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Protein Page:
ACTG2 (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
ACTG2 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. 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; cytoskeleton; cytosol
Molecular Function: ATP binding
Biological Process: muscle contraction
Reference #:  P63267 (UniProtKB)
Alt. Names/Synonyms: ACTA3; ACTE; ACTG2; ACTH; actin, gamma 2, smooth muscle, enteric; Actin, gamma-enteric smooth muscle; actin-like protein; ACTL3; ACTSG; alpha-actin 3; Alpha-actin-3; Gamma-2-actin; smooth muscle gamma actin; Smooth muscle gamma-actin
Gene Symbols: ACTG2
Molecular weight: 41,877 Da
Basal Isoelectric point: 5.31  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

ACTG2

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

 
1 98 S34-p APRAVFPsIVGRPRH
0 60 K51-ac VMVGMGQkDsyVGDE
0 114 K51-ub VMVGMGQkDsyVGDE
0 404 S53-p VGMGQkDsyVGDEAQ
0 1057 Y54-p GMGQkDsyVGDEAQs
0 12 S61-p yVGDEAQskRGILtL
0 255 K62-ac VGDEAQskRGILtLk
0 119 K62-ub VGDEAQskRGILtLk
0 11 T67-p QskRGILtLkyPIEH
0 8 K69-ac kRGILtLkyPIEHGI
0 4 K69-m1 kRGILtLkyPIEHGI
0 45 K69-ub kRGILtLkyPIEHGI
0 24 Y70-p RGILtLkyPIEHGII
0 3 T78-p PIEHGIItNWDDMEk
0 3 K85-ac tNWDDMEkIWHHSFY
0 2 K85-m1 tNWDDMEkIWHHSFY
0 1 R96-m1 HSFYNELrVAPEEHP
0 1 K114-ac TEAPLNPkANREKMT
0 15 K114-ub TEAPLNPkANREKMT
0 16 Y144-p IQAVLSLyASGRTTG
0 92 Y167-p VTHNVPIyEGyALPH
0 75 Y170-p NVPIyEGyALPHAIM
0 2 T187-p DLAGRDLtDyLMkIL
0 234 Y189-p AGRDLtDyLMkILtE
0 6 K192-ac DLtDyLMkILtERGy
0 94 K192-ub DLtDyLMkILtERGy
0 22 T195-p DyLMkILtERGysFV
0 207 Y199-p kILtERGysFVTTAE
1 7 S200-p ILtERGysFVTTAER
0 5 K214-ac REIVRDIkEkLCyVA
0 1 K216-ac IVRDIkEkLCyVALD
0 1 K216-m1 IVRDIkEkLCyVALD
0 1 K216 IVRDIkEKLCyVALD
0 18 Y219-p DIkEkLCyVALDFEN
0 3 S234-p EMATAASssSLEksy
0 1 S235-p MATAASssSLEksyE
0 3 K239-ub ASssSLEksyELPDG
0 15 S240-p SssSLEksyELPDGQ
0 34 Y241-p ssSLEksyELPDGQV
0 16 T250-p LPDGQVItIGNERFR
0 2 S266-p PETLFQPsFIGMESA
0 14 Y280-p AGIHETTyNSIMKCD
0 76 Y295-p IDIRKDLyANNVLSG
0 69 Y307-p LSGGTTMyPGIADRM
0 9 K316-ac GIADRMQkEItALAP
0 103 K316-ub GIADRMQkEItALAP
0 8 T319-p DRMQkEItALAPstM
0 8 S324-p EItALAPstMkIkII
0 7 T325-p ItALAPstMkIkIIA
0 11 K327-ac ALAPstMkIkIIAPP
0 135 K327-ub ALAPstMkIkIIAPP
0 9 K329-ac APstMkIkIIAPPER
0 106 K329-ub APstMkIkIIAPPER
0 2 Y363-p MWISKPEyDEAGPSI
  mouse

