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 Q6TLK4

Entry ID Method Resolution Chain Position Source
AF-Q6TLK4-F1 Predicted AlphaFoldDB

No variants for Q6TLK4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6TLK4

No associated diseases with Q6TLK4

6 regional properties for Q6TLK4

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 677 - 866 IPR000198
domain WW domain 246 - 280 IPR001202-1
domain WW domain 299 - 333 IPR001202-2
domain WW domain 414 - 447 IPR001202-3
domain SH3 domain 6 - 69 IPR001452
domain Pleckstrin homology domain 477 - 595 IPR001849

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Membrane ; Peripheral membrane protein
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.
endosome A vacuole to which materials ingested by endocytosis are delivered.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

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.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.

4 GO annotations of biological process

Name Definition
positive regulation of GTPase activity Any process that activates or increases the activity of a GTPase.
receptor-mediated endocytosis An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.
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.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8IWW6 ARHGAP12 Rho GTPase-activating protein 12 Homo sapiens (Human) PR
Q12979 ABR Active breakpoint cluster region-related protein Homo sapiens (Human) PR
Q6ZUM4 ARHGAP27 Rho GTPase-activating protein 27 Homo sapiens (Human) PR
Q5SSL4 Abr Active breakpoint cluster region-related protein Mus musculus (Mouse) PR
A2AB59 Arhgap27 Rho GTPase-activating protein 27 Mus musculus (Mouse) PR
10 20 30 40 50 60
MAADVEGDVY VLVEHPFEYT GKDGRLIAIQ PNERCRLLRR STEHWWHVRR EPGGRPFYLP
70 80 90 100 110 120
AQYVRELPAL GDPVPAPQPS VLQQRPTVPE PLAYDYRFVS TPVGADGSSA EPRGRASSLC
130 140 150 160 170 180
GPARQRTSGQ RNSLAPGGPA CLYLRPAAPV RPAQSLDDLA RGGTAPPAGL LGSAGHFKAS
190 200 210 220 230 240
SVAGSWVCPR PLARSDSENV YEAIPDLRCP PRAKSPKQVD EPPEPVYANV ERQPQVTSPR
250 260 270 280 290 300
SAAAPPRLSP VWETHTDAGT GRPYYYNPDT GVTTWESPFE APEGATSPTT SRASVGSGES
310 320 330 340 350 360
LETEWGQYWD EESGRVFFYN PLTGETVWED ETEELEDDPE EQLEMQPSLS PRSPGQQRPP
370 380 390 400 410 420
TPETDYPELL TSYPEEDYSP VGSFSDLGPT SPLVAPPGWS CQITPEKQML YTNQFTQEQW
430 440 450 460 470 480
VRLEDQEGKP YFYNPEDSSV QWELPQVPVP APRSGRKSSQ DSDTPAQASP PEEKIKTLDK
490 500 510 520 530 540
AGVLHRTKTV DKGKRLRKKH WNASWTVLEG GVLTFFKDSK TSAASGLRQP SKLSTPEYTV
550 560 570 580 590 600
ELRGASLSWA PKDKSSKKNV LELRSRDGSE YLIQHDSEAI ISTWHKAIAE GIEELSADLP
610 620 630 640 650 660
QREEGEPSSA DFGSSERLGS WKEEDVRPNA ASPSLNPGSQ ESDLSRVRHK LRKFLQRRPT
670 680 690 700 710 720
LQSLREKGYI KDQVFGCALA QLCERERSPV PRFVQQCIRT VEARGLDIDG LYRISGNLAT
730 740 750 760 770 780
IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE PLFPFSHFHQ FIAAIKLQDP
790 800 810 820 830 840
AQRSRCVRDL VRTLPAPNHD TLRLLIQHLC RVIEHGEQNR MSVQNVAIVF GPTLLRPEME
850 860
EASMPMTMVF QNQVVELILH QCADIFPPH