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 Q6ZQ82

Entry ID Method Resolution Chain Position Source
AF-Q6ZQ82-F1 Predicted AlphaFoldDB

41 variants for Q6ZQ82

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389447934 55 S>L No EVA
rs3389512165 68 K>N No EVA
rs3389501567 69 F>L No EVA
rs3389503827 76 E>* No EVA
rs3389466271 128 R>M No EVA
rs3389499211 143 G>A No EVA
rs3389492501 152 S>F No EVA
rs3389410478 157 E>V No EVA
rs3389501555 172 Q>* No EVA
rs3389499266 198 E>K No EVA
rs3389410550 250 M>V No EVA
rs3389494576 267 T>I No EVA
rs3389496049 287 H>Y No EVA
rs3389500308 288 Y>C No EVA
rs3389466300 311 G>E No EVA
rs3389494591 346 V>L No EVA
rs3389410523 375 R>G No EVA
rs3408357828 408 Q>R No EVA
rs3389457539 439 D>V No EVA
rs3389501571 486 V>L No EVA
rs3389499237 525 V>L No EVA
rs3389457487 547 I>F No EVA
rs3389479134 551 K>N No EVA
rs3389503754 554 N>S No EVA
rs3389466274 567 I>T No EVA
rs29932603 598 K>E No EVA
rs3389479097 607 V>M No EVA
rs3406562303 616 R>T No EVA
rs224576102 640 S>N No EVA
rs3389499249 642 Q>H No EVA
rs3389514597 648 S>C No EVA
rs3389479118 673 L>F No EVA
rs3407400281 692 T>P No EVA
rs3389512227 742 L>P No EVA
rs3389457572 751 R>S No EVA
rs3408358905 758 F>L No EVA
rs3408500790 761 A>S No EVA
rs3389492548 767 C>Y No EVA
rs3389512198 789 S>A No EVA
rs3389494562 797 G>A No EVA
rs3389500323 810 Y>F No EVA

No associated diseases with Q6ZQ82

7 regional properties for Q6ZQ82

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 383 - 568 IPR000198
domain SH3 domain 756 - 814 IPR001452
domain Pleckstrin homology domain 265 - 371 IPR001849
domain BAR domain 6 - 249 IPR004148
domain GRAF, SH3 domain 759 - 814 IPR035481
domain GRAF, BAR domain 19 - 225 IPR035483
domain GRAF, PH domain 267 - 371 IPR047225

Functions

Description
EC Number
Subcellular Localization
  • Cell junction, focal adhesion
  • Cytoplasm, cytoskeleton
  • Endosome membrane
  • Colocalizes with actin stress fibers and cortical actin structures
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).

2 GO annotations of molecular function

Name Definition
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.

3 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
regulation of small GTPase mediated signal transduction Any process that modulates the frequency, rate or extent of small GTPase mediated signal transduction.
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.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZMW5 ARHGAP26 Rho GTPase-activating protein 26 Gallus gallus (Chicken) PR
Q7YQL6 OPHN1 Oligophrenin-1 Pan troglodytes (Chimpanzee) PR
O60890 OPHN1 Oligophrenin-1 Homo sapiens (Human) PR
A6NI28 ARHGAP42 Rho GTPase-activating protein 42 Homo sapiens (Human) PR
Q9UNA1 ARHGAP26 Rho GTPase-activating protein 26 Homo sapiens (Human) PR
B2RQE8 Arhgap42 Rho GTPase-activating protein 42 Mus musculus (Mouse) PR
Q99J31 Ophn1 Oligophrenin-1 Mus musculus (Mouse) PR
P0CAX5 Ophn1 Oligophrenin-1 Rattus norvegicus (Rat) PR
B5DFQ4 arhgap26 Rho GTPase-activating protein 26 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MGLPALEFSD CCLDSPHFRE TLKSHEAELD KTNKFIKELI KDGKSLISAL KNLSSAKRKF
70 80 90 100 110 120
ADSLNEFKFQ CIGDAETDDE MCIARSLQEF AAVLRNLEDE RSRMIENASE VLITPLEKFR
130 140 150 160 170 180
KEQIGAAREA KKKYDKETEK YCGTLEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
190 200 210 220 230 240
YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FGDFKTQLTI SIQNTRNRFE
250 260 270 280 290 300
GTRSEVESLM KKMKENPLEH KTISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRDSKQITM
310 320 330 340 350 360
VPFDQKSGGK GGEDESVTLK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
370 380 390 400 410 420
MEAMDGREPV YNSNRDSQSE GTAQLDSIGF SIIRKCIHAV ETRGINEQGL YRIVGVNSRV
430 440 450 460 470 480
QKLLSVLMDP KAASETETDI CAEWEIKTVT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
490 500 510 520 530 540
NQETRVSEIH SLVHRLPEKN RQMLQLLMNH LANVANNHKQ NLMTVANLGV VFGPTLLRPQ
550 560 570 580 590 600
EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPDVPLTNAQ LHLSRKKSSD SKPPSCSKRP
610 620 630 640 650 660
LTLFHAVPST EKQEQRNSII NSSLESVSSS ANSILNSSSS LQPNLNSSDS NLDVVKPSRP
670 680 690 700 710 720
SSLPPNPSPT SPLSPSWPMF SAPSSPMPTS STSSDSSPIR SVAGFVWFSV AAVVLSLAWS
730 740 750 760 770 780
SLHAVFSLLV NFVPCHPNLH LLFDRPEEAV REDSSTPFRK AKALYACQAE HDSELSFTAG
790 800 810
TVFDNVHPSQ EPGWLEGTLN GKTGLIPENY VEFL