 
S34-p APRAVFPsIVGRPRH
K51-ac VMVGMGQkDsyVGDE
K51-ub VMVGMGQkDsyVGDE
S53-p VGMGQkDsyVGDEAQ
Y54-p GMGQkDsyVGDEAQs
S61-p yVGDEAQskRGILtL
K62-ac VGDEAQskRGILtLk
K62-ub VGDEAQskRGILtLk
T67-p QskRGILtLkyPIEH
K69-ac kRGILtLkyPIEHGI
K69 kRGILtLKyPIEHGI
K69-ub kRGILtLkyPIEHGI
Y70-p RGILtLkyPIEHGII
T78-p PIEHGIItNWDDMEk
K85-ac tNWDDMEkIWHHSFY
K85 tNWDDMEKIWHHSFY
R96 HSFYNELRVAPEEHP
K114 TEAPLNPKANREKMT
K114-ub TEAPLNPkANREKMT
Y144-p IQAVLSLyASGRTTG
Y167-p VTHNVPIyEGyALPH
Y170-p NVPIyEGyALPHAIM
T187-p DLAGRDLtDyLMkIL
Y189-p AGRDLtDyLMkILtE
K192-ac DLtDyLMkILtERGy
K192-ub DLtDyLMkILtERGy
T195-p DyLMkILtERGysFV
Y199-p kILtERGysFVTTAE
S200-p ILtERGysFVTTAER
K214-ac REIVRDIkEkLCyVA
K216 IVRDIkEKLCyVALD
K216 IVRDIkEKLCyVALD
K216-ub IVRDIkEkLCyVALD
Y219-p DIkEkLCyVALDFEN
S234-p EMATAASsSSLEKsy
S235 MATAASsSSLEKsyE
K239 ASsSSLEKsyELPDG
S240-p SsSSLEKsyELPDGQ
Y241-p sSSLEKsyELPDGQV
T250-p LPDGQVItIGNERFR
S266-p PETLFQPsFIGMESA
Y280-p AGIHETTyNSIMKCD
Y295 IDIRKDLYANNVLSG
Y307 LSGGTTMYPGIADRM
K316-ac GIADRMQkEItALAP
K316-ub GIADRMQkEItALAP
T319-p DRMQkEItALAPstM
S324-p EItALAPstMkIkII
T325-p ItALAPstMkIkIIA
K327-ac ALAPstMkIkIIAPP
K327-ub ALAPstMkIkIIAPP
K329-ac APstMkIkIIAPPER
K329-ub APstMkIkIIAPPER
Y363 MWISKPEYDEAGPSI
  rat

 
S34-p APRAVFPsIVGRPRH
K51 VMVGMGQKDsyVGDE
K51-ub VMVGMGQkDsyVGDE
S53-p VGMGQkDsyVGDEAQ
Y54-p GMGQkDsyVGDEAQS
S61 yVGDEAQSkRGILTL
K62-ac VGDEAQSkRGILTLK
K62-ub VGDEAQSkRGILTLK
T67 QSkRGILTLKYPIEH
K69 kRGILTLKYPIEHGI
K69 kRGILTLKYPIEHGI
K69 kRGILTLKYPIEHGI
Y70 RGILTLKYPIEHGII
T78 PIEHGIITNWDDMEK
K85 TNWDDMEKIWHHSFY
K85 TNWDDMEKIWHHSFY
R96 HSFYNELRVAPEEHP
K114 TEAPLNPKANREKMT
K114 TEAPLNPKANREKMT
Y144 IQAVLSLYASGRTTG
Y167-p VTHNVPIyEGyALPH
Y170-p NVPIyEGyALPHAIM
T187 DLAGRDLTDyLMkIL
Y189-p AGRDLTDyLMkILTE
K192 DLTDyLMKILTERGy
K192-ub DLTDyLMkILTERGy
T195 DyLMkILTERGysFV
Y199-p kILTERGysFVTTAE
S200-p ILTERGysFVTTAER
K214 REIVRDIKEKLCyVA
K216 IVRDIKEKLCyVALD
K216 IVRDIKEKLCyVALD
K216 IVRDIKEKLCyVALD
Y219-p DIKEKLCyVALDFEN
S234 EMATAASSSSLEKsy
S235 MATAASSSSLEKsyE
K239 ASSSSLEKsyELPDG
S240-p SSSSLEKsyELPDGQ
Y241-p SSSLEKsyELPDGQV
T250 LPDGQVITIGNERFR
S266 PETLFQPSFIGMESA
Y280 AGIHETTYNSIMKCD
Y295-p IDIRKDLyANNVLSG
Y307-p LSGGTTMyPGIADRM
K316-ac GIADRMQkEITALAP
K316-ub GIADRMQkEITALAP
T319 DRMQkEITALAPSTM
S324 EITALAPSTMkIkII
T325 ITALAPSTMkIkIIA
K327-ac ALAPSTMkIkIIAPP
K327-ub ALAPSTMkIkIIAPP
K329 APSTMkIKIIAPPER
K329-ub APSTMkIkIIAPPER
Y363 MWISKPEYDEAGPSI
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