ELN_HUMAN - dbPTM
ELN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELN_HUMAN
UniProt AC P15502
Protein Name Elastin
Gene Name ELN
Organism Homo sapiens (Human).
Sequence Length 786
Subcellular Localization Secreted, extracellular space, extracellular matrix . Extracellular matrix of elastic fibers.
Protein Description Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity)..
Protein Sequence MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGPGGKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAAYKAAKAGAGLGGVPGVGGLGVSAGAVVPQPGAGVKPGKVPGVGLPGVYPGGVLPGARFPGVGVLPGVPTGAGVKPKAPGVGGAFAGIPGVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQAAAAAAAKAAAKFGAGAAGVLPGVGGAGVPGVPGAIPGIGGIAGVGTPAAAAAAAAAAKAAKYGAAAGLVPGGPGFGPGVVGVPGAGVPGVGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKAAAKAAKYGARPGVGVGGIPTYGVGAGGFPGFGVGVGGIPGVAGVPGVGGVPGVGGVPGVGISPEAQAAAAAKAAKYGAAGAGVLGGLVPGPQAAVPGVPGTGGVPGVGTPAAAAAKAAAKAAQFGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVGAGVPGLGVGAGVPGFGAGADEGVRRSLSPELREGDPSSSQHLPSTPSSPRVPGALAAAKAAKYGAAVPGVLGGLGALGGVGIPGGVVGAGPAAAAAAAKAAAKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAAAAKAAKYGAAGLGGVLGGAGQFPLGGVAARPGFGLSPIFPGGACLGKACGRKRK
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
34HydroxylationGGVPGAIPGGVPGGV
CCCCCCCCCCCCCCC		32.7116161116
65HydroxylationPGGKPLKPVPGGLAG
CCCCCCCCCCCCCCC		45.2616078697
67HydroxylationGKPLKPVPGGLAGAG
CCCCCCCCCCCCCCC		39.3916078697
86O-linked_GlycosylationLGAFPAVTFPGALVP
CCCCCCCCCCCCCCC		26.64OGP
88HydroxylationAFPAVTFPGALVPGG
CCCCCCCCCCCCCCC		20.1316078697
104AllysineADAAAAYKAAKAGAG
HHHHHHHHHHHCCCC		36.82-
104DeaminationADAAAAYKAAKAGAG
HHHHHHHHHHHCCCC		36.82-
107DeaminationAAAYKAAKAGAGLGG
HHHHHHHHCCCCCCC		52.81-
116HydroxylationGAGLGGVPGVGGLGV
CCCCCCCCCCCCCCC		34.7216078697
156HydroxylationVYPGGVLPGARFPGV
CCCCCCCCCCCCCCC		31.8016078697
167HydroxylationFPGVGVLPGVPTGAG
CCCCCCCCCCCCCCC		39.0516161116
170HydroxylationVGVLPGVPTGAGVKP
CCCCCCCCCCCCCCC		30.9116161116
177HydroxylationPTGAGVKPKAPGVGG
CCCCCCCCCCCCCCC		35.3216078697
190HydroxylationGGAFAGIPGVGPFGG
CCCCCCCCCCCCCCC		30.4216161116
206PhosphorylationQPGVPLGYPIKAPKL
CCCCCCCCCCCCCCC		14.96-
241DeaminationGVAGAAGKAGYPTGT
CCCCCCCCCCCCCCC		33.63-
241AllysineGVAGAAGKAGYPTGT
CCCCCCCCCCCCCCC		33.63-
241AcetylationGVAGAAGKAGYPTGT
CCCCCCCCCCCCCCC		33.6319806569
261DeaminationAAAAAAAKAAAKFGA
HHHHHHHHHHHHHCC		33.56-
261AllysineAAAAAAAKAAAKFGA
HHHHHHHHHHHHHCC		33.56-
265DeaminationAAAKAAAKFGAGAAG
HHHHHHHHHCCCHHC		39.34-
265AllysineAAAKAAAKFGAGAAG
HHHHHHHHHCCCHHC		39.34-
283HydroxylationGVGGAGVPGVPGAIP
CCCCCCCCCCCCCCC		36.8316161116
286HydroxylationGAGVPGVPGAIPGIG
CCCCCCCCCCCCCCC		32.2016161116
