EMIL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EMIL2_HUMAN
• UniProt AC: Q9BXX0
• Protein Name: EMILIN-2
• Gene Name: EMILIN2
• Organism: Homo sapiens (Human).
• Sequence Length: 1053
• 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: MWQPRRPWPRVPWRWALALLALVGAGLCHAGPQPGYPARPSARNKNWCAYIVNKNVSCSVLEGSESFIQAQYNCAWNQMPCPSALVYRVNFRPRYVTRYKTVTQLEWRCCPGFRGGDCQEGPKDPVKTLRPTPARPRNSLKKATDNEPSQFSEPRKTLSPTGTAQPSWGVDPKEGPQELQEKKIQVLEEKVLRLTRTVLDLQSSLAGVSENLKHATQDDASRTRAPGLSSQHPKPDTTVSGDTETGQSPGVFNTKESGMKDIKSELAEVKDTLKNKSDKLEELDGKVKGYEGQLRQLQEAAQGPTVTMTTNELYQAYVDSKIDALREELMEGMDRKLADLKNSCEYKLTGLQQQCDDYGSSYLGVIELIGEKETSLRKEINNLRARLQEPSAQANCCDSEKNGDIGQQIKTLDQKIERVAEATRMLNGRLDNEFDRLIVPEPDVDFDAKWNELDARINVTEKNAEEHCFYIEETLRGAINGEVGDLKQLVDQKIQSLEDRLGSVLLQMTNNTGAELSPPGAAALPGVSGSGDERVMMELNHLKDKVQVVEDICLLNIQGKPHGMEGALPNREDRAVRDSLHLLKSLNDTMHRKFQETEQTIQKLQQDFSFLYSQLNHTENDVTHLQKEMSNCRAGENAGMGRFTKVGEQERTVDTLPSPQHPVAHCCSQLEERWQRLQSQVISELDACKECTQGVQREVSMVEGRVSHMEKTCSKLDSISGNLQRIKEGLNKHVSSLWNCVRQMNGTLRSHSRDISGLKNSVQQFYSHVFQISTDLQDLVKFQPSAKAPSPPPPAEAPKEPLQPEPAPPRPSGPATAEDPGRRPVLPQRPPEERPPQPPGSTGVIAETGQAGPPAGAGVSGRGLPRGVDGQTGSGTVPGAEGFAGAPGYPKSPPVASPGAPVPSLVSFSAGLTQKPFPSDGGVVLFNKVLVNDGDVYNPSTGVFTAPYDGRYLITATLTPERDAYVEAVLSVSNASVAQLHTAGYRREFLEYHRPPGALHTCGGPGAFHLIVHLKAGDAVNVVVTGGKLAHTDFDEMYSTFSGVFLYPFLSHL

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
55	N-linked_Glycosylation	CAYIVNKNVSCSVLE EEEEECCCCCEEEEE	26.23	UniProtKB CARBOHYD
144	O-linked_Glycosylation	RNSLKKATDNEPSQF CCCCCCCCCCCCCCC	48.51	55832075
152	Phosphorylation	DNEPSQFSEPRKTLS CCCCCCCCCCCCCCC	38.77	19060867
157	Phosphorylation	QFSEPRKTLSPTGTA CCCCCCCCCCCCCCC	33.47	-
159	Phosphorylation	SEPRKTLSPTGTAQP CCCCCCCCCCCCCCC	26.16	-
159	O-linked_Glycosylation	SEPRKTLSPTGTAQP CCCCCCCCCCCCCCC	26.16	46204943
161	O-linked_Glycosylation	PRKTLSPTGTAQPSW CCCCCCCCCCCCCCC	43.73	46204955
161	Phosphorylation	PRKTLSPTGTAQPSW CCCCCCCCCCCCCCC	43.73	25954137
163	Phosphorylation	KTLSPTGTAQPSWGV CCCCCCCCCCCCCCC	25.29	25954137
163	O-linked_Glycosylation	KTLSPTGTAQPSWGV CCCCCCCCCCCCCCC	25.29	55827695
167	Phosphorylation	PTGTAQPSWGVDPKE CCCCCCCCCCCCCCC	25.12	25954137
223	O-linked_Glycosylation	TQDDASRTRAPGLSS CCCHHHHCCCCCCCC	28.78	55829623
238	O-linked_Glycosylation	QHPKPDTTVSGDTET CCCCCCCCCCCCCCC	21.76	55824443
245	O-linked_Glycosylation	TVSGDTETGQSPGVF CCCCCCCCCCCCCCC	42.48	OGP
248	O-linked_Glycosylation	GDTETGQSPGVFNTK CCCCCCCCCCCCCCC	25.60	OGP
275	N-linked_Glycosylation	EVKDTLKNKSDKLEE HHHHHHCCCHHHHHH	52.77	UniProtKB CARBOHYD
305	O-linked_Glycosylation	QEAAQGPTVTMTTNE HHHHCCCEEEEEHHH	35.12	OGP
307	O-linked_Glycosylation	AAQGPTVTMTTNELY HHCCCEEEEEHHHHH	15.98	OGP
309	O-linked_Glycosylation	QGPTVTMTTNELYQA CCCEEEEEHHHHHHH	19.66	OGP
310	O-linked_Glycosylation	GPTVTMTTNELYQAY CCEEEEEHHHHHHHH	18.84	OGP
458	N-linked_Glycosylation	NELDARINVTEKNAE HHHHEEEECCCCCHH	29.16	UniProtKB CARBOHYD
510	N-linked_Glycosylation	SVLLQMTNNTGAELS HHHHHHCCCCCCCCC	38.43	UniProtKB CARBOHYD
517	Phosphorylation	NNTGAELSPPGAAAL CCCCCCCCCCCCCCC	22.13	-
530	Phosphorylation	ALPGVSGSGDERVMM CCCCCCCCCCHHHHH	35.25	-
579	Phosphorylation	EDRAVRDSLHLLKSL HHHHHHHHHHHHHHC	13.71	24719451
587	N-linked_Glycosylation	LHLLKSLNDTMHRKF HHHHHHCHHHHHHHH	50.20	UniProtKB CARBOHYD
616	N-linked_Glycosylation	SFLYSQLNHTENDVT HHHHHHCCCCHHHHH	32.19	19159218
644	Phosphorylation	NAGMGRFTKVGEQER CCCCCCCEECCCEEC	24.37	26437602
658	O-linked_Glycosylation	RTVDTLPSPQHPVAH CCCCCCCCCCCHHHH	40.06	55834967
700	Phosphorylation	QGVQREVSMVEGRVS HHHHHHHHHHHHHHH	16.62	28961369
745	N-linked_Glycosylation	WNCVRQMNGTLRSHS HHHHHHCCCCHHHCC	31.77	UniProtKB CARBOHYD
790	O-linked_Glycosylation	QPSAKAPSPPPPAEA CCCCCCCCCCCCCCC	55.70	OGP
812	O-linked_Glycosylation	EPAPPRPSGPATAED CCCCCCCCCCCCCCC	59.70	OGP
842	O-linked_Glycosylation	PPQPPGSTGVIAETG CCCCCCCCCEEEECC	41.19	OGP
974	N-linked_Glycosylation	EAVLSVSNASVAQLH HHHHCCCCCHHHHHH	33.79	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EMIL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EMIL2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EMIL2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of EMIL2_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-616, AND MASSSPECTROMETRY.
PubMed: 19159218

Phosphorylation

"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASSSPECTROMETRY.
PubMed: 17693683