P98084
SS
Gene name |
Apba2 (X11l) |
Protein name |
Amyloid-beta A4 precursor protein-binding family A member 2 |
Names |
Adapter protein X11beta , Neuron-specific X11L protein , Neuronal Munc18-1-interacting protein 2 , Mint-2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:11784 |
EC number |
|
Protein Class |
|
Descriptions
Mint adaptor proteins bind to the amyloid precursor protein (APP) and regulate APP processing associated with Alzheimer’s disease. The Mint1 phosphotyrosine binding (PTB) domain that binds to APP is intramolecularly inhibited by the adjacent C-terminal linker region (the autoinhibitory helix) that folds back onto the core structure of the PTB domain and sterically hinders the APP binding site. This intramolecular interaction is disrupted by mutation of Tyr633 within Mint1 autoinhibitory helix, enhancing APP binding and β-amyloid production. As a result, Mint1 undergoes a conformational transition between a closed state that does not bind APP and an open state that involves APP binding and its proteolytic processing.
Autoinhibitory domains (AIDs)
Target domain |
363-546 (PTB domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P98084
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P98084-F1 | Predicted | AlphaFoldDB |
46 variants for P98084
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388917497 | 8 | S>N | No | EVA | |
| rs3388920556 | 57 | T>M | No | EVA | |
| rs3388920519 | 59 | E>D | No | EVA | |
| rs3388917466 | 95 | E>G | No | EVA | |
| rs3388898166 | 107 | D>G | No | EVA | |
| rs3388907101 | 119 | E>Q | No | EVA | |
| rs259659766 | 125 | G>S | No | EVA | |
| rs216890566 | 161 | P>T | No | EVA | |
| rs3388889260 | 166 | P>S | No | EVA | |
| rs3388898231 | 193 | Y>C | No | EVA | |
| rs212054850 | 208 | A>T | No | EVA | |
| rs3388919663 | 226 | D>V | No | EVA | |
| rs3388889242 | 227 | I>L | No | EVA | |
| rs3388898153 | 245 | S>R | No | EVA | |
| rs3388917428 | 250 | S>N | No | EVA | |
| rs219481853 | 271 | T>A | No | EVA | |
| rs3388916986 | 276 | G>S | No | EVA | |
| rs13479300 | 297 | L>P | No | EVA | |
| rs3388874462 | 313 | K>N | No | EVA | |
| rs3388903930 | 321 | N>Y | No | EVA | |
| rs247604514 | 323 | L>I | No | EVA | |
| rs3388914480 | 324 | E>K | No | EVA | |
| rs3388912995 | 325 | Q>E | No | EVA | |
| rs3388904014 | 331 | R>H | No | EVA | |
| rs3388907160 | 357 | A>T | No | EVA | |
| rs3388914448 | 373 | F>I | No | EVA | |
| rs3397951215 | 375 | A>S | No | EVA | |
| rs3388920549 | 429 | E>D | No | EVA | |
| rs3388912785 | 492 | Q>R | No | EVA | |
| rs3388919651 | 497 | Q>H | No | EVA | |
| rs3388913050 | 502 | C>Y | No | EVA | |
| rs3388874389 | 506 | E>D | No | EVA | |
| rs3388898199 | 507 | S>* | No | EVA | |
| rs3388917221 | 519 | Q>H | No | EVA | |
| rs3388917239 | 526 | Q>R | No | EVA | |
| rs3388919661 | 544 | Y>H | No | EVA | |
| rs3388920521 | 596 | V>M | No | EVA | |
| rs3388898243 | 606 | P>T | No | EVA | |
| rs3388898202 | 608 | A>V | No | EVA | |
| rs3388889188 | 683 | S>N | No | EVA | |
| rs3388895597 | 687 | G>R | No | EVA | |
| rs3388914476 | 693 | G>S | No | EVA | |
| rs3388920516 | 695 | V>G | No | EVA | |
| rs3388916984 | 697 | V>L | No | EVA | |
| rs3388910181 | 733 | M>V | No | EVA | |
| rs3388904073 | 746 | T>N | No | EVA |
No associated diseases with P98084
3 regional properties for P98084
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PDZ domain | 568 - 656 | IPR001478-1 |
| domain | PDZ domain | 658 - 736 | IPR001478-2 |
