| UniProt ID | ABRX1_HUMAN | |
|---|---|---|
| UniProt AC | Q6UWZ7 | |
| Protein Name | BRCA1-A complex subunit Abraxas 1 {ECO:0000312|HGNC:HGNC:25829} | |
| Gene Name | ABRAXAS1 {ECO:0000312|HGNC:HGNC:25829} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 409 | |
| Subcellular Localization | Nucleus . Localizes at sites of DNA damage at double-strand breaks (DSBs). | |
| Protein Description | Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX.. | |
| Protein Sequence | MEGESTSAVLSGFVLGALAFQHLNTDSDTEGFLLGEVKGEAKNSITDSQMDDVEVVYTIDIQKYIPCYQLFSFYNSSGEVNEQALKKILSNVKKNVVGWYKFRRHSDQIMTFRERLLHKNLQEHFSNQDLVFLLLTPSIITESCSTHRLEHSLYKPQKGLFHRVPLVVANLGMSEQLGYKTVSGSCMSTGFSRAVQTHSSKFFEEDGSLKEVHKINEMYASLQEELKSICKKVEDSEQAVDKLVKDVNRLKREIEKRRGAQIQAAREKNIQKDPQENIFLCQALRTFFPNSEFLHSCVMSLKNRHVSKSSCNYNHHLDVVDNLTLMVEHTDIPEASPASTPQIIKHKALDLDDRWQFKRSRLLDTQDKRSKADTGSSNQDKASKMSSPETDEEIEKMKGFGEYSRSPTF | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | VKGEAKNSITDSQMD ECCCCCCCCCHHHCC | 27251275 | ||
| 46 | Phosphorylation | GEAKNSITDSQMDDV CCCCCCCCHHHCCCE | 27251275 | ||
| 48 | Phosphorylation | AKNSITDSQMDDVEV CCCCCCHHHCCCEEE | 27732954 | ||
| 87 | Ubiquitination | VNEQALKKILSNVKK CCHHHHHHHHHHHHH | - | ||
| 90 | Phosphorylation | QALKKILSNVKKNVV HHHHHHHHHHHHHHC | 21712546 | ||
| 93 | Ubiquitination | KKILSNVKKNVVGWY HHHHHHHHHHHCCHH | - | ||
| 155 | Ubiquitination | RLEHSLYKPQKGLFH CCCCCCCCCCCCCCC | - | ||
| 158 | Ubiquitination | HSLYKPQKGLFHRVP CCCCCCCCCCCCCCC | 21890473 | ||
| 174 | Phosphorylation | VVANLGMSEQLGYKT EEEECCCCHHHCCEE | 23286773 | ||
| 200 | Phosphorylation | RAVQTHSSKFFEEDG HHHHHCHHHHHCCCC | 23286773 | ||
| 201 | Ubiquitination | AVQTHSSKFFEEDGS HHHHCHHHHHCCCCC | 21890473 | ||
| 210 | Ubiquitination | FEEDGSLKEVHKINE HCCCCCHHHHHHHHH | - | ||
| 242 | Ubiquitination | DSEQAVDKLVKDVNR CHHHHHHHHHHHHHH | - | ||
| 268 | Ubiquitination | QIQAAREKNIQKDPQ HHHHHHHHCCCCCHH | - | ||
| 272 | Ubiquitination | AREKNIQKDPQENIF HHHHCCCCCHHHCHH | - | ||
| 285 | Dimethylation | IFLCQALRTFFPNSE HHHHHHHHHHCCCCH | - | ||
| 302 | Ubiquitination | HSCVMSLKNRHVSKS HHHHHHHHCCCCCHH | - | ||
| 309 | Phosphorylation | KNRHVSKSSCNYNHH HCCCCCHHHCCCCCC | 27080861 | ||
| 310 | Phosphorylation | NRHVSKSSCNYNHHL CCCCCHHHCCCCCCC | 27080861 | ||
| 313 | Phosphorylation | VSKSSCNYNHHLDVV CCHHHCCCCCCCHHC | 27080861 | ||
| 324 | Phosphorylation | LDVVDNLTLMVEHTD CHHCCCEEEEEECCC | 27080861 | ||
| 330 | Phosphorylation | LTLMVEHTDIPEASP EEEEEECCCCCCCCC | 27080861 | ||
| 336 | Phosphorylation | HTDIPEASPASTPQI CCCCCCCCCCCCCHH | 27422710 | ||
| 339 | Phosphorylation | IPEASPASTPQIIKH CCCCCCCCCCHHHHC | 26074081 | ||
| 340 | Phosphorylation | PEASPASTPQIIKHK CCCCCCCCCHHHHCC | 26074081 | ||
| 345 | Ubiquitination | ASTPQIIKHKALDLD CCCCHHHHCCCCCCC | - | ||
| 347 | Ubiquitination | TPQIIKHKALDLDDR CCHHHHCCCCCCCCC | 21890473 | ||
| 358 | Ubiquitination | LDDRWQFKRSRLLDT CCCCHHHHHHHHCCC | 21890473 | ||
| 358 | Methylation | LDDRWQFKRSRLLDT CCCCHHHHHHHHCCC | - | ||
| 365 | Phosphorylation | KRSRLLDTQDKRSKA HHHHHCCCCCHHHCC | 17525332 | ||
| 368 | Ubiquitination | RLLDTQDKRSKADTG HHCCCCCHHHCCCCC | - | ||
| 371 | Ubiquitination | DTQDKRSKADTGSSN CCCCHHHCCCCCCCC | - | ||
| 383 | Phosphorylation | SSNQDKASKMSSPET CCCHHHHHHCCCCCC | 18669648 | ||
| 384 | Ubiquitination | SNQDKASKMSSPETD CCHHHHHHCCCCCCH | 21890473 | ||
| 386 | Phosphorylation | QDKASKMSSPETDEE HHHHHHCCCCCCHHH | 29255136 | ||
| 387 | Phosphorylation | DKASKMSSPETDEEI HHHHHCCCCCCHHHH | 29255136 | ||
| 390 | Phosphorylation | SKMSSPETDEEIEKM HHCCCCCCHHHHHHH | 29255136 | ||
| 396 | Ubiquitination | ETDEEIEKMKGFGEY CCHHHHHHHCCCCCC | 21890473 | ||
| 398 | Sumoylation | DEEIEKMKGFGEYSR HHHHHHHCCCCCCCC | - | ||
| 398 | Ubiquitination | DEEIEKMKGFGEYSR HHHHHHHCCCCCCCC | 21906983 | ||
| 398 | Sumoylation | DEEIEKMKGFGEYSR HHHHHHHCCCCCCCC | - | ||
| 403 | Phosphorylation | KMKGFGEYSRSPTF- HHCCCCCCCCCCCC- | 23927012 | ||
| 404 | Phosphorylation | MKGFGEYSRSPTF-- HCCCCCCCCCCCC-- | 23927012 | ||
| 406 | Phosphorylation | GFGEYSRSPTF---- CCCCCCCCCCC---- | 23927012 | ||
| 408 | Phosphorylation | GEYSRSPTF------ CCCCCCCCC------ | 23401153 |
* 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 ABRX1_HUMAN !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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