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 B9EJ86

Entry ID Method Resolution Chain Position Source
AF-B9EJ86-F1 Predicted AlphaFoldDB

43 variants for B9EJ86

Variant ID(s) Position Change Description Diseaes Association Provenance
rs29341995 4 A>G No EVA
rs30833859 33 D>E No EVA
rs3401540184 39 T>P No EVA
rs3401895316 42 K>R No EVA
rs3401617596 43 M>L No EVA
rs3389127286 44 S>C No EVA
rs221147698 50 D>E No EVA
rs3389123990 51 A>V No EVA
rs233996283 52 N>Y No EVA
rs3389066499 64 L>F No EVA
rs3389129119 109 S>N No EVA
rs1134017736 179 Y>* No EVA
rs1134672000 180 K>E No EVA
rs3389135355 225 G>C No EVA
rs3389125936 227 K>N No EVA
rs3389066569 248 T>I No EVA
rs3389125943 256 W>* No EVA
rs3389126331 263 A>T No EVA
rs3389066519 270 L>F No EVA
rs3389103280 314 S>G No EVA
rs3389123431 315 E>K No EVA
rs3389123410 499 P>A No EVA
rs3389099876 511 Q>* No EVA
rs3389099897 517 P>L No EVA
rs3389066562 522 Y>* No EVA
rs3389127278 524 S>R No EVA
rs3389124032 580 Y>D No EVA
rs3389135415 587 L>F No EVA
rs3389066528 638 H>L No EVA
rs3389119001 641 S>N No EVA
rs3389066575 649 K>R No EVA
rs3389135376 652 N>K No EVA
rs3389092236 664 K>N No EVA
rs3401619219 719 D>V No EVA
rs3401778651 741 W>R No EVA
rs3401778688 769 K>R No EVA
rs3401895312 770 V>L No EVA
rs3389099929 814 S>F No EVA
rs3389066581 814 S>T No EVA
rs3389127302 819 T>R No EVA
rs3389066540 821 R>K No EVA
rs3389092160 824 G>V No EVA
rs1132378008 849 M>I No EVA

No associated diseases with B9EJ86

2 regional properties for B9EJ86

Type Name Position InterPro Accession
domain Pleckstrin homology domain 148 - 267 IPR001849
conserved_site Oxysterol-binding protein, conserved site 510 - 520 IPR018494

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
  • Nucleus membrane
  • The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
cortical endoplasmic reticulum A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
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).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
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.
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.

6 GO annotations of molecular function

Name Definition
cholesterol binding Binding to cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
phosphatidylinositol-4-phosphate binding Binding to phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
phosphatidylserine binding Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine.
phosphatidylserine transfer activity Removes phosphatidylserine from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
sterol binding Binding to a sterol, a steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol.
sterol transporter activity Enables the directed movement of sterols into, out of or within a cell, or between cells. Sterol are steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.

9 GO annotations of biological process

Name Definition
activation of protein kinase B activity Any process that initiates the activity of the inactive enzyme protein kinase B.
fat cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an adipocyte, an animal connective tissue cell specialized for the synthesis and storage of fat.
negative regulation of cell migration Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
negative regulation of sequestering of triglyceride Any process that decreases the rate, frequency or extent of sequestering of triglyceride. Triglyceride sequestration is the process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
phospholipid transport The directed movement of phospholipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Phospholipids are any lipids containing phosphoric acid as a mono- or diester.
positive regulation of glucose import Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
positive regulation of insulin receptor signaling pathway Any process that increases the frequency, rate or extent of insulin receptor signaling.
positive regulation of protein kinase B signaling Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
protein localization to nuclear pore A process in which a protein is transported to, or maintained in, a nuclear pore.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P35843 HES1 Oxysterol-binding protein homolog 5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P35844 KES1 Oxysterol-binding protein homolog 4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P38755 OSH7 Oxysterol-binding protein homolog 7 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9H0X9 OSBPL5 Oxysterol-binding protein-related protein 5 Homo sapiens (Human) PR
Q9BZF1 OSBPL8 Oxysterol-binding protein-related protein 8 Homo sapiens (Human) PR
Q5QNQ6 Osbp2 Oxysterol-binding protein 2 Mus musculus (Mouse) PR
Q8BX94 Osbpl2 Oxysterol-binding protein-related protein 2 Mus musculus (Mouse) PR
Q3B7Z2 Osbp Oxysterol-binding protein 1 Mus musculus (Mouse) PR
10 20 30 40 50 60
MEAALADGEP DRSSLLGDSK DVLGPSTVVA NSDEPQHLTP GKMSQRQGRD ANPTPTRDLP
70 80 90 100 110 120
QPSLSPASLH SQGFERGKED ISQNKDDSSL SMSKSKSESK LYNGSEKDSS TSSKLTKKES
130 140 150 160 170 180
LKVQKKNYRE EKKRATKELL STITDPSVIV MADWLKIRGT LKSWTKLWCV LKPGVLLIYK
190 200 210 220 230 240
TQKNGQWVGT VLLNACEIIE RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS
250 260 270 280 290 300
SYLIIRATSE SDGRCWMDAL ELALKCSSLL KRTMVREGKE HDLSISSDST HVTLYGLLRA
310 320 330 340 350 360
NNLHSGDNFQ LNDSEIERQH FKDQDLYSDK SDKENDPEHD ESDNEVLGKS EESDTDTSER
370 380 390 400 410 420
QDDSYIDPEP VEPLKETTYM EQSHEELGEA GEASQTETVS EENKSLIWTL LKQVRPGMDL
430 440 450 460 470 480
SRVVLPTFIL EPRSFLDKLS DYYYHADFLS EAALEENPYF RLKKVVKWYL SGFYKKPKGL
490 500 510 520 530 540
KKPYNPILGE TFRCLWIHPR TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS
550 560 570 580 590 600
KFYGNSLSAI LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
610 620 630 640 650 660
SAILEFKLKP FLGSSDYVNQ ISGKLKLGKE VLATLEGHWD SEVFINDKKT DNSEIFWNPT
670 680 690 700 710 720
PDIKQWRLIR HTVKFEEQDD FESEKLWQRV TKAINAKDQT EATQEKYVLE EAQRQAARDR
730 740 750 760 770 780
KTKTQEWVCK LFELDPLTGE WHYKFSDTRP WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP
790 800 810 820 830 840
KMKHKPTRQQ KKVVKGYSSP EPDIQDSSGS EAQSVKPSTR RKKGIDLGDI QSSIESIKQT
850 860 870 880
QEEIKRNIMA LRNHLLSSTP ATDYFLQQKD YFVIFLLILL QVIINFIFK