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 P97573

Entry ID Method Resolution Chain Position Source
AF-P97573-F1 Predicted AlphaFoldDB

No variants for P97573

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P97573

No associated diseases with P97573

3 regional properties for P97573

Type Name Position InterPro Accession
domain Inositol polyphosphate-related phosphatase 404 - 720 IPR000300
domain SH2 domain 6 - 104 IPR000980
domain Endonuclease/exonuclease/phosphatase 411 - 703 IPR005135

Functions

Description
EC Number 3.1.3.36 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Peripheral membrane protein
  • Membrane raft
  • Cytoplasm, cytoskeleton
  • Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type
  • Translocates from the cytoplasm to membrane ruffles in a FCGR3/CD16-dependent manner
  • Colocalizes with FC-gamma-RIIB receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles
  • Tyrosine phosphorylation may also participate in membrane localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
actin filament A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
cortical cytoskeleton The portion of the cytoskeleton that lies just beneath the plasma membrane.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane raft Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

7 GO annotations of molecular function

Name Definition
inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Catalysis of the reaction: 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
inositol-1,4,5-trisphosphate 5-phosphatase activity Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate.
inositol-4,5-bisphosphate 5-phosphatase activity Catalysis of the reaction: 1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.
inositol-polyphosphate 5-phosphatase activity Catalysis of the reactions: D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate, and 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + 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-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.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.

21 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
determination of adult lifespan The pathways that regulate the duration of the adult phase of the life-cycle of an animal.
immunoglobulin mediated immune response An immune response mediated by immunoglobulins, whether cell-bound or in solution.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
negative regulation of B cell activation Any process that stops, prevents, or reduces the frequency, rate or extent of B cell activation.
negative regulation of B cell proliferation Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
negative regulation of bone resorption Any process that stops, prevents, or reduces the frequency, rate or extent of bone resorption.
negative regulation of granulocyte differentiation Any process that stops, prevents, or reduces the frequency, rate or extent of granulocyte differentiation.
negative regulation of immune response Any process that stops, prevents, or reduces the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus.
negative regulation of interleukin-6 production Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-6 production.
negative regulation of monocyte differentiation Any process that stops, prevents, or reduces the frequency, rate or extent of monocyte differentiation.
negative regulation of neutrophil differentiation Any process that stops, prevents, or reduces the frequency, rate or extent of neutrophil differentiation.
negative regulation of osteoclast differentiation Any process that stops, prevents, or reduces the frequency, rate or extent of osteoclast differentiation.
negative regulation of signal transduction Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
positive regulation of B cell differentiation Any process that activates or increases the frequency, rate or extent of B cell differentiation.
positive regulation of erythrocyte differentiation Any process that activates or increases the frequency, rate or extent of erythrocyte differentiation.
positive regulation of lymphocyte differentiation Any process that activates or increases the frequency, rate or extent of lymphocyte differentiation.
regulation of immune response Any process that modulates the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus.
regulation of signal transduction Any process that modulates the frequency, rate or extent of signal transduction.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NRR6 INPP5E Phosphatidylinositol polyphosphate 5-phosphatase type IV Homo sapiens (Human) PR
P32019 INPP5B Type II inositol 1,4,5-trisphosphate 5-phosphatase Homo sapiens (Human) PR
Q92835 INPP5D Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Homo sapiens (Human) PR
Q6NVF0 Ocrl Inositol polyphosphate 5-phosphatase OCRL Mus musculus (Mouse) PR
Q8K337 Inpp5b Type II inositol 1,4,5-trisphosphate 5-phosphatase Mus musculus (Mouse) PR
Q9ES52 Inpp5d Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Mus musculus (Mouse) PR
10 20 30 40 50 60
MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP
70 80 90 100 110 120
NEDDKFTVQA SEGVPMRFFT KLDQLIEFYK KENMGLVTHL QFPVPLEEED AIDEPEEDTE
130 140 150 160 170 180
SVMSPPELPP RNIPVSGGPC EAKDLPLPTE NPRAPEVTRL SLSETLFQRL QSMDTSGLPE
190 200 210 220 230 240
EHLKAIQDYL STQLMLDSDF LKTGSSNLPH LKKLTSLLCK ELHGEVIRTL PSLESLQRLF
250 260 270 280 290 300
DQQLSPGLRP RPQVPGEANP ITMVAKLSQL TSLLSSIEDK VKALLHEGSE STNRRSLIPP
310 320 330 340 350 360
VTFEVKSESL GIPQKMHLKV DVESGKLIIK KSRDGSEDKF YSHKKILQLI KSQKFLNKLV
370 380 390 400 410 420
ILVETEKEKI LRKEYVFSDS KKREGFCQLL QQMKNKHSEQ SEPDMITIFI GTWNMGNAPP
430 440 450 460 470 480
PKKITSWFLS KGQGKTRDDS ADYIPHDIYV IGTQEDPLGE KEWLEILRHS LQEVTSMTFK
490 500 510 520 530 540
TVAIHTLWNI RIVVLAKPEH ENRISHICTD NVKTGIANTL GNKGAVGVSF MFNGTSLGFV
550 560 570 580 590 600
NSHLTSGSEK KLRRNQNYMN ILRFLALGDK KLSPFNITHR FTHLFWLGDL NYRVELPTWE
610 620 630 640 650 660
AEAIIQKIKQ QQYSDLLAHD QLLLERKEQE VFLHFEEEEI TFAPTYRFER LTRDKYAYTK
670 680 690 700 710 720
QKATGMKYNL PSWCDRVLWK SYPLVHVVCQ SYGSTSDIMT SDHSPVFATF EAGVTSQFVS
730 740 750 760 770 780
KNGPGAVDSQ GQIEFLACYA TLKTKSQTKF YLELHSSCLE SFVKSQEGEN EEGDEGELVV
790 800 810 820 830 840
RFGETLPKLK PIISDPEYLL DQHILISIKS SDSDESYGEG CIALRLETTE SQLPIYTPLT
850 860 870 880 890 900
HHGEMTGHFR GEIKLQTSEG KMREKLYDFV KTERDESSGM KCLKNLTSHD PMRQWEPAGR
910 920 930 940 950 960
VPACGISSLN EIINPNYIGM GPFGQPLHGK STLSPDQQLT AWSYDQLPKD SSLGPGRGEG
970 980 990 1000 1010 1020
PPTPPSQPPL SPKKFSSSTA NRGSCPRVQE TRPGDLGKVE ALPQEDLPLT KPEMFENPLY
1030 1040 1050 1060 1070 1080
GSVSPFPKLV PRKEQESPKM MRKEPPPCPD PGVSSPSIML PKAQEVENVK GTSKQAPVPV
1090 1100 1110 1120 1130 1140
FGPTPRIRSF TCSSSAEGRM PSGDKSQGKP KAPASSQAPV PVKRPVKPSR SEMSQQTTPI
1150 1160 1170 1180
PAPRPPLPVK SPAVLQLQHS KGRDYRDNTE LPHHGKHRQE ESLLGRTAMQ