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

186-206 (Activation loop from InterPro)

Target domain

46-300 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q922R0

Entry ID Method Resolution Chain Position Source
AF-Q922R0-F1 Predicted AlphaFoldDB

30 variants for Q922R0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs217940284 4 P>L No EVA
rs3389563528 9 A>V No EVA
rs3389579062 13 D>N No EVA
rs231116765 28 A>V No EVA
rs3389560831 39 A>G No EVA
rs3389560352 59 R>H No EVA
rs3410655480 74 L>* No EVA
rs3389515065 77 M>I No EVA
rs3389563496 88 E>D No EVA
rs3389566686 112 T>A No EVA
rs3389545938 127 P>L No EVA
rs3389579088 141 F>L No EVA
rs3411395255 147 V>L* No EVA
rs3410810088 150 A>G No EVA
rs3409393175 152 E>D No EVA
rs3410388670 152 E>Q No EVA
rs3410760864 153 I>N No EVA
rs3409393040 154 V>L No EVA
rs3411135442 156 A>G No EVA
rs3411022215 157 I>V No EVA
rs3389581531 169 D>N No EVA
rs3410914887 198 T>A No EVA
rs3411022200 199 W>* No EVA
rs3389576666 238 F>I No EVA
rs3389563474 250 Y>H No EVA
rs3389545956 257 K>E No EVA
rs213422169 311 R>K No EVA
rs3389514975 324 D>E No EVA
rs3389566621 333 Y>C No EVA
rs3410879511 334 P>T No EVA

No associated diseases with Q922R0

5 regional properties for Q922R0

Type Name Position InterPro Accession
domain PDZ domain 115 - 196 IPR001478-1
domain PDZ domain 223 - 301 IPR001478-2
domain PDZ domain 329 - 412 IPR001478-3
domain PDZ domain 467 - 548 IPR001478-4
domain PDZ domain 6 492 - 532 IPR041489

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • cAMP induces nuclear translocation
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cAMP-dependent protein kinase complex An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cAMP-dependent protein kinase activity cAMP-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.

14 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
cell adhesion The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
cell-substrate adhesion The attachment of a cell to the underlying substrate via adhesion molecules.
endothelial cell migration The orderly movement of an endothelial cell into the extracellular matrix to form an endothelium.
endothelial cell proliferation The multiplication or reproduction of endothelial cells, resulting in the expansion of a cell population. Endothelial cells are thin flattened cells which line the inside surfaces of body cavities, blood vessels, and lymph vessels, making up the endothelium.
epithelial tube morphogenesis The process in which the anatomical structures of a tube are generated and organized from an epithelium. Epithelial tubes transport gases, liquids and cells from one site to another and form the basic structure of many organs and tissues, with tube shape and organization varying from the single-celled excretory organ in Caenorhabditis elegans to the branching trees of the mammalian kidney and insect tracheal system.
kidney morphogenesis Morphogenesis of a kidney. A kidney is an organ that filters the blood and excretes the end products of body metabolism in the form of urine.
myeloid cell differentiation The process in which a relatively unspecialized myeloid precursor cell acquires the specialized features of any cell of the myeloid leukocyte, megakaryocyte, thrombocyte, or erythrocyte lineages.
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
regulation of cell adhesion Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix.
regulation of cell migration Any process that modulates the frequency, rate or extent of cell migration.
regulation of epithelial cell differentiation involved in kidney development Any process that modulates the frequency, rate or extent of epithelial cell differentiation involved in kidney development.
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.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P00517 PRKACA cAMP-dependent protein kinase catalytic subunit alpha Bos taurus (Bovine) PR
Q03043 for cGMP-dependent protein kinase, isozyme 2 forms cD4/T1/T3A/T3B Drosophila melanogaster (Fruit fly) SS
P16911 Pka-C2 cAMP-dependent protein kinase catalytic subunit 2 Drosophila melanogaster (Fruit fly) PR
P17612 PRKACA cAMP-dependent protein kinase catalytic subunit alpha Homo sapiens (Human) PR
P05132 Prkaca cAMP-dependent protein kinase catalytic subunit alpha Mus musculus (Mouse) PR
P0C605 Prkg1 cGMP-dependent protein kinase 1 Mus musculus (Mouse) SS
Q61410 Prkg2 cGMP-dependent protein kinase 2 Mus musculus (Mouse) PR
P36887 PRKACA cAMP-dependent protein kinase catalytic subunit alpha Sus scrofa (Pig) PR
O62846 PRKACG cAMP-dependent protein kinase catalytic subunit gamma Macaca mulatta (Rhesus macaque) PR
P21137 kin-1 cAMP-dependent protein kinase catalytic subunit Caenorhabditis elegans PR
Q7JP68 F47F2.1 cAMP-dependent protein kinase, catalytic subunit-like Caenorhabditis elegans PR
10 20 30 40 50 60
MEPPAGAAAT VKDPDHDPVK TKVSAPAADP KPRTSSQKAG HSLQDWDTIA TVGTGTFGRV
70 80 90 100 110 120
NLVKEKTGRQ YCALKIMSIP DVIRLKQEQH VQNEKAVLKE INHPFLIKLL WTGHDNRFLY
130 140 150 160 170 180
MLMEFVPGGE LFTYLRNRGR FSSVASVFYA TEIVCAIEYL HSKEIVYRDL KPENILLDRE
190 200 210 220 230 240
GHIKLTDFGF AKKLVDRTWT LCGTPEYLAP EVIQSKGHGR AVDWWALGIL IFEMLSGFPP
250 260 270 280 290 300
FFDDNPFGIY QKILACKIDF PRQLDFTSKD LIKKLLVVDR TRRLGNMKNG AEDIKRHRWF
310 320 330 340 350
RGVEWESVPQ RKLKPPIVPK LSGDGDISNF ETYPESELDK TPSVSDKDLE TFKNF