Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

7 structures for Q2M3X8

Entry ID Method Resolution Chain Position Source
4B1U X-ray 200 A M 133-164 PDB
4B1V X-ray 175 A M/N 133-164 PDB
4B1W X-ray 195 A M 417-448 PDB
4B1X X-ray 180 A M 455-486 PDB
4B1Y X-ray 129 A M 493-524 PDB
4B1Z X-ray 330 A M/N 414-528 PDB
AF-Q2M3X8-F1 Predicted AlphaFoldDB

24 variants for Q2M3X8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389279238 41 L>F No EVA
rs3389276176 54 D>V No EVA
rs3389253274 73 A>P No EVA
rs3389263589 78 S>Y No EVA
rs3389272990 80 N>K No EVA
rs3389263588 130 S>G No EVA
rs3389280211 138 A>S No EVA
rs3389208558 141 E>G No EVA
rs3389208539 142 R>K No EVA
rs3389277359 145 S>T No EVA
rs3413117599 159 L>S No EVA
rs3389253259 176 D>N No EVA
rs3389280210 208 S>P No EVA
rs3389288873 242 P>Q No EVA
rs3412243596 266 S>I No EVA
rs3389296118 273 Q>H No EVA
rs3389272946 275 H>L No EVA
rs3404168074 320 L>H No EVA
rs3389253323 368 V>L No EVA
rs3389279173 377 E>D No EVA
rs3389281247 416 M>K No EVA
rs3389276224 440 K>E No EVA
rs3389276194 562 S>C No EVA
rs3389288870 570 L>F No EVA

No associated diseases with Q2M3X8

1 regional properties for Q2M3X8

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 147 - 416 IPR017452

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Synapse
  • Nucleus
  • Enriched at synapses (By similarity)
  • Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation
  • Interaction with actin prevents nuclear import
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
protein phosphatase 1 binding Binding to a protein phosphatase 1.
protein phosphatase inhibitor activity Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.

9 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
actin cytoskeleton reorganization A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins.
actomyosin structure organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments.
cell motility Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another.
cerebral cortex development The progression of the cerebral cortex over time from its initial formation until its mature state. The cerebral cortex is the outer layered region of the telencephalon.
dendrite arborization The process in which the anatomical structures of a dendritic tree are generated and organized into dendritic branches.
regulation of neuron migration Any process that modulates the frequency, rate or extent of neuron migration.
regulation of phosphorylation Any process that modulates the frequency, rate or extent of addition of phosphate groups into a molecule.
stress fiber assembly The aggregation, arrangement and bonding together of a set of components to form a stress fiber. A stress fiber is a contractile actin filament bundle that consists of short actin filaments with alternating polarity.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P33304 AFR1 Protein AFR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9C0D0 PHACTR1 Phosphatase and actin regulator 1 Homo sapiens (Human) PR
Q8IZ21 PHACTR4 Phosphatase and actin regulator 4 Homo sapiens (Human) PR
P62024 Phactr1 Phosphatase and actin regulator 1 Rattus norvegicus (Rat) PR
Q6PEI3 phactr4b Phosphatase and actin regulator 4B Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS SEDDIDRRPI
70 80 90 100 110 120
RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP GTHTPPIRRR SKFANLGRIF
130 140 150 160 170 180
KPWKWRKKKS EKFKHTSAAL ERKISMRQSR EELIKRGVLK EIYDKDGELS ISNEDDSLEN
190 200 210 220 230 240
GQSLSSSQLS LPALSEMEPV PMPRDPCSYE VLQASDIMDG PDPGAPVKLP CLPVKLSPPL
250 260 270 280 290 300
PPKKVLICMP VGGPELTLAS YAAQKSSQQA VAQHHHTVLP SQMQHQLQYG SHGQHLPSST
310 320 330 340 350 360
GTLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSSDG ITKAGPMGLP
370 380 390 400 410 420
EIRQVPTVVI ECDDNKENVP HEPDYEDSPC LYGREEEEEE EDEDDDASLY TSSLAMKVCR
430 440 450 460 470 480
KDSLAIKLSN RPSKRELEEK NILPRQTDEE RLELRQQIGT KLTRRLSQRP TAEELEQRNI
490 500 510 520 530 540
LKPRNEQEEQ EEKREIKRRL TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK
550 560 570
PWTRLTAADK AAIRKELNEF KSTEMEVHEL SRHLTRFHRP