| UniProt ID | SP30L_HUMAN | |
|---|---|---|
| UniProt AC | Q9HAJ7 | |
| Protein Name | Histone deacetylase complex subunit SAP30L | |
| Gene Name | SAP30L | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 183 | |
| Subcellular Localization |
Isoform 1: Nucleus, nucleolus . Isoform 2: Nucleus, nucleolus . Isoform 3: Nucleus, nucleolus . |
|
| Protein Description | Isoform 1: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes. [PubMed: 16820529] | |
| Protein Sequence | MNGFSTEEDSREGPPAAPAAAAPGYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSVRHLYICDFHKNFIQSVRNKRKRKTSDDGGDSPEHDTDIPEVDLFQLQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVKSNKSRLDQKSEGGKQLE | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MNGFSTEE -------CCCCCCHH | 11.32 | 22814378 | |
| 5 | Phosphorylation | ---MNGFSTEEDSRE ---CCCCCCHHHCCC | 35.99 | 25159151 | |
| 46 | Phosphorylation | VRPAGNASFSKRVQK EEECCCCCHHHHHHH | 33.77 | 24719451 | |
| 54 | Phosphorylation | FSKRVQKSISQKKLK HHHHHHHHHCCCCCC | 15.47 | 30631047 | |
| 56 | Phosphorylation | KRVQKSISQKKLKLD HHHHHHHCCCCCCCC | 42.93 | 30631047 | |
| 67 | Phosphorylation | LKLDIDKSVRHLYIC CCCCCCHHHCEEEEC | 22.19 | 24260401 | |
| 78 | Methylation | LYICDFHKNFIQSVR EEECHHHHHHHHHHH | 54.25 | - | |
| 92 | Phosphorylation | RNKRKRKTSDDGGDS HHHCCCCCCCCCCCC | 41.23 | 30266825 | |
| 93 | Phosphorylation | NKRKRKTSDDGGDSP HHCCCCCCCCCCCCC | 36.42 | 30266825 | |
| 99 | Phosphorylation | TSDDGGDSPEHDTDI CCCCCCCCCCCCCCC | 35.15 | 30266825 | |
| 104 | Phosphorylation | GDSPEHDTDIPEVDL CCCCCCCCCCCCCCE | 37.42 | 30266825 | |
| 118 | Phosphorylation | LFQLQVNTLRRYKRH EEHHHHHHHHHHHHH | 23.84 | 20068231 | |
| 130 | Phosphorylation | KRHYKLQTRPGFNKA HHHHCCCCCCCCCHH | 49.63 | 24719451 | |
| 144 | Phosphorylation | AQLAETVSRHFRNIP HHHHHHHHHHHHCCC | 27.70 | 24719451 | |
| 157 | Phosphorylation | IPVNEKETLAYFIYM CCCCCHHHHHHHHHH | 27.96 | 29759185 | |
| 163 | Phosphorylation | ETLAYFIYMVKSNKS HHHHHHHHHHHCCCH | 5.97 | 29759185 | |
| 167 | Phosphorylation | YFIYMVKSNKSRLDQ HHHHHHHCCCHHHHH | 37.77 | 29759185 | |
| 170 | Phosphorylation | YMVKSNKSRLDQKSE HHHHCCCHHHHHCCC | 42.18 | 24719451 | |
| 176 | Phosphorylation | KSRLDQKSEGGKQLE CHHHHHCCCCCCCCC | 35.52 | 24719451 |
| 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 SP30L_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SP30L_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 SP30L_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SIN3A_HUMAN | SIN3A | physical | 16820529 | |
| SP30L_HUMAN | SAP30L | physical | 16820529 | |
| HDAC1_HUMAN | HDAC1 | physical | 16820529 | |
| HDAC2_HUMAN | HDAC2 | physical | 16820529 | |
| HDAC3_HUMAN | HDAC3 | physical | 16820529 | |
| SIN3A_HUMAN | SIN3A | physical | 18070604 |
| 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 THR-92 AND SER-99, AND MASSSPECTROMETRY. | |
| "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 THR-104, AND MASSSPECTROMETRY. | |