EMIL1_HUMAN - dbPTM
EMIL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EMIL1_HUMAN
UniProt AC Q9Y6C2
Protein Name EMILIN-1
Gene Name EMILIN1
Organism Homo sapiens (Human).
Sequence Length 1016
Subcellular Localization Secreted, extracellular space, extracellular matrix . Found mainly at the interface between amorphous elastin and microfibrils.
Protein Description May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity..
Protein Sequence MAPRTLWSCYLCCLLTAAAGAASYPPRGFSLYTGSSGALSPGGPQAQIAPRPASRHRNWCAYVVTRTVSCVLEDGVETYVKYQPCAWGQPQCPQSIMYRRFLRPRYRVAYKTVTDMEWRCCQGYGGDDCAESPAPALGPASSTPRPLARPARPNLSGSSAGSPLSGLGGEGPGESEKVQQLEEQVQSLTKELQGLRGVLQGLSGRLAEDVQRAVETAFNGRQQPADAAARPGVHETLNEIQHQLQLLDTRVSTHDQELGHLNNHHGGSSSSGGSRAPAPASAPPGPSEELLRQLEQRLQESCSVCLAGLDGFRRQQQEDRERLRAMEKLLASVEERQRHLAGLAVGRRPPQECCSPELGRRLAELERRLDVVAGSVTVLSGRRGTELGGAAGQGGHPPGYTSLASRLSRLEDRFNSTLGPSEEQEESWPGAPGGLSHWLPAARGRLEQLGGLLANVSGELGGRLDLLEEQVAGAMQACGQLCSGAPGEQDSQVSEILSALERRVLDSEGQLRLVGSGLHTVEAAGEARQATLEGLQEVVGRLQDRVDAQDETAAEFTLRLNLTAARLGQLEGLLQAHGDEGCGACGGVQEELGRLRDGVERCSCPLLPPRGPGAGPGVGGPSRGPLDGFSVFGGSSGSALQALQGELSEVILSFSSLNDSLNELQTTVEGQGADLADLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQAGQCPSLEGRLGRLEGVCERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSLQLLEDRLHQLSLKDLTGPAGEAGPPGPPGLQGPPGPAGPPGSPGKDGQEGPIGPPGPQGEQGVEGAPAAPVPQVAFSAALSLPRSEPGTVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHRHEKVEAVLSRSNQGVARVDSGGYEPEGLENKPVAESQPSPGTLGVFSLILPLQAGDTVCVDLVMGQLAHSEEPLTIFSGALLYGDPELEHA
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
98PhosphorylationQCPQSIMYRRFLRPR
CCCHHHHHHHHHCCC		9.2927067055
154N-linked_GlycosylationLARPARPNLSGSSAG
CCCCCCCCCCCCCCC		41.09UniProtKB CARBOHYD
159O-linked_GlycosylationRPNLSGSSAGSPLSG
CCCCCCCCCCCCCCC		39.93OGP
203PhosphorylationRGVLQGLSGRLAEDV
HHHHHHHHHHHHHHH		28.7923911959
252PhosphorylationQLLDTRVSTHDQELG
HHHHHCCCCCHHHCC		19.4123312004
253PhosphorylationLLDTRVSTHDQELGH
HHHHCCCCCHHHCCC		26.9823312004
268PhosphorylationLNNHHGGSSSSGGSR
CCCCCCCCCCCCCCC		31.4723312004
269PhosphorylationNNHHGGSSSSGGSRA
CCCCCCCCCCCCCCC		31.6223312004
270PhosphorylationNHHGGSSSSGGSRAP
CCCCCCCCCCCCCCC		34.4023312004
271PhosphorylationHHGGSSSSGGSRAPA
CCCCCCCCCCCCCCC		49.4723312004
274O-linked_GlycosylationGSSSSGGSRAPAPAS
CCCCCCCCCCCCCCC		28.8855830337
274PhosphorylationGSSSSGGSRAPAPAS
CCCCCCCCCCCCCCC		28.8823312004
281O-linked_GlycosylationSRAPAPASAPPGPSE
CCCCCCCCCCCCCCH		40.00OGP
281PhosphorylationSRAPAPASAPPGPSE
CCCCCCCCCCCCCCH		40.0028060719
380PhosphorylationAGSVTVLSGRRGTEL
EECEEEEECCCCCCC		26.3924719451
385PhosphorylationVLSGRRGTELGGAAG
EEECCCCCCCCCCCC		26.6528857561
400PhosphorylationQGGHPPGYTSLASRL
CCCCCCCHHHHHHHH		10.0323312004
401PhosphorylationGGHPPGYTSLASRLS
CCCCCCHHHHHHHHH		24.1523312004
402PhosphorylationGHPPGYTSLASRLSR
CCCCCHHHHHHHHHH		17.2923312004
402O-linked_GlycosylationGHPPGYTSLASRLSR
CCCCCHHHHHHHHHH		17.29OGP
405PhosphorylationPGYTSLASRLSRLED
CCHHHHHHHHHHHHH		38.7623312004
415N-linked_GlycosylationSRLEDRFNSTLGPSE
HHHHHHHHCCCCCCH		34.6719159218
417O-linked_GlycosylationLEDRFNSTLGPSEEQ
HHHHHHCCCCCCHHH		36.52OGP
455N-linked_GlycosylationQLGGLLANVSGELGG
HHHHHHHHHCCCCCC		28.5816263699
483O-linked_GlycosylationQACGQLCSGAPGEQD
HHHHHHHCCCCCCCH		46.73OGP
507PhosphorylationLERRVLDSEGQLRLV
HHHHHCCCCCCEEEE		39.1922617229
557PhosphorylationDETAAEFTLRLNLTA
