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Protein Page:
dystrophin (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
dystrophin Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin- associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. Defects in DMD are the cause of Duchenne muscular dystrophy (DMD). DMD is the most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment. Defects in DMD are the cause of Becker muscular dystrophy (BMD). BMD resembles DMD in hereditary and clinical features but is later in onset and more benign. Defects in DMD are a cause of cardiomyopathy dilated X- linked type 3B (CMD3B); also known as X-linked dilated cardiomyopathy (XLCM). 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. 6 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Cytoskeletal protein
Cellular Component: protein complex; costamere; cell surface; syntrophin complex; Z disc; cytosol; actin cytoskeleton; lipid raft; cell-matrix junction; dystrophin-associated glycoprotein complex; postsynaptic membrane; cytoskeleton; plasma membrane; nucleus; sarcolemma; lateral plasma membrane; filopodium
Molecular Function: protein binding; myosin binding; zinc ion binding; structural constituent of cytoskeleton; structural constituent of muscle; calcium ion binding; nitric-oxide synthase binding; actin binding; vinculin binding
Biological Process: regulation of skeletal muscle contraction via regulation of the release of sequestered calcium ion; extracellular matrix organization and biogenesis; skeletal muscle development; muscle development; establishment of blood-nerve barrier; neurotransmitter receptor metabolic process; regulation of heart rate; olfactory nerve structural organization; negative regulation of peptidyl-serine phosphorylation; myotube cell development; nucleus localization; peptide biosynthetic process; muscle filament sliding; muscle maintenance; cellular protein complex assembly; regulation of transcription, DNA-dependent; regulation of skeletal muscle contraction; muscle fiber development; positive regulation of cell-matrix adhesion; positive regulation of neuron differentiation; cardiac muscle contraction
Reference #:  P11532 (UniProtKB)
Alt. Names/Synonyms: BMD; CMD3B; DMD; DXS142; DXS164; DXS206; DXS230; DXS239; DXS268; DXS269; DXS270; DXS272; Dystrophin
Gene Symbols: DMD
Molecular weight: 426,750 Da
Basal Isoelectric point: 5.64  Predict pI for various phosphorylation states
Select Structure to View Below

