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

1 structures for Q91WF7

Entry ID Method Resolution Chain Position Source
AF-Q91WF7-F1 Predicted AlphaFoldDB

47 variants for Q91WF7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389095958 51 V>E No EVA
rs3389083341 64 R>G No EVA
rs3389106680 65 E>K No EVA
rs3389070471 100 R>S No EVA
rs3389097938 102 L>F No EVA
rs3389070510 198 Q>H No EVA
rs3389092096 261 L>V No EVA
rs3389105338 266 P>S No EVA
rs3401367046 284 F>I No EVA
rs1135218776 297 N>K No EVA
rs3389100655 298 E>G No EVA
rs3389096154 312 S>F No EVA
rs3389091968 315 A>T No EVA
rs3389041029 385 K>* No EVA
rs3389095897 406 P>S No EVA
rs3389098121 439 S>R No EVA
rs3389095926 442 K>R No EVA
rs3389070499 464 W>R No EVA
rs3389089594 477 L>F No EVA
rs3389083406 505 L>P No EVA
rs3389096118 519 N>D No EVA
rs3401077174 570 I>T No EVA
rs3389070495 572 Q>K No EVA
rs3389105390 596 G>V No EVA
rs3389096166 605 P>A No EVA
rs3389063496 619 K>Q No EVA
rs3389096505 628 R>I No EVA
rs3389106264 638 E>K No EVA
rs3401088072 648 D>E No EVA
rs3389098166 648 D>G No EVA
rs3401088140 649 E>A No EVA
rs3389106267 650 V>D No EVA
rs3389040980 657 K>* No EVA
rs3389096469 666 R>K No EVA
rs3389105386 707 G>S No EVA
rs225624568 730 N>S No EVA
rs3389100633 753 A>T No EVA
rs3389070511 779 V>A No EVA
rs3389070489 791 T>S No EVA
rs3389092054 837 Q>R No EVA
rs3389096537 869 D>N No EVA
rs3401063473 876 F>L No EVA
rs3401063507 877 Q>E No EVA
rs3400509748 890 L>CQGAA* No EVA
rs3401063534 892 K>* No EVA
rs3400980138 892 K>T No EVA
rs36444045 905 R>C No EVA

1 associated diseases with Q91WF7

Without disease ID

1 regional properties for Q91WF7

Type Name Position InterPro Accession
domain SAC domain 93 - 547 IPR002013

Functions

Description
EC Number 3.1.3.16 Phosphoric monoester hydrolases
Subcellular Localization
  • Endosome membrane
  • Localization requires VAC14 and PIKFYVE
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endosome membrane The lipid bilayer surrounding an endosome.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
lipid droplet An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
recycling endosome An organelle consisting of a network of tubules that functions in targeting molecules, such as receptors transporters and lipids, to the plasma membrane.

7 GO annotations of molecular function

Name Definition
phosphatidylinositol bisphosphate phosphatase activity Catalysis of the reaction: phosphatidylinositol bisphosphate + H2O = phosphatidylinositol phosphate + phosphate.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Catalysis of the reaction: phosphatidylinositol-3,4,5-trisphosphate + H2O = phosphatidylinositol-3,4-bisphosphate + phosphate.
phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Catalysis of the reaction: phosphatidylinositol-3,5-bisphosphate + H2O = phosphatidylinositol-3-phosphate + orthophosphate.
phosphatidylinositol-3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.
phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
phosphatidylinositol-4-phosphate phosphatase activity Catalysis of the reaction: phosphatidylinositol-4-phosphate + H2O = phosphatidylinositol + orthophosphate.
protein serine/threonine phosphatase activity Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.

10 GO annotations of biological process

Name Definition
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.
myelin assembly The process in which the wraps of cell membrane that constitute myelin are laid down around an axon in the central or peripheral nervous system.
myelination The process in which myelin sheaths are formed and maintained around neurons. Oligodendrocytes in the brain and spinal cord and Schwann cells in the peripheral nervous system wrap axons with compact layers of their plasma membrane. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
negative regulation of myelination Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
neuron development The process whose specific outcome is the progression of a neuron over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
phosphatidylinositol metabolic process The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
pigmentation The accumulation of pigment in an organism, tissue or cell, either by increased deposition or by increased number of cells.
positive regulation of neuron projection development Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
vacuole organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a vacuole.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P42837 FIG4 Polyphosphoinositide phosphatase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q92562 FIG4 Polyphosphoinositide phosphatase Homo sapiens (Human) PR
10 20 30 40 50 60
MPTAAAPIIS SVQKLVLYET RARYFLVGSN HAETKYRVLK IDRTEPKDLV VIDDRHVYTQ
70 80 90 100 110 120
QEVRELLGRL DLGNRTKMSQ KGSSGLFRAV SAFGVVGFVR FLEGYYIVLI TKRRKMADIG
130 140 150 160 170 180
GHAIYKIEDT SMIYIPNDSV RISHPDEARY LRIFQNVDLS SNFYFSYSYD LSHSLQYNLT
190 200 210 220 230 240
VLRMPLEMLK SETSKACQES FDIFEDEGLI TQGGSGVFGI SSEPYMKYVW NGELLDIIKN
250 260 270 280 290 300
TVHRDWLLYI IHGFCGQSKL LIYGRPVYVT LIARRSSRFA GTRFLKRGAN CEGDVANEVE
310 320 330 340 350 360
TEQILCDASV MSFTAGSYSS YVQVRGSVPL FWSQDISTMM PKPPITLDQA DPFAHVAALH
370 380 390 400 410 420
FDQMLQRFGS PIIILNLVKE REKRKHERIL SEELVAAVTY LNQFLPPEHT IVYIPWDMAK
430 440 450 460 470 480
YTKSKLCNVL DRLNVIAESV VKKTGFFVNR PDSYCSILRP DEKWNELGGH VIPTGRLQTG
490 500 510 520 530 540
ILRTNCVDCL DRTNTAQFMV GKCALAYQLY SLGLIDKPNL QFDTDAVRLF EELYEDHGDT
550 560 570 580 590 600
LSLQYGGSQL VHRVKTYRKI APWTQHSKDI MQTLSRYYSN AFSDADRQDS INLFLGVFHP
610 620 630 640 650 660
TEGKPHLWEL PTDFYLHHKN TMSLLPPRRS YTYWWTPEVV KHLPLPYDEV ICAANLKKLM
670 680 690 700 710 720
VKKFHRWEEE IDIHNEFFRP YELSSFDDTF CLAMTSSARD FMPKTVGIDP SPFTVRKPDE
730 740 750 760 770 780
TGKSVLGNKN TREEAVLQRK TAASAPPPPS EEAVSSSSED DSGTDREDEG SISQRSTPVK
790 800 810 820 830 840
MTDTGDSAKA TENVVQPMKE VYGVSLSSSL SEEDHSIYAR FVQLGQSQHK QDRGNQQLCS
850 860 870 880 890 900
RCSDGVIKLT PISAFSQDNI YEVQPPRVDR KSTEIFQAHI QASQGIMQPL GKEDTAMYRE
YIRNRYL