UniProt ID | CI040_HUMAN | |
---|---|---|
UniProt AC | Q8IXQ3 | |
Protein Name | Uncharacterized protein C9orf40 | |
Gene Name | C9orf40 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 194 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MAKRRAAEPVTFHVPWKRLLLCDFAEQPPPPPLWIRPPGVAHAGQLLGVPEQHRKRKIDAGTMAEPSASPSKRRDSGDNSAPSGQEREDHGLETGDPPLPPPPVLPGPGEELPGARLPGGGGDDGAGRAGPPRGDWGVASRQHNEEFWQYNTFQYWRNPLPPIDLADIEDLSEDTLTEATLQGRNEGAEVDMES | |
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 |
---|---|---|---|---|---|
17 | Acetylation | VTFHVPWKRLLLCDF EEEECCHHHEEECCC | 27.39 | 25953088 | |
17 | Ubiquitination | VTFHVPWKRLLLCDF EEEECCHHHEEECCC | 27.39 | 21890473 | |
62 | Phosphorylation | KRKIDAGTMAEPSAS CCCCCCCCCCCCCCC | 18.22 | 23927012 | |
67 | Phosphorylation | AGTMAEPSASPSKRR CCCCCCCCCCCCCCC | 32.65 | 23401153 | |
69 | Phosphorylation | TMAEPSASPSKRRDS CCCCCCCCCCCCCCC | 33.76 | 19664994 | |
71 | Phosphorylation | AEPSASPSKRRDSGD CCCCCCCCCCCCCCC | 35.98 | 30266825 | |
72 | Ubiquitination | EPSASPSKRRDSGDN CCCCCCCCCCCCCCC | 55.63 | - | |
76 | Phosphorylation | SPSKRRDSGDNSAPS CCCCCCCCCCCCCCC | 46.35 | 23401153 | |
80 | Phosphorylation | RRDSGDNSAPSGQER CCCCCCCCCCCCCHH | 46.42 | 30278072 | |
83 | Phosphorylation | SGDNSAPSGQEREDH CCCCCCCCCCHHHHC | 53.47 | 23927012 | |
94 | Phosphorylation | REDHGLETGDPPLPP HHHCCCCCCCCCCCC | 52.51 | 28464451 |
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 CI040_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CI040_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 CI040_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CI040_HUMAN !! |
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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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND MASSSPECTROMETRY. | |
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASSSPECTROMETRY. |