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Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

PRKACA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca2+, leading to reduced amplitude and increased frequency of store overload-induced Ca2+ release (SOICR) characterized by an increased rate of Ca2+ release and propagation velocity of spontaneous Ca2+ waves, despite reduced wave amplitude and resting cytosolic Ca2+. PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Allosterically activated by various compounds, including ATP. Activated by cAMP; the nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of apo PKA, enhancing the enzyme dynamics synchronously and priming it for catalysis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATP
Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATP
Nucleotide bindingi122 – 1287ATPPROSITE-ProRule annotation
Nucleotide bindingi169 – 1724ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase activity Source: UniProtKB
  3. protein kinase activity Source: AgBase
  4. protein serine/threonine/tyrosine kinase activity Source: Ensembl

GO - Biological processi

  1. cellular response to glucose stimulus Source: Ensembl
  2. cellular response to parathyroid hormone stimulus Source: Ensembl
  3. mesoderm formation Source: AgBase
  4. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: Ensembl
  5. neural tube closure Source: Ensembl
  6. peptidyl-serine phosphorylation Source: Ensembl
  7. peptidyl-threonine phosphorylation Source: Ensembl
  8. positive regulation of cell cycle arrest Source: Ensembl
  9. positive regulation of protein export from nucleus Source: Ensembl
  10. protein autophosphorylation Source: Ensembl
  11. protein phosphorylation Source: AgBase
  12. regulation of osteoblast differentiation Source: Ensembl
  13. regulation of proteasomal protein catabolic process Source: Ensembl
  14. regulation of protein processing Source: Ensembl
  15. regulation of synaptic transmission Source: Ensembl
  16. regulation of tight junction assembly Source: Ensembl
  17. sperm capacitation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.11. 908.
ReactomeiREACT_273496. Recruitment of mitotic centrosome proteins and complexes.
REACT_274117. PKA activation.
REACT_279372. PKA-mediated phosphorylation of CREB.
REACT_286999. Interleukin-3, 5 and GM-CSF signaling.
REACT_288981. PKA-mediated phosphorylation of key metabolic factors.
REACT_289962. Loss of Nlp from mitotic centrosomes.
REACT_301041. DARPP-32 events.
REACT_305537. Gluconeogenesis.
REACT_318110. PKA activation in glucagon signalling.
REACT_325957. Hedgehog 'off' state.
REACT_327729. Degradation of GLI2 by the proteasome.
REACT_333090. GLI3 is processed to GLI3R by the proteasome.
REACT_335146. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_335730. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_335907. Factors involved in megakaryocyte development and platelet production.
REACT_337384. Degradation of GLI1 by the proteasome.
REACT_337905. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_340866. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_341360. Regulation of PLK1 Activity at G2/M Transition.
REACT_344993. Regulation of insulin secretion.
REACT_346955. Anchoring of the basal body to the plasma membrane.
REACT_348169. Rap1 signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit alpha (EC:2.7.11.11)
Short name:
PKA C-alpha
Gene namesi
Name:PRKACA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 7

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. Cell membrane By similarity. Mitochondrion By similarity
Note: Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes (By similarity).By similarity

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: Ensembl
  2. centrosome Source: Ensembl
  3. ciliary base Source: Ensembl
  4. cytoplasm Source: AgBase
  5. extracellular vesicular exosome Source: Ensembl
  6. mitochondrion Source: UniProtKB-SubCell
  7. neuromuscular junction Source: AgBase
  8. nucleus Source: UniProtKB-SubCell
  9. plasma membrane Source: UniProtKB-SubCell
  10. sperm midpiece Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31N → D: No myristoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit alphaPRO_0000086049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei3 – 31Deamidated asparagine; partial3 Publications
Modified residuei11 – 111Phosphoserine; by autocatalysisBy similarity
Modified residuei49 – 491PhosphothreonineBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei196 – 1961PhosphothreonineBy similarity
Modified residuei198 – 1981Phosphothreonine; by PDPK11 Publication
Modified residuei202 – 2021PhosphothreonineBy similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei339 – 3391Phosphoserine1 Publication

Post-translational modificationi

Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-3' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form.4 Publications
Autophosphorylated. Phosphorylation is enhanced by vitamin K2. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (By similarity).By similarity
Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP00517.
PRIDEiP00517.