290HydroxylationPGVPGAIPGIGGIAG
CCCCCCCCCCCCCCC		28.0216078697
300O-linked_GlycosylationGGIAGVGTPAAAAAA
CCCCCCCCHHHHHHH		13.83OGP
312AllysineAAAAAAAKAAKYGAA
HHHHHHHHHHHHCHH		44.12-
312DeaminationAAAAAAAKAAKYGAA
HHHHHHHHHHHHCHH		44.12-
315AllysineAAAAKAAKYGAAAGL
HHHHHHHHHCHHCCC		49.42-
315DeaminationAAAAKAAKYGAAAGL
HHHHHHHHHCHHCCC		49.42-
327HydroxylationAGLVPGGPGFGPGVV
CCCCCCCCCCCCCCC		40.6316161116
342HydroxylationGVPGAGVPGVGVPGA
CCCCCCCCCCCCCCC		30.7316161116
347HydroxylationGVPGVGVPGAGIPVV
CCCCCCCCCCCCCCC		22.4616161116
352HydroxylationGVPGAGIPVVPGAGI
CCCCCCCCCCCCCCC		21.8216161116
355HydroxylationGAGIPVVPGAGIPGA
CCCCCCCCCCCCCCC		27.4416161116
360HydroxylationVVPGAGIPGAAVPGV
CCCCCCCCCCCCCCC		26.0016161116
375AllysineVSPEAAAKAAAKAAK
CCHHHHHHHHHHHHH		33.56-
375DeaminationVSPEAAAKAAAKAAK
CCHHHHHHHHHHHHH		33.56-
379DeaminationAAAKAAAKAAKYGAR
HHHHHHHHHHHHCCC		44.12-
379AllysineAAAKAAAKAAKYGAR
HHHHHHHHHHHHCCC		44.12-
382DeaminationKAAAKAAKYGARPGV
HHHHHHHHHCCCCCC		49.42-
382AllysineKAAAKAAKYGARPGV
HHHHHHHHHCCCCCC		49.42-
415HydroxylationGVGVGGIPGVAGVPG
CCCCCCCCCCCCCCC		34.1816078697
421HydroxylationIPGVAGVPGVGGVPG
CCCCCCCCCCCCCCC		30.7316161116
427HydroxylationVPGVGGVPGVGGVPG
CCCCCCCCCCCCCCC		34.7216161116
448DeaminationAQAAAAAKAAKYGAA
HHHHHHHHHHHHCCC		44.12-
451DeaminationAAAAKAAKYGAAGAG
HHHHHHHHHCCCCCC		49.42-
451AllysineAAAAKAAKYGAAGAG
HHHHHHHHHCCCCCC		49.42-
465HydroxylationGVLGGLVPGPQAAVP
CCCCCCCCCCCCCCC		54.5116078697
467HydroxylationLGGLVPGPQAAVPGV
CCCCCCCCCCCCCCC		17.9916078697
481HydroxylationVPGTGGVPGVGTPAA
CCCCCCCCCCCCHHH		34.7216078697
492AllysineTPAAAAAKAAAKAAQ
CHHHHHHHHHHHHHH		33.56-
492DeaminationTPAAAAAKAAAKAAQ
CHHHHHHHHHHHHHH		33.56-
496AllysineAAAKAAAKAAQFGLV
HHHHHHHHHHHHCCC		39.26-
496DeaminationAAAKAAAKAAQFGLV
HHHHHHHHHHHHCCC		39.26-
522HydroxylationAPGVGVAPGVGLAPG
CCCCCCCCCCCCCCC		35.2816078697
550HydroxylationGVAPGIGPGGVAAAA
CCCCCCCHHHHHHHH		34.1516161116
558AllysineGGVAAAAKSAAKVAA
HHHHHHHHHHHHHHH		35.58-
558DeaminationGGVAAAAKSAAKVAA
HHHHHHHHHHHHHHH		35.58-
562AllysineAAAKSAAKVAAKAQL
HHHHHHHHHHHHHHH		31.93-
562DeaminationAAAKSAAKVAAKAQL
HHHHHHHHHHHHHHH		31.93-
566AllysineSAAKVAAKAQLRAAA
HHHHHHHHHHHHHHH		27.25-
566DeaminationSAAKVAAKAQLRAAA
HHHHHHHHHHHHHHH		27.25-
580HydroxylationAGLGAGIPGLGVGVG
HCCCCCCCCCCCCCC		30.9116161116
589HydroxylationLGVGVGVPGLGVGAG
CCCCCCCCCCCCCCC		26.7716161116
598HydroxylationLGVGAGVPGLGVGAG
CCCCCCCCCCCCCCC		31.2316161116
607HydroxylationLGVGAGVPGFGAGAD
CCCCCCCCCCCCCCC		31.3216078697
631PhosphorylationELREGDPSSSQHLPS
HHHCCCCCCCCCCCC		47.57-
641PhosphorylationQHLPSTPSSPRVPGA
CCCCCCCCCCCCCHH		53.73-
646HydroxylationTPSSPRVPGALAAAK
CCCCCCCCHHHHHHH		24.5016078697
653AllysinePGALAAAKAAKYGAA
