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 Q99K30

Entry ID Method Resolution Chain Position Source
AF-Q99K30-F1 Predicted AlphaFoldDB

35 variants for Q99K30

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3412926984 11 P>L No EVA
rs3388944762 13 A>T No EVA
rs3388958657 27 M>K No EVA
rs3388932664 39 Y>F No EVA
rs3388955795 54 V>M No EVA
rs3388955187 92 V>I No EVA
rs220262610 98 D>N No EVA
rs3411928441 112 L>P No EVA
rs3388938443 122 H>D No EVA
rs3388959749 141 Q>H No EVA
rs3388959844 157 E>D No EVA
rs3388959714 199 L>I No EVA
rs3388962782 208 I>L No EVA
rs248229924 236 G>A No EVA
rs3388955221 305 L>H No EVA
rs3388932613 314 E>G No EVA
rs3388938504 319 D>E No EVA
rs3388955773 320 C>Y No EVA
rs3388948457 324 T>P No EVA
rs3388955771 356 L>M No EVA
rs3388962376 360 T>I No EVA
rs3411505396 375 L>V No EVA
rs3388958656 389 P>S No EVA
rs3388932621 430 L>P No EVA
rs3388959842 476 D>V No EVA
rs243297528 477 I>N No EVA
rs258134016 480 P>A No EVA
rs225384065 480 P>L No EVA
rs258379319 489 G>S No EVA
rs263045959 557 V>M No EVA
rs3388962771 568 Y>* No EVA
rs252727954 634 D>E No EVA
rs3388964744 666 K>N No EVA
rs3388955825 668 E>K No EVA
rs3388955828 689 A>T No EVA

No associated diseases with Q99K30

6 regional properties for Q99K30

Type Name Position InterPro Accession
domain SH3 domain 495 - 554 IPR001452
domain PTB/PI domain 47 - 184 IPR006020
domain Tensin/EPS8 phosphotyrosine-binding domain 51 - 181 IPR013625
domain Epidermal growth factor receptor kinase substrate, phosphotyrosine-binding domain 48 - 178 IPR033928
domain Eps8, SH3 domain 499 - 549 IPR035462
domain SAM domain 626 - 685 IPR041418

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell projection, stereocilium
  • Localizes at the tips of the stereocilia of the inner and outer hair cells
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.
ruffle membrane The portion of the plasma membrane surrounding a ruffle.
stereocilium bundle A bundle of cross-linked stereocilia, arranged around a kinocilium on the apical surface of a sensory hair cell (e.g. a neuromast, auditory or vestibular hair cell). Stereocilium bundles act as mechanosensory organelles by responding to fluid motion or fluid pressure changes.
stereocilium tip A distinct compartment at the tip of a stereocilium, distal to the site of attachment to the apical cell surface. It consists of a dense matrix bridging the barbed ends of the stereocilium actin filaments with the overlying plasma membrane, is dynamic compared to the shaft, and is required for stereocilium elongation.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.

5 GO annotations of biological process

Name Definition
positive regulation of ruffle assembly Any process that activates or increases the frequency, rate or extent of ruffle assembly.
Rac protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Rac family of proteins switching to a GTP-bound active state.
regulation of Rho protein signal transduction Any process that modulates the frequency, rate or extent of Rho protein signal transduction.
Rho protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Rho family of proteins switching to a GTP-bound active state.
sensory perception of sound The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8TE67 EPS8L3 Epidermal growth factor receptor kinase substrate 8-like protein 3 Homo sapiens (Human) PR
Q8TE68 EPS8L1 Epidermal growth factor receptor kinase substrate 8-like protein 1 Homo sapiens (Human) PR
Q9H6S3 EPS8L2 Epidermal growth factor receptor kinase substrate 8-like protein 2 Homo sapiens (Human) PR
Q8R5F8 Eps8l1 Epidermal growth factor receptor kinase substrate 8-like protein 1 Mus musculus (Mouse) PR
Q91WL0 Eps8l3 Epidermal growth factor receptor kinase substrate 8-like protein 3 Mus musculus (Mouse) PR
Q08509 Eps8 Epidermal growth factor receptor kinase substrate 8 Mus musculus (Mouse) PR
10 20 30 40 50 60
MSQSASMSCC PGAANGSLGR SDGVPRMSAK DLFEQRKKYS NSNVIMHETS QYHVQHLATF
70 80 90 100 110 120
IMDKSEAIAS VDDAIRKLVQ LSSKEKVWAQ EVLLQVNDKS LRLLDVESQE ELENFPLPTV
130 140 150 160 170 180
QHSQTVLNQL RYPSVLLLVC QDSDQNKPDI HFFHCDEVEA ELVQEDIESA LADYRLGKKM
190 200 210 220 230 240
RPQTLKGHQE KIRQRQSILP PPQSPAPIPF QRQPGDSPQA KNRVGLPLPV PFSEPGYRRR
250 260 270 280 290 300
ESQDEEPRAV LAQRIEKETQ ILNCTLDDIE WFVARLQKAA EAFKQLNQRK KGKKKNKKGP
310 320 330 340 350 360
AEGVLTLRAR PPSEGEFVDC FQKTKLAINL LAKLQKHIQN PSAAELVHFL FGPLDLIINT
370 380 390 400 410 420
CGSPDIARSV SSPLLSTDAV SFLRGHLVPK EMTLWESLGE TWMRPRSEWP REPQVPLYVP
430 440 450 460 470 480
KFRSGWEPPL DVLQEAPWEV EGLASVPSDQ LTPKNRLSVR HSPKHSLSSE SQAPEDIAPP
490 500 510 520 530 540
GSSPHANRGY QPTPAMTKYV KILYDFTARN ANELSVLKDE VLEVLEDGRQ WWKLRNRSGQ
550 560 570 580 590 600
AGYVPCNILA EARQEDVGAP LEQSGQKYWG PASPTHKLPP IFAGNKEELI HHMDEVNDEL
610 620 630 640 650 660
MKKISHIKTQ PQRNFRVERS QPVHLPLTFE SGPDEVRAWL EAKAFSARIV ENLGILTGPQ
670 680 690 700 710 720
LFSLNKEELK KVCGEEGSRV YSQLTVQKAF LEKQQSGSEL EKLMSKIRRA EDSYTSQHTS
PESEGAPHL