UniProt ID | DEF1_HUMAN | |
---|---|---|
UniProt AC | P59665 | |
Protein Name | Neutrophil defensin 1 | |
Gene Name | DEFA1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 94 | |
Subcellular Localization | Secreted. | |
Protein Description | Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.. | |
Protein Sequence | MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIAADIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPACIAGERRYGTCIYQGRLWAFCC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
67 | Phosphorylation | SRKNMACYCRIPACI CCCCCEEEEECCCHH | 3.84 | 21253578 | |
78 | ADP-ribosylation | PACIAGERRYGTCIY CCHHCCCCCCEEEEE | 35.88 | - | |
78 | ADP-ribosylation | PACIAGERRYGTCIY CCHHCCCCCCEEEEE | 35.88 | 21904558 | |
80 | Phosphorylation | CIAGERRYGTCIYQG HHCCCCCCEEEEEEC | 24.02 | 21253578 | |
82 | Phosphorylation | AGERRYGTCIYQGRL CCCCCCEEEEEECEE | 6.18 | 28442448 | |
83 | S-nitrosylation | GERRYGTCIYQGRLW CCCCCEEEEEECEEE | 2.07 | 25040305 | |
85 | Phosphorylation | RRYGTCIYQGRLWAF CCCEEEEEECEEEEE | 13.68 | 21904558 | |
88 | ADP-ribosylation | GTCIYQGRLWAFCC- EEEEEECEEEEEEC- | 16.13 | - | |
88 | ADP-ribosylation | GTCIYQGRLWAFCC- EEEEEECEEEEEEC- | 16.13 | 21904558 |
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 DEF1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DEF1_HUMAN !! |
* 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 DEF1_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
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. | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Structural and functional consequences induced by post-translationalmodifications in alpha-Defensins."; Balducci E., Bonucci A., Picchianti M., Pogni R., Talluri E.; Int. J. Pept. 2011:594723-594723(2011). Cited for: ADP-RIBOSYLATION AT ARG-78 AND ARG-88 BY ART1, AND PHOSPHORYLATION ATTYR-85. | |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85, AND MASSSPECTROMETRY. |