Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ACTN2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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
Chromosomal Location of Human Ortholog: 1q42-q43
Cellular Component: cortical actin cytoskeleton; focal adhesion; cytoskeleton; extracellular region; dendritic spine; actin filament; pseudopodium; cytosol; Z disc; filopodium
Molecular Function: protein dimerization activity; integrin binding; actin filament binding; identical protein binding; LIM domain binding; protein 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; muscle filament sliding; protein homotetramerization; regulation of apoptosis; synaptic transmission; regulation of membrane potential; platelet degranulation; microspike biogenesis; cell adhesion; blood coagulation
Disease: Cardiomyopathy, Dilated, 1aa
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.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 3 K42-ub AWEKQQRkTFTAWCN
0 2 T57-p SHLRKAGtQIENIEE
0 1 R83-m1 LEVISGErLPkPDRG
0 1 K86-m1 ISGErLPkPDRGKMR
0 1 K96 RGKMRFHKIANVNKA
0 1 K102 HKIANVNKALDyIAS
0 4 Y106-p NVNKALDyIASKGVK
0 15 S147-p RFAIQDIsVEETSAK
0 12 K181-ac QNFHTSWkDGLGLCA
0 43 Y200-p HRPDLIDysKLNKDD
0 7 S201-p RPDLIDysKLNKDDP
0 1 K221 LAMEIAEKHLDIPKM
0 5 T237-p DAEDIVNtPKPDERA
0 1 K239 EDIVNtPKPDERAIM
0 1 K239 EDIVNtPKPDERAIM
0 1 K271 TAANRICKVLAVNQE
0 2 S291-p EEYERLAsELLEWIR
0 1 K311 LENRTPEKTMQAMQK
0 1 K311 LENRTPEKTMQAMQK
0 46 K338-ub KPPKVQEkCQLEINF
0 1 S355-p LQTKLRIsNRPAFMP
0 1 K366 AFMPSEGKMVSDIAG
0 1 K366 AFMPSEGKMVSDIAG
0 1 S369 PSEGKMVSDIAGAWQ
0 1 K405 RLEHLAEKFRQKAST
0 1 K405 RLEHLAEKFRQKAST
0 1 K409 LAEKFRQKASTHETW
0 1 S411 EKFRQKASTHETWAY
0 1 K420 HETWAYGKEQILLQK
0 1 K427 KEQILLQKDYEsAsL
0 3 S431-p LLQKDYEsAsLtEVR
0 4 S433-p QKDYEsAsLtEVRAL
0 3 T435-p DYEsAsLtEVRALLR
0 2 T495 DQWDRLGTLTQkRRE
0 6 K499-ac RLGTLTQkRREALER
0 6 K523-ac QLHLEFAkRAAPFNN
0 1 T556 EEIQSLITAHEQFKA
0 2 S574 EADGERQSIMAIQNE
0 2 K584 AIQNEVEKVIQsyNI
0 1 S588-p EVEKVIQsyNIRIss
0 26 Y589-p VEKVIQsyNIRIsss
0 4 N590 EKVIQsyNIRIsssN
0 2 S594-p QsyNIRIsssNPyST
0 1 S595-p syNIRIsssNPySTV
0 2 S596-p yNIRIsssNPySTVT
0 3 Y599-p RIsssNPySTVTMDE
0 1 K613 ELRTKWDKVKQLVPI
0 1 K615 RTKWDKVKQLVPIRD
0 1 S624 LVPIRDQSLQEELAR
0 1 K679 EDQMNQLKQyEHNII
0 1 Y681-p QMNQLKQyEHNIINY
0 1 Y715-p FDNKHTNyTMEHIRV
0 1 T744 EVETQILTRDAKGIT
0 1 K748 QILTRDAKGITQEQM
0 1 K748 QILTRDAKGITQEQM
0 1 T822 IDFMTRETADTDTAE
0 2 T825 MTRETADTDTAEQVI
0 3 S840-p ASFRILAsDKPyILA
0 1 K842 FRILAsDKPyILAEE
0 1 K842 FRILAsDKPyILAEE
0 5 Y844-p ILAsDKPyILAEELR
0 1 Y861-p LPPDQAQyCIKRMPA
0 1 K864 DQAQyCIKRMPAYSG
0 3 S892-p SSALYGEsDL_____
  mouse

 
K42-ub AWEKQQRkTFTAWCN
T57 SHLRKAGTQIENIEE
R83 LEVISGERLPKPDRG
K86 ISGERLPKPDRGKMR
K96-ub RGKMRFHkIANVNkA
K102-ub HkIANVNkALDYIAS
