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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)DescriptionActionsGraphical viewLength
Binding sitei73ATP1
Active sitei167Proton acceptorPROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 58ATP9
Nucleotide bindingi122 – 128ATPPROSITE-ProRule annotation7
Nucleotide bindingi169 – 172ATPPROSITE-ProRule annotation4

GO - Molecular functioni

GO - Biological processi

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.
ReactomeiR-BTA-163615. PKA activation.
R-BTA-164378. PKA activation in glucagon signalling.
R-BTA-180024. DARPP-32 events.
R-BTA-194223. HDL-mediated lipid transport.
R-BTA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-BTA-380259. Loss of Nlp from mitotic centrosomes.
R-BTA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-BTA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-BTA-392517. Rap1 signalling.
R-BTA-422356. Regulation of insulin secretion.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-BTA-5578775. Ion homeostasis.
R-BTA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-BTA-5610787. Hedgehog 'off' state.
R-BTA-5620912. Anchoring of the basal body to the plasma membrane.
R-BTA-5621575. CD209 (DC-SIGN) signaling.
R-BTA-5687128. MAPK6/MAPK4 signaling.
R-BTA-8854518. AURKA Activation by TPX2.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

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
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Cell membrane By similarity
  • Mitochondrion By similarity
  • Membrane By similarity; Lipid-anchor 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3N → D: No myristoylation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2654.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000860492 – 351cAMP-dependent protein kinase catalytic subunit alphaAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei3Deamidated asparagine; partial3 Publications1
Modified residuei11Phosphoserine; by autocatalysisBy similarity1
Modified residuei49PhosphothreonineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei196PhosphothreonineBy similarity1
Modified residuei198Phosphothreonine; by PDPK11 Publication1
Modified residuei202PhosphothreonineBy similarity1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei339Phosphoserine1 Publication1

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.
PeptideAtlasiP00517.
PRIDEiP00517.

PTM databases

iPTMnetiP00517.

Miscellaneous databases

PMAP-CutDBP00517.

Expressioni

Tissue specificityi

Ubiquitously expressed in mammalian tissues.

Gene expression databases

BgeeiENSBTAG00000006642.

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. 9 interactors.
IntActiP00517. 4 interactors.
STRINGi9913.ENSBTAP00000008727.

Chemistry databases

BindingDBiP00517.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni11 – 13Combined sources3
Helixi18 – 32Combined sources15
Helixi41 – 43Combined sources3
Beta strandi44 – 53Combined sources10
Beta strandi56 – 63Combined sources8
Turni64 – 66Combined sources3
Beta strandi69 – 76Combined sources8
Helixi77 – 82Combined sources6
Helixi86 – 98Combined sources13
Beta strandi107 – 112Combined sources6
Beta strandi114 – 122Combined sources9
Helixi129 – 136Combined sources8
Helixi141 – 160Combined sources20
Helixi170 – 172Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi181 – 183Combined sources3
Helixi186 – 188Combined sources3
Beta strandi199 – 201Combined sources3
Helixi203 – 205Combined sources3
Helixi208 – 211Combined sources4
Helixi219 – 234Combined sources16
Helixi244 – 253Combined sources10
Beta strandi260 – 262Combined sources3
Helixi264 – 273Combined sources10
Turni278 – 280Combined sources3
Turni282 – 284Combined sources3
Turni286 – 289Combined sources4
Helixi290 – 293Combined sources4
Helixi296 – 298Combined sources3
Helixi303 – 307Combined sources5
Beta strandi322 – 325Combined sources4
Beta strandi326 – 328Combined sources3
Turni345 – 350Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YXRX-ray2.00A2-351[»]
4YXSX-ray2.11A2-351[»]
4Z83X-ray1.80E2-351[»]
4Z84X-ray1.55A1-351[»]
ProteinModelPortaliP00517.
SMRiP00517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 298Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini299 – 351AGC-kinase C-terminalAdd BLAST53

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOVERGENiHBG108317.
InParanoidiP00517.
KOiK04345.
OMAiNAATANK.
OrthoDBiEOG091G10O8.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti202T → N AA sequence (PubMed:6286662).Curated1
Sequence conflicti204E → Q AA sequence (PubMed:6286662).Curated1
Sequence conflicti206L → S AA sequence (PubMed:6286662).Curated1
Sequence conflicti287N → D AA sequence (PubMed:6262777).Curated1
Sequence conflicti287N → D AA sequence (PubMed:6311252).Curated1

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
PDB 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[»]
4YXRX-ray2.00A2-351[»]
4YXSX-ray2.11A2-351[»]
4Z83X-ray1.80E2-351[»]
4Z84X-ray1.55A1-351[»]
ProteinModelPortaliP00517.
SMRiP00517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159584. 9 interactors.
IntActiP00517. 4 interactors.
STRINGi9913.ENSBTAP00000008727.

Chemistry databases

BindingDBiP00517.
ChEMBLiCHEMBL2654.

PTM databases

iPTMnetiP00517.

Proteomic databases

PaxDbiP00517.
PeptideAtlasiP00517.
PRIDEiP00517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5566.

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOVERGENiHBG108317.
InParanoidiP00517.
KOiK04345.
OMAiNAATANK.
OrthoDBiEOG091G10O8.
TreeFamiTF313399.

Enzyme and pathway databases

BRENDAi2.7.11.11. 908.
ReactomeiR-BTA-163615. PKA activation.
R-BTA-164378. PKA activation in glucagon signalling.
R-BTA-180024. DARPP-32 events.
R-BTA-194223. HDL-mediated lipid transport.
R-BTA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-BTA-380259. Loss of Nlp from mitotic centrosomes.
R-BTA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-BTA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-BTA-392517. Rap1 signalling.
R-BTA-422356. Regulation of insulin secretion.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-BTA-5578775. Ion homeostasis.
R-BTA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-BTA-5610787. Hedgehog 'off' state.
R-BTA-5620912. Anchoring of the basal body to the plasma membrane.
R-BTA-5621575. CD209 (DC-SIGN) signaling.
R-BTA-5687128. MAPK6/MAPK4 signaling.
R-BTA-8854518. AURKA Activation by TPX2.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP00517.
PMAP-CutDBP00517.
PROiP00517.

Gene expression databases

BgeeiENSBTAG00000006642.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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...

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: November 2, 2016
This is version 174 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

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 one 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.