| UniProt ID | HAX1_MOUSE | |
|---|---|---|
| UniProt AC | O35387 | |
| Protein Name | HCLS1-associated protein X-1 | |
| Gene Name | Hax1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 280 | |
| Subcellular Localization |
Mitochondrion . Endoplasmic reticulum . Nucleus membrane . Cytoplasmic vesicle . Cytoplasm, cell cortex . Cell membrane Peripheral membrane protein Cytoplasmic side . Sarcoplasmic reticulum . Cytoplasm, P-body . Cytoplasm . Nucleus . Predominantl |
|
| Protein Description | Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools.. | |
| Protein Sequence | MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPDWGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETTVTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSVFDLFRG ------CCHHHHHCC | 31.34 | - | |
| 67 | Phosphorylation | PPEEFGFSFSPRGGM CCHHHCCEECCCCCC | 25.79 | 30352176 | |
| 69 | Phosphorylation | EEFGFSFSPRGGMRF HHHCCEECCCCCCCE | 16.70 | 25159016 | |
| 132 | Ubiquitination | TLRDSMLKYPDSHQP CHHHHHHCCCCCCCC | 46.20 | - | |
| 154 | Phosphorylation | ESHAKPESPKPAPDW HHHCCCCCCCCCCCC | 46.91 | 27841257 | |
| 177 | Phosphorylation | LDDTWPVSPHSRAKE CCCCCCCCCCCCHHH | 16.90 | 26643407 | |
| 180 | Phosphorylation | TWPVSPHSRAKEDKD CCCCCCCCCHHHCCC | 37.00 | 28066266 | |
| 190 | Phosphorylation | KEDKDLDSQVSQEGL HHCCCHHHHHHHCCC | 39.52 | 21454597 | |
| 193 | Phosphorylation | KDLDSQVSQEGLGPL CCHHHHHHHCCCHHH | 18.19 | 26370283 | |
| 206 | Ubiquitination | PLLQPQPKSYFKSIS HHCCCCCHHHEEEEE | 53.17 | - | |
| 259 | Phosphorylation | SDPDSQRSSALDDPF CCCCHHHHHHHCCHH | 16.60 | 26239621 |
| 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 HAX1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HAX1_MOUSE !! | ||||||
* 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 HAX1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ADT3_HUMAN | SLC25A6 | physical | 26496610 | |
| CH60_HUMAN | HSPD1 | physical | 26496610 | |
| ITA1_HUMAN | ITGA1 | physical | 26496610 | |
| SPT6H_HUMAN | SUPT6H | physical | 26496610 | |
| KIF3B_HUMAN | KIF3B | physical | 26496610 | |
| LGAT1_HUMAN | LPGAT1 | physical | 26496610 | |
| DJC13_HUMAN | DNAJC13 | physical | 26496610 | |
| TRAM1_HUMAN | TRAM1 | physical | 26496610 | |
| NUP62_HUMAN | NUP62 | physical | 26496610 | |
| RBSK_HUMAN | RBKS | physical | 26496610 | |
| DERL1_HUMAN | DERL1 | physical | 26496610 | |
| ZN768_HUMAN | ZNF768 | physical | 26496610 | |
| CLPB_HUMAN | CLPB | physical | 26496610 | |
| T126A_HUMAN | TMEM126A | physical | 26496610 | |
| TIM23_HUMAN | TIMM23 | physical | 26496610 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...