UniProt ID | ADAT3_HUMAN | |
---|---|---|
UniProt AC | Q96EY9 | |
Protein Name | Probable inactive tRNA-specific adenosine deaminase-like protein 3 | |
Gene Name | ADAT3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 351 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MEPAPGLVEQPKCLEAGSPEPEPAPWQALPVLSEKQSGDVELVLAYAAPVLDKRQTSRLLKEVSALHPLPAQPHLKRVRPSRDAGSPHALEMLLCLAGPASGPRSLAELLPRPAVDPRGLGQPFLVPVPARPPLTRGQFEEARAHWPTSFHEDKQVTSALAGRLFSTQERAAMQSHMERAVWAARRAAARGLRAVGAVVVDPASDRVLATGHDCSCADNPLLHAVMVCVDLVARGQGRGTYDFRPFPACSFAPAAAPQAVRAGAVRKLDADEDGLPYLCTGYDLYVTREPCAMCAMALVHARILRVFYGAPSPDGALGTRFRIHARPDLNHRFQVFRGVLEEQCRWLDPDT | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MEPAPGLV -------CCCCCCCC | 14.54 | 19413330 | |
18 | Phosphorylation | PKCLEAGSPEPEPAP CCCCCCCCCCCCCCC | 32.89 | 25850435 | |
33 | Phosphorylation | WQALPVLSEKQSGDV CCCCCCCCCCCCCCE | 42.87 | 50563667 | |
34 | Phosphorylation | QALPVLSEKQSGDVE CCCCCCCCCCCCCEE | 51.45 | 27251275 | |
77 | Ubiquitination | PAQPHLKRVRPSRDA CCCCCHHCCCCCCCC | 35.72 | - | |
86 | Phosphorylation | RPSRDAGSPHALEML CCCCCCCCHHHHHHH | 18.42 | 24719451 | |
102 | Phosphorylation | CLAGPASGPRSLAEL HHHCCCCCCHHHHHH | 24.60 | - | |
166 | Phosphorylation | ALAGRLFSTQERAAM HHHHHHHCHHHHHHH | 33.50 | 24719451 | |
167 | Phosphorylation | LAGRLFSTQERAAMQ HHHHHHCHHHHHHHH | 27.41 | 17525332 | |
175 | Phosphorylation | QERAAMQSHMERAVW HHHHHHHHHHHHHHH | 16.24 | 24719451 | |
183 | Phosphorylation | HMERAVWAARRAAAR HHHHHHHHHHHHHHH | 5.63 | 17525332 |
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 ADAT3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ADAT3_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 ADAT3_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615286 | Mental retardation, autosomal recessive 36 (MRT36) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND MASSSPECTROMETRY. |