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

2 structures for Q8K337

Entry ID Method Resolution Chain Position Source
2KIG NMR - A 1-156 PDB
AF-Q8K337-F1 Predicted AlphaFoldDB

61 variants for Q8K337

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388710429 3 Q>H No EVA
rs3388697418 7 I>N No EVA
rs3388705049 36 L>F No EVA
rs3388712978 62 I>F No EVA
rs3388712692 79 F>C No EVA
rs3388717236 100 Q>H No EVA
rs3388705368 115 G>C No EVA
rs3388712961 119 R>I No EVA
rs3388699347 122 L>P No EVA
rs3388715495 140 E>D No EVA
rs258555119 142 E>K No EVA
rs27569320 148 T>R No EVA
rs228479457 153 D>H No EVA
rs3388708857 166 P>Q No EVA
rs244670005 173 A>P No EVA
rs214072899 177 G>E No EVA
rs27569319 178 S>G No EVA
rs3388699397 178 S>N No EVA
rs27569317 219 H>Y No EVA
rs3394712083 225 R>I No EVA
rs27569316 230 L>R No EVA
rs3388710463 242 D>E No EVA
rs3388708798 243 W>R No EVA
rs226516197 259 V>G No EVA
rs215749350 262 V>L No EVA
rs27553892 281 P>L No EVA
rs3388697452 303 R>H No EVA
rs3388711857 304 S>P No EVA
rs3388710412 307 V>L No EVA
rs3388699328 320 K>* No EVA
rs3388712947 322 G>A No EVA
rs234123379 329 R>K No EVA
rs3388711447 393 F>L No EVA
rs3388708865 396 T>S No EVA
rs3388708745 429 L>F No EVA
rs3388703338 478 N>I No EVA
rs3388711852 523 L>M No EVA
rs3388704974 542 K>R No EVA
rs27553830 545 E>Q No EVA
rs3388712680 573 E>V No EVA
rs3388699346 617 S>C No EVA
rs3388711846 675 R>W No EVA
rs3388711884 681 N>K No EVA
rs3388712950 685 M>V No EVA
rs3388717234 718 W>C No EVA
rs3388711866 726 G>V No EVA
rs27553789 766 E>D No EVA
rs3388705391 771 Y>C No EVA
rs3388711501 820 R>M No EVA
rs3388699381 844 A>V No EVA
rs250583060 874 Q>H No EVA
rs215534666 876 C>R No EVA
rs3388708860 905 S>N No EVA
rs3388705423 920 I>V No EVA
rs227763350 921 L>S No EVA
rs3394536588 930 V>A No EVA
rs3394712795 931 F>I No EVA
rs3394786789 932 N>K No EVA
rs3394805459 933 Y>* No EVA
rs3388704976 948 N>D No EVA
rs13468788 993 L>P No EVA

No associated diseases with Q8K337

6 regional properties for Q8K337

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 821 - 993 IPR000198
domain Inositol polyphosphate-related phosphatase 343 - 644 IPR000300
domain Endonuclease/exonuclease/phosphatase 350 - 629 IPR005135
domain INPP5B, PH domain 1 - 147 IPR031896
domain OCRL1/INPP5B, INPP5c domain 345 - 638 IPR037793
domain Inositol polyphosphate 5-phosphatase OCRL, RhoGAP 772 - 990 IPR047078

Functions

Description
EC Number 3.1.3.36 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm, cytosol
  • Endoplasmic reticulum-Golgi intermediate compartment
  • Early endosome membrane
  • Membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cytoplasmic vesicle, phagosome membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
early endosome membrane The lipid bilayer surrounding an early endosome.
endoplasmic reticulum-Golgi intermediate compartment A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
phagocytic vesicle membrane The lipid bilayer surrounding a phagocytic vesicle.

4 GO annotations of molecular function

Name Definition
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-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.
metal ion binding Binding to a metal ion.
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.

