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Protein Page:
dystrophin (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
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: Cytoskeletal protein; Motility/polarity/chemotaxis
Cellular Component: filopodium membrane; costamere; cell surface; protein complex; syntrophin complex; cytosol; lipid raft; actin cytoskeleton; dystrophin-associated glycoprotein complex; postsynaptic membrane; cytoskeleton; plasma membrane; nucleus; cell junction; 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; muscle development; cellular protein complex assembly; regulation of heart rate; regulation of skeletal muscle contraction; negative regulation of peptidyl-serine phosphorylation; positive regulation of neuron differentiation; peptide biosynthetic process; muscle filament sliding; 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 1 K19-ac EREDVQKkTFTKWVN
0 1 T58 LDLLEGLTGQKLPKE
0 27 K225-ac VDTTYPDkKSILMYI
0 1 K225 VDTTYPDKKSILMYI
0 1 T289-p LAQGYERtssPKPRF
0 1 S290-p AQGYERtssPKPRFK
0 1 S291-p QGYERtssPKPRFKS
0 1 T313-p YVTTSDPtRSPFPSQ
0 1 T390-p EGYMMDLtAHQGRVG
0 1 K487-ac GPDLEDLkRQVQQHK
0 1 K614-ub KADLEKKkQsMGKLY
0 1 S616-p DLEKKkQsMGKLYSL
0 1 S622 QsMGKLYSLKQDLLS
0 1 S988-p ELQALQSsLQEQQSG
0 1 K1017-ac APSEISRkYQSEFEE
1 0 T1136-p TELKELNtQWDHMCQ
0 1 K1201-ac QKAVEEMkRAKEEAQ
0 13 S1273 ACWHELLSYLEKANK
0 3 K1288-ub WLNEVEFkLKTTENI
0 2 K1428 EISLEEMKKHNQGKE
0 1 S1455-p QKKLQDVsMKFRLFQ
0 23 Y1509-p LNHCVNLyKSLSEVK
0 1 S1517-p KSLSEVKsEVEMVIK
0 1 T1525-p EVEMVIKtGRQIVQK
0 1 Y1552-p VTALKLHyNELGAKV
0 1 K1563 GAKVTERKQQLEKCL
0 1 T1590-p LTEWLAAtDMELTKR
0 1 K1644-ub ALKTVLGkKETLVED
0 1 S1658-p DKLSLLNsNWIAVTS
0 1 S1768 NHRFAAISHRIKTGK
0 1 T1839 DNLQQRITDERKREE
0 4 K1911-ac PEPRDERkIKEIDRE
0 1 K1921 EIDRELQKKKEELNA
0 1 T2060-p DIIHSKKtAALQSAT
0 1 P2068 AALQSATPVERVKLQ
0 1 S2306-p NLQWIKVsRALPEKQ
0 1 Y2651-p ALKLLRDysADDtRK
0 1 S2652-p LKLLRDysADDtRKV
1 1 T2656-p RDysADDtRKVHMIT
0 1 S2672-p NINASWRsIHKRVSE
0 1 - gap
0 2 K2808-ac EASSDQWkRLHLSLQ
0 1 K2843 GDFPAVQKQNDVHRA
0 1 T2868-p VIMSTLEtVRIFLTE
0 2 Y2885-p LEGLEKLyQEPRELP
