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Protein Page:
emerin (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
emerin a single pass membrane protein that spans the inner nuclear membrane. A serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It interacts with lamins A and C, and mediates membrane anchorage to the cytoskeleton. Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through an exportin 1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Colocalized with BAF at the central region of the assembling nuclear rim, near spindle-attachment sites. Hyper-phosphorylated on tyrosine in cells overexpressing HER2. Directly phosphorylated by Src and Abl. Phosphorylated by Src at Y59, Y74 and Y95. May function as a downstream effector and signal integrator for tyrosine kinase signaling pathways at the nuclear envelope. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Cytoskeletal protein
Cellular Component: microtubule; nuclear outer membrane; integral to membrane; nuclear inner membrane; nuclear envelope
Molecular Function: protein binding; beta-tubulin binding; actin binding
Biological Process: positive regulation of protein export from nucleus; mitotic nuclear envelope reassembly; muscle development; muscle contraction; negative regulation of fibroblast proliferation; mitotic nuclear envelope disassembly; mitotic cell cycle
Reference #:  P50402 (UniProtKB)
Alt. Names/Synonyms: EDMD; EMD; Emerin; LEM domain containing 5; LEMD5; STA
Gene Symbols: EMD
Molecular weight: 28,994 Da
Basal Isoelectric point: 5.29  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

emerin

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: Y4‑p, Y19‑p, Y34‑p, Y161‑p, S175‑p

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

 
1 2 Y4-p ____MDNyADLsDtE
0 6 S8-p MDNyADLsDtELTTL
0 2 T10-p NyADLsDtELTTLLR
1 0 Y19-p LTTLLRRyNIPHGPV
0 3 S29-p PHGPVVGsTRRLyEK
1 0 Y34-p VGsTRRLyEKKIFEy
0 1 K37 TRRLyEKKIFEyETQ
1 75 Y41-p yEKKIFEyETQRRRL
1 24 S49-p ETQRRRLsPPsssAA
0 3 S52-p RRRLsPPsssAAsSy
0 3 S53-p RRLsPPsssAAsSys
1 0 S53-gl RRLsPPsssAAsSys
0 7 S54-p RLsPPsssAAsSysF
1 0 S54-gl RLsPPsssAAsSysF
0 4 S57-p PPsssAAsSysFsDL
1 32 Y59-p sssAAsSysFsDLNs
0 39 S60-p ssAAsSysFsDLNst
0 3 S62-p AAsSysFsDLNstRG
0 1 S66-p ysFsDLNstRGDADM
0 1 T67-p sFsDLNstRGDADMy
0 1 R68 FsDLNstRGDADMyD
1 128 Y74-p tRGDADMyDLPKkED
0 6 K79-u DMyDLPKkEDALLyQ
1 136 Y85-p KkEDALLyQskGyND
0 17 S87-p EDALLyQskGyNDDy
1 0 S87-gl EDALLyQskGyNDDy
0 12 K88-u DALLyQskGyNDDyy
1 31 Y90-p LLyQskGyNDDyyEE
1 317 Y94-p skGyNDDyyEEsyFt
1 158 Y95-p kGyNDDyyEEsyFtT
0 9 S98-p NDDyyEEsyFtTRty
1 171 Y99-p DDyyEEsyFtTRtyG
0 9 T101-p yyEEsyFtTRtyGEP
0 2 R103 EEsyFtTRtyGEPEs
0 10 T104-p EsyFtTRtyGEPEsA
1 88 Y105-p syFtTRtyGEPEsAG
0 4 S110-p RtyGEPEsAGPSRAV
0 8 R115 PEsAGPSRAVRQsVT
0 2 A116 EsAGPSRAVRQsVTS
0 3 S120-p PSRAVRQsVTSFPDA
0 4 S141-p VHDDDLLsssEEECK
0 8 S142-p HDDDLLsssEEECKD
0 4 S143-p DDDLLsssEEECKDR
1 1 Y155-p KDRERPMyGRDsAyQ
0 3 S159-p RPMyGRDsAyQsItH
1 229 Y161-p MyGRDsAyQsItHyR
0 7 S163-p GRDsAyQsItHyRPV
0 13 T165-p DsAyQsItHyRPVsA
1 151 Y167-p AyQsItHyRPVsAsR
0 15 S171-p ItHyRPVsAsRsSLD
1 0 S171-gl ItHyRPVsAsRsSLD
0 8 S173-p HyRPVsAsRsSLDLs
1 0 S173-gl HyRPVsAsRsSLDLs
1 3 S175-p RPVsAsRsSLDLsyy
0 3 S180-p sRsSLDLsyyPTSSS
1 13 Y181-p RsSLDLsyyPTSSST
1 0 Y182-p sSLDLsyyPTSSSTS
  mouse

