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 Q9D300

Entry ID Method Resolution Chain Position Source
AF-Q9D300-F1 Predicted AlphaFoldDB

17 variants for Q9D300

Variant ID(s) Position Change Description Diseaes Association Provenance
rs258935740 15 S>N No EVA
rs3389125021 18 P>S No EVA
rs3389128909 19 P>H No EVA
rs217454052 25 E>G No EVA
rs3389140173 39 S>T No EVA
rs3389156285 75 E>D No EVA
rs3389125053 84 C>F No EVA
rs3389160128 149 G>V No EVA
rs220473822 150 S>N No EVA
rs216644446 152 V>I No EVA
rs3389155046 166 L>F No EVA
rs229290041 240 R>C No EVA
rs3389156248 381 C>S No EVA
rs3413126640 408 W>* No EVA
rs3389128952 410 Q>L No EVA
rs3389125039 419 P>Q No EVA
rs3389152650 463 L>M No EVA

No associated diseases with Q9D300

9 regional properties for Q9D300

Type Name Position InterPro Accession
domain SH3 domain 215 - 284 IPR001452
domain PDZ domain 130 - 209 IPR001478
domain L27 domain 1 - 110 IPR004172
domain Guanylate kinase-like domain 338 - 525 IPR008144
domain Guanylate kinase/L-type calcium channel beta subunit 337 - 528 IPR008145
domain L27 domain, C-terminal 1 - 53 IPR014775-1
domain L27 domain, C-terminal 58 - 108 IPR014775-2
conserved_site Guanylate kinase, conserved site 373 - 390 IPR020590
domain MPP6, SH3 domain 219 - 279 IPR035603

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

1 GO annotations of molecular function

Name Definition
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.

2 GO annotations of biological process

Name Definition
positive regulation of GTPase activity Any process that activates or increases the activity of a GTPase.
Ras protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state.

14 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8N9B8 RASGEF1A Ras-GEF domain-containing family member 1A Homo sapiens (Human) PR
Q8N431 RASGEF1C Ras-GEF domain-containing family member 1C Homo sapiens (Human) PR
Q02384 Sos2 Son of sevenless homolog 2 Mus musculus (Mouse) SS
Q62245 Sos1 Son of sevenless homolog 1 Mus musculus (Mouse) SS
Q8VCC8 Rapgef3 Rap guanine nucleotide exchange factor 3 Mus musculus (Mouse) SS
Q9EQZ6 Rapgef4 Rap guanine nucleotide exchange factor 4 Mus musculus (Mouse) EV
Q03385 Ralgds Ral guanine nucleotide dissociation stimulator Mus musculus (Mouse) PR
Q9Z1S3 Rasgrp1 RAS guanyl-releasing protein 1 Mus musculus (Mouse) SS
Q8BTM9 Rasgrp4 RAS guanyl-releasing protein 4 Mus musculus (Mouse) SS
Q9QUG9 Rasgrp2 RAS guanyl-releasing protein 2 Mus musculus (Mouse) SS
Q9ERD6 Ralgps2 Ras-specific guanine nucleotide-releasing factor RalGPS2 Mus musculus (Mouse) PR
A2AR50 Ralgps1 Ras-specific guanine nucleotide-releasing factor RalGPS1 Mus musculus (Mouse) PR
Q28EC1 rasgef1b Ras-GEF domain-containing family member 1B Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
A0JM95 rasgef1a Ras-GEF domain-containing family member 1A Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MPRTLTASDM VTPGSLSPPP TESTEGEQAG QPLLDGAPSS ASLDTLIQHL VPTADYYPEK
70 80 90 100 110 120
AYIFTFLLSS RLFIEPRELL ARVCHLCIEQ QQLDKPVLDK ARVRKFGAKL LQLLAEWTET
130 140 150 160 170 180
FPRDFEEEST IGHLTDVVGR ISPCDETYGS RVHQLLQTLH QKLASLGQGP ESLVGADKPI
190 200 210 220 230 240
SYRTKPPASI HRELLGVCSD PYTLAQQLTH VELERLRHIG PEEFVQAFVN KDPLAGTKPR
250 260 270 280 290 300
FSDKTNNVEA YVKWFNRLCY LVATEICMPA KKKQRAQVIE FFIDVARECF NIGNFNSLMA
310 320 330 340 350 360
IISGMNMSPV SRLKKTWAKV KTAKFFILEH QMDPTGNFCN YRTALRGAAH RSLTAHSSRE
370 380 390 400 410 420
KIVIPFFSLL IKDIYFLNEG CANRLPNGHV NFEKFLELAK QVGEFITWKQ VECPFEQDPS
430 440 450 460
ITHYLYTAPI FSEDGLYLAS YESESPESQT EKERWKSLRS SILGKT