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P17612

- KAPCA_HUMAN

UniProt

P17612 - KAPCA_HUMAN

Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

PRKACA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.12 Publications

    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. Inhibited by H89 (N-[2-[[3-(4-Bromophenyl)-2-propenyl]amino]ethyl]-5-isoquinolinesulfonamide), spiroindoline, azole-based inhibitors, (3s)-amino-aminomethylbenzamide analogs, ARC-1032 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-carbamoylbutyl]hexanamide), ARC-1034 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]hexanamide), ARC-582, ARC-902 (Adc-6-aminohexanoic acid-(D-Arg)(6)-NH2), ARC-1012 ((2R)-6-amino-2-(6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}hexanamido)-N-(5-{[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)hexanamide) and ARC-1039 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-1-[(5-{[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)carbamoyl]ethyl]he xanamide).6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731ATPPROSITE-ProRule annotation
    Active sitei167 – 1671Proton acceptorPROSITE-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: BHF-UCL
    3. protein binding Source: BHF-UCL
    4. protein kinase A regulatory subunit binding Source: BHF-UCL
    5. protein kinase binding Source: BHF-UCL
    6. protein serine/threonine/tyrosine kinase activity Source: MGI
    7. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. activation of protein kinase A activity Source: Reactome
    3. blood coagulation Source: Reactome
    4. calcium-mediated signaling using intracellular calcium source Source: BHF-UCL
    5. carbohydrate metabolic process Source: Reactome
    6. cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
    7. cellular response to epinephrine stimulus Source: BHF-UCL
    8. cellular response to glucagon stimulus Source: Reactome
    9. cellular response to glucose stimulus Source: UniProtKB
    10. cellular response to parathyroid hormone stimulus Source: Ensembl
    11. cytosolic calcium ion homeostasis Source: BHF-UCL
    12. energy reserve metabolic process Source: Reactome
    13. epidermal growth factor receptor signaling pathway Source: Reactome
    14. fibroblast growth factor receptor signaling pathway Source: Reactome
    15. G2/M transition of mitotic cell cycle Source: Reactome
    16. gluconeogenesis Source: Reactome
    17. glucose metabolic process Source: Reactome
    18. innate immune response Source: Reactome
    19. intracellular signal transduction Source: Reactome
    20. mesoderm formation Source: Ensembl
    21. mitotic cell cycle Source: Reactome
    22. neurotrophin TRK receptor signaling pathway Source: Reactome
    23. peptidyl-serine phosphorylation Source: BHF-UCL
    24. positive regulation of cell cycle arrest Source: UniProtKB
    25. positive regulation of protein export from nucleus Source: Ensembl
    26. protein autophosphorylation Source: Ensembl
    27. protein phosphorylation Source: UniProtKB
    28. regulation of cardiac muscle contraction Source: BHF-UCL
    29. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    30. regulation of heart rate Source: BHF-UCL
    31. regulation of insulin secretion Source: Reactome
    32. regulation of osteoblast differentiation Source: UniProtKB
    33. regulation of proteasomal protein catabolic process Source: UniProtKB
    34. regulation of protein binding Source: BHF-UCL
    35. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    36. regulation of synaptic transmission Source: Ensembl
    37. regulation of tight junction assembly Source: UniProtKB
    38. signal transduction Source: Reactome
    39. small molecule metabolic process Source: Reactome
    40. sperm capacitation Source: UniProtKB
    41. transmembrane transport Source: Reactome
    42. triglyceride catabolic process Source: Reactome
    43. water transport Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, cAMP, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.11. 2681.
    ReactomeiREACT_1520. Gluconeogenesis.
    REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15334. DARPP-32 events.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15497. PKA-mediated phosphorylation of CREB.
    REACT_15530. PKA activation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18325. Regulation of insulin secretion.
    REACT_1946. PKA activation in glucagon signalling.
    REACT_20625. CREB phosphorylation through the activation of Adenylate Cyclase.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23898. Rap1 signalling.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    SignaLinkiP17612.

