| UniProt ID | SPT22_HUMAN | |
|---|---|---|
| UniProt AC | Q8NHS9 | |
| Protein Name | Spermatogenesis-associated protein 22 | |
| Gene Name | SPATA22 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 363 | |
| Subcellular Localization | Chromosome. Localizes on meiotic chromosome axes. Accumulates on resected DNA. Localization is dependent on MEIOB (By similarity).. | |
| Protein Description | Meiosis-specific protein required for homologous recombination in meiosis I.. | |
| Protein Sequence | MKRSLNENSARSTAGCLPVPLFNQKKRNRQPLTSNPLKDDSGISTPSDNYDFPPLPTDWAWEAVNPELAPVMKTVDTGQIPHSVSRPLRSQDSVFNSIQSNTGRSQGGWSYRDGNKNTSLKTWNKNDFKPQCKRTNLVANDGKNSCPVSSGAQQQKQLRIPEPPNLSRNKETELLRQTHSSKISGCTMRGLDKNSALQTLKPNFQQNQYKKQMLDDIPEDNTLKETSLYQLQFKEKASSLRIISAVIESMKYWREHAQKTVLLFEVLAVLDSAVTPGPYYSKTFLMRDGKNTLPCVFYEIDRELPRLIRGRVHRCVGNYDQKKNIFQCVSVRPASVSEQKTFQAFVKIADVEMQYYINVMNET | |
| 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 |
|---|---|---|---|---|---|
| 167 | Phosphorylation | IPEPPNLSRNKETEL CCCCCCCCCCHHHHH | 40.21 | - | |
| 195 | Phosphorylation | MRGLDKNSALQTLKP ECCCCCCCHHHHHCC | 35.78 | 29978859 | |
| 199 | Phosphorylation | DKNSALQTLKPNFQQ CCCCHHHHHCCCHHH | 37.28 | 29978859 | |
| 222 | Phosphorylation | DDIPEDNTLKETSLY HCCCCCCCCCCCEEE | 52.08 | 26074081 | |
| 226 | Phosphorylation | EDNTLKETSLYQLQF CCCCCCCCEEEEHHH | 23.57 | 26074081 | |
| 227 | Phosphorylation | DNTLKETSLYQLQFK CCCCCCCEEEEHHHH | 26.60 | 26074081 | |
| 229 | Phosphorylation | TLKETSLYQLQFKEK CCCCCEEEEHHHHHH | 13.62 | 26074081 | |
| 238 | Phosphorylation | LQFKEKASSLRIISA HHHHHHHHHHHHHHH | 40.76 | - | |
| 239 | Phosphorylation | QFKEKASSLRIISAV HHHHHHHHHHHHHHH | 26.91 | - | |
| 244 | Phosphorylation | ASSLRIISAVIESMK HHHHHHHHHHHHHHH | 17.70 | - | |
| 249 | Phosphorylation | IISAVIESMKYWREH HHHHHHHHHHHHHHH | 14.95 | - | |
| 252 | Phosphorylation | AVIESMKYWREHAQK HHHHHHHHHHHHHHH | 10.89 | - | |
| 269 (in isoform 3) | Phosphorylation | - | 5.51 | - | |
| 279 | Phosphorylation | SAVTPGPYYSKTFLM HCCCCCCCCCCEEEE | 26.70 | 17053785 | |
| 280 | Phosphorylation | AVTPGPYYSKTFLMR CCCCCCCCCCEEEEE | 13.56 | 17053785 |
| 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 SPT22_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT22_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 SPT22_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| KDM1A_HUMAN | KDM1A | physical | 23455924 | |
| ANM6_HUMAN | PRMT6 | physical | 23455924 | |
| DESM_HUMAN | DES | physical | 28514442 | |
| ACTA_HUMAN | ACTA2 | physical | 28514442 | |
| ACTBL_HUMAN | ACTBL2 | physical | 28514442 |
| 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 |
| "Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279 AND TYR-280, ANDMASS SPECTROMETRY. | |