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 P16911

Entry ID Method Resolution Chain Position Source
AF-P16911-F1 Predicted AlphaFoldDB

No variants for P16911

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P16911

No associated diseases with P16911

9 regional properties for P16911

Type Name Position InterPro Accession
repeat Armadillo 112 - 196 IPR000225-1
repeat Armadillo 198 - 239 IPR000225-2
repeat Armadillo 242 - 281 IPR000225-3
repeat Armadillo 283 - 323 IPR000225-4
repeat Armadillo 325 - 365 IPR000225-5
repeat Armadillo 367 - 407 IPR000225-6
repeat Armadillo 410 - 450 IPR000225-7
domain Importin-alpha, importin-beta-binding domain 1 - 102 IPR002652
repeat Atypical Arm repeat 464 - 513 IPR032413

Functions

Description
EC Number 2.7.11.1 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
nucleotide-activated protein kinase complex A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
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.

5 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 kinase A regulatory subunit binding Binding to one or both of the regulatory subunits of protein kinase A.
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.

2 GO annotations of biological process

Name Definition
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
protein kinase A signaling A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase A, which occurs as a result of a single trigger reaction or compound.

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
Q8MJ44 PRKACA cAMP-dependent protein kinase catalytic subunit alpha Canis lupus familiaris (Dog) (Canis familiaris) 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
Q922R0 Prkx cAMP-dependent protein kinase catalytic subunit PRKX Mus musculus (Mouse) PR
P05132 Prkaca cAMP-dependent protein kinase catalytic subunit alpha 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
Q7JP68 F47F2.1 cAMP-dependent protein kinase, catalytic subunit-like Caenorhabditis elegans PR
P21137 kin-1 cAMP-dependent protein kinase catalytic subunit Caenorhabditis elegans PR
10 20 30 40 50 60
MSQHTSQYVF NSKEDYNVIL DNMSREFEER WNHQTQSPYT NLENYITRAV LGNGSFGTVM
70 80 90 100 110 120
LVREKSGKNY YAAKMMSKED LVRLKQVAHV HNEKHVLNAA RFPFLIYLVD STKCFDYLYL
130 140 150 160 170 180
ILPLVNGGEL FSYHRRVRKF NEKHARFYAA QVALALEYMH KMHLMYRDLK PENILLDQRG
190 200 210 220 230 240
YIKITDFGFT KRVDGRTSTL CGTPEYLAPE IVQLRPYNKS VDWWAFGILV YEFVAGRSPF
250 260 270 280 290 300
AIHNRDVILM YSKICICDYK MPSYFTSQLR SLVESLMQVD TSKRLGNSND GSSDVKSHPW
310 320 330 340 350
FQGVDWFGIL NQEVTAPYQP TISGAEDLSN FENFEFKDRY KSRINRHPEL FANF