| UniProt ID | AT7L3_HUMAN | |
|---|---|---|
| UniProt AC | Q14CW9 | |
| Protein Name | Ataxin-7-like protein 3 {ECO:0000255|HAMAP-Rule:MF_03047} | |
| Gene Name | ATXN7L3 {ECO:0000255|HAMAP-Rule:MF_03047} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 347 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. [PubMed: 18206972] | |
| Protein Sequence | MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYNNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDSFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN | |
| 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 |
|---|---|---|---|---|---|
| 123 | Phosphorylation | ANRRIANSNNMNKSE HHHHHHCCCCCCCCC | 22.13 | 28450419 | |
| 129 | Phosphorylation | NSNNMNKSESDQEDN CCCCCCCCCCCCCCC | 37.01 | 30175587 | |
| 131 | Phosphorylation | NNMNKSESDQEDNDD CCCCCCCCCCCCCCC | 52.24 | 22115753 | |
| 145 | Phosphorylation | DINDNDWSYGSEKKA CCCCCCCCHHHHHHH | 23.60 | 27251275 | |
| 146 | Phosphorylation | INDNDWSYGSEKKAK CCCCCCCHHHHHHHH | 22.03 | 27251275 | |
| 148 | Phosphorylation | DNDWSYGSEKKAKKR CCCCCHHHHHHHHHC | 37.70 | 27251275 | |
| 157 | Phosphorylation | KKAKKRKSDKNPNSP HHHHHCCCCCCCCCH | 58.83 | 20068231 | |
| 162 (in isoform 2) | Phosphorylation | - | 74.23 | - | |
| 163 | Phosphorylation | KSDKNPNSPRRSKSL CCCCCCCCHHHHHHC | 22.50 | 24719451 | |
| 170 (in isoform 2) | Phosphorylation | - | 8.50 | 28450419 | |
| 180 | Phosphorylation | KNGELSNSDPFKYNN CCCCCCCCCCCCCCC | 43.20 | 21815630 | |
| 184 | Acetylation | LSNSDPFKYNNSTGI CCCCCCCCCCCCCCC | 53.08 | 24886847 | |
| 213 | Phosphorylation | TTQCGVISEHTKKMC HHHHCCCCHHHHHHH | 22.40 | 28674419 | |
| 277 | Phosphorylation | SRLQWDGSSDLSPSD HHHCCCCCCCCCCCC | 20.43 | 30266825 | |
| 278 | Phosphorylation | RLQWDGSSDLSPSDS HHCCCCCCCCCCCCC | 48.37 | 30266825 | |
| 281 | Phosphorylation | WDGSSDLSPSDSGSS CCCCCCCCCCCCCCC | 27.61 | 22167270 | |
| 283 | Phosphorylation | GSSDLSPSDSGSSKT CCCCCCCCCCCCCCC | 40.82 | 30266825 | |
| 285 | Phosphorylation | SDLSPSDSGSSKTSE CCCCCCCCCCCCCCC | 44.93 | 30266825 | |
| 287 | Phosphorylation | LSPSDSGSSKTSENQ CCCCCCCCCCCCCCC | 32.39 | 23663014 | |
| 288 | Phosphorylation | SPSDSGSSKTSENQG CCCCCCCCCCCCCCC | 43.40 | 30266825 | |
| 290 | Phosphorylation | SDSGSSKTSENQGWG CCCCCCCCCCCCCCC | 43.13 | - | |
| 302 | Phosphorylation | GWGLGTNSSESRKTK CCCCCCCCHHHHCCC | 35.01 | 21815630 | |
| 312 | Acetylation | SRKTKKKKSHLSLVG HHCCCCCHHHHHHHH | 52.57 | 7369519 | |
| 313 | Phosphorylation | RKTKKKKSHLSLVGT HCCCCCHHHHHHHHH | 38.24 | - | |
| 316 | Phosphorylation | KKKKSHLSLVGTASG CCCHHHHHHHHHHCC | 18.65 | 28450419 | |
| 320 | Phosphorylation | SHLSLVGTASGLGSN HHHHHHHHHCCCCCC | 15.35 | 28450419 | |
| 322 | Phosphorylation | LSLVGTASGLGSNKK HHHHHHHCCCCCCCC | 34.10 | 28450419 | |
| 326 | Phosphorylation | GTASGLGSNKKKKPK HHHCCCCCCCCCCCC | 50.98 | 25159151 | |
| 328 | Acetylation | ASGLGSNKKKKPKPP HCCCCCCCCCCCCCC | 68.61 | 7369527 | |
| 339 | Phosphorylation | PKPPAPPTPSIYDDI CCCCCCCCCCCCCCC | 28.71 | 30576142 | |
| 341 | Phosphorylation | PPAPPTPSIYDDIN- CCCCCCCCCCCCCC- | 35.94 | 28985074 | |
| 343 | Phosphorylation | APPTPSIYDDIN--- CCCCCCCCCCCC--- | 16.35 | 23312004 |
| 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 AT7L3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AT7L3_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 AT7L3_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 |
| "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 SER-278 AND SER-281, ANDMASS SPECTROMETRY. | |
| "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-281, 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-281, AND MASSSPECTROMETRY. | |