| UniProt ID | 1433S_HUMAN | |
|---|---|---|
| UniProt AC | P31947 | |
| Protein Name | 14-3-3 protein sigma | |
| Gene Name | SFN | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 248 | |
| Subcellular Localization | Cytoplasm. Nucleus. Secreted. May be secreted by a non-classical secretory pathway. | |
| Protein Description | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53.; p53-regulated inhibitor of G2/M progression.. | |
| Protein Sequence | MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPQEPQS | |
| 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 | ---MERASLIQKAKL ---CCHHHHHHHHHH | 32.02 | 20068231 | |
| 9 | Ubiquitination | ERASLIQKAKLAEQA CHHHHHHHHHHHHHH | 40.26 | 23000965 | |
| 11 | Ubiquitination | ASLIQKAKLAEQAER HHHHHHHHHHHHHHH | 56.09 | 23000965 | |
| 11 | Acetylation | ASLIQKAKLAEQAER HHHHHHHHHHHHHHH | 56.09 | 7868811 | |
| 11 (in isoform 2) | Ubiquitination | - | 56.09 | 21890473 | |
| 11 (in isoform 1) | Ubiquitination | - | 56.09 | 21890473 | |
| 19 | Phosphorylation | LAEQAERYEDMAAFM HHHHHHHHHHHHHHH | 14.05 | 40379 | |
| 32 | Acetylation | FMKGAVEKGEELSCE HHHHHHHHCCCCCHH | 66.09 | 23236377 | |
| 32 | Ubiquitination | FMKGAVEKGEELSCE HHHHHHHHCCCCCHH | 66.09 | 33845483 | |
| 38 | S-nitrosylation | EKGEELSCEERNLLS HHCCCCCHHHHHHHH | 11.14 | 22178444 | |
| 45 | Phosphorylation | CEERNLLSVAYKNVV HHHHHHHHHHHHHHH | 14.10 | 19664994 | |
| 48 | Phosphorylation | RNLLSVAYKNVVGGQ HHHHHHHHHHHHCHH | 10.84 | 22617229 | |
| 49 (in isoform 2) | Ubiquitination | - | 33.26 | 21890473 | |
| 49 (in isoform 1) | Ubiquitination | - | 33.26 | 21890473 | |
| 49 | Acetylation | NLLSVAYKNVVGGQR HHHHHHHHHHHCHHH | 33.26 | 26051181 | |
| 49 | Ubiquitination | NLLSVAYKNVVGGQR HHHHHHHHHHHCHHH | 33.26 | 23000965 | |
| 63 | Phosphorylation | RAAWRVLSSIEQKSN HHHHHHHHHHHHHHC | 26.81 | 30108239 | |
| 64 | Phosphorylation | AAWRVLSSIEQKSNE HHHHHHHHHHHHHCC | 26.45 | 27794612 | |
| 68 (in isoform 1) | Ubiquitination | - | 42.32 | 21890473 | |
| 68 (in isoform 2) | Ubiquitination | - | 42.32 | 21890473 | |
| 68 | Acetylation | VLSSIEQKSNEEGSE HHHHHHHHHCCCCCC | 42.32 | 23236377 | |
| 68 | Ubiquitination | VLSSIEQKSNEEGSE HHHHHHHHHCCCCCC | 42.32 | 21906983 | |
| 69 | Phosphorylation | LSSIEQKSNEEGSEE HHHHHHHHCCCCCCC | 49.52 | 29396449 | |
| 74 | Phosphorylation | QKSNEEGSEEKGPEV HHHCCCCCCCCCHHH | 45.95 | 28176443 | |
| 74 (in isoform 2) | Phosphorylation | - | 45.95 | 29116813 | |
| 77 (in isoform 2) | Ubiquitination | - | 75.59 | 21890473 | |
| 77 | Ubiquitination | NEEGSEEKGPEVREY CCCCCCCCCHHHHHH | 75.59 | 21906983 | |
| 77 (in isoform 1) | Ubiquitination | - | 75.59 | 21890473 | |
| 87 | Ubiquitination | EVREYREKVETELQG HHHHHHHHHHHHHHH | 36.05 | 29967540 | |
| 90 (in isoform 2) | Ubiquitination | - | 45.01 | 21890473 | |
| 92 (in isoform 2) | Ubiquitination | - | 7.58 | 21890473 | |
| 109 | Ubiquitination | LLDSHLIKEAGDAES HHHHHHHHHHCCCHH | 48.12 | 29967540 | |
| 116 | Phosphorylation | KEAGDAESRVFYLKM HHHCCCHHHEEEEEE | 35.15 | 25159151 | |
| 120 | Phosphorylation | DAESRVFYLKMKGDY CCHHHEEEEEECCCH | 11.53 | - | |
| 122 | Acetylation | ESRVFYLKMKGDYYR HHHEEEEEECCCHHH | 27.47 | 19608861 | |
| 122 (in isoform 1) | Ubiquitination | - | 27.47 | 21890473 | |