0 1 K2928 HSADWQRKIDETLER
0 1 K2989 RGEIAPLKENVsHVN
0 1 S2993-p APLKENVsHVNDLAR
1 0 S3066-p GPWERAIsPNKVPYY
0 1 K3069 ERAIsPNKVPYYINH
0 1 - gap
1 0 T3081-p INHETQTtCWDHPKM
0 1 K3220 DKYRYLFKQVASSTG
0 7 K3308-ub VAAAETAkHQAkCNI
0 4 K3312-ub ETAkHQAkCNICKEC
0 6 Y3354-p AKGHKMHyPMVEyCt
1 0 Y3359-p MHyPMVEyCtPTTSG
1 1 T3361-p yPMVEyCtPTTSGED
0 1 K3388 RTKRYFAKHPRMGYL
0 1 T3399 MGYLPVQTVLEGDNM
0 1 T3408 LEGDNMETPVTLINF
1 1 S3424-p PVDSAPAssPQLsHD
1 1 S3425-p VDSAPAssPQLsHDD
1 4 S3429-p PAssPQLsHDDTHSR
0 1 T3433 PQLsHDDTHSRIEHY
0 3 S3435 LsHDDTHSRIEHYAS
1 1 S3483-p CQSLNQDsPLSQPRs
1 4 S3490-p sPLSQPRsPAQILIS
0 2 S3500-p QILISLEsEERGELE
0 1 Y3524-p NRNLQAEyDRLKQQH
0 2 S3537-p QHEHKGLsPLPsPPE
0 2 S3541-p KGLsPLPsPPEMMPt
1 1 T3548-p sPPEMMPtsPQsPRD
1 2 S3549-p PPEMMPtsPQsPRDA
1 2 S3552-p MMPtsPQsPRDAELI
0 2 K3563-ub AELIAEAkLLRQHKG
0 1 T3610-p EAKVNGTtVssPsts
0 6 S3612-p KVNGTtVssPstsLQ
0 11 S3613-p VNGTtVssPstsLQR
1 1 S3615-p GTtVssPstsLQRsD
0 2 T3616-p TtVssPstsLQRsDs
0 6 S3617-p tVssPstsLQRsDss
1 4 S3621-p PstsLQRsDssQPML
1 18 S3623-p tsLQRsDssQPMLLR
1 6 S3624-p sLQRsDssQPMLLRV
0 2 S3666-p VMEQLNNsFPSSRGR
0 7 T3675-p PSSRGRNtPGKPMRE
0 35 T3684-p GKPMREDtM______
0 2 - gap
  dystrophin iso5  
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K6 __MREQLKGHETQTT
T13 KGHETQTTCWDHPKM
K152 DKYRYLFKQVASSTG
K240 VAAAETAKHQAKCNI
K244 ETAKHQAKCNICKEC
Y286 AKGHKMHYPMVEYCT
Y291 MHYPMVEYCTPTTSG
T293 YPMVEYCTPTTSGED
K320 RTKRYFAKHPRMGYL
T331-p MGYLPVQtVLEGDNM
T340-p LEGDNMEtPAssPQL
S343-p DNMEtPAssPQLsHD
S344-p NMEtPAssPQLsHDD
S348-p PAssPQLsHDDtHsR
T352-p PQLsHDDtHsRIEHY
S354-p LsHDDtHsRIEHYAS
S402 CQSLNQDSPLSQPRS
S409 SPLSQPRSPAQILIS
S419 QILISLESEERGELE
Y443 NRNLQAEYDRLKQQH
S456 QHEHKGLSPLPSPPE
S460 KGLSPLPSPPEMMPT
T467 SPPEMMPTSPQSPRD
S468 PPEMMPTSPQSPRDA
S471 MMPTSPQSPRDAELI
K482 AELIAEAKLLRQHKG
T529-p EAKVNGTtVSSPSTS
S531 KVNGTtVSSPSTSLQ
S532 VNGTtVSSPSTSLQR
S534 GTtVSSPSTSLQRSD
T535 TtVSSPSTSLQRSDs
S536 tVSSPSTSLQRSDsS
S540 PSTSLQRSDsSQPML
S542-p TSLQRSDsSQPMLLR
S543 SLQRSDsSQPMLLRV
S585 VMEQLNNSFPSSRGH
- gap
- gap
T616-p ESLVSVMtDEEGAE_
  mouse

► Hide Isoforms
 
K19 EREDVQKKTFTKWIN
T58-p LDLLEGLtGQKLPKE
