UniProt ID | EFCB3_HUMAN | |
---|---|---|
UniProt AC | Q8N7B9 | |
Protein Name | EF-hand calcium-binding domain-containing protein 3 | |
Gene Name | EFCAB3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 438 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MAVSEIKPKLKLNPLTKVPISHNKRDRDLPGSLQCQLQHKEKKLSASQMAAFQDAYNFFYKDKTGCIDFHGLMCTVAKLGMNLTKHDVYNELKCADIDRDGKVNFSDFIKVLTDKNLFLKAVVPEKETCLDLAGNPGILLFEILSRLLETSALPRKSIIEIVSYFQRKFQHTGPGMLWSPYTMGYGKRTLKPDICTPPSSSMAAFANAARIAIMKEKDLFKFLEELKRCNSGSDSPYSKIPIFPLFPNVDGVVMGKPFKDMQKLEMLRIKEPLHFFEDYFFHKRDWKTQAANIKSMDPASGYSNNIFTIDQMLKKKQTCTVADATAIKQHVKRATDTYNLGIALEHRKEMLNLWQKIRGDLIGMDSRNESFYDTFSTYTWSWNVCQELLSPKDLRLYDAYVNRNSSHNSRSSSSSDTSECYTDSGRKRKRKGLKGFQQ | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MAVSEIKPKLK ----CCHHHCCCCCC | 24.86 | 18187866 | |
9 (in isoform 2) | Phosphorylation | - | 53.93 | 25999147 | |
32 | Phosphorylation | RDRDLPGSLQCQLQH CCCCCCCCHHHHHHH | 17.21 | 30622161 | |
145 | Phosphorylation | ILLFEILSRLLETSA HHHHHHHHHHHHCCC | 26.92 | 24719451 | |
151 | Phosphorylation | LSRLLETSALPRKSI HHHHHHCCCCCHHHH | 20.59 | 24719451 | |
157 | Phosphorylation | TSALPRKSIIEIVSY CCCCCHHHHHHHHHH | 30.03 | 27174698 | |
163 | Phosphorylation | KSIIEIVSYFQRKFQ HHHHHHHHHHHHHCC | 26.37 | 27174698 | |
164 | Phosphorylation | SIIEIVSYFQRKFQH HHHHHHHHHHHHCCC | 7.88 | 27174698 | |
189 | Phosphorylation | TMGYGKRTLKPDICT CCCCCCCCCCCCCCC | 42.49 | 24719451 | |
196 | Phosphorylation | TLKPDICTPPSSSMA CCCCCCCCCCCHHHH | 38.27 | 24719451 | |
199 | Phosphorylation | PDICTPPSSSMAAFA CCCCCCCCHHHHHHH | 35.93 | 25693802 | |
200 | Phosphorylation | DICTPPSSSMAAFAN CCCCCCCHHHHHHHH | 29.88 | 25693802 | |
201 | Phosphorylation | ICTPPSSSMAAFANA CCCCCCHHHHHHHHH | 19.44 | 25693802 | |
241 | Phosphorylation | DSPYSKIPIFPLFPN CCCCCCCCCCCCCCC | 26.38 | 24719451 | |
248 | Phosphorylation | PIFPLFPNVDGVVMG CCCCCCCCCCEEEEC | 36.86 | 24719451 | |
279 | Phosphorylation | PLHFFEDYFFHKRDW CHHHHHHHHHHCCCH | 10.84 | 30622161 | |
300 | Phosphorylation | IKSMDPASGYSNNIF CCCCCCCCCCCCCCE | 43.59 | - | |
372 | Phosphorylation | DSRNESFYDTFSTYT CCCCCCHHHHCHHHE | 24.29 | - | |
390 | Phosphorylation | NVCQELLSPKDLRLY HHHHHHCCHHHHHHH | 42.39 | 24719451 | |
406 | Phosphorylation | AYVNRNSSHNSRSSS HHCCCCCCCCCCCCC | 30.18 | 16964243 | |
409 | Phosphorylation | NRNSSHNSRSSSSSD CCCCCCCCCCCCCCC | 28.28 | 16964243 | |
418 | Phosphorylation | SSSSSDTSECYTDSG CCCCCCCHHCCCCCC | 30.57 | - | |
422 | Phosphorylation | SDTSECYTDSGRKRK CCCHHCCCCCCHHHC | 35.03 | - |
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 EFCB3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EFCB3_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 EFCB3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EFCB3_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 |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY. |