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 Q7JP68

Entry ID Method Resolution Chain Position Source
AF-Q7JP68-F1 Predicted AlphaFoldDB

No variants for Q7JP68

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7JP68

No associated diseases with Q7JP68

4 regional properties for Q7JP68

Type Name Position InterPro Accession
domain Protein kinase domain 90 - 344 IPR000719
domain AGC-kinase, C-terminal 345 - 398 IPR000961
active_site Serine/threonine-protein kinase, active site 209 - 221 IPR008271
binding_site Protein kinase, ATP binding site 96 - 119 IPR017441

Functions

Description
EC Number 2.7.11.11 Protein-serine/threonine kinases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 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.

4 GO annotations of molecular function

Name Definition
AMP-activated protein kinase activity Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of AMP.
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.

2 GO annotations of biological process

Name Definition
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
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.

10 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
P16911 Pka-C2 cAMP-dependent protein kinase catalytic subunit 2 Drosophila melanogaster (Fruit fly) PR
Q03043 for cGMP-dependent protein kinase, isozyme 2 forms cD4/T1/T3A/T3B Drosophila melanogaster (Fruit fly) SS
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
Q922R0 Prkx cAMP-dependent protein kinase catalytic subunit PRKX 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
O76360 egl-4 cGMP-dependent protein kinase egl-4 Caenorhabditis elegans PR
10 20 30 40 50 60
MVILSHHKRS PPLLMRLFRI CRFFRRLMSS STSSVESVED ESCSNECSAS FTFDTNNNSR
70 80 90 100 110 120
GNNQVNELAE ETHMKLSITP TRESFSLSQL ERIITIGKGT FGRVELARDK ITGAHYALKV
130 140 150 160 170 180
LNIRRVVDMR QTQHVHNEKR VLLQLKHPFI VKMYASEKDS NHLYMIMEFV PGGEMFSYLR
190 200 210 220 230 240
ASRSFSNSMA RFYASEIVCA LEYIHSLGIV YRDLKPENLM LSKEGHIKMA DFGFAKELRD
250 260 270 280 290 300
RTYTICGTPD YLAPESLART GHNKGVDWWA LGILIYEMMV GKPPFRGKTT SEIYDAIIEH
310 320 330 340 350 360
KLKFPRSFNL AAKDLVKKLL EVDRTQRIGC MKNGTQDVKD HKWFEKVNWD DTLHLRVEPP
370 380 390
IVPTLYHPGD TGNFDDYEED TTGGPLCSQR DRDLFAEW