K225 VATTYPDKKSILMYI
K225-ub VATTYPDkKSILMYI
T290 LAQGYEQTSSSPKPR
S291 AQGYEQTSSSPKPRF
S292 QGYEQTSSSPKPRFK
T315 YVATSDSTQSPYPSQ
T392 EGFMMDLTSHQGLVG
K489 GPDLEDLKCQVQQHK
K616 KIDLEKKKPTMEKLS
T618 DLEKKKPTMEKLSsL
S624-p PTMEKLSsLNQDLLS
S990 KLQALQSSLKEQQNG
K1019 APSEICQKYLSEFEE
T1138 TELRELNTQWDHICR
K1203 QTAVEEMKRAKEEAL
S1275-p ACWHELLsYLEKANK
K1290 WLNEVELKLKTMENV
K1430-ac EISLEEMkKHNQGKD
S1457 QKKLQDVSMKFRLFQ
Y1511 LSHCVNLYKSLSEVK
S1519 KSLSEVKSEVEMVIK
T1527 EVEMVIKTGRQIVQK
Y1554 VTALKLHYNELGAKV
K1565-ub GAKVTERkQQLEKCL
T1592 LTEWLAATDTELTKR
K1646 SLKMVLGKKETLVED
S1660 DKLSLLNSNWIAVTS
S1770-p NRRFAAIsHRIKTGK
T1841-p DNLQQRItDERKREE
K1913-ac PEPRDERkLKEIDRE
K1923-ac EIDRELQkKKEELNA
T2062 DIIHKKKTAALQSAT
S2070-p AALQSATsMEKVKVQ
S2306 NLQWIKVSRALPEKQ
Y2644 ALKLLRDYSADDTRK
S2645 LKLLRDYSADDTRKV
T2649 RDYSADDTRKVHMIT
N2665 NINTSWGNIHKRVSE
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K2801 EASSDQWKRLHLSLQ
K2836-ub GDFPAVQkQNDIHRA
T2861 VIMSTLETVRIFLTE
Y2878 LEGLEKLYQEPRELP
K2921-ub RSADWQRkIDEALER
K2982-ub RGEIAPLkENVNRVN
N2986 APLkENVNRVNDLAH
S3059 GPWERAISPNkVPYY
K3062-ub ERAISPNkVPYYINH
- gap
T3074 INHETQTTCWDHPKM
K3213-ub DKYRYLFkQVASSTG
K3301-ub VAAAETAkHQAKCNI
K3305 ETAkHQAKCNICKEC
Y3347 AKGHKMHYPMVEYCT
Y3352 MHYPMVEYCTPTTSG
T3354 YPMVEYCTPTTSGED
K3381-ub RTKRYFAkHPRMGYL
T3392 MGYLPVQTVLEGDNM
T3401 LEGDNMETPVTLINF
S3417 PVDSAPASSPQLsHD
S3418 VDSAPASSPQLsHDD
S3422-p PASSPQLsHDDTHSR
T3426 PQLsHDDTHSRIEHY
S3428 LsHDDTHSRIEHYAS
S3476 CQSLNQDSPLSQPRs
S3483-p SPLSQPRsPAQILIS
S3493-p QILISLEsEERGELE
Y3517 NRNLQAEYDRLKQQH
S3530-p QHEHKGLsPLPsPPE
S3534-p KGLsPLPsPPEMMPT
T3541 sPPEMMPTSPQSPRD
S3542 PPEMMPTSPQSPRDA
S3545 MMPTSPQSPRDAELI
K3556-ub AELIAEAkLLRQHKG
T3603 EAKVNGTTVssPSts
S3605-p KVNGTTVssPStsLQ
S3606-p VNGTTVssPStsLQR
S3608 GTTVssPStsLQRsD
T3609-p TTVssPStsLQRsDs
S3610-p TVssPStsLQRsDss
S3614-p PStsLQRsDssQPML
S3616-p tsLQRsDssQPMLLR
S3617-p sLQRsDssQPMLLRV
S3659 VMEQLNNSFPSSRGR
A3668 PSSRGRNAPGKPMRE
T3677-p GKPMREDtM______
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  dystrophin iso3  
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K6-ub __MREHLkGHETQTT
