ENAH_MOUSE - dbPTM
ENAH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENAH_MOUSE
UniProt AC Q03173
Protein Name Protein enabled homolog
Gene Name Enah
Organism Mus musculus (Mouse).
Sequence Length 802
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, filopodium. Cell junction, synapse. Cell junction, focal adhesion. Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at
Protein Description Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation..
Protein Sequence MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQEAAQSKVTATQDSTNLRCIFCGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERMERERLERERLERERLERERLEQEQLERQRQEREHVERLERERLERLERERQERERERLEQLEREQVEWERERRMSNAAPSSDSSLSSAPLPEYSSCQPPSAPPPSYAKVISAPVSDATPDYAVVTALPPTSTPPTPPLRHAATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPVNTPSSQPPAAKSCAWPTSNFSPLPPSPPIMISSPPGKATGPRPVLPVCVSSPVPQMPPSPTAPNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPLPPPPLPPLASLSHCGSQASPPPGTPLASTPSSKPSVLPSPSAGAPASAETPLNPELGDSSASEPGLQAASQPAESPTPQGLVLGPPAPPPPPPLPSGPAYASALPPPPGPPPPPPLPSTGPPPPPPPPPPLPNQAPPPPPPPPAPPLPASGIFSGSTSEDNRPLTGLAAAIAGAKLRKVSRVEDGSFPGGGNTGSVSLASSKADAGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDRNEDAEPITAKAPSTSTPEPTRKPWERTNTMNGSKSPVISRPKSTPSSQPSANGVQTEGLDYDRLKQDILDEMRKELAKLKEELIDAIRQELSKSNTA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
69UbiquitinationCAIPKGLKYNQATQT
EEECCCCCCCHHHCC		51.31-
125 (in isoform 6)Phosphorylation-39.9529514104
125 (in isoform 3)Phosphorylation-39.9529514104
125 (in isoform 4)Phosphorylation-39.9529514104
144PhosphorylationPTLPRQNSQLPAQVQ
CCCCCCCCCCCHHHH		25.4225521595
255PhosphorylationWERERRMSNAAPSSD
HHHHHHHHCCCCCCC		22.8526643407
260PhosphorylationRMSNAAPSSDSSLSS
HHHCCCCCCCCCCCC		41.8926643407
261PhosphorylationMSNAAPSSDSSLSSA
HHCCCCCCCCCCCCC		40.2226643407
263PhosphorylationNAAPSSDSSLSSAPL
CCCCCCCCCCCCCCC		34.8226643407
264PhosphorylationAAPSSDSSLSSAPLP
CCCCCCCCCCCCCCC		36.9426643407
266PhosphorylationPSSDSSLSSAPLPEY
CCCCCCCCCCCCCCC		26.8026643407
292 (in isoform 3)O-linked_Glycosylation-9.4422517741
293 (in isoform 4)O-linked_Glycosylation-21.2522517741
310PhosphorylationVVTALPPTSTPPTPP
EEEECCCCCCCCCCC		43.2026643407
311PhosphorylationVTALPPTSTPPTPPL
EEECCCCCCCCCCCH		44.6926643407
312PhosphorylationTALPPTSTPPTPPLR
EECCCCCCCCCCCHH		35.4526643407
315PhosphorylationPPTSTPPTPPLRHAA
CCCCCCCCCCHHHHH		38.4529899451
327PhosphorylationHAATRFATSLGSAFH
HHHHHHHHHHHHHHC		23.05-
328PhosphorylationAATRFATSLGSAFHP
HHHHHHHHHHHHHCC		27.57-
351PhosphorylationPRPLNKNSRPSSPVN
CCCCCCCCCCCCCCC		47.3725521595
354PhosphorylationLNKNSRPSSPVNTPS
CCCCCCCCCCCCCCC		46.2825521595
355PhosphorylationNKNSRPSSPVNTPSS
CCCCCCCCCCCCCCC		35.2325521595
359PhosphorylationRPSSPVNTPSSQPPA
CCCCCCCCCCCCCCC		25.4525521595
361PhosphorylationSSPVNTPSSQPPAAK
CCCCCCCCCCCCCHH		39.3024925903
362PhosphorylationSPVNTPSSQPPAAKS
CCCCCCCCCCCCHHC		48.1624925903
362O-linked_GlycosylationSPVNTPSSQPPAAKS
CCCCCCCCCCCCHHC		48.1622517741
374PhosphorylationAKSCAWPTSNFSPLP
HHCCCCCCCCCCCCC		26.1226643407
375PhosphorylationKSCAWPTSNFSPLPP
HCCCCCCCCCCCCCC		31.6226643407
378PhosphorylationAWPTSNFSPLPPSPP
CCCCCCCCCCCCCCC		29.7626643407
383PhosphorylationNFSPLPPSPPIMISS
CCCCCCCCCCEEEEC		41.1726643407
389PhosphorylationPSPPIMISSPPGKAT
CCCCEEEECCCCCCC		21.2926643407
390PhosphorylationSPPIMISSPPGKATG
