| UniProt ID | DLX2_HUMAN | |
|---|---|---|
| UniProt AC | Q07687 | |
| Protein Name | Homeobox protein DLX-2 | |
| Gene Name | DLX2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 328 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Acts as a transcriptional activator. Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina. Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.. | |
| Protein Sequence | MTGVFDSLVADMHSTQIAASSTYHQHQQPPSGGGAGPGGNSSSSSSLHKPQESPTLPVSTATDSSYYTNQQHPAGGGGGGGSPYAHMGSYQYQASGLNNVPYSAKSSYDLGYTAAYTSYAPYGTSSSPANNEPEKEDLEPEIRIVNGKPKKVRKPRTIYSSFQLAALQRRFQKTQYLALPERAELAASLGLTQTQVKIWFQNRRSKFKKMWKSGEIPSEQHPGASASPPCASPPVSAPASWDFGVPQRMAGGGGPGSGGSGAGSSGSSPSSAASAFLGNYPWYHQTSGSASHLQATAPLLHPTQTPQPHHHHHHHGGGGAPVSAGTIF | |
| 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 |
|---|---|---|---|---|---|
| 122 | Phosphorylation | AYTSYAPYGTSSSPA EEEECCCCCCCCCCC | 25.51 | 18669648 | |
| 127 | Phosphorylation | APYGTSSSPANNEPE CCCCCCCCCCCCCCC | 28.00 | - | |
| 157 | Phosphorylation | KKVRKPRTIYSSFQL CCCCCCCCHHHHHHH | 32.56 | 24114839 | |
| 159 | Phosphorylation | VRKPRTIYSSFQLAA CCCCCCHHHHHHHHH | 9.54 | 24114839 | |
| 160 | Phosphorylation | RKPRTIYSSFQLAAL CCCCCHHHHHHHHHH | 22.33 | 24114839 | |
| 161 | Phosphorylation | KPRTIYSSFQLAALQ CCCCHHHHHHHHHHH | 10.47 | 24114839 | |
| 173 | Ubiquitination | ALQRRFQKTQYLALP HHHHHHHHHHHHCCH | 34.58 | 21890473 | |
| 173 | Ubiquitination | ALQRRFQKTQYLALP HHHHHHHHHHHHCCH | 34.58 | 21890473 | |
| 173 | Ubiquitination | ALQRRFQKTQYLALP HHHHHHHHHHHHCCH | 34.58 | 21890473 | |
| 213 | Phosphorylation | KFKKMWKSGEIPSEQ HHHHHHHCCCCCCCC | 26.58 | 26074081 | |
| 218 | Phosphorylation | WKSGEIPSEQHPGAS HHCCCCCCCCCCCCC | 56.39 | 28387310 | |
| 225 | Phosphorylation | SEQHPGASASPPCAS CCCCCCCCCCCCCCC | 34.88 | 30576142 | |
| 227 | Phosphorylation | QHPGASASPPCASPP CCCCCCCCCCCCCCC | 27.21 | 22617229 | |
| 232 | Phosphorylation | SASPPCASPPVSAPA CCCCCCCCCCCCCCC | 36.13 | 22617229 | |
| 236 | Phosphorylation | PCASPPVSAPASWDF CCCCCCCCCCCCCCC | 34.02 | 26074081 | |
| 240 | Phosphorylation | PPVSAPASWDFGVPQ CCCCCCCCCCCCCCC | 26.56 | 26074081 | |
| 257 | Phosphorylation | AGGGGPGSGGSGAGS CCCCCCCCCCCCCCC | 43.01 | - |
| 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 DLX2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DLX2_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 DLX2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MSX1_HUMAN | MSX1 | physical | 9111364 | |
| MSX2_HUMAN | MSX2 | physical | 9111364 | |
| DLX2_HUMAN | DLX2 | physical | 9111364 | |
| DLX5_HUMAN | DLX5 | physical | 9111364 | |
| HXC8_HUMAN | HOXC8 | physical | 9111364 | |
| P85A_HUMAN | PIK3R1 | physical | 21988832 | |
| GRN_HUMAN | GRN | physical | 25416956 |
| 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 |
| "Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-232, ANDMASS SPECTROMETRY. | |