Descriptions
Autoinhibitory domains (AIDs)
Target domain |
63-251 (Sec7 domain) |
Relief mechanism |
Partner binding |
Assay |
|
Target domain |
63-251 (Sec7 domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Malaby AW et al. (2013) "Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors", Proceedings of the National Academy of Sciences of the United States of America, 110, 14213-8
- DiNitto JP et al. (2007) "Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors", Molecular cell, 28, 569-83
Autoinhibited structure

Activated structure

1 structures for P97696
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-P97696-F1 | Predicted | AlphaFoldDB |
No variants for P97696
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P97696 |
No associated diseases with P97696
Functions
6 GO annotations of cellular component
Name | Definition |
---|---|
adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
bicellular tight junction | An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
2 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. |
phosphatidylinositol-3,4,5-trisphosphate binding | Binding to phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions. |
4 GO annotations of biological process
Name | Definition |
---|---|
establishment of epithelial cell polarity | The specification and formation of anisotropic intracellular organization of an epithelial cell. |
Golgi vesicle transport | The directed movement of substances into, out of or within the Golgi apparatus, mediated by vesicles. |
positive regulation of cell adhesion | Any process that activates or increases the frequency, rate or extent of cell adhesion. |
regulation of ARF protein signal transduction | Any process that modulates the frequency, rate or extent of ARF protein signal transduction. |
15 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q2KI41 | CYTH2 | Cytohesin-2 | Bos taurus (Bovine) | SS |
Q9UIA0 | CYTH4 | Cytohesin-4 | Homo sapiens (Human) | SS |
Q15438 | CYTH1 | Cytohesin-1 | Homo sapiens (Human) | SS |
Q99418 | CYTH2 | Cytohesin-2 | Homo sapiens (Human) | SS |
O43739 | CYTH3 | Cytohesin-3 | Homo sapiens (Human) | EV |
Q9QX11 | Cyth1 | Cytohesin-1 | Mus musculus (Mouse) | SS |
Q80YW0 | Cyth4 | Cytohesin-4 | Mus musculus (Mouse) | SS |
P63034 | Cyth2 | Cytohesin-2 | Mus musculus (Mouse) | SS |
O08967 | Cyth3 | Cytohesin-3 | Mus musculus (Mouse) | EV |
P63035 | Cyth2 | Cytohesin-2 | Rattus norvegicus (Rat) | SS |
P97694 | Cyth1 | Cytohesin-1 | Rattus norvegicus (Rat) | SS |
D4A631 | Arfgef1 | Brefeldin A-inhibited guanine nucleotide-exchange protein 1 | Rattus norvegicus (Rat) | PR |
Q7TSU1 | Arfgef2 | Brefeldin A-inhibited guanine nucleotide-exchange protein 2 | Rattus norvegicus (Rat) | PR |
Q76M68 | Iqsec3 | IQ motif and SEC7 domain-containing protein 3 | Rattus norvegicus (Rat) | SS |
A0A0G2JUG7 | Iqsec1 | IQ motif and SEC7 domain-containing protein 1 | Rattus norvegicus (Rat) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MDEGGGGEGG | SVPEDLSLEE | REELLDIRRR | KKELIDDIER | LKYEIAEVMT | EIDNLTSVEE |
70 | 80 | 90 | 100 | 110 | 120 |
SKTTQRNKQI | AMGRKKFNMD | PKKGIQFLIE | NDLLQSSPED | VAQFLYKGEG | LNKTVIGDYL |
130 | 140 | 150 | 160 | 170 | 180 |
GERDDFNIKV | LQAFVELHEF | ADLNLVQALR | QFLWSFRLPG | EAQKIDRMME | AFASRYCLCN |
190 | 200 | 210 | 220 | 230 | 240 |
PGVFQSTDTC | YVLSFAIIML | NTSLHNHNVR | DKPTAERFIT | MNRGINEGGD | LPEELLRNLY |
250 | 260 | 270 | 280 | 290 | 300 |
ESIKNEPFKI | PEDDGNDLTH | TFFNPDREGW | LLKLGGGRVK | TWKRRWFILT | DNCLYYFEYT |
310 | 320 | 330 | 340 | 350 | 360 |
TDKEPRGIIP | LENLSIREVE | DPRKPNCFEL | YNPSHKGQVI | KACKTEADGR | VVEGNHVVYR |
370 | 380 | 390 | |||
ISAPSPEEKE | EWMKSIKASI | SRDPFYDMLA | TRKRRIANKK |