dystrophin

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

► Hide Isoforms
 
0 27 K225-a VDTTYPDkKSILMYI
0 1 K225 VDTTYPDKKSILMYI
0 12 S1273 ACWHELLSYLEKANK
0 3 K1288-u WLNEVEFkLKTTENI
0 2 K1428 EISLEEMKKHNQGKE
0 19 Y1509-p LNHCVNLyKSLSEVK
0 1 K1563 GAKVTERKQQLEKCL
0 1 T1590-p LTEWLAAtDMELTKR
0 1 S1768 NHRFAAISHRIKTGK
0 4 K1911-a PEPRDERkIKEIDRE
0 1 P2068 AALQSATPVERVKLQ
0 1 S2672-p NINASWRsIHKRVSE
0 1 - gap
0 2 K2808-a EASSDQWkRLHLSLQ
0 1 K2843 GDFPAVQKQNDVHRA
0 2 Y2885-p LEGLEKLyQEPRELP
0 1 K2928 HSADWQRKIDETLER
0 1 K2989 RGEIAPLKENVSHVN
0 1 K3069 ERAISPNKVPYYINH
0 1 - gap
0 1 K3220 DKYRYLFKQVASSTG
0 7 K3308-u VAAAETAkHQAkCNI
0 4 K3312-u ETAkHQAkCNICKEC
0 6 Y3354-p AKGHKMHyPMVEYCT
0 1 T3399 MGYLPVQTVLEGDNM
0 1 T3408 LEGDNMETPVTLINF
0 1 S3424 PVDSAPASSPQLSHD
0 1 S3425 VDSAPASSPQLSHDD
0 4 S3429 PASSPQLSHDDTHSR
0 2 S3435 LSHDDTHSRIEHYAS
0 1 S3483-p CQSLNQDsPLSQPRS
0 3 S3490 sPLSQPRSPAQILIS
0 1 S3500 QILISLESEERGELE
0 2 S3537-p QHEHKGLsPLPsPPE
0 2 S3541-p KGLsPLPsPPEMMPt
0 1 T3548-p sPPEMMPtsPQsPRD
0 2 S3549-p PPEMMPtsPQsPRDA
0 1 S3552-p MMPtsPQsPRDAELI
0 2 K3563-u AELIAEAkLLRQHKG
0 4 S3612-p KVNGTTVssPSTsLQ
0 9 S3613-p VNGTTVssPSTsLQR
0 1 T3616 TTVssPSTsLQRsDs
0 5 S3617-p TVssPSTsLQRsDss
0 3 S3621-p PSTsLQRsDssQPML
0 14 S3623-p TsLQRsDssQPMLLR
0 5 S3624-p sLQRsDssQPMLLRV
0 1 S3666-p VMEQLNNsFPSSRGR
0 6 T3675-p PSSRGRNtPGKPMRE
0 34 T3684-p GKPMREDtM______
0 1 - gap
  dystrophin iso5  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K6 __MREQLKGHETQTT
K152 DKYRYLFKQVASSTG
K240 VAAAETAKHQAKCNI
K244 ETAKHQAKCNICKEC
Y286 AKGHKMHYPMVEYCT
T331-p MGYLPVQtVLEGDNM
T340-p LEGDNMEtPAssPQL
S343-p DNMEtPAssPQLsHD
S344-p NMEtPAssPQLsHDD
S348-p PAssPQLsHDDTHsR
S354-p LsHDDTHsRIEHYAS
S402 CQSLNQDSPLSQPRS
S409 SPLSQPRSPAQILIS
S419 QILISLESEERGELE
S456 QHEHKGLSPLPSPPE
S460 KGLSPLPSPPEMMPT
T467 SPPEMMPTSPQSPRD
S468 PPEMMPTSPQSPRDA
S471 MMPTSPQSPRDAELI
K482 AELIAEAKLLRQHKG
S531 KVNGTTVSSPSTSLQ
S532 VNGTTVSSPSTSLQR
T535 TTVSSPSTSLQRSDs
S536 TVSSPSTSLQRSDsS
S540 PSTSLQRSDsSQPML
S542-p TSLQRSDsSQPMLLR
S543 SLQRSDsSQPMLLRV
S585 VMEQLNNSFPSSRGH
- gap
- gap
T616-p ESLVSVMtDEEGAE_
  mouse