| domain | PTB/PI domain | 368 - 556 | IPR006020 |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| presynapse | The part of a synapse that is part of the presynaptic cell. |
| Schaffer collateral - CA1 synapse | A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| amyloid-beta binding | Binding to an amyloid-beta peptide/protein. |
| identical protein binding | Binding to an identical protein or proteins. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| chemical synaptic transmission | The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse. |
| in utero embryonic development | The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus. |
| locomotory behavior | The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions. |
| multicellular organism growth | The increase in size or mass of an entire multicellular organism, as opposed to cell growth. |
| presynaptic modulation of chemical synaptic transmission | Any process, acting in the presynapse that results in modulation of chemical synaptic transmission. |
| protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| regulation of gene expression | Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q02410 | APBA1 | Amyloid-beta A4 precursor protein-binding family A member 1 | Homo sapiens (Human) | SS |
| Q99767 | APBA2 | Amyloid-beta A4 precursor protein-binding family A member 2 | Homo sapiens (Human) | SS |
| B2RUJ5 | Apba1 | Amyloid-beta A4 precursor protein-binding family A member 1 | Mus musculus (Mouse) | SS |
| Q99JZ0 | Sdcbp2 | Syntenin-2 | Mus musculus (Mouse) | SS |
| O08992 | Sdcbp | Syntenin-1 | Mus musculus (Mouse) | SS |
| O35430 | Apba1 | Amyloid-beta A4 precursor protein-binding family A member 1 | Rattus norvegicus (Rat) | EV |
| O35431 | Apba2 | Amyloid-beta A4 precursor protein-binding family A member 2 | Rattus norvegicus (Rat) | SS |
| O17583 | lin-10 | Protein lin-10 | Caenorhabditis elegans | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAHRKRQSTA | SSMLDHRARP | GPIPHDQEPE | SEDTELPLES | YVPTGLELGT | LRPESPTPEE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QECHNHSPDG | DSSSDYVNNT | SEEEDYDEGL | PEEEEGVTYY | IRYCPEDDSY | LEGMDCNGEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YIAHGAHPVD | TDECQEAVED | WTDSVGPHTH | SHGAENSQEY | PDGHLPIPED | DPTVLEVHDQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EEDGHYCSSK | ESYQDYYPPE | TNGNTGGASP | YRMRRGDGDL | EEQEEDIDQI | VAEIKMSLSM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TSITSASEAS | PEHMPELDPG | DSTEACPPSD | TGHGPGRQEA | RPKSLNLPPE | VKHPGDLQRG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LKTKTRTPEE | RPKWPQEQVC | NGLEQPRKQQ | RSDLNGPTDN | NNIPETKKVA | SFPSFVAVPG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PCEAEDLIDG | IIFAANYLGS | TQLLSERNPS | KNIRMMQAQE | AVSRVKRMQK | AAKIKKKANS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EGDAQTLTEV | DLFISTQRIK | VLNADTQETM | MDHALRTISY | IADIGNIVVL | MARRRMPRSA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SQDCIETTPG | AQEGKKQYKM | ICHVFESEDA | QLIAQSIGQA | FSVAYQEFLR | ANGINPEDLS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QKEYSDIINT | QEMYNDDLIH | FSNSENCKEL | QLEKHKGEIL | GVVVVESGWG | SILPTVILAN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MMNGGPAARS | GKLSIGDQIM | SINGTSLVGL | PLATCQGIIK | GLKNQTQVKL | NIVSCPPVTT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VLIKRPDLKY | QLGFSVQNGI | ICSLMRGGIA | ERGGVRVGHR | IIEINGQSVV | ATAHEKIVQA |
| 730 | 740 | ||||
| LSNSVGEIHM | KTMPAAMFRL | LTGQETPLYI |