UniProt ID | ENDD1_HUMAN | |
---|---|---|
UniProt AC | O94919 | |
Protein Name | Endonuclease domain-containing 1 protein | |
Gene Name | ENDOD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 500 | |
Subcellular Localization | Secreted . | |
Protein Description | May act as a DNase and a RNase.. | |
Protein Sequence | MGTARWLALGSLFALAGLLEGRLVGEEEAGFGECDKFFYAGTPPAGLAADSHVKICQRAEGAERFATLYSTRDRIPVYSAFRAPRPAPGGAEQRWLVEPQIDDPNSNLEEAINEAEAITSVNSLGSKQALNTDYLDSDYQRGQLYPFSLSSDVQVATFTLTNSAPMTQSFQERWYVNLHSLMDRALTPQCGSGEDLYILTGTVPSDYRVKDKVAVPEFVWLAACCAVPGGGWAMGFVKHTRDSDIIEDVMVKDLQKLLPFNPQLFQNNCGETEQDTEKMKKILEVVNQIQDEERMVQSQKSSSPLSSTRSKRSTLLPPEASEGSSSFLGKLMGFIATPFIKLFQLIYYLVVAILKNIVYFLWCVTKQVINGIESCLYRLGSATISYFMAIGEELVSIPWKVLKVVAKVIRALLRILCCLLKAICRVLSIPVRVLVDVATFPVYTMGAIPIVCKDIALGLGGTVSLLFDTAFGTLGGLFQVVFSVCKRIGYKVTFDNSGEL | |
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 |
---|---|---|---|---|---|
137 | Phosphorylation | LNTDYLDSDYQRGQL CCCCCCCCCCCCCCC | 35.31 | - | |
207 | Phosphorylation | TGTVPSDYRVKDKVA ECCCCCCCCCCCCCC | 22.95 | - | |
250 | Sulfoxidation | SDIIEDVMVKDLQKL CCCCHHHHHHHHHHH | 4.85 | 21406390 | |
300 | Ubiquitination | ERMVQSQKSSSPLSS HHHHHCCCCCCCCCC | 58.51 | 21906983 | |
301 | Phosphorylation | RMVQSQKSSSPLSST HHHHCCCCCCCCCCC | 28.54 | 26437602 | |
301 | O-linked_Glycosylation | RMVQSQKSSSPLSST HHHHCCCCCCCCCCC | 28.54 | OGP | |
302 | Phosphorylation | MVQSQKSSSPLSSTR HHHCCCCCCCCCCCC | 42.90 | 28857561 | |
303 | Phosphorylation | VQSQKSSSPLSSTRS HHCCCCCCCCCCCCC | 36.63 | 28857561 | |
306 | Phosphorylation | QKSSSPLSSTRSKRS CCCCCCCCCCCCCCC | 32.80 | 22817900 | |
307 | Phosphorylation | KSSSPLSSTRSKRST CCCCCCCCCCCCCCC | 35.21 | 22817900 | |
308 | Phosphorylation | SSSPLSSTRSKRSTL CCCCCCCCCCCCCCC | 35.27 | 26437602 | |
310 | Phosphorylation | SPLSSTRSKRSTLLP CCCCCCCCCCCCCCC | 32.29 | 22817900 | |
313 | Phosphorylation | SSTRSKRSTLLPPEA CCCCCCCCCCCCCCC | 27.43 | - | |
314 | Phosphorylation | STRSKRSTLLPPEAS CCCCCCCCCCCCCCC | 36.03 | - | |
407 | Acetylation | KVLKVVAKVIRALLR HHHHHHHHHHHHHHH | 26.95 | 19608861 | |
490 | Phosphorylation | SVCKRIGYKVTFDNS HHHHHHCCEEEECCC | 10.42 | 24719451 |
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 ENDD1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ENDD1_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 ENDD1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
STOM_HUMAN | STOM | physical | 27173435 |
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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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND MASS SPECTROMETRY. |