► Hide Isoforms
 
K225 VATTYPDKKSILMYI
K225-u VATTYPDkKSILMYI
S1275-p ACWHELLsYLEKANK
K1290 WLNEVELKLKTMENV
K1430-a EISLEEMkKHNQGKD
Y1511 LSHCVNLYKSLSEVK
K1565-u GAKVTERkQQLEKCL
T1592 LTEWLAATDTELTKR
S1770-p NRRFAAIsHRIKTGK
K1913-a PEPRDERkLKEIDRE
S2070-p AALQSATsMEKVKVQ
N2665 NINTSWGNIHKRVSE
- gap
K2801 EASSDQWKRLHLSLQ
K2836-u GDFPAVQkQNDIHRA
Y2878 LEGLEKLYQEPRELP
K2921-u RSADWQRkIDEALER
K2982-u RGEIAPLkENVNRVN
K3062-u ERAISPNkVPYYINH
- gap
K3213-u DKYRYLFkQVASSTG
K3301-u VAAAETAkHQAKCNI
K3305 ETAkHQAKCNICKEC
Y3347 AKGHKMHYPMVEYCT
T3392 MGYLPVQTVLEGDNM
T3401 LEGDNMETPVTLINF
S3417 PVDSAPASSPQLsHD
S3418 VDSAPASSPQLsHDD
S3422-p PASSPQLsHDDTHSR
S3428 LsHDDTHSRIEHYAS
S3476 CQSLNQDSPLSQPRs
S3483-p SPLSQPRsPAQILIS
S3493-p QILISLEsEERGELE
S3530-p QHEHKGLsPLPsPPE
S3534-p KGLsPLPsPPEMMPT
T3541 sPPEMMPTSPQSPRD
S3542 PPEMMPTSPQSPRDA
S3545 MMPTSPQSPRDAELI
K3556-u AELIAEAkLLRQHKG
S3605-p KVNGTTVssPStsLQ
S3606-p VNGTTVssPStsLQR
T3609-p TTVssPStsLQRsDs
S3610-p TVssPStsLQRsDss
S3614-p PStsLQRsDssQPML
S3616-p tsLQRsDssQPMLLR
S3617-p sLQRsDssQPMLLRV
S3659 VMEQLNNSFPSSRGR
- gap
T3677-p GKPMREDtM______
- gap
  dystrophin iso3  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K6-u __MREHLkGHETQTT
K152 DKYRYLFKQVASSTG
K240 VAAAETAKHQAKCNI
K244 ETAKHQAKCNICKEC
Y286 AKGHKMHYPMVEYCT
T331 MGYLPVQTVLEGDNM
T340 LEGDNMETPASSPQL
S343 DNMETPASSPQLSHD
S344 NMETPASSPQLSHDD
S348 PASSPQLSHDDTHSR
S354 LSHDDTHSRIEHYAS
S402 CQSLNQDSPLSQPRS
S409 SPLSQPRSPAQILIS
S419 QILISLESEERGELE
S456 QHEHKGLSPLPSPPE
S460 KGLSPLPSPPEMMPT
T467 SPPEMMPTSPQSPRD
S468 PPEMMPTSPQSPRDA
S471 MMPTSPQSPRDAELI
K482 AELIAEAKLLRQHKG
S531 KVNGTTVSSPSTSLQ
S532 VNGTTVSSPSTSLQR
T535 TTVSSPSTSLQRSDS
S536 TVSSPSTSLQRSDSS
S540 PSTSLQRSDSSQPML
S542 TSLQRSDSSQPMLLR
S543 SLQRSDSSQPMLLRV
S585 VMEQLNNSFPSSRGR
- gap
T603 GKPMREDTM______
- gap
  dystrophin iso6  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S8-p MQQDQCCsPRFKLKM
K93 EASSDQWKRLHLSLQ
K128 GDFPAVQKQNDIHRA
Y170 LEGLEKLYQEPRELP
K213 RSADWQRKIDEALER
K274 RGEIAPLKENVNRVN
K354 ERAISPNKVPYYIK_
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  rat

 
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K6 __MREHLKGHETQTT
K152 DKYRYLFKQVASSTG
K240 VAAAETAKHQAKCNI
K244 ETAKHQAKCNICKEC
Y286 AKGHKMHYPMVEYCT
T331 MGYLPVQTVLEGDNM
T340 LEGDNMETPASSPQL
S343 DNMETPASSPQLSHD
S344 NMETPASSPQLSHDD
S348 PASSPQLSHDDTHSR
S354 LSHDDTHSRIEHYAS
S402 CQSLNQDSPLSQPRs
S409-p SPLSQPRsPAQILIS
S419 QILISLESEERGELE
S456 QHEHKGLSPLPSPPE
S460 KGLSPLPSPPEMMPT
T467 SPPEMMPTSPQSPRD
S468 PPEMMPTSPQSPRDA
S471 MMPTSPQSPRDAELI
K482 AELIAEAKLLRQHKG
S531 KVNGTTVSsPSTsLQ
S532-p VNGTTVSsPSTsLQR
T535 TTVSsPSTsLQRSDS
S536-p TVSsPSTsLQRSDSS
S540 PSTsLQRSDSSQPML
S542 TsLQRSDSSQPMLLR
S543 sLQRSDSSQPMLLRV
S585 VMEQLNNSFPSSRGH
- gap
- gap
- gap
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