| UniProt ID | SIVA_HUMAN | |
|---|---|---|
| UniProt AC | O15304 | |
| Protein Name | Apoptosis regulatory protein Siva | |
| Gene Name | SIVA1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 175 | |
| Subcellular Localization | Cytoplasm . Nucleus . In the nucleus, accumulates in dot-like structures. | |
| Protein Description | Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis.. | |
| Protein Sequence | MPKRSCPFADVAPLQLKVRVSQRELSRGVCAERYSQEVFEKTKRLLFLGAQAYLDHVWDEGCAVVHLPESPKPGPTGAPRAARGQMLIGPDGRLIRSLGQASEADPSGVASIACSSCVRAVDGKAVCGQCERALCGQCVRTCWGCGSVACTLCGLVDCSDMYEKVLCTSCAMFET | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MPKRSCPFADVA ---CCCCCCCCCCCC | 32.06 | 25159151 | |
| 17 | Ubiquitination | DVAPLQLKVRVSQRE CCCCCEEEEEEHHHH | 18.29 | 21963094 | |
| 17 (in isoform 1) | Ubiquitination | - | 18.29 | 21890473 | |
| 31 (in isoform 2) | Ubiquitination | - | 11.25 | 21890473 | |
| 34 | Phosphorylation | RGVCAERYSQEVFEK CCCCHHHHCHHHHHH | 13.25 | 11278261 | |
| 41 | Ubiquitination | YSQEVFEKTKRLLFL HCHHHHHHHHHHHHH | 48.13 | 22817900 | |
| 41 (in isoform 1) | Ubiquitination | - | 48.13 | 21890473 | |
| 43 | Ubiquitination | QEVFEKTKRLLFLGA HHHHHHHHHHHHHHH | 52.71 | 22817900 | |
| 53 | Phosphorylation | LFLGAQAYLDHVWDE HHHHHHHHHHHHCCC | 10.69 | 20727854 | |
| 59 | Ubiquitination | AYLDHVWDEGCAVVH HHHHHHCCCCEEEEE | 41.12 | 33845483 | |
| 70 | Phosphorylation | AVVHLPESPKPGPTG EEEECCCCCCCCCCC | 35.96 | 22617229 | |
| 76 | Phosphorylation | ESPKPGPTGAPRAAR CCCCCCCCCCCCCCC | 52.47 | 27251275 | |
| 124 | Ubiquitination | CVRAVDGKAVCGQCE CEEECCCCEECCCCH | 32.93 | 33845483 | |
| 162 | Phosphorylation | LVDCSDMYEKVLCTS CCCCHHHHHHHHCHH | 20.00 | 20727854 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIVA_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 SIVA_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LPAR2_HUMAN | LPAR2 | physical | 19293149 | |
| PXMP2_HUMAN | PXMP2 | physical | 16683188 | |
| P53_HUMAN | TP53 | physical | 19590512 | |
| MDM2_HUMAN | MDM2 | physical | 19590512 | |
| XIAP_HUMAN | XIAP | physical | 19584092 | |
| A4_HUMAN | APP | physical | 21832049 | |
| CDN2A_HUMAN | CDKN2A | physical | 23462994 | |
| ARF_HUMAN | CDKN2A | physical | 23462994 | |
| UB2D1_HUMAN | UBE2D1 | physical | 23462994 | |
| TA2R_HUMAN | TBXA2R | physical | 22343716 | |
| PCNA_HUMAN | PCNA | physical | 24958773 | |
| RAD18_HUMAN | RAD18 | physical | 24958773 | |
| TYK2_HUMAN | TYK2 | physical | 20727854 | |
| CD4_HUMAN | CD4 | physical | 17653867 | |
| TELT_HUMAN | TCAP | physical | 18849585 | |
| STMN1_HUMAN | STMN1 | physical | 21768358 | |
| KCC2G_HUMAN | CAMK2G | physical | 21768358 | |
| P53_HUMAN | TP53 | physical | 25431847 |
| 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 |
| "The ARG tyrosine kinase interacts with Siva-1 in the apoptoticresponse to oxidative stress."; Cao C., Ren X., Kharbanda S., Koleske A., Prasad K.V.S., Kufe D.; J. Biol. Chem. 276:11465-11468(2001). Cited for: PHOSPHORYLATION AT TYR-34, AND MUTAGENESIS OF TYR-34 AND TYR-53. | |