7 GO annotations of biological process

Name Definition
flagellated sperm motility The directed, self-propelled movement of a cilium (aka flagellum) that contributes to the movement of a flagellated sperm.
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.
inositol phosphate dephosphorylation The process of removing a phosphate group from any mono- or polyphosphorylated inositol.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
regulation of protein processing Any process that modulates the frequency, rate or extent of protein processing, a protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
spermatogenesis The developmental process by which male germ line stem cells self renew or give rise to successive cell types resulting in the development of a spermatozoa.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VDS5 RhoGAP92B Rho GTPase-activating protein 92B Drosophila melanogaster (Fruit fly) PR
Q9NRR6 INPP5E Phosphatidylinositol polyphosphate 5-phosphatase type IV Homo sapiens (Human) PR
Q92835 INPP5D Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Homo sapiens (Human) PR
Q9Y3L3 SH3BP1 SH3 domain-binding protein 1 Homo sapiens (Human) PR
P32019 INPP5B Type II inositol 1,4,5-trisphosphate 5-phosphatase Homo sapiens (Human) PR
Q9ES52 Inpp5d Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Mus musculus (Mouse) PR
Q8K2H3 Fam13b Protein FAM13B Mus musculus (Mouse) PR
P55194 Sh3bp1 SH3 domain-binding protein 1 Mus musculus (Mouse) PR
Q8BYW1 Arhgap25 Rho GTPase-activating protein 25 Mus musculus (Mouse) PR
Q6NVF0 Ocrl Inositol polyphosphate 5-phosphatase OCRL Mus musculus (Mouse) PR
P97573 Inpp5d Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MDQSVAIQET LVEGEYCVIA VQGVLCKGDS RQSRLLGLVR YRLENDAQEH ALFLYTHRRM
70 80 90 100 110 120
AITGDDVSLD QIVPLSKDFM LEEVSPDGEL YILGSDVTVQ LNTAELKLVF QLPFGSHTRT
130 140 150 160 170 180
FLQEVARACP GFDPETRDPE FEWLSRHTCA EPDAESPKPR EWNSDPGTRS GFAPIGGSRH
190 200 210 220 230 240
QSRNARRGLE DVLPRGPGYI LLWGGAAEEP EFLLAEEMHE GGPVRGRRPL AGRRDEALEE
250 260 270 280 290 300
ADWEMSAGGG SRERDCAGVS NVDSSRPNGR GPDQPSGARC PEKPENSLTR QNKSKSDMSE
310 320 330 340 350 360
KVRSATVTVS DKAHILSVQK FGLRDTIVRS HLVQKEENYT YIQNFRFFVG TYNVNGQSPK
370 380 390 400 410 420
ECLRPWLSHS ALAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSESL HPDAKYAKVK
430 440 450 460 470 480
FVRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQLH NTSICVVNSH
490 500 510 520 530 540
LAAHTEEYER RNQDYRDICS RMQFPQVDPS QPPLTINKHD VILWLGDLNY RIEELDVGKV
550 560 570 580 590 600
KKLVEEKAFQ TLYAHDQLKI QVAARTIFDG FTEGEITFQP TYKYDTGSDD WDTSEKCRAP
610 620 630 640 650 660
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNEELYRK TLEEIVRSLD
670 680 690 700 710 720
KMENANIPSV TLSKREFCFE NVKYMQLQTE SFTIHNSQVP CQFEFINKPD EESYCKQWLT
730 740 750 760 770 780
ARPSKGFLLP DSHVEIELEL FVNKSTATKL NSGKDTIEDI LVLHLERGKD YFLSVSGNYL
790 800 810 820 830 840
PSCFGSPIHT LCYMREPILD LPLKTVSDLT LMSVQTADDR SQLENPMEIP KELWMMVDYL
850 860 870 880 890 900
YRNAVQQEDL FQQPGLRPEF DHIRDCLDTG MIDQLCANNH SVAEALLLFL ESLPEPVICY
910 920 930 940 950 960
SAYHSCLECS GNYAASKQII LTLPSFHKNV FNYLMAFLQE LLKNSANNHL DENILASIFG
970 980 990
SLLLRNPARH QKLDMAEKKK AQEFIHQFLC GPL