Miscellaneous databases

PMAP-CutDBP00517.

Expressioni

Tissue specificityi

Ubiquitously expressed in mammalian tissues.

Interactioni

Subunit structurei

A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Activates cAMP-sensitive PKAI and PKAII holoenzymes by interacting with regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively. Interacts with NFKB1, NFKB2 and NFKBIA in platelets; these interactions are disrupted by thrombin and collagen. Binds to ABL1 in spermatozoa and with CDC25B in oocytes (By similarity). Interacts with APOBEC3G and AICDA (By similarity). Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnj3P632516EBI-7251007,EBI-7250981From a different organism.

Protein-protein interaction databases

BioGridi159584. 8 interactions.
IntActiP00517. 4 interactions.
STRINGi9913.ENSBTAP00000008727.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 133Combined sources
Helixi16 – 3217Combined sources
Helixi41 – 433Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi56 – 638Combined sources
Turni64 – 663Combined sources
Beta strandi69 – 768Combined sources
Helixi77 – 826Combined sources
Helixi86 – 9611Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi114 – 1229Combined sources
Helixi129 – 1368Combined sources
Helixi141 – 16020Combined sources
Helixi170 – 1723Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi181 – 1833Combined sources
Helixi186 – 1883Combined sources
Beta strandi199 – 2013Combined sources
Helixi203 – 2053Combined sources
Helixi208 – 2114Combined sources
Helixi219 – 23416Combined sources
Helixi244 – 2529Combined sources
Beta strandi260 – 2623Combined sources
Helixi264 – 27310Combined sources
Turni278 – 2803Combined sources
Turni282 – 2843Combined sources
Turni286 – 2894Combined sources
Helixi290 – 2934Combined sources
Helixi296 – 2983Combined sources
Helixi303 – 3075Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi326 – 3283Combined sources
Turni345 – 3506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KMUmodel-C9-351[»]
1KMWmodel-C9-351[»]
1Q24X-ray2.60A2-351[»]
1Q61X-ray2.10A2-351[»]
1Q62X-ray2.30A2-351[»]
1Q8TX-ray2.00A2-351[»]
1Q8UX-ray1.90A2-351[»]
1Q8WX-ray2.20A2-351[»]
1SMHX-ray2.04A2-351[»]
1STCX-ray2.30E2-351[»]
1SVEX-ray2.49A2-351[»]
1SVGX-ray2.02A2-351[»]
1SVHX-ray2.30A2-351[»]
1SZMX-ray2.50A/B2-351[»]
1VEBX-ray2.89A2-351[»]
1XH4X-ray2.45A2-351[»]
1XH5X-ray2.05A2-351[»]
