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 Q91XU3

Entry ID Method Resolution Chain Position Source
AF-Q91XU3-F1 Predicted AlphaFoldDB

13 variants for Q91XU3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389141797 38 V>E No EVA
rs3389123767 60 N>D No EVA
rs3400571019 123 L>F No EVA
rs3389141169 147 R>L No EVA
rs3389118651 159 I>S No EVA
rs3401551926 185 F>L No EVA
rs3401763459 185 F>Y No EVA
rs29359742 276 L>M No EVA
rs3389096666 293 G>D No EVA
rs3389134603 343 G>D No EVA
rs3389129792 380 D>G No EVA
rs3389071051 395 G>E No EVA
rs3389123710 408 Y>* No EVA

No associated diseases with Q91XU3

1 regional properties for Q91XU3

Type Name Position InterPro Accession
domain Phosphatidylinositol-4-phosphate 5-kinase, core 43 - 421 IPR002498

Functions

Description
EC Number 2.7.1.149 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Endoplasmic reticulum
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
autophagosome A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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).
intracellular organelle Organized structure of distinctive morphology and function, occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 GO annotations of molecular function

Name Definition
1-phosphatidylinositol-4-phosphate 5-kinase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4-phosphate + ATP = 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + ADP + 2 H(+).
1-phosphatidylinositol-5-phosphate 4-kinase activity Catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
identical protein binding Binding to an identical protein or proteins.

7 GO annotations of biological process

Name Definition
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
negative regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity Any process that decreases the frequency, rate or extent of the catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
negative regulation of insulin receptor signaling pathway Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling.
phosphatidylinositol phosphate biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylinositol phosphate.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
positive regulation of autophagosome assembly Any process that activates or increases the frequency, rate or extent of autophagic vacuole assembly.
regulation of autophagy Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.

15 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q17QS4 PIP5KL1 Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 Bos taurus (Bovine) PR
Q0P5F7 PIP4K2C Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma Bos taurus (Bovine) PR
Q99755 PIP5K1A Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha Homo sapiens (Human) PR
P78356 PIP4K2B Phosphatidylinositol 5-phosphate 4-kinase type-2 beta Homo sapiens (Human) PR
Q5T9C9 PIP5KL1 Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 Homo sapiens (Human) PR
Q8TBX8 PIP4K2C Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma Homo sapiens (Human) PR
Q80XI4 Pip4k2b Phosphatidylinositol 5-phosphate 4-kinase type-2 beta Mus musculus (Mouse) PR
Q6U7H8 Pip5kl1 Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 Mus musculus (Mouse) PR
O88370 Pip4k2c Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma Rattus norvegicus (Rat) PR
O48709 PIP5K3 Phosphatidylinositol 4-phosphate 5-kinase 3 Arabidopsis thaliana (Mouse-ear cress) PR
Q56YP2 PIP5K1 Phosphatidylinositol 4-phosphate 5-kinase 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SFB8 PIP5K6 Phosphatidylinositol 4-phosphate 5-kinase 6 Arabidopsis thaliana (Mouse-ear cress) PR
Q8L796 PIP5K2 Phosphatidylinositol 4-phosphate 5-kinase 2 Arabidopsis thaliana (Mouse-ear cress) PR
Q6GL14 pip4k2c Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q6IQE1 pip4k2c Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MASSSVPPAT APAAAGGPGP GFGFASKTKK KHFVQQKVKV FRAADPLVGV FLWGVAHSIN
70 80 90 100 110 120
ELSQVPPPVM LLPDDFKASS KIKVNNHFFH RENLPSHFKF KEYCPQVFRN LRDRFAIDDH
130 140 150 160 170 180
DYLVSLTRSP PSETEGSDGR FLISYDRTLV IKEVSSEDIA DMHSNLSNYH QYIVKCHGNT
190 200 210 220 230 240
LLPQFLGMYR VSVENEDSYM LVMRNMFSHR LPVHRKYDLK GSLVSREASD KEKVKELPTL
250 260 270 280 290 300
KDMDFLNKNQ KVYIGEEEKK VFLEKLKRDV EFLVQLKIMD YSLLLGIHDI IRGSEPEEEG
310 320 330 340 350 360
PVREEESEWD GDCNLAGPPA LVGSYGTSPE GIGGYIHSHR PLGPGEFESF IDVYAIRSAE
370 380 390 400 410 420
GAPQKEVYFM GLIDILTQYD AKKKAAHAAK TVKHGAGAEI STVHPEQYAK RFLDFIANIF
A