RL18_HUMANRPL18physical
22939629
RS23_HUMANRPS23physical
22939629
RL14_HUMANRPL14physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RL17_HUMANRPL17physical
22939629
RS16_HUMANRPS16physical
22939629
RS26_HUMANRPS26physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
MYH10_HUMANMYH10physical
22939629
ACTC_HUMANACTC1physical
22939629
MYO1C_HUMANMYO1Cphysical
22939629
TPM1_HUMANTPM1physical
22939629
RM47_HUMANMRPL47physical
22939629
SYAC_HUMANAARSphysical
22939629
FSCN1_HUMANFSCN1physical
22939629
UBAP1_HUMANUBAP1physical
22939629
ZYX_HUMANZYXphysical
22939629
RT02_HUMANMRPS2physical
22939629
RT07_HUMANMRPS7physical
22939629
GSTP1_HUMANGSTP1physical
22939629
SPTN1_HUMANSPTAN1physical
22939629
CNN2_HUMANCNN2physical
22939629
LOX12_HUMANALOX12physical
17379189

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=ACTA2 mutations predispose patients to a variety of diffuse and diverse vascular diseases, premature onset coronary artery disease (CAD), premature ischemic strokes and Moyamoya disease.
611788
614042Moyamoya disease 5 (MYMY5)
613834Multisystemic smooth muscle dysfunction syndrome (MSMDYS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTA_HUMAN

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"The human pituitary nitroproteome: detection of nitrotyrosyl-proteinswith two-dimensional Western blotting, and amino acid sequencedetermination with mass spectrometry.";
Zhan X., Desiderio D.M.;
Biochem. Biophys. Res. Commun. 325:1180-1186(2004).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-296, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND MASSSPECTROMETRY.

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