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Protein Page:
ACTA2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ACTA2 Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Up-regulated in response to enterovirus 71 (EV71) infection. Belongs to the actin family. Note: This description may include information from UniProtKB.
Protein type: Contractile protein; Motility/polarity/chemotaxis; Cytoskeletal protein
Cellular Component: extracellular space; smooth muscle contractile fiber; protein complex; cytoplasm; cytosol; actin cytoskeleton
Molecular Function: protein kinase binding; ATP binding
Biological Process: muscle contraction; regulation of blood pressure; response to virus; vascular smooth muscle contraction
Reference #:  P62736 (UniProtKB)
Alt. Names/Synonyms: AAT6; ACTA; ACTA2; actin, alpha 2, smooth muscle, aorta; Actin, aortic smooth muscle; ACTSA; ACTVS; alpha 2 actin; Alpha-actin-2; alpha-cardiac actin; Cell growth-inhibiting gene 46 protein; growth-inhibiting gene 46
Gene Symbols: ACTA2
Molecular weight: 42,009 Da
Basal Isoelectric point: 5.24  Predict pI for various phosphorylation states
CST Pathways:  Death Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ACTA2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 97 S35-p APRAVFPsIVGRPRH
0 60 K52-ac VMVGMGQkDsyVGDE
0 105 K52-ub VMVGMGQkDsyVGDE
0 402 S54-p VGMGQkDsyVGDEAQ
0 991 Y55-p GMGQkDsyVGDEAQs
0 12 S62-p yVGDEAQskRGILtL
0 253 K63-ac VGDEAQskRGILtLk
0 110 K63-ub VGDEAQskRGILtLk
0 11 T68-p QskRGILtLkyPIEH
0 8 K70-ac kRGILtLkyPIEHGI
0 4 K70-m1 kRGILtLkyPIEHGI
0 45 K70-ub kRGILtLkyPIEHGI
0 24 Y71-p RGILtLkyPIEHGII
0 3 T79-p PIEHGIItNWDDMEk
0 3 K86-ac tNWDDMEkIWHHSFY
0 2 K86-m1 tNWDDMEkIWHHSFY
0 1 R97-m1 HSFYNELrVAPEEHP
0 1 K115-ac TEAPLNPkANREKMT
0 15 K115-ub TEAPLNPkANREKMT
0 16 Y145-p IQAVLSLyASGRTTG
0 53 Y168-p VTHNVPIyEGyALPH
0 62 Y171-p NVPIyEGyALPHAIM
0 2 T188-p DLAGRDLtDyLMkIL
0 217 Y190-p AGRDLtDyLMkILtE
0 6 K193-ac DLtDyLMkILtERGy
0 87 K193-ub DLtDyLMkILtERGy
0 22 T196-p DyLMkILtERGysFV
0 159 Y200-p kILtERGysFVTTAE
0 6 S201-p ILtERGysFVTTAER
0 3 T205 RGysFVTTAEREIVR
0 5 K215-ac REIVRDIkEkLCyVA
0 1 K217-ac IVRDIkEkLCyVALD
0 1 K217-m1 IVRDIkEkLCyVALD
0 1 K217 IVRDIkEKLCyVALD
0 12 Y220-p DIkEkLCyVALDFEN
0 3 S235-p EMATAASssSLEksy
0 1 S236-p MATAASssSLEksyE
0 3 K240-ub ASssSLEksyELPDG
0 15 S241-p SssSLEksyELPDGQ
0 25 Y242-p ssSLEksyELPDGQV
0 16 T251-p LPDGQVItIGNERFR
0 1 T262 ERFRCPETLFQPsFI
0 2 S267-p PETLFQPsFIGMESA
0 14 Y281-p AGIHETTyNSIMKCD
0 7 K317-ac GIADRMQkEItALAP
0 101 K317-ub GIADRMQkEItALAP
0 8 T320-p DRMQkEItALAPstM
0 9 S325-p EItALAPstMkIkII
0 8 T326-p ItALAPstMkIkIIA
0 9 K328-ac ALAPstMkIkIIAPP
0 128 K328-ub ALAPstMkIkIIAPP
0 9 K330-ac APstMkIkIIAPPER
0 103 K330-ub APstMkIkIIAPPER
0 21 Y364-p MWISKQEyDEAGPSI
  mouse

 
S35-p APRAVFPsIVGRPRH
K52-ac VMVGMGQkDsyVGDE
K52-ub VMVGMGQkDsyVGDE
S54-p VGMGQkDsyVGDEAQ
Y55-p GMGQkDsyVGDEAQs
S62-p yVGDEAQskRGILtL
K63-ac VGDEAQskRGILtLk
K63-ub VGDEAQskRGILtLk
T68-p QskRGILtLkyPIEH
K70-ac kRGILtLkyPIEHGI
K70 kRGILtLKyPIEHGI
K70-ub kRGILtLkyPIEHGI
Y71-p RGILtLkyPIEHGII
T79-p PIEHGIItNWDDMEk
K86-ac tNWDDMEkIWHHSFY
K86 tNWDDMEKIWHHSFY
R97 HSFYNELRVAPEEHP
K115 TEAPLNPKANREKMT
K115-ub TEAPLNPkANREKMT
Y145-p IQAVLSLyASGRTTG
Y168-p VTHNVPIyEGyALPH
Y171-p NVPIyEGyALPHAIM
T188-p DLAGRDLtDyLMkIL
Y190-p AGRDLtDyLMkILtE
K193-ac DLtDyLMkILtERGy
K193-ub DLtDyLMkILtERGy
T196-p DyLMkILtERGysFV
Y200-p kILtERGysFVTtAE
S201-p ILtERGysFVTtAER
T205-p RGysFVTtAEREIVR
K215-ac REIVRDIkEkLCyVA
K217 IVRDIkEKLCyVALD
K217 IVRDIkEKLCyVALD
K217-ub IVRDIkEkLCyVALD
Y220-p DIkEkLCyVALDFEN
S235-p EMATAASsSSLEKsy
S236 MATAASsSSLEKsyE
K240 ASsSSLEKsyELPDG
S241-p SsSSLEKsyELPDGQ
Y242-p sSSLEKsyELPDGQV
T251-p LPDGQVItIGNERFR
T262-p ERFRCPEtLFQPsFI
S267-p PEtLFQPsFIGMESA
Y281-p AGIHETTyNSIMKCD
K317-ac GIADRMQkEItALAP
K317-ub GIADRMQkEItALAP
T320-p DRMQkEItALAPstM
S325-p EItALAPstMkIkII
T326-p ItALAPstMkIkIIA
K328-ac ALAPstMkIkIIAPP
K328-ub ALAPstMkIkIIAPP
K330-ac APstMkIkIIAPPER
K330-ub APstMkIkIIAPPER
Y364-p MWISKQEyDEAGPSI
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