 
Y4 ____MDDYAVLSDTE
S8 MDDYAVLSDTELAAV
T10 DYAVLSDTELAAVLR
Y19 LAAVLRQYNIPHGPI
S29-p PHGPIVGsTRKLYEK
Y34 VGsTRKLYEKkIFEY
K37-u TRKLYEKkIFEYETQ
Y41 YEKkIFEYETQRRRL
L49 ETQRRRLLPPNSSSS
S53 RRLLPPNSSSSSFSY
S54 RLLPPNSSSSSFSYQ
S54 RLLPPNSSSSSFSYQ
S55 LLPPNSSSSSFSYQF
S55 LLPPNSSSSSFSYQF
S57 PPNSSSSSFSYQFSD
Y60 SSSSSFSYQFSDLDS
Q61 SSSSFSYQFSDLDSA
S63 SSFSYQFSDLDSAAV
S67 YQFSDLDSAAVDSDM
A68 QFSDLDSAAVDSDMy
A69 FSDLDSAAVDSDMyD
Y75-p AAVDSDMyDLPKkED
K80-u DMyDLPKkEDALLyQ
Y86-p KkEDALLyQskDYND
S88-p EDALLyQskDYNDDy
S88 EDALLyQSkDYNDDy
K89-u DALLyQskDYNDDyy
Y91 LLyQskDYNDDyyEE
Y95-p skDYNDDyyEESYLT
Y96-p kDYNDDyyEESYLTT
S99 NDDyyEESYLTTkty
Y100 DDyyEESYLTTktyG
T102 yyEESYLTTktyGEP
K104-u EESYLTTktyGEPES
T105-p ESYLTTktyGEPESV
Y106-p SYLTTktyGEPESVG
S111 ktyGEPESVGMSksF
K116-u PESVGMSksFRQPGT
S117-p ESVGMSksFRQPGTS
P121 MSksFRQPGTSLVDA
S141-p QVRDDIFssLEEEGK
S142-p VRDDIFssLEEEGKD
L143 RDDIFssLEEEGKDR
Y155-p KDRERLIyGQDsAyQ
S159-p RLIyGQDsAyQSIAH
Y161-p IyGQDsAyQSIAHyR
S163 GQDsAyQSIAHyRPI
A165 DsAyQSIAHyRPISN
Y167-p AyQSIAHyRPISNVS
S171 IAHyRPISNVSRsSL
S171 IAHyRPISNVSRsSL
S174 yRPISNVSRsSLGLs
S174 yRPISNVSRsSLGLs
S176-p PISNVSRsSLGLsYY
S181-p SRsSLGLsYYPTSST
Y182 RsSLGLsYYPTSSTS
Y183 sSLGLsYYPTSSTSS
  rat

 
Y4 ____MDDYAVLSDTE
S8 MDDYAVLSDTELAAV
T10 DYAVLSDTELAAVLR
Y19 LAAVLRQYNIPHGPI
S29 PHGPILGSTRKLYEK
Y34 LGSTRKLYEKKIFEY
K37 TRKLYEKKIFEYETQ
Y41 YEKKIFEYETQRRRL
S49 ETQRRRLSPPSSSSS
S52 RRRLSPPSSSSSSFS
S53 RRLSPPSSSSSSFSY
S53 RRLSPPSSSSSSFSY
S54 RLSPPSSSSSSFSYR
S54 RLSPPSSSSSSFSYR
S57 PPSSSSSSFSYRFSD
Y60 SSSSSFSYRFSDLDS
R61 SSSSFSYRFSDLDSA
S63 SSFSYRFSDLDSAsV
S67 YRFSDLDSAsVDSDM
A68 RFSDLDSAsVDSDMY
S69-p FSDLDSAsVDSDMYD
Y75 AsVDSDMYDLPKKED
K80 DMYDLPKKEDALLYQ
Y86 KKEDALLYQSKDYND
S88 EDALLYQSKDYNDDY
S88 EDALLYQSKDYNDDY
K89 DALLYQSKDYNDDYY
Y91 LLYQSKDYNDDYYEE
Y95 SKDYNDDYYEESYLT
Y96 KDYNDDYYEESYLTT
S99 NDDYYEESYLTTRTY
Y100 DDYYEESYLTTRTYG
T102 YYEESYLTTRTYGEP
R104 EESYLTTRTYGEPES
T105 ESYLTTRTYGEPESV
Y106 SYLTTRTYGEPESVG
S111 RTYGEPESVGMSKSF
K116 PESVGMSKSFRRPGT
S117 ESVGMSKSFRRPGTS
P121 MSKSFRRPGTSLVDA
S142 QVRDDIFSSSEEEGK
S143 VRDDIFSSSEEEGKD
S144 RDDIFSSSEEEGKDR
Y156 KDRERPIYGRDSAYQ
S160 RPIYGRDSAYQSIAE
Y162 IYGRDSAYQSIAEYR
S164 GRDSAYQSIAEYRPI
A166 DSAYQSIAEYRPISN
Y168 AYQSIAEYRPISNVS
S172 IAEYRPISNVSRSSL
S172 IAEYRPISNVSRSSL
S175 YRPISNVSRSSLGLS
S175 YRPISNVSRSSLGLS
S177 PISNVSRSSLGLSYY
S182 SRSSLGLSYYPRSST
Y183 RSSLGLSYYPRSSTS
Y184 SSLGLSYYPRSSTSS
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