| UniProt ID | CD38_HUMAN | |
|---|---|---|
| UniProt AC | P28907 | |
| Protein Name | ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 | |
| Gene Name | CD38 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 300 | |
| Subcellular Localization |
Membrane Single-pass type II membrane protein. |
|
| Protein Description | Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system.. | |
| Protein Sequence | MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI | |
| 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 |
|---|---|---|---|---|---|
| 13 | Ubiquitination | FSPVSGDKPCCRLSR ECCCCCCCCCHHHHH | 43.40 | - | |
| 51 | Phosphorylation | PRWRQQWSGPGTTKR HHHHHHCCCCCCCCC | 30.67 | 28842319 | |
| 100 | N-linked_Glycosylation | FISKHPCNITEEDYQ HHCCCCCCCCHHHCH | 48.98 | 19159218 | |
| 158 | Phosphorylation | GYLADDLTWCGEFNT HHHHCCCCEECCCCC | 26.21 | 30576142 | |
| 164 | N-linked_Glycosylation | LTWCGEFNTSKINYQ CCEECCCCCCCCCCC | 38.86 | UniProtKB CARBOHYD | |
| 166 | Phosphorylation | WCGEFNTSKINYQSC EECCCCCCCCCCCCC | 32.42 | 30576142 | |
| 181 | Phosphorylation | PDWRKDCSNNPVSVF CCHHHHCCCCCCHHH | 50.18 | 27732954 | |
| 186 | Phosphorylation | DCSNNPVSVFWKTVS HCCCCCCHHHHHHHH | 16.92 | 27732954 | |
| 209 | N-linked_Glycosylation | DVVHVMLNGSRSKIF CEEEEECCCCCCCCC | 28.44 | 19159218 | |
| 219 | N-linked_Glycosylation | RSKIFDKNSTFGSVE CCCCCCCCCCCCCEE | 48.39 | 19159218 | |
| 219 | N-linked_Glycosylation | RSKIFDKNSTFGSVE CCCCCCCCCCCCCEE | 48.39 | 19349973 | |
| 220 | O-linked_Glycosylation | SKIFDKNSTFGSVEV CCCCCCCCCCCCEEE | 30.74 | OGP | |
| 221 | O-linked_Glycosylation | KIFDKNSTFGSVEVH CCCCCCCCCCCEEEE | 41.21 | OGP | |
| 229 | N-linked_Glycosylation | FGSVEVHNLQPEKVQ CCCEEEECCCHHHEE | 45.61 | 19349973 | |
| 229 | N-linked_Glycosylation | FGSVEVHNLQPEKVQ CCCEEEECCCHHHEE | 45.61 | 19349973 | |
| 258 | Phosphorylation | RDLCQDPTIKELESI CHHHCCCHHHHHHHH | 53.63 | - | |
| 264 | Phosphorylation | PTIKELESIISKRNI CHHHHHHHHHHHCCC | 37.53 | 24719451 | |
| 268 | 2-Hydroxyisobutyrylation | ELESIISKRNIQFSC HHHHHHHHCCCEEEC | 38.77 | - |
| 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 CD38_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CD38_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 CD38_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| FCG3A_HUMAN | FCGR3A | physical | 11895784 | |
| CD3E_HUMAN | CD3E | physical | 14523017 | |
| CD3Z_HUMAN | CD247 | physical | 14523017 | |
| LCK_HUMAN | LCK | physical | 14523017 | |
| ZAP70_HUMAN | ZAP70 | physical | 14523017 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00005 | Chronic lymphocytic leukemia (CLL) | |||||
| 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 |
| "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-219, AND MASSSPECTROMETRY. | |
| "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-100; ASN-209 AND ASN-219,AND MASS SPECTROMETRY. | |