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 Q62172

Entry ID Method Resolution Chain Position Source
AF-Q62172-F1 Predicted AlphaFoldDB

35 variants for Q62172

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389479240 3 E>G No EVA
rs108901963 9 S>T No EVA
rs3389435036 37 K>N No EVA
rs50973005 53 V>I No EVA
rs3389386469 58 P>H No EVA
rs52227810 65 D>E No EVA
rs3389386513 65 D>V No EVA
rs3389483894 70 K>N No EVA
rs3407531190 87 A>V No EVA
rs3408047188 89 Q>L No EVA
rs51817668 186 V>F No EVA
rs51817668 186 V>L No EVA
rs3389469200 194 L>M No EVA
rs50820629 195 V>A No EVA
rs228739362 207 V>I No EVA
rs262984807 222 K>R No EVA
rs3389454742 315 H>L No EVA
rs3407801303 320 W>R No EVA
rs3406958056 322 I>L No EVA
rs3407801276 325 L>V No EVA
rs3406956850 326 D>V No EVA
rs234003797 330 A>S No EVA
rs3389386546 375 Q>L No EVA
rs3407812145 389 P>H No EVA
rs3389492672 415 D>V No EVA
rs3389477125 420 I>L No EVA
rs3389476948 445 E>V No EVA
rs50354953 515 D>N No EVA
rs50354953 515 D>Y No EVA
rs3389442977 593 L>P No EVA
rs3389467671 599 A>V No EVA
rs3389476907 612 E>V No EVA
rs3389475347 613 R>S No EVA
rs48356103 617 I>T No EVA
rs243068605 617 I>V No EVA

No associated diseases with Q62172

1 regional properties for Q62172

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 192 - 380 IPR000198

Functions

Description
EC Number 7.6.2.2 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
  • Cytoplasm, cytosol
  • Cytoplasm, cytoskeleton, spindle pole
  • Nucleus
  • Mitochondrion
  • Cytosolic protein that transiently associates with the mitotic spindle poles in early prophase, and dissociates from them after completion of mitosis (By similarity)
  • Targeted to the plasma membrane through its interaction with RALB, directed by FGF signaling
  • Docking on the membrane is required to transduce the Ral signal (By similarity)
  • Recruited by RALA to the mitochondrion during mitosis where it regulates mitochondrial fission
  • Nuclear localization is cell cycle dependent while membrane localization is seen in adherent cells
  • The region involved in membrane association could form transmembrane domains and expose a part of the protein extracellularly (By similarity)
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.

8 GO annotations of molecular function

Name Definition
ABC-type glutathione S-conjugate transporter activity Catalysis of the reaction: ATP + H2O + glutathione S-conjugate(in) -> ADP + phosphate + glutathione S-conjugate(out).
ABC-type xenobiotic transporter activity Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATPase-coupled transmembrane transporter activity Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source.
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
small GTPase binding Binding to a small monomeric GTPase.
transmembrane transporter activity Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.
xenobiotic transmembrane transporter activity Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.

10 GO annotations of biological process

Name Definition
doxorubicin transport The directed movement of a doxorubicin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
positive regulation of GTPase activity Any process that activates or increases the activity of a GTPase.
positive regulation of mitochondrial fission Any process that increases the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
positive regulation of protein phosphorylation Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
regulation of Cdc42 protein signal transduction Any process that modulates the frequency, rate or extent of Cdc42 protein signal transduction.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.
small GTPase mediated signal transduction The series of molecular signals in which a small monomeric GTPase relays a signal.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
xenobiotic detoxification by transmembrane export across the plasma membrane A process that reduces or removes the toxicity of a xenobiotic by exporting it outside the cell.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VDG2 Rlip RalA-binding protein 1 Drosophila melanogaster (Fruit fly) PR
Q15311 RALBP1 RalA-binding protein 1 Homo sapiens (Human) PR
10 20 30 40 50 60
MTECFLPPSS SPSEHRRAEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDVLHEPPDT
70 80 90 100 110 120
VSDDDKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKVKRSKGIH VFKKPSFSKK
130 140 150 160 170 180
KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ
190 200 210 220 230 240
MDAPSVKPIF GVPLVDAVER TMMYDGVRLP AVFRECVDYM EKHGMKCEGV YRVSGIKSKV
250 260 270 280 290 300
DELKAAYDRE ESPNLEEYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGKTTEMEKV
310 320 330 340 350 360
QEFQRLLREL PECNHLLLSW LIVHLDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVL
370 380 390 400 410 420
FTHVQELFGT VVLKQVTRPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI
430 440 450 460 470 480
KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN
490 500 510 520 530 540
ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIDRLRAE IAEIQSRQQH GRSETEEYSS
550 560 570 580 590 600
DSESESEDEE ELQLILEDLQ RQNEELEIKN NHLNQAVHEE REAIIELRVQ LRLLQMQRAK
610 620 630 640
SEQQPQEEEE PERRGGIGPP PCDGVLEVRV AKEQAKASPS KDRKETPI