dbPTM

ELNE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ELNE_HUMAN
UniProt AC	P08246
Protein Name	Neutrophil elastase
Gene Name	ELANE
Organism	Homo sapiens (Human).
Sequence Length	267
Subcellular Localization
Protein Description	Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis..
Protein Sequence	MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
88	N-linked_Glycosylation	RVVLGAHNLSRREPT HHHHCCCCCCCCCCC	38.90	19159218
90	Phosphorylation	VLGAHNLSRREPTRQ HHCCCCCCCCCCCHH	34.31	23312004
124	N-linked_Glycosylation	DIVILQLNGSATINA CEEEEEECCCEEECC	29.43	3550808
151	S-nitrosylation	RLGNGVQCLAMGWGL CCCCHHHHHHHHCHH	2.13	25040305
167	Phosphorylation	GRNRGIASVLQELNV CCCCCHHHHHHHCCH	22.80	24043423
173	N-linked_Glycosylation	ASVLQELNVTVVTSL HHHHHHCCHHHHHHH	27.02	19159218
175	Phosphorylation	VLQELNVTVVTSLCR HHHHCCHHHHHHHHH	14.26	24043423
178	Phosphorylation	ELNVTVVTSLCRRSN HCCHHHHHHHHHCCC	16.20	24043423
179	Phosphorylation	LNVTVVTSLCRRSNV CCHHHHHHHHHCCCC	17.54	24043423
184	Phosphorylation	VTSLCRRSNVCTLVR HHHHHHCCCCEEEEC	17.79	24043423
188	Phosphorylation	CRRSNVCTLVRGRQA HHCCCCEEEECCCCC	24.81	24043423

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 ELNE_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ELNE_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 ELNE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NT2NL_HUMAN	NOTCH2NL	physical	14673143
AACT_HUMAN	SERPINA3	physical	8718849
A2AP_HUMAN	SERPINF2	physical	6980881
IC1_HUMAN	SERPING1	physical	6980881
A1AT_HUMAN	SERPINA1	physical	10867014
ILEU_HUMAN	SERPINB1	physical	10924364
A2AP_HUMAN	SERPINF2	physical	2437112
KNG1_HUMAN	KNG1	physical	12887060

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
162800	Cyclic haematopoiesis (CH)
202700	Neutropenia, severe congenital 1, autosomal dominant (SCN1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ELNE_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-88 AND ASN-173, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Primary structure of human neutrophil elastase."; Sinha S., Watorek W., Karr S., Giles J., Bode W., Travis J.; Proc. Natl. Acad. Sci. U.S.A. 84:2228-2232(1987). Cited for: PROTEIN SEQUENCE OF 30-247.	3550808 [Abstract]