Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00517

- KAPCA_BOVIN

UniProt

P00517 - KAPCA_BOVIN

Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

PRKACA

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 acceptor1 PublicationPROSITE-ProRule annotation

    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 binding Source: IntAct
    4. protein kinase activity Source: AgBase

    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. peptidyl-serine phosphorylation Source: Ensembl
    5. positive regulation of cell cycle arrest Source: Ensembl
    6. positive regulation of protein export from nucleus Source: Ensembl
    7. protein autophosphorylation Source: Ensembl
    8. protein phosphorylation Source: AgBase
    9. regulation of osteoblast differentiation Source: Ensembl
    10. regulation of proteasomal protein catabolic process Source: Ensembl
    11. regulation of synaptic transmission Source: Ensembl
    12. regulation of tight junction assembly Source: Ensembl
    13. sperm capacitation Source: Ensembl

    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_202137. Regulation of water balance by renal Aquaporins.
    REACT_205006. Loss of Nlp from mitotic centrosomes.
    REACT_205490. DARPP-32 events.
    REACT_209110. Regulation of insulin secretion.
    REACT_209315. PKA-mediated phosphorylation of CREB.
    REACT_213932. PKA activation.
    REACT_214027. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    REACT_214141. Rap1 signalling.
    REACT_214350. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_215067. Factors involved in megakaryocyte development and platelet production.
    REACT_215812. Recruitment of mitotic centrosome proteins and complexes.
    REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_219718. PKA activation in glucagon signalling.
    REACT_223056. PKA-mediated phosphorylation of key metabolic factors.
    REACT_224118. Regulation of PLK1 Activity at G2/M Transition.
    REACT_227222. Gluconeogenesis.

    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: 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. cytoplasm Source: AgBase
    4. mitochondrion Source: UniProtKB-SubCell
    5. neuromuscular junction Source: AgBase
    6. nucleus Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB-SubCell
    8. sperm midpiece Source: Ensembl

    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. 7 interactions.
    IntActiP00517. 4 interactions.
    STRINGi9913.ENSBTAP00000008727.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00550000074358.
    HOVERGENiHBG108317.
    InParanoidiP00517.
    KOiK04345.
    OMAiGQHFAMK.
    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_dom.
    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

    MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WENPAQNTAH LDQFERIKTL    50
    GTGSFGRVML VKHMETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN 100
    FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ 150
    IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC 200
    GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK 250
    IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT 300
    TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE 350
    F 351
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67154 mRNA. Translation: CAA47627.1 .
    PIRi S27159. OKBO2C.
    RefSeqi NP_777009.1. NM_174584.2.
    UniGenei Bt.4420.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KMU model - C 9-351 [» ]
    1KMW model - C 9-351 [» ]
    1Q24 X-ray 2.60 A 2-351 [» ]
    1Q61 X-ray 2.10 A 2-351 [» ]
    1Q62 X-ray 2.30 A 2-351 [» ]
    1Q8T X-ray 2.00 A 2-351 [» ]
    1Q8U X-ray 1.90 A 2-351 [» ]
    1Q8W X-ray 2.20 A 2-351 [» ]
    1SMH X-ray 2.04 A 2-351 [» ]
    1STC X-ray 2.30 E 2-351 [» ]
    1SVE X-ray 2.49 A 2-351 [» ]
    1SVG X-ray 2.02 A 2-351 [» ]
    1SVH X-ray 2.30 A 2-351 [» ]
    1SZM X-ray 2.50 A/B 2-351 [» ]
    1VEB X-ray 2.89 A 2-351 [» ]
    1XH4 X-ray 2.45 A 2-351 [» ]
    1XH5 X-ray 2.05 A 2-351 [» ]
    1XH6 X-ray 1.90 A 2-351 [» ]
    1XH7 X-ray 2.47 A 2-351 [» ]
    1XH8 X-ray 1.60 A 2-351 [» ]
    1XH9 X-ray 1.64 A 2-351 [» ]
    1XHA X-ray 2.46 A 2-351 [» ]
    1YDR X-ray 2.20 E 2-351 [» ]
    1YDS X-ray 2.20 E 2-351 [» ]
    1YDT X-ray 2.30 E 2-351 [» ]
    2C1A X-ray 1.95 A 2-351 [» ]
    2C1B X-ray 2.00 A 2-351 [» ]
    2F7E X-ray 2.00 E 1-351 [» ]
    2F7X X-ray 1.90 E 1-351 [» ]
    2F7Z X-ray 3.00 E 1-351 [» ]
    2GFC X-ray 1.87 A 2-351 [» ]
    2GNF X-ray 2.28 A 2-351 [» ]
    2GNG X-ray 1.87 A 2-351 [» ]
    2GNH X-ray 2.05 A 2-351 [» ]
    2GNI X-ray 2.27 A 2-351 [» ]
    2GNJ X-ray 2.28 A 2-351 [» ]
    2GNL X-ray 2.60 A 2-351 [» ]
    2JDS X-ray 2.00 A 2-351 [» ]
    2JDT X-ray 2.15 A 2-351 [» ]
    2JDV X-ray 2.08 A 2-351 [» ]
    2OH0 X-ray 2.20 E 1-351 [» ]
    2OJF X-ray 2.10 E 1-351 [» ]
    2UVX X-ray 2.00 A 2-351 [» ]
    2UVY X-ray 1.95 A 2-351 [» ]
    2UVZ X-ray 1.94 A 2-351 [» ]
    2UW0 X-ray 2.00 A 2-351 [» ]
    2UW3 X-ray 2.19 A 2-351 [» ]
    2UW4 X-ray 2.00 A 2-351 [» ]
    2UW5 X-ray 2.14 A 2-351 [» ]
    2UW6 X-ray 2.23 A 2-351 [» ]
    2UW7 X-ray 2.10 A 2-351 [» ]
    2UW8 X-ray 2.00 A 2-351 [» ]
    2UZT X-ray 2.10 A 16-351 [» ]
    2UZU X-ray 2.40 E 16-351 [» ]
    2UZV X-ray 2.50 A 16-351 [» ]
    2UZW X-ray 2.20 E 16-351 [» ]
    2VNW X-ray 2.09 A 1-351 [» ]
    2VNY X-ray 1.96 A 1-351 [» ]
    2VO0 X-ray 1.94 A 1-351 [» ]
    2VO3 X-ray 1.98 A 1-351 [» ]
    2VO6 X-ray 1.97 A 1-351 [» ]
    2VO7 X-ray 1.98 A 1-351 [» ]
    3AG9 X-ray 2.00 A/B 1-351 [» ]
    3BWJ X-ray 2.30 A 2-351 [» ]
    3DND X-ray 2.26 A 2-351 [» ]
    3DNE X-ray 2.00 A 2-351 [» ]
    3E8C X-ray 2.20 A/B/C/D/E/F 2-351 [» ]
    3E8E X-ray 2.00 A/B/E/I/L/P 2-351 [» ]
    3KKV X-ray 1.80 A 2-351 [» ]
    3ZO1 X-ray 2.00 A 1-351 [» ]
    3ZO2 X-ray 1.98 A 1-351 [» ]
    3ZO3 X-ray 2.10 A 1-351 [» ]
    3ZO4 X-ray 1.65 A 1-351 [» ]
    4AXA X-ray 1.90 A 1-351 [» ]
    4C33 X-ray 1.70 A 1-351 [» ]
    4C34 X-ray 1.78 A 1-351 [» ]
    4C35 X-ray 2.19 A 1-351 [» ]
    4C36 X-ray 1.98 A 1-351 [» ]
    4C37 X-ray 1.70 A 1-351 [» ]
    4C38 X-ray 1.58 A 1-351 [» ]
    4IE9 X-ray 1.92 A 1-351 [» ]
    4IJ9 X-ray 2.55 A 2-351 [» ]
    ProteinModelPortali P00517.
    SMRi P00517. Positions 8-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 159584. 7 interactions.
    IntActi P00517. 4 interactions.
    STRINGi 9913.ENSBTAP00000008727.

    Chemistry

    BindingDBi P00517.
    ChEMBLi CHEMBL2111446.

    Proteomic databases

    PaxDbi P00517.
    PRIDEi P00517.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000008727 ; ENSBTAP00000008727 ; ENSBTAG00000006642 .
    GeneIDi 282322.
    KEGGi bta:282322.

    Organism-specific databases

    CTDi 5566.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074358.
    HOVERGENi HBG108317.
    InParanoidi P00517.
    KOi K04345.
    OMAi GQHFAMK.
    OrthoDBi EOG7VX8WD.
    TreeFami TF313399.

    Enzyme and pathway databases

    BRENDAi 2.7.11.11. 908.
    Reactomei REACT_202137. Regulation of water balance by renal Aquaporins.
    REACT_205006. Loss of Nlp from mitotic centrosomes.
    REACT_205490. DARPP-32 events.
    REACT_209110. Regulation of insulin secretion.
    REACT_209315. PKA-mediated phosphorylation of CREB.
    REACT_213932. PKA activation.
    REACT_214027. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    REACT_214141. Rap1 signalling.
    REACT_214350. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_215067. Factors involved in megakaryocyte development and platelet production.
    REACT_215812. Recruitment of mitotic centrosome proteins and complexes.
    REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_219718. PKA activation in glucagon signalling.
    REACT_223056. PKA-mediated phosphorylation of key metabolic factors.
    REACT_224118. Regulation of PLK1 Activity at G2/M Transition.
    REACT_227222. Gluconeogenesis.

    Miscellaneous databases

    EvolutionaryTracei P00517.
    NextBioi 20806119.
    PMAP-CutDB P00517.
    PROi P00517.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. 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 ]
    ProtoNeti Search...

    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(1992) [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(1981) [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(1983) [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(1982) [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(1998) [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(2000) [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(2000) [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(2004) [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(1996) [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(1997) [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: October 1, 2014
    This is version 152 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