| UniProt ID | DNS2A_HUMAN | |
|---|---|---|
| UniProt AC | O00115 | |
| Protein Name | Deoxyribonuclease-2-alpha | |
| Gene Name | DNASE2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 360 | |
| Subcellular Localization | Lysosome. | |
| Protein Description | Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the degradation of nuclear DNA in cellular apoptosis during development. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver, where it degrades nuclear DNA expelled from erythroid precursor cells.. | |
| Protein Sequence | MIPLLLAALLCVPAGALTCYGDSGQPVDWFVVYKLPALRGSGEAAQRGLQYKYLDESSGGWRDGRALINSPEGAVGRSLQPLYRSNTSQLAFLLYNDQPPQPSKAQDSSMRGHTKGVLLLDHDGGFWLVHSVPNFPPPASSAAYSWPHSACTYGQTLLCVSFPFAQFSKMGKQLTYTYPWVYNYQLEGIFAQEFPDLENVVKGHHVSQEPWNSSITLTSQAGAVFQSFAKFSKFGDDLYSGWLAAALGTNLQVQFWHKTVGILPSNCSDIWQVLNVNQIAFPGPAGPSFNSTEDHSKWCVSPKGPWTCVGDMNRNQGEEQRGGGTLCAQLPALWKAFQPLVKNYQPCNGMARKPSRAYKI | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 20 | Phosphorylation | PAGALTCYGDSGQPV CCCCEEECCCCCCEE | 20.80 | - | |
| 41 | Phosphorylation | KLPALRGSGEAAQRG ECHHCCCCHHHHHCC | 27.33 | - | |
| 52 | Ubiquitination | AQRGLQYKYLDESSG HHCCCCEEEECCCCC | 26.78 | - | |
| 52 | Ubiquitination | AQRGLQYKYLDESSG HHCCCCEEEECCCCC | 26.78 | - | |
| 70 | Phosphorylation | DGRALINSPEGAVGR CCCEECCCCCCCHHC | 19.82 | 21406692 | |
| 86 | N-linked_Glycosylation | LQPLYRSNTSQLAFL CHHHHHCCCCEEEEE | 34.45 | UniProtKB CARBOHYD | |
| 86 | N-linked_Glycosylation | LQPLYRSNTSQLAFL CHHHHHCCCCEEEEE | 34.45 | 11906178 | |
| 212 | N-linked_Glycosylation | HVSQEPWNSSITLTS CCCCCCCCCCEEEEH | 36.27 | 11906178 | |
| 212 | N-linked_Glycosylation | HVSQEPWNSSITLTS CCCCCCCCCCEEEEH | 36.27 | 10080942 | |
| 266 | N-linked_Glycosylation | TVGILPSNCSDIWQV CCCCCCCCCCHHHHH | 27.63 | 11906178 | |
| 266 | N-linked_Glycosylation | TVGILPSNCSDIWQV CCCCCCCCCCHHHHH | 27.63 | 10080942 | |
| 290 | N-linked_Glycosylation | GPAGPSFNSTEDHSK CCCCCCCCCCCCCCC | 52.97 | 11906178 | |
| 290 | N-linked_Glycosylation | GPAGPSFNSTEDHSK CCCCCCCCCCCCCCC | 52.97 | UniProtKB CARBOHYD | |
| 321 | Methylation | RNQGEEQRGGGTLCA CCCCCCCCCCCCHHH | 49.34 | - | |
| 335 | Acetylation | AQLPALWKAFQPLVK HHHHHHHHHHHHHHH | 39.92 | 19824125 | |
| 353 | Acetylation | PCNGMARKPSRAYKI CCCCCCCCCCCCCCC | 37.49 | 19824133 | |
| 355 | Phosphorylation | NGMARKPSRAYKI-- CCCCCCCCCCCCC-- | 32.36 | 20068231 | |
| 358 | Phosphorylation | ARKPSRAYKI----- CCCCCCCCCC----- | 14.22 | 20068231 |
| 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 DNS2A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNS2A_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 DNS2A_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RUVB2_HUMAN | RUVBL2 | physical | 17353931 | |
| RUVB1_HUMAN | RUVBL1 | physical | 17353931 | |
| OPA1_HUMAN | OPA1 | physical | 22939629 | |
| RIR1_HUMAN | RRM1 | physical | 22939629 | |
| CALX_HUMAN | CANX | physical | 28514442 |
| 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. | ||||||
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| 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-212, AND MASSSPECTROMETRY. | |
| "Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-212. | |