| 122 | Ubiquitination | ESRVFYLKMKGDYYR HHHEEEEEECCCHHH | 27.47 | 23000965 | |
| 124 | Acetylation | RVFYLKMKGDYYRYL HEEEEEECCCHHHHH | 47.22 | 26051181 | |
| 124 (in isoform 1) | Ubiquitination | - | 47.22 | 21890473 | |
| 124 | Ubiquitination | RVFYLKMKGDYYRYL HEEEEEECCCHHHHH | 47.22 | 23000965 | |
| 127 | Phosphorylation | YLKMKGDYYRYLAEV EEEECCCHHHHHHHH | 9.86 | 28152594 | |
| 127 (in isoform 2) | Ubiquitination | - | 9.86 | - | |
| 128 | Phosphorylation | LKMKGDYYRYLAEVA EEECCCHHHHHHHHH | 9.49 | 28152594 | |
| 130 | Phosphorylation | MKGDYYRYLAEVATG ECCCHHHHHHHHHCC | 8.31 | 28152594 | |
| 136 | Phosphorylation | RYLAEVATGDDKKRI HHHHHHHCCCCHHHH | 46.44 | 37008999 | |
| 140 | Acetylation | EVATGDDKKRIIDSA HHHCCCCHHHHHHHH | 49.01 | 23236377 | |
| 140 | Ubiquitination | EVATGDDKKRIIDSA HHHCCCCHHHHHHHH | 49.01 | 33845483 | |
| 141 | Acetylation | VATGDDKKRIIDSAR HHCCCCHHHHHHHHH | 56.69 | 19811623 | |
| 146 | Phosphorylation | DKKRIIDSARSAYQE CHHHHHHHHHHHHHH | 18.38 | 20068231 | |
| 149 | Phosphorylation | RIIDSARSAYQEAMD HHHHHHHHHHHHHHH | 30.92 | 50558013 | |
| 151 | Phosphorylation | IDSARSAYQEAMDIS HHHHHHHHHHHHHCC | 14.24 | 46155643 | |
| 155 | Sulfoxidation | RSAYQEAMDISKKEM HHHHHHHHHCCCCCC | 4.65 | 28465586 | |
| 159 | Ubiquitination | QEAMDISKKEMPPTN HHHHHCCCCCCCCCC | 53.76 | 23000965 | |
| 159 | Acetylation | QEAMDISKKEMPPTN HHHHHCCCCCCCCCC | 53.76 | 23236377 | |
| 160 | Ubiquitination | EAMDISKKEMPPTNP HHHHCCCCCCCCCCC | 53.07 | 23000965 | |
| 186 | Phosphorylation | FHYEIANSPEEAISL EEEEECCCHHHHHHH | 25.35 | 22817900 | |
| 196 | Phosphorylation | EAISLAKTTFDEAMA HHHHHHHHHHHHHHH | 27.39 | 25338102 | |
| 197 | Phosphorylation | AISLAKTTFDEAMAD HHHHHHHHHHHHHHH | 28.51 | 20068231 | |
| 202 | Sulfoxidation | KTTFDEAMADLHTLS HHHHHHHHHHHHHCC | 2.54 | 28465586 | |
| 207 | Phosphorylation | EAMADLHTLSEDSYK HHHHHHHHCCCCCCC | 39.00 | 30266825 | |
| 209 | Phosphorylation | MADLHTLSEDSYKDS HHHHHHCCCCCCCCH | 40.28 | 30266825 | |
| 212 | Phosphorylation | LHTLSEDSYKDSTLI HHHCCCCCCCCHHHH | 29.99 | 30266825 | |
| 213 | Phosphorylation | HTLSEDSYKDSTLIM HHCCCCCCCCHHHHH | 31.01 | 30266825 | |
| 216 | Phosphorylation | SEDSYKDSTLIMQLL CCCCCCCHHHHHHHH | 22.44 | 16964243 | |
| 217 | Phosphorylation | EDSYKDSTLIMQLLR CCCCCCHHHHHHHHH | 30.36 | 19664994 | |
| 228 | Phosphorylation | QLLRDNLTLWTADNA HHHHCCCEEEECCCC | 26.89 | 20067319 | |
| 231 | Phosphorylation | RDNLTLWTADNAGEE HCCCEEEECCCCCCC | 27.52 | 30576142 | |
| 248 | Phosphorylation | EAPQEPQS------- CCCCCCCC------- | 53.56 | 20201521 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 186 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM25 | Q14258 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | RFFL | Q8WZ73 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | COP1 | Q8NHY2 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 1433S_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 1433S_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 |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, 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-248, AND MASSSPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASSSPECTROMETRY. | |