1XH6X-ray1.90A2-351[»]
1XH7X-ray2.47A2-351[»]
1XH8X-ray1.60A2-351[»]
1XH9X-ray1.64A2-351[»]
1XHAX-ray2.46A2-351[»]
1YDRX-ray2.20E2-351[»]
1YDSX-ray2.20E2-351[»]
1YDTX-ray2.30E2-351[»]
2C1AX-ray1.95A2-351[»]
2C1BX-ray2.00A2-351[»]
2F7EX-ray2.00E1-351[»]
2F7XX-ray1.90E1-351[»]
2F7ZX-ray3.00E1-351[»]
2GFCX-ray1.87A2-351[»]
2GNFX-ray2.28A2-351[»]
2GNGX-ray1.87A2-351[»]
2GNHX-ray2.05A2-351[»]
2GNIX-ray2.27A2-351[»]
2GNJX-ray2.28A2-351[»]
2GNLX-ray2.60A2-351[»]
2JDSX-ray2.00A2-351[»]
2JDTX-ray2.15A2-351[»]
2JDVX-ray2.08A2-351[»]
2OH0X-ray2.20E1-351[»]
2OJFX-ray2.10E1-351[»]
2UVXX-ray2.00A2-351[»]
2UVYX-ray1.95A2-351[»]
2UVZX-ray1.94A2-351[»]
2UW0X-ray2.00A2-351[»]
2UW3X-ray2.19A2-351[»]
2UW4X-ray2.00A2-351[»]
2UW5X-ray2.14A2-351[»]
2UW6X-ray2.23A2-351[»]
2UW7X-ray2.10A2-351[»]
2UW8X-ray2.00A2-351[»]
2UZTX-ray2.10A16-351[»]
2UZUX-ray2.40E16-351[»]
2UZVX-ray2.50A16-351[»]
2UZWX-ray2.20E16-351[»]
2VNWX-ray2.09A1-351[»]
2VNYX-ray1.96A1-351[»]
2VO0X-ray1.94A1-351[»]
2VO3X-ray1.98A1-351[»]
2VO6X-ray1.97A1-351[»]
2VO7X-ray1.98A1-351[»]
3AG9X-ray2.00A/B1-351[»]
3BWJX-ray2.30A2-351[»]
3DNDX-ray2.26A2-351[»]
3DNEX-ray2.00A2-351[»]
3E8CX-ray2.20A/B/C/D/E/F2-351[»]
3E8EX-ray2.00A/B/E/I/L/P2-351[»]
3KKVX-ray1.80A2-351[»]
3ZO1X-ray2.00A1-351[»]
3ZO2X-ray1.98A1-351[»]
3ZO3X-ray2.10A1-351[»]
3ZO4X-ray1.65A1-351[»]
4AXAX-ray1.90A1-351[»]
4C33X-ray1.70A1-351[»]
4C34X-ray1.78A1-351[»]
4C35X-ray2.19A1-351[»]
4C36X-ray1.98A1-351[»]
4C37X-ray1.70A1-351[»]
4C38X-ray1.58A1-351[»]
4IE9X-ray1.92A1-351[»]
4IJ9X-ray2.55A2-351[»]
ProteinModelPortaliP00517.
SMRiP00517. Positions 8-351.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 298255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35153AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121885.
HOVERGENiHBG108317.
InParanoidiP00517.
KOiK04345.
OMAiGKEFTEF.
OrthoDBiEOG7VX8WD.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WENPAQNTAH LDQFERIKTL
60 70 80 90 100
GTGSFGRVML VKHMETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN
110 120 130 140 150
FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ
160 170 180 190 200
IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC
210 220 230 240 250
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK
260 270 280 290 300
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
310 320 330 340 350
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE

F
Length:351
Mass (Da):40,620
Last modified:January 23, 2007 - v3
Checksum:i59DDD227D2DEEE5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021T → N AA sequence (PubMed:6286662).Curated
Sequence conflicti204 – 2041E → Q AA sequence (PubMed:6286662).Curated
Sequence conflicti206 – 2061L → S AA sequence (PubMed:6286662).Curated
Sequence conflicti287 – 2871N → D AA sequence (PubMed:6262777).Curated
Sequence conflicti287 – 2871N → D AA sequence (PubMed:6311252).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67154 mRNA. Translation: CAA47627.1.
PIRiS27159. OKBO2C.
RefSeqiNP_777009.1. NM_174584.2.
UniGeneiBt.4420.

Genome annotation databases

EnsembliENSBTAT00000008727; ENSBTAP00000008727; ENSBTAG00000006642.
GeneIDi282322.
KEGGibta:282322.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67154 mRNA. Translation: CAA47627.1.
PIRiS27159. OKBO2C.
RefSeqiNP_777009.1. NM_174584.2.
UniGeneiBt.4420.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KMUmodel-C9-351[»]
1KMWmodel-C9-351[»]
1Q24X-ray2.60A2-351[»]
1Q61X-ray2.10A2-351[»]
1Q62X-ray2.30A2-351[»]
1Q8TX-ray2.00A2-351[»]
1Q8UX-ray1.90A2-351[»]
1Q8WX-ray2.20A2-351[»]
1SMHX-ray2.04A2-351[»]
1STCX-ray2.30E2-351[»]
1SVEX-ray2.49A2-351[»]
1SVGX-ray2.02A2-351[»]
1SVHX-ray2.30A2-351[»]
1SZMX-ray2.50A/B2-351[»]
1VEBX-ray2.89A2-351[»]
1XH4X-ray2.45A2-351[»]
1XH5X-ray2.05A2-351[»]
1XH6X-ray1.90A2-351[»]
1XH7X-ray2.47A2-351[»]
1XH8X-ray1.60A2-351[»]
1XH9X-ray1.64A2-351[»]
1XHAX-ray2.46A2-351[»]
1YDRX-ray2.20E2-351[»]
1YDSX-ray2.20E2-351[»]
1YDTX-ray2.30E2-351[»]
2C1AX-ray1.95A2-351[»]
2C1BX-ray2.00A2-351[»]
2F7EX-ray2.00E1-351[»]
2F7XX-ray1.90E1-351[»]
2F7ZX-ray3.00E1-351[»]
2GFCX-ray1.87A2-351[»]
2GNFX-ray2.28A2-351[»]
2GNGX-ray1.87A2-351[»]
2GNHX-ray2.05A2-351[»]
2GNIX-ray2.27A2-351[»]
2GNJX-ray2.28A2-351[»]
2GNLX-ray2.60A2-351[»]
2JDSX-ray2.00A2-351[»]
2JDTX-ray2.15A2-351[»]
2JDVX-ray2.08A2-351[»]
2OH0X-ray2.20E1-351[»]
2OJFX-ray2.10E1-351[»]
2UVXX-ray2.00A2-351[»]
2UVYX-ray1.95A2-351[»]
2UVZX-ray1.94A2-351[»]
2UW0X-ray2.00A2-351[»]
2UW3X-ray2.19A2-351[»]
2UW4X-ray2.00A2-351[»]
2UW5X-ray2.14A2-351[»]
2UW6X-ray2.23A2-351[»]
2UW7X-ray2.10A2-351[»]
2UW8X-ray2.00A2-351[»]
2UZTX-ray2.10A16-351[»]
2UZUX-ray2.40E16-351[»]
2UZVX-ray2.50A16-351[»]
2UZWX-ray2.20E16-351[»]
2VNWX-ray2.09A1-351[»]
2VNYX-ray1.96A1-351[»]
2VO0X-ray1.94A1-351[»]
2VO3X-ray1.98A1-351[»]
2VO6X-ray1.97A1-351[»]
2VO7X-ray1.98A1-351[»]
3AG9X-ray2.00A/B1-351[»]
3BWJX-ray2.30A2-351[»]
3DNDX-ray2.26A2-351[»]
3DNEX-ray2.00A2-351[»]
3E8CX-ray2.20A/B/C/D/E/F2-351[»]
3E8EX-ray2.00A/B/E/I/L/P2-351[»]
3KKVX-ray1.80A2-351[»]
3ZO1X-ray2.00A1-351[»]
3ZO2X-ray1.98A1-351[»]
3ZO3X-ray2.10A1-351[»]
3ZO4X-ray1.65A1-351[»]
4AXAX-ray1.90A1-351[»]
4C33X-ray1.70A1-351[»]
4C34X-ray1.78A1-351[»]
4C35X-ray2.19A1-351[»]
4C36X-ray1.98A1-351[»]
4C37X-ray1.70A1-351[»]
4C38X-ray1.58A1-351[»]
4IE9X-ray1.92A1-351[»]
4IJ9X-ray2.55A2-351[»]
ProteinModelPortaliP00517.
SMRiP00517. Positions 8-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159584. 8 interactions.
IntActiP00517. 4 interactions.
STRINGi9913.ENSBTAP00000008727.

Chemistry

BindingDBiP00517.
ChEMBLiCHEMBL2654.

Proteomic databases

PaxDbiP00517.
PRIDEiP00517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008727; ENSBTAP00000008727; ENSBTAG00000006642.
GeneIDi282322.
KEGGibta:282322.

Organism-specific databases

CTDi5566.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121885.
HOVERGENiHBG108317.
InParanoidiP00517.
KOiK04345.
OMAiGKEFTEF.
OrthoDBiEOG7VX8WD.
TreeFamiTF313399.

