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Protein Page:
CSRP3 (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
CSRP3 Positive regulator of myogenesis. Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation. Defects in CSRP3 are the cause of cardiomyopathy dilated type 1M (CMD1M). 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. Defects in CSRP3 are the cause of familial hypertrophic cardiomyopathy type 12 (CMH12). Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. Note: This description may include information from UniProtKB.
Protein type: Transcription regulation
Cellular Component: cytoskeleton; nucleus; Z disc
Molecular Function: actinin binding; protein binding; telethonin binding; zinc ion binding; structural constituent of muscle
Biological Process: cellular calcium ion homeostasis; cardiac muscle development; skeletal muscle development; protein localization in organelle; cardiac myofibril assembly; regulation of the force of heart contraction; cardiac muscle contraction
Reference #:  P50461 (UniProtKB)
Alt. Names/Synonyms: cardiac LIM domain protein; Cardiac LIM protein; CLP; CMD1M; CMH12; CRP3; CSRP3; Cysteine and glycine-rich protein 3; cysteine and glycine-rich protein 3 (cardiac LIM protein); Cysteine-rich protein 3; LIM domain only 4; LIM domain protein, cardiac; LMO4; MGC14488; MGC61993; MLP; Muscle LIM protein
Gene Symbols: CSRP3
Molecular weight: 20,969 Da
Basal Isoelectric point: 8.89  Predict pI for various phosphorylation states
Select Structure to View Below

CSRP3

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 1 K15 AKCGACEKtVyHAEE
0 1 T16-p KCGACEKtVyHAEEI
0 99 Y18-p GACEKtVyHAEEIQC
0 1 K32 CNGRSFHKTCFHCMA
0 1 K42 FHCMACRKALDSTTV
0 3 S54-p TTVAAHEsEIyCKVC
0 37 Y57-p AAHEsEIyCKVCYGR
1 0 K69-ac YGRRYGPkGIGyGQG
0 2 Y73-p YGPkGIGyGQGAGCL
0 1 T84 AGCLSTDTGEHLGLQ
0 14 S95-p LGLQFQQsPKPARsV
0 1 S101-p QsPKPARsVTTSNPS
0 1 K109 VTTSNPSKFTAKFGE
0 2 T111 TSNPSKFTAKFGESE
0 1 K113 NPSKFTAKFGESEKC
0 1 S117 FTAKFGESEKCPRCG
0 1 K125 EKCPRCGKSVYAAEk
0 2 K132-ub KSVYAAEkVMGGGKP
0 1 S153 RCAICGKSLESTNVT
0 8 Y167-p TDKDGELyCKVCyAK
0 1 K169 KDGELyCKVCyAKNF
0 40 Y172-p ELyCKVCyAKNFGPT
  mouse

 
K15-ub AKCGACEkTVyHAEE
T16 KCGACEkTVyHAEEI
Y18-p GACEkTVyHAEEIQC
K32-ac CNGRSFHkTCFHCMA
K42-ub FHCMACRkALDSTTV
S54 TTVAAHESEIyCKVC
Y57-p AAHESEIyCKVCYGR
K69 YGRRYGPKGIGFGQG
F73 YGPKGIGFGQGAGCL
T84-p AGCLSTDtGEHLGLQ
S95-p LGLQFQQsPKPARAA
A101 QsPKPARAATTSNPS
K109-ub ATTSNPSkFsAkFGE
S111-p TSNPSkFsAkFGEsE
K113-ub NPSkFsAkFGEsEKC
S117-p FsAkFGEsEKCPRCG
K125-ub EKCPRCGkSVYAAEK
K132 kSVYAAEKVMGGGKP
S153-p RCAICGKsLESTNVT
Y167 TDKDGELYCkVCYAK
K169-ub KDGELYCkVCYAKNF
Y172 ELYCkVCYAKNFGPT
  rat

 
K15 AKCGACDKTVyHAEE
T16 KCGACDKTVyHAEEI
Y18-p GACDKTVyHAEEIQC
K32 CNGRSFHKTCFHCMA
K42 FHCMACRKALDSTTV
S54 TTVAAHESEIyCKVC
Y57-p AAHESEIyCKVCYGR
K69 YGRKYGPKGIGFGQG
F73 YGPKGIGFGQGAGCL
T84 AGCLSTDTGEHLGLQ
S95 LGLQFQQSPKPARAA
A101 QSPKPARAATTSNPS
K109 ATTSNPSKFSAKFGE
S111 TSNPSKFSAKFGESE
K113 NPSKFSAKFGESEKC
S117 FSAKFGESEKCPRCG
K125 EKCPRCGKSVYAAEK
K132 KSVYAAEKVMGGGKP
S153-p PCAICGKsLESTNVT
Y167 TDKDGELYCKVCyAK
K169 KDGELYCKVCyAKNF
Y172-p ELYCKVCyAKNFGPT
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