CHHHHHHHHHHHCCC		44.12-
653DeaminationPGALAAAKAAKYGAA
CHHHHHHHHHHHCCC		44.12-
656AllysineLAAAKAAKYGAAVPG
HHHHHHHHHCCCCCC		49.42-
656DeaminationLAAAKAAKYGAAVPG
HHHHHHHHHCCCCCC		49.42-
677HydroxylationALGGVGIPGGVVGAG
HHCCCCCCCCCCCHH		27.7916161116
693AllysineAAAAAAAKAAAKAAQ
HHHHHHHHHHHHHHH		33.56-
693DeaminationAAAAAAAKAAAKAAQ
HHHHHHHHHHHHHHH		33.56-
697DeaminationAAAKAAAKAAQFGLV
HHHHHHHHHHHHCCC		39.26-
697AllysineAAAKAAAKAAQFGLV
HHHHHHHHHHHHCCC		39.26-
735DeaminationIPPAAAAKAAKYGAA
CCHHHHHHHHHHCCC		44.12-
735AllysineIPPAAAAKAAKYGAA
CCHHHHHHHHHHCCC		44.12-
738AllysineAAAAKAAKYGAAGLG
HHHHHHHHHCCCCCC		49.42-
738DeaminationAAAAKAAKYGAAGLG
HHHHHHHHHCCCCCC		49.42-
769HydroxylationRPGFGLSPIFPGGAC
CCCCCCCCCCCCCCH		36.9616078697
772HydroxylationFGLSPIFPGGACLGK
CCCCCCCCCCCHHHH		40.8216078697
784AcetylationLGKACGRKRK-----
HHHHHCCCCC-----		50.237704171
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

Oops, there are no upstream regulatory protein records of ELN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELN_HUMAN !!
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 ELN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGS1_HUMANBGNphysical
11723132
PGS2_HUMANDCNphysical
11723132
FBN1_HUMANFBN1physical
10825173
FBN2_HUMANFBN2physical
10825173
FBLN1_HUMANFBLN1physical
10544250
FBLN2_HUMANFBLN2physical
10544250
NID2_HUMANNID2physical
10544250
CLUS_HUMANCLUphysical
17872975
MAGH1_HUMANMAGEH1physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
123700Cutis laxa, autosomal dominant, 1 (ADCL1)
185500Supravalvular aortic stenosis (SVAS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELN_HUMAN

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Related Literatures of Post-Translational Modification
Hydroxylation
ReferencePubMed
"Characterization of peptides resulting from digestion of human skinelastin with elastase.";
Getie M., Schmelzer C.E.H., Neubert R.H.H.;
Proteins 61:649-657(2005).
Cited for: HYDROXYLATION AT PRO-34; PRO-167; PRO-170; PRO-190; PRO-283; PRO-286;PRO-327; PRO-342; PRO-347; PRO-352; PRO-355; PRO-360; PRO-421;PRO-427; PRO-550; PRO-580; PRO-589; PRO-598 AND PRO-677, AND MASSSPECTROMETRY.
"Mass spectrometric characterization of human skin elastin peptidesproduced by proteolytic digestion with pepsin and thermitase.";
Schmelzer C.E.H., Getie M., Neubert R.H.H.;
J. Chromatogr. A 1083:120-126(2005).
Cited for: HYDROXYLATION AT PRO-65; PRO-67; PRO-88; PRO-116; PRO-156; PRO-177;PRO-190; PRO-286; PRO-290; PRO-415; PRO-427; PRO-465; PRO-467;PRO-481; PRO-522; PRO-580; PRO-607; PRO-646; PRO-677; PRO-769 ANDPRO-772, AND MASS SPECTROMETRY.

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