Enzyme and pathway databases

BRENDAi2.7.11.11. 908.
ReactomeiREACT_273496. Recruitment of mitotic centrosome proteins and complexes.
REACT_274117. PKA activation.
REACT_279372. PKA-mediated phosphorylation of CREB.
REACT_286999. Interleukin-3, 5 and GM-CSF signaling.
REACT_288981. PKA-mediated phosphorylation of key metabolic factors.
REACT_289962. Loss of Nlp from mitotic centrosomes.
REACT_301041. DARPP-32 events.
REACT_305537. Gluconeogenesis.
REACT_318110. PKA activation in glucagon signalling.
REACT_325957. Hedgehog 'off' state.
REACT_327729. Degradation of GLI2 by the proteasome.
REACT_333090. GLI3 is processed to GLI3R by the proteasome.
REACT_335146. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_335730. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_335907. Factors involved in megakaryocyte development and platelet production.
REACT_337384. Degradation of GLI1 by the proteasome.
REACT_337905. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_340866. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_341360. Regulation of PLK1 Activity at G2/M Transition.
REACT_344993. Regulation of insulin secretion.
REACT_346955. Anchoring of the basal body to the plasma membrane.
REACT_348169. Rap1 signalling.

Miscellaneous databases

EvolutionaryTraceiP00517.
NextBioi20806119.
PMAP-CutDBP00517.
PROiP00517.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent protein kinase."
    Wiemann S., Kinzel V., Pyerin W.
    Biochim. Biophys. Acta 1171:93-96(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase."
    Shoji S., Parmelee D.C., Wade R.D., Kumar S., Ericsson L.H., Walsh K.A., Neurath H., Lonh G.L., Demaille J.G., Fischer E.H., Titani K.
    Proc. Natl. Acad. Sci. U.S.A. 78:848-851(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-351, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT THR-198 AND SER-339.
  3. "Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3',5'-phosphate dependent protein kinase."
    Shoji S., Ericsson L.H., Walsh K.A., Fischer E.H., Titani K.
    Biochemistry 22:3702-3709(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-351.
  4. "Modification of the catalytic subunit of bovine heart cAMP-dependent protein kinase with affinity labels related to peptide substrates."
    Bramson H.N., Thomas N., Matsueda R., Nelson N.C., Taylor S.S., Kaiser E.T.
    J. Biol. Chem. 257:10575-10581(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 196-214, ACTIVE SITE.
  5. "A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry."
    Jedrzejewski P.T., Girod A., Tholey A., Koenig N., Thullner S., Kinzel V., Bossemeyer D.
    Protein Sci. 7:457-469(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8, MUTAGENESIS OF ASN-3, DEAMIDATION AT ASN-3.
  6. "Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation."
    Pepperkok R., Hotz-Wagenblatt A., Koenig N., Girod A., Bossemeyer D., Kinzel V.
    J. Cell Biol. 148:715-726(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEAMIDATION AT ASN-3, SUBCELLULAR LOCATION.
  7. "The amino terminus of PKA catalytic subunit- a site for introduction of posttranslational heterogeneities by deamidation: D-Asp2 and D-isoAsp2 containing isozymes."
    Kinzel V., Koenig N., Pipkorn R., Bossemeyer D., Lehmann W.D.
    Protein Sci. 9:2269-2277(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEAMIDATION AT ASN-3, CHARACTERIZATION OF ASP-3 ISOMERS.
  8. "Rab13 regulates PKA signaling during tight junction assembly."
    Koehler K., Louvard D., Zahraoui A.
    J. Cell Biol. 165:175-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB13.
  9. "Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity."
    Engh R.A., Girod A., Kinzel V., Huber R., Bossemeyer D.
    J. Biol. Chem. 271:26157-26164(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  10. "Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential."
    Prade L., Engh R.A., Girod A., Kinzel V., Huber R., Bossemeyer D.
    Structure 5:1627-1637(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiKAPCA_BOVIN
AccessioniPrimary (citable) accession number: P00517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.