CCCHHHHHHHHHHHH		11.5024719451
561N-linked_GlycosylationAEFTLRLNLTAARLG
HHHHHHHHHHHHHHH		28.98UniProtKB CARBOHYD
622PhosphorylationGPGVGGPSRGPLDGF
CCCCCCCCCCCCCCC		53.82-
622O-linked_GlycosylationGPGVGGPSRGPLDGF
CCCCCCCCCCCCCCC		53.8272839795
658N-linked_GlycosylationILSFSSLNDSLNELQ
HHHHHHHHHHHHHHH		38.48UniProtKB CARBOHYD
697PhosphorylationNRLQQEATEHATESE
HHHHHHHHHHHCHHH		27.7923312004
701PhosphorylationQEATEHATESEERFR
HHHHHHHCHHHHHHC		41.7822985185
703PhosphorylationATEHATESEERFRGL
HHHHHCHHHHHHCCH		40.1626657352
766N-linked_GlycosylationWAGLRETNTTSQMQA
HHHHHHCCCCHHHHH		36.2817660510
794N-linked_GlycosylationGRRLGALNSSLQLLE
HHHHHHHHHHHHHHH		29.0817660510
795O-linked_GlycosylationRRLGALNSSLQLLED
HHHHHHHHHHHHHHH		33.0228657654
839PhosphorylationGPAGPPGSPGKDGQE
CCCCCCCCCCCCCCC		35.9328270605
878PhosphorylationVAFSAALSLPRSEPG
EEEHHHHCCCCCCCC		31.4424719451
934PhosphorylationEKVEAVLSRSNQGVA
HHHHHHHCCCCCCEE		27.36-
936PhosphorylationVEAVLSRSNQGVARV
HHHHHCCCCCCEEEE		30.08-
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 EMIL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EMIL1_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 EMIL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTMR9_HUMANMTMR9physical
16189514
EMIL1_HUMANEMILIN1physical
10821830
EMIL2_HUMANEMILIN2physical
11278945
DC1I1_HUMANDYNC1I1physical
17609108
DCTN2_HUMANDCTN2physical
17609108
CDC27_HUMANCDC27physical
17609108
NUMA1_HUMANNUMA1physical
17609108
FZR1_HUMANFZR1physical
17609108
CDC23_HUMANCDC23physical
17609108
MTMR9_HUMANMTMR9physical
19447967
EMIL1_HUMANEMILIN1physical
25416956
BEX3_HUMANNGFRAP1physical
25416956
MTMR9_HUMANMTMR9physical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
IFT20_HUMANIFT20physical
25416956
RIBC1_HUMANRIBC1physical
25416956
PLAC9_HUMANPLAC9physical
25416956
BEX5_HUMANBEX5physical
25416956
MTMR9_HUMANMTMR9physical
21516116
TAB2_HUMANTAB2physical
28514442
TAB3_HUMANTAB3physical
28514442
LIPA3_HUMANPPFIA3physical
28514442
UBXN1_HUMANUBXN1physical
28514442
CCD18_HUMANCCDC18physical
28514442
TAXB1_HUMANTAX1BP1physical
28514442
M3K7_HUMANMAP3K7physical
28514442
TAB1_HUMANTAB1physical
28514442
DDHD2_HUMANDDHD2physical
28514442
MET15_HUMANMETTL15physical
28514442
FBX28_HUMANFBXO28physical
28514442
HOME1_HUMANHOMER1physical
28514442
ODF2L_HUMANODF2Lphysical
28514442
RDH13_HUMANRDH13physical
28514442
SPC24_HUMANSPC24physical
28514442
WDCP_HUMANC2orf44physical
28514442
TRAF6_HUMANTRAF6physical
28514442
RRBP1_HUMANRRBP1physical
28514442
TNIP2_HUMANTNIP2physical
28514442
TRM61_HUMANTRMT61Aphysical
28514442
ARRB2_HUMANARRB2physical
28514442
CE170_HUMANCEP170physical
28514442
NFRKB_HUMANNFRKBphysical
28514442
LRIF1_HUMANLRIF1physical
28514442
SPAG5_HUMANSPAG5physical
28514442
ZMYM6_HUMANZMYM6physical
28514442
FBX46_HUMANFBXO46physical
28514442
IF4G1_HUMANEIF4G1physical
28514442
PAPD1_HUMANMTPAPphysical
28514442
ADRO_HUMANFDXRphysical
28514442
RL23_HUMANRPL23physical
28514442
DJC12_HUMANDNAJC12physical
28514442
NU214_HUMANNUP214physical
28514442
PDLI5_HUMANPDLIM5physical
28514442
RUSD3_HUMANRPUSD3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EMIL1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415; ASN-455; ASN-766 ANDASN-794, AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-455, AND MASSSPECTROMETRY.

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