Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

104-276 (PDZ tandem)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O08992

Entry ID Method Resolution Chain Position Source
AF-O08992-F1 Predicted AlphaFoldDB

13 variants for O08992

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388666416 9 D>V No EVA
rs3388669293 23 S>F No EVA
rs3388671065 63 N>K No EVA
rs250297689 79 A>T No EVA
rs3388651280 99 G>D No EVA
rs3388659120 104 I>F No EVA
rs3388666497 157 D>N No EVA
rs3388666472 159 V>L No EVA
rs3388670215 161 Q>* No EVA
rs3388666872 194 R>S No EVA
rs27663392 222 I>L No EVA
rs3388675725 227 S>Y No EVA
rs3388675176 270 I>N No EVA

No associated diseases with O08992

3 regional properties for O08992

Type Name Position InterPro Accession
domain Pyruvate kinase, barrel 86 - 418 IPR015793
domain Pyruvate kinase, C-terminal 455 - 571 IPR015795
active_site Pyruvate kinase, active site 308 - 320 IPR018209

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus, nucleolus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

14 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.
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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
extracellular exosome A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
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).
interleukin-5 receptor complex A protein complex that binds interleukin-3; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-5 receptor, whereas the beta chain is shared with the receptors for granulocyte-macrophage colony-stimulating factor and interleukin-3.
melanosome A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
membrane raft Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
presynapse The part of a synapse that is part of the presynaptic cell.

13 GO annotations of molecular function

Name Definition
cell adhesion molecule binding Binding to a cell adhesion molecule.
ephrin receptor binding Binding to an ephrin receptor.
frizzled binding Binding to a frizzled (fz) receptor.
growth factor binding Binding to a growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate.
identical protein binding Binding to an identical protein or proteins.
interleukin-5 receptor binding Binding to an interleukin-5 receptor.
ionotropic glutamate receptor binding Binding to an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels.
neurexin family protein binding Binding to a neurexin, a synaptic cell surface protein related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals.
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
protein heterodimerization activity Binding to a nonidentical protein to form a heterodimer.
protein sequestering activity Binding to a protein to prevent it from interacting with other partners or to inhibit its localization to the area of the cell or complex where it is active.
protein-containing complex binding Binding to a macromolecular complex.
syndecan binding Binding to syndecan, an integral membrane proteoglycan (250-300 kDa) associated largely with epithelial cells.

13 GO annotations of biological process

Name Definition
negative regulation of receptor internalization Any process that stops, prevents, or reduces the frequency, rate or extent of receptor internalization.
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
positive regulation of cell growth Any process that activates or increases the frequency, rate, extent or direction of cell growth.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
positive regulation of cell population proliferation Any process that activates or increases the rate or extent of cell proliferation.
positive regulation of epithelial to mesenchymal transition Any process that increases the rate, frequency, or extent of epithelial to mesenchymal transition. Epithelial to mesenchymal transition is where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell.
positive regulation of exosomal secretion Any process that activates or increases the frequency, rate or extent of exosomal secretion.
positive regulation of extracellular exosome assembly Any process that activates or increases the frequency, rate or extent of extracellular vesicular exosome assembly.
positive regulation of phosphorylation Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
positive regulation of transforming growth factor beta receptor signaling pathway Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
presynapse assembly The aggregation, arrangement and bonding together of a set of components to form a presynapse.
Ras protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state.
regulation of mitotic cell cycle Any process that modulates the rate or extent of progress through the mitotic cell cycle.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O00560 SDCBP Syntenin-1 Homo sapiens (Human) EV
Q9H190 SDCBP2 Syntenin-2 Homo sapiens (Human) SS
B2RUJ5 Apba1 Amyloid-beta A4 precursor protein-binding family A member 1 Mus musculus (Mouse) SS
P98084 Apba2 Amyloid-beta A4 precursor protein-binding family A member 2 Mus musculus (Mouse) SS
Q99JZ0 Sdcbp2 Syntenin-2 Mus musculus (Mouse) SS
Q9JI92 Sdcbp Syntenin-1 Rattus norvegicus (Rat) SS
Q4KLN0 Sdcbp2 Syntenin-2 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MVVGTKKYSN LDFVPTISDS EDDVPILDSS DDEKVEAKKT TKKRKGKNNK KKVSEGDNLD
70 80 90 100 110 120
EDVHEDLDAG FKFDLDADDT TSNFQGWNFL AEGESNKDDA EAFVKKDVDL DKIIRRKGGL
130 140 150 160 170 180
VKMAHIDSKQ EEETEKEKVE KENDSDDEEL AMDGFGMGAP MNNGDENQSE EEEEEEEKEE
190 200 210 220 230 240
EEEEEEEQEE MTLEKGGKDD EIDEEDDSEE AKADFYAPET EGDEAKKQMY ENFNSLSLSR
250 260 270 280 290 300
PVLKGLASLG YVKPSPIQSA TIPIALLGKD IIAGAVTGSG KTAAFMIPII ERLLYKPAKI
310 320 330 340 350 360
ASTRVIVLLP TRELAIQVAD VGKQIARFVS GITFGLAVGG LNLRQQEQML KSRPDIVIAT
370 380 390 400 410 420
PGRFIDHIRN SASFNVDSVE ILVMDEADRM LEEGFQDELN EIMGLLPSNR QNLLFSATMN
430 440 450 460 470 480
SKIKSLVSLS LKKPVRIMID PPKKAATKLT QEFVRIRKRD HLKPALLFNL IRKLDPTGQK
490 500 510 520 530 540
RIVVFVARKE TAHRLRIIMG LLGMSVGELH GSLTQEQRLD SVNKFKNLEV PVLICTDLAS
550 560 570 580 590 600
RGLDIPKIEV VINYDMPKSY EIYLHRVGRT ARAGREGRSV TFVGESSQDR SIVRAAIKSV
610 620 630 640 650 660
EENKSLTQGK ALGRNVDWVQ IEETNKLVES MNDTIEDILV EEKEEKEILR AEMQLRKGEN
670 680 690 700 710 720
MLKHKKEIQA RPRRTWFQSE SDKKNSKVLG ALSRNKKVTN SKKRKREEAK ADGNGARSYR
730 740 750
KTKTDRIADQ ERTFKKQKST NSNKKKGFKS RR