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 Q9VDS5

Entry ID Method Resolution Chain Position Source
AF-Q9VDS5-F1 Predicted AlphaFoldDB

No variants for Q9VDS5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VDS5

No associated diseases with Q9VDS5

2 regional properties for Q9VDS5

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 251 - 448 IPR000198
domain BAR domain 23 - 229 IPR004148

Functions

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

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
neuromuscular junction The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.

3 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.
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.

11 GO annotations of biological process

Name Definition
imaginal disc-derived leg morphogenesis The process in which the anatomical structures of a leg derived from an imaginal disc are generated and organized. A leg is a limb on which an animal walks and stands. An example of this is found in Drosophila melanogaster.
negative regulation of actin filament polymerization Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
neuromuscular synaptic transmission The process of synaptic transmission from a neuron to a muscle, across a synapse.
positive regulation of BMP secretion Any process that activates or increases the frequency, rate or extent of BMP secretion.
positive regulation of GTPase activity Any process that activates or increases the activity of a GTPase.
positive regulation of synaptic assembly at neuromuscular junction Any process that activates or increases the frequency, rate or extent of synaptic assembly at neuromuscular junction.
protein localization Any process in which a protein is transported to, or maintained in, a specific location.
regulation of actin cytoskeleton organization Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
regulation of Rac protein signal transduction Any process that modulates the frequency, rate or extent of Rac protein 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.
subsynaptic reticulum organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a subsynaptic reticulum. A subsynaptic reticulum is an elaborate tubulolamellar membrane system that underlies the postsynaptic cell membrane.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32019 INPP5B Type II inositol 1,4,5-trisphosphate 5-phosphatase Homo sapiens (Human) PR
Q9Y3L3 SH3BP1 SH3 domain-binding protein 1 Homo sapiens (Human) PR
Q8K2H3 Fam13b Protein FAM13B Mus musculus (Mouse) PR
Q8K337 Inpp5b Type II inositol 1,4,5-trisphosphate 5-phosphatase Mus musculus (Mouse) PR
Q8BYW1 Arhgap25 Rho GTPase-activating protein 25 Mus musculus (Mouse) PR
P55194 Sh3bp1 SH3 domain-binding protein 1 Mus musculus (Mouse) PR
10 20 30 40 50 60
MKRQFAKIKI AAENLSRSSK SDSKDSELEA IERQVDRYRD TIEKIVRKLP ALSGGGGSGS
70 80 90 100 110 120
GSSEEQDKRT KKNSHYKIAQ ALDESAKELP KDMPLQKVLA NCGELEKTMA ECIIESELET
130 140 150 160 170 180
EAKVVRRLKN ILDKEIQEIS TLKRNVSRTL QEYTSLKRSH EAAIRLEEPA AKVNHIKSQQ
190 200 210 220 230 240
EECELKLEKE RDAWAAQMLE LIAKEDEIVS CIRDYVLNQR NYHERALQHV NASLARIQDT
250 260 270 280 290 300
IQGTEKSRFG TSLKEHLTST NREISYIVEL CCCCLLEHGL EEEGLLRVGC ASTKLRRMKH
310 320 330 340 350 360
ALEAQHVKTP LPLDYQDPHV IGSILKLYLR ELPEPLLTYN LYKDFIRIAE RHSEAERKTE
370 380 390 400 410 420
IKAILTKLPK ENYANLRYLT RFLSIVQQRS ALNKMSSQNL AIVMSPNMLW PRIDKSSNAP
430 440 450 460 470 480
ADYIGQVNSS SAANIIVELL ISQWDYFFIG EVEFYLTLQK QKLFVEGKSK SNSSNENLDR
490 500 510 520 530 540
NDSEVMESPR YGTLRRQKAN APSPPTTNGN GIIMTTSQTS HRPHAKELFP QQTPEKQEKP
550 560 570 580 590 600
AKPPLPNLPQ FQSPAASQPT QTQLEPLPPP PVTPAKPVPM TRTQFFGLDN LPSPTADRKS
610 620 630 640 650 660
TDSIGSFKLK PDVPQKPLLP KRPTVLGVGV PKADGKSDDE GGTTPTQATI DNGNGSVRFK
670 680 690 700 710 720
TEHFLDKLRQ ENGETNGTRE VSSTTKENNH NHDPPATAAD QNQQQAQPQV TTPISPNSFQ
730
TPKRPTVPAP PPPTNWKSSD