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Protein Page:
ACTN2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ACTN2 F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Defects in ACTN2 are the cause of cardiomyopathy dilated type 1AA (CMD1AA). Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Belongs to the alpha-actinin family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Cytoskeletal protein
Cellular Component: focal adhesion; cytoskeleton; extracellular region; dendritic spine; actin filament; pseudopodium; Z disc; cytosol; filopodium
Molecular Function: actin filament binding; integrin binding; protein dimerization activity; identical protein binding; protein binding; LIM domain binding; structural constituent of muscle; cytoskeletal protein binding; titin binding; calcium ion binding; FATZ binding; thyroid hormone receptor coactivator activity
Biological Process: focal adhesion formation; platelet activation; negative regulation of potassium ion transport; positive regulation of potassium ion transport; protein homotetramerization; muscle filament sliding; regulation of apoptosis; synaptic transmission; regulation of membrane potential; platelet degranulation; microspike biogenesis; blood coagulation; cell adhesion
Reference #:  P35609 (UniProtKB)
Alt. Names/Synonyms: actinin, alpha 2; ACTN2; alpha-actinin skeletal muscle; Alpha-actinin skeletal muscle isoform 2; Alpha-actinin-2; CMD1AA
Gene Symbols: ACTN2
Molecular weight: 103,854 Da
Basal Isoelectric point: 5.31  Predict pI for various phosphorylation states
Select Structure to View Below

ACTN2

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 3 K42-u AWEKQQRkTFTAWCN
0 1 K102 HKIANVNKALDyIAS
0 3 Y106-p NVNKALDyIASKGVK
0 13 S147-p RFAIQDIsVEETSAK
0 12 K181-a QNFHTSWkDGLGLCA
0 40 Y200-p HRPDLIDysKLNKDD
0 3 S201-p RPDLIDysKLNKDDP
0 3 T237-p DAEDIVNtPKPDERA
0 1 K239 EDIVNtPKPDERAIM
0 1 K271 TAANRICKVLAVNQE
0 1 K311 LENRTPEKTMQAMQK
0 47 K338-u KPPKVQEkCQLEINF
0 1 S355-p LQTKLRIsNRPAFMP
0 1 K405 RLEHLAEKFRQKAST
0 1 K409 LAEKFRQKASTHETW
0 1 K420 HETWAYGKEQILLQK
0 1 K427 KEQILLQKDYEsAsL
0 1 S431-p LLQKDYEsAsLtEVR
0 2 S433-p QKDYEsAsLtEVRAL
0 2 T435-p DYEsAsLtEVRALLR
0 6 K499-a RLGTLTQkRREALER
0 6 K523-a QLHLEFAkRAAPFNN
0 2 K584 AIQNEVEKVIQSyNI
0 17 Y589-p VEKVIQSyNIRIsss
0 2 N590 EKVIQSyNIRIsssN
0 1 S594-p QSyNIRIsssNPyST
0 1 S595-p SyNIRIsssNPySTV
0 2 S596-p yNIRIsssNPySTVT
0 3 Y599-p RIsssNPySTVTMDE
0 1 K748 QILTRDAKGITQEQM
0 2 T825 MTRETADTDTAEQVI
0 1 S840-p ASFRILAsDKPyILA
0 1 K842 FRILAsDKPyILAEE
0 5 Y844-p ILAsDKPyILAEELR
0 1 K864 DQAQYCIKRMPAYSG
  mouse

 
K42-u AWEKQQRkTFTAWCN
K102-u HKIANVNkALDYIAS
Y106 NVNkALDYIASKGVK
S147-p RFAIQDIsVEETSAK
K181 QNFHTSWKDGLGLCA
Y200-p HRPDLIDysKLNKDD
S201-p RPDLIDysKLNKDDP
T237-p DAEDIVNtPkPDERA
K239-u EDIVNtPkPDERAIM
K271-u TAANRICkVLAVNQE
K311-u LENRTPEkTMQAMQK
K338-u KPPKVQEkCQLEINF
S355 LQTKLRISNRPAFMP
K405-u RLEHLAEkFRQkAST
K409-u LAEkFRQkASTHETW
K420-u HETWAYGkEQILLQk
K427-u kEQILLQkDYESAsL
S431 LLQkDYESAsLTEVR
S433-p QkDYESAsLTEVRAL
T435 DYESAsLTEVRALLR
K499 RLGTLTQKRREALER
K523 QLHLEFAKRAAPFNN
K584-u AIQNEVEkVIQSYsI
Y589 VEkVIQSYsIRISSs
S590-p EkVIQSYsIRISSsN
S594 QSYsIRISSsNPYST
S595 SYsIRISSsNPYSTV
S596-p YsIRISSsNPYSTVT
Y599 RISSsNPYSTVTMDE
K748-u QILTRDAkGITQEQM
T825-p MTRETADtDTAEQVI
S840 ASFRILASDkPYILA
K842-u FRILASDkPYILAEE
Y844 ILASDkPYILAEELR
K864-u DQAQYCIkRMPPYSG
  rat

 
K42 AWEKQQRKTFTAWCN
K102 HKIANVNKALDYIAS
Y106 NVNKALDYIASKGVK
S147-p RFAIQDIsVEETSAK
K181 QNFHTSWKDGLGLCA
Y200-p HRPDLIDySKLNKDD
S201 RPDLIDySKLNKDDP
T237 DAEDIVNTPKPDERA
K239 EDIVNTPKPDERAIM
K298 TAANRICKVLAVNQE
K338 LENRTPEKTMQAMQK
K365-u KPPKVQEkCQLEINF
S382 LQTKLRISNRPAFMP
K432 RLEHLAEKFRQKAST
K436 LAEKFRQKASTHETW
K447 HETWAYGKEQILLQK
K454 KEQILLQKDYESASL
S458 LLQKDYESASLTEVR
S460 QKDYESASLTEVRAL
T462 DYESASLTEVRALLR
K526 RLGTLTQKRREALER
K550 QLHLEFAKRAAPFNN
K611-u AIQNEVEkVIQSYSI
Y616 VEkVIQSYSIRISSS
S617 EkVIQSYSIRISSSN
S621 QSYSIRISSSNPyST
S622 SYSIRISSSNPySTV
S623 YSIRISSSNPySTVT
Y626-p RISSSNPySTVTMDE
K775 QILTRDAKGITQEQM
T852 MTRETADTDTAEQVI
S867 ASFRILASDKPYILA
K869 FRILASDKPYILAEE
Y871 ILASDKPYILAEELR
K891 DQAQYCIKRMPPYSG
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