CCCEEEECCCCCCCC		24.9626643407
557PhosphorylationPLPSGPAYASALPPP
CCCCCCCCCCCCCCC		12.2912672821
637PhosphorylationGAKLRKVSRVEDGSF
HCEECEEEEECCCCC		33.3725521595
643PhosphorylationVSRVEDGSFPGGGNT
EEEECCCCCCCCCCC		40.3626239621
650PhosphorylationSFPGGGNTGSVSLAS
CCCCCCCCCCEEEEC		33.8225266776
652PhosphorylationPGGGNTGSVSLASSK
CCCCCCCCEEEECCC		13.3926643407
654PhosphorylationGGNTGSVSLASSKAD
CCCCCCEEEECCCCC		21.6626643407
664MethylationSSKADAGRGNGPLPL
CCCCCCCCCCCCCCC		36.80-
695PhosphorylationRRIAEKGSTIETEQK
HHHHHHCCCCHHHCC		36.9626239621
696PhosphorylationRIAEKGSTIETEQKE
HHHHHCCCCHHHCCC		31.3426824392
699PhosphorylationEKGSTIETEQKEDRN
HHCCCCHHHCCCCCC		39.6126643407
701 (in isoform 4)O-linked_Glycosylation-62.9522517741
702 (in isoform 4)O-linked_Glycosylation-56.1822517741
718PhosphorylationPITAKAPSTSTPEPT
CCCCCCCCCCCCCCC		39.5926239621
719PhosphorylationITAKAPSTSTPEPTR
CCCCCCCCCCCCCCC		35.2423737553
720PhosphorylationTAKAPSTSTPEPTRK
CCCCCCCCCCCCCCC		46.4323737553
721PhosphorylationAKAPSTSTPEPTRKP
CCCCCCCCCCCCCCC		31.5925521595
725PhosphorylationSTSTPEPTRKPWERT
CCCCCCCCCCCCCCC		50.0628066266
732PhosphorylationTRKPWERTNTMNGSK
CCCCCCCCCCCCCCC		24.4324759943
734PhosphorylationKPWERTNTMNGSKSP
CCCCCCCCCCCCCCC		16.0527742792
738PhosphorylationRTNTMNGSKSPVISR
CCCCCCCCCCCCCCC		25.5927742792
740PhosphorylationNTMNGSKSPVISRPK
CCCCCCCCCCCCCCC		26.5425521595
744PhosphorylationGSKSPVISRPKSTPS
CCCCCCCCCCCCCCC		42.6426745281
748PhosphorylationPVISRPKSTPSSQPS
CCCCCCCCCCCCCCC		48.5127087446
749PhosphorylationVISRPKSTPSSQPSA
CCCCCCCCCCCCCCC		33.0627087446
751PhosphorylationSRPKSTPSSQPSANG
CCCCCCCCCCCCCCC		41.5125293948
752PhosphorylationRPKSTPSSQPSANGV
CCCCCCCCCCCCCCC		47.5225293948
755PhosphorylationSTPSSQPSANGVQTE
CCCCCCCCCCCCCCC		27.0825293948
785AcetylationRKELAKLKEELIDAI
HHHHHHHHHHHHHHH		48.7322826441
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
236SPhosphorylationKinasePRKCAP17252
GPS
255SPhosphorylationKinasePKA-FAMILY-GPS
255SPhosphorylationKinasePKA-Uniprot
296YPhosphorylationKinaseABL1P00520
GPS
296YPhosphorylationKinaseABL-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
255SPhosphorylation

12134088
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ENAH_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABL1_MOUSEAbl1physical
8861907
SRC_MOUSESrcphysical
8861907
FYN_MOUSEFynphysical
8861907
ZYX_MOUSEZyxphysical
8861907
VINC_MOUSEVclphysical
8861907
PROF1_MOUSEPfn1physical
8861907
TRIM9_MOUSETrim9physical
26702829
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENAH_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Critical role of Ena/VASP proteins for filopodia formation in neuronsand in function downstream of netrin-1.";
Lebrand C., Dent E.W., Strasser G.A., Lanier L.M., Krause M.,Svitkina T.M., Borisy G.G., Gertler F.B.;
Neuron 42:37-49(2004).
Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-255.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND MASSSPECTROMETRY.
"Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalianenabled (Mena) by c-Abl kinase.";
Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,Shishido T.;
J. Biol. Chem. 278:21685-21692(2003).
Cited for: ALTERNATIVE SPLICING (ISOFORM 6), PHOSPHORYLATION AT TYR-557, ANDINTERACTION WITH ABI1.

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