T13 kGHETQTTCWDHPKM
K152 DKYRYLFKQVASSTG
K240 VAAAETAKHQAKCNI
K244 ETAKHQAKCNICKEC
Y286 AKGHKMHYPMVEYCT
Y291 MHYPMVEYCTPTTSG
T293 YPMVEYCTPTTSGED
K320 RTKRYFAKHPRMGYL
T331 MGYLPVQTVLEGDNM
T340 LEGDNMETPASSPQL
S343 DNMETPASSPQLSHD
S344 NMETPASSPQLSHDD
S348 PASSPQLSHDDTHSR
T352 PQLSHDDTHSRIEHY
S354 LSHDDTHSRIEHYAS
S402 CQSLNQDSPLSQPRS
S409 SPLSQPRSPAQILIS
S419 QILISLESEERGELE
Y443 NRNLQAEYDRLKQQH
S456 QHEHKGLSPLPSPPE
S460 KGLSPLPSPPEMMPT
T467 SPPEMMPTSPQSPRD
S468 PPEMMPTSPQSPRDA
S471 MMPTSPQSPRDAELI
K482 AELIAEAKLLRQHKG
T529 EAKVNGTTVSSPSTS
S531 KVNGTTVSSPSTSLQ
S532 VNGTTVSSPSTSLQR
S534 GTTVSSPSTSLQRSD
T535 TTVSSPSTSLQRSDS
S536 TVSSPSTSLQRSDSS
S540 PSTSLQRSDSSQPML
S542 TSLQRSDSSQPMLLR
S543 SLQRSDSSQPMLLRV
S585 VMEQLNNSFPSSRGR
A594 PSSRGRNAPGKPMRE
T603 GKPMREDTM______
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  dystrophin iso6  
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S8-p MQQDQCCsPRFKLKM
K93 EASSDQWKRLHLSLQ
K128 GDFPAVQKQNDIHRA
T153 VIMSTLETVRIFLTE
Y170 LEGLEKLYQEPRELP
K213 RSADWQRKIDEALER
K274 RGEIAPLKENVNRVN
N278 APLKENVNRVNDLAH
S351 GPWERAISPNKVPYY
K354 ERAISPNKVPYYIK_
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  rat

 
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K6 __MREHLKGHETQTT
T13 KGHETQTTCWDHPKM
K152 DKYRYLFKQVASSTG
K240 VAAAETAKHQAKCNI
K244 ETAKHQAKCNICKEC
Y286 AKGHKMHYPMVEYCT
Y291 MHYPMVEYCTPTTSG
T293 YPMVEYCTPTTSGED
K320 RTKRYFAKHPRMGYL
T331 MGYLPVQTVLEGDNM
T340 LEGDNMETPASSPQL
S343 DNMETPASSPQLSHD
S344 NMETPASSPQLSHDD
S348 PASSPQLSHDDTHSR
T352 PQLSHDDTHSRIEHY
S354 LSHDDTHSRIEHYAS
S402 CQSLNQDSPLSQPRs
S409-p SPLSQPRsPAQILIS
S419 QILISLESEERGELE
Y443 NQNLQAEYDRLKQQH
S456 QHEHKGLSPLPSPPE
S460 KGLSPLPSPPEMMPT
T467 SPPEMMPTSPQSPRD
S468 PPEMMPTSPQSPRDA
S471 MMPTSPQSPRDAELI
K482 AELIAEAKLLRQHKG
T529 EAKVNGTTVSsPSTs
S531 KVNGTTVSsPSTsLQ
S532-p VNGTTVSsPSTsLQR
S534 GTTVSsPSTsLQRSD
T535 TTVSsPSTsLQRSDs
S536-p TVSsPSTsLQRSDss
S540 PSTsLQRSDssQPML
S542-p TsLQRSDssQPMLLR
S543-p sLQRSDssQPMLLRV
S585 VMEQLNNSFPSSRGH
- gap
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I616 ESLVSVMIDEEGAE_
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