Y106 NVNkALDYIASKGVK
S147-p RFAIQDIsVEETSAK
K181 QNFHTSWKDGLGLCA
Y200-p HRPDLIDysKLNKDD
S201-p RPDLIDysKLNKDDP
K221 LAMEIAEKHLDIPKM
T237-p DAEDIVNtPkPDERA
K239 EDIVNtPKPDERAIM
K239-ub EDIVNtPkPDERAIM
K271-ub TAANRICkVLAVNQE
S291-p EEYERLAsELLEWIR
K311 LENRTPEKTMQAMQK
K311-ub LENRTPEkTMQAMQK
K338-ub KPPKVQEkCQLEINF
S355 LQTKLRISNRPAFMP
K366 AFMPSEGKMVSDIAG
K366 AFMPSEGKMVSDIAG
S369 PSEGKMVSDIAGAWQ
K405 RLEHLAEKFRQkAST
K405-ub RLEHLAEkFRQkAST
K409-ub LAEkFRQkASTHETW
S411 EkFRQkASTHETWAY
K420-ub HETWAYGkEQILLQk
K427-ub kEQILLQkDYEsAsL
S431-p LLQkDYEsAsLTEVR
S433-p QkDYEsAsLTEVRAL
T435 DYEsAsLTEVRALLR
T495-p DQWDRLGtLTQKRRE
K499 RLGtLTQKRREALER
K523 QLHLEFAKRAAPFNN
T556-p EEIQSLItAHEQFKA
S574-p EADGERQsILAIQNE
K584-ub AIQNEVEkVIQSYsI
S588 EVEkVIQSYsIRISS
Y589 VEkVIQSYsIRISSs
S590-p EkVIQSYsIRISSsN
S594 QSYsIRISSsNPYST
S595 SYsIRISSsNPYSTV
S596-p YsIRISSsNPYSTVT
Y599 RISSsNPYSTVTMDE
K613 ELRNKWDKVKQLVPV
K615 RNKWDKVKQLVPVRD
S624 LVPVRDQSLQEELAR
K679 EDQMNQLKQYEHNII
Y681 QMNQLKQYEHNIINY
Y715 FDNKHTNYTMEHIRV
T744 EVETQILTRDAkGIT
K748 QILTRDAKGITQEQM
K748-ub QILTRDAkGITQEQM
T822-p IDFMTREtADtDTAE
T825-p MTREtADtDTAEQVI
S840-p ASFRILAsDkPYILA
K842 FRILAsDKPYILAEE
K842-ub FRILAsDkPYILAEE
Y844 ILAsDkPYILAEELR
Y861 LPPDQAQYCIkRMPP
K864-ub DQAQYCIkRMPPYSG
S892-p SSALYGEsDL_____
  rat

 
K42 AWEKQQRKTFTAWCN
T57-p SHLRKAGtQIENIEE
R83 LEVISGERLPKPDRG
K86 ISGERLPKPDRGKMR
K96 RGKMRFHKIANVNKA
K102 HKIANVNKALDYIAS
Y106 NVNKALDYIASKGVK
S147-p RFAIQDIsVEETSAK
K181 QNFHTSWKDGLGLCA
Y200-p HRPDLIDysKLNKDD
S201-p RPDLIDysKLNKDDP
K221-ac LAMEIAEkHLDIPKM
T237-p DAEDIVNtPkPDERA
K239-ac EDIVNtPkPDERAIM
K239 EDIVNtPKPDERAIM
K298 TAANRICKVLAVNQE
S318-p EEYERLAsELLEWIR
K338-ac LENRTPEkTMQAMQK
K338 LENRTPEKTMQAMQK
K365-ub KPPKVQEkCQLEINF
S382 LQTKLRISNRPAFMP
K393-ac AFMPSEGkMVsDIAG
K393-ub AFMPSEGkMVsDIAG
S396-p PSEGkMVsDIAGAWQ
K432-ac RLEHLAEkFRQKAsT
K432 RLEHLAEKFRQKAsT
K436 LAEkFRQKAsTHETW
S438-p EkFRQKAsTHETWAY
K447 HETWAYGKEQILLQK
K454 KEQILLQKDYEsAsL
S458-p LLQKDYEsAsLtEVR
S460-p QKDYEsAsLtEVRAL
T462-p DYEsAsLtEVRALLR
T522-p DQWDRLGtLTQKRRE
K526 RLGtLTQKRREALER
K550 QLHLEFAKRAAPFNN
T583 EEIQSLITAHEQFKA
S601-p EADGERQsILAIQNE
K611-ub AIQNEVEkVIQSYsI
S615 EVEkVIQSYsIRIsS
Y616 VEkVIQSYsIRIsSS
S617-p EkVIQSYsIRIsSSN
S621-p QSYsIRIsSSNPyST
S622 SYsIRIsSSNPySTV
S623 YsIRIsSSNPySTVT
Y626-p RIsSSNPySTVTMDE
K640-ac ELRNKWDkVkQLVPV
K642-ac RNKWDkVkQLVPVRD
S651-p LVPVRDQsLQEELAR
K706-ac EDQMNQLkQYEHNII
Y708 QMNQLkQYEHNIINY
Y742 FDNKHTNYTMEHIRV
T771-p EVETQILtRDAkGIT
K775-ac QILtRDAkGITQEQM
K775 QILtRDAKGITQEQM
T849 IDFMTRETADTDTAE
T852 MTRETADTDTAEQVI
S867-p ASFRILAsDkPYILA
K869-ac FRILAsDkPYILAEE
K869 FRILAsDKPYILAEE
Y871 ILAsDkPYILAEELR
Y888 LPPDQAQYCIKRMPP
K891 DQAQYCIKRMPPYSG
S919-p SSALYGEsDL_____
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.