    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
    Synonyms:PKACA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9380. PRKACA.

    Subcellular locationi

    Cytoplasm. Cell membrane. Nucleus 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
    Isoform 2 : Cell projectionciliumflagellum
    Note: Expressed in the midpiece region of the sperm flagellum.

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: BHF-UCL
    2. calcium channel complex Source: BHF-UCL
    3. cAMP-dependent protein kinase complex Source: UniProtKB
    4. centrosome Source: UniProtKB
    5. cilium Source: UniProtKB-KW
    6. cytosol Source: Reactome
    7. extracellular vesicular exosome Source: UniProt
    8. mitochondrion Source: UniProtKB-SubCell
    9. neuromuscular junction Source: Ensembl
    10. nucleus Source: UniProt
    11. plasma membrane Source: UniProtKB-SubCell
    12. sperm midpiece Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Cytoplasm, Flagellum, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481K → R: Enhanced basal kinase activity; when associated with Q-96, L-121, A-124, K-182 and A-184. 1 Publication
    Mutagenesisi96 – 961L → Q: Enhanced basal kinase activity; when associated with R-48, L-121, A-124, K-182 and A-184. 1 Publication
    Mutagenesisi121 – 1211M → L: Enhanced basal kinase activity; when associated with R-48, Q-96, A-124, K-182 and A-184. 1 Publication
    Mutagenesisi124 – 1241V → A: Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, K-182 and A-184. 1 Publication
    Mutagenesisi182 – 1821Q → K: Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, A-124 and A-184. 1 Publication
    Mutagenesisi184 – 1841T → A: Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, A-124 and K-182. 1 Publication
    Mutagenesisi195 – 1951R → A: No phosphorylation. 1 Publication
    Mutagenesisi201 – 2011G → A: No phosphorylation. 1 Publication
    Mutagenesisi202 – 2021T → A: No phosphorylation. 1 Publication
    Mutagenesisi205 – 2051Y → A: Loss of allosteric regulation. 1 Publication

    Organism-specific databases

    PharmGKBiPA33748.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit alphaPRO_0000086052Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei3 – 31Deamidated asparagineBy similarity
    Modified residuei11 – 111Phosphoserine; by autocatalysisBy similarity
    Modified residuei49 – 491Phosphothreonine2 Publications
    Modified residuei140 – 1401PhosphoserineBy similarity
    Modified residuei196 – 1961Phosphothreonine2 Publications
    Modified residuei198 – 1981Phosphothreonine; by PDPK18 Publications
    Modified residuei202 – 2021Phosphothreonine1 Publication
    Modified residuei331 – 3311PhosphotyrosineBy similarity
    Modified residuei339 – 3391Phosphoserine9 Publications

    Post-translational modificationi

    Asn-3 is partially deaminated to Asp giving rise to 2 major isoelectric variants, called CB and CA respectively.By similarity
    Autophosphorylated. Phosphorylation is enhanced by vitamin K2. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity.10 Publications
    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

    MaxQBiP17612.
    PaxDbiP17612.
    PRIDEiP17612.

    PTM databases

    PhosphoSiteiP17612.

    Expressioni

    Tissue specificityi

    Isoform 1 is ubiquitous. Isoform 2 is sperm-specific and is enriched in pachytene spermatocytes but is not detected in round spermatids.2 Publications

    Gene expression databases

    ArrayExpressiP17612.
    BgeeiP17612.
    CleanExiHS_PRKACA.
    GenevestigatoriP17612.

    Organism-specific databases

    HPAiCAB010361.

    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. The cAMP-dependent protein kinase catalytic subunit binds PJA2. Both isoforms 1 and 2 forms activate 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. Interacts with APOBEC3G and AICDA. Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKIP1Q9NQ314EBI-476586,EBI-517035
    ALOX5P099172EBI-476586,EBI-79934
    GSK3BP498415EBI-476586,EBI-373586
    LRRK2Q5S0076EBI-476586,EBI-5323863
    PRKAR1AP106442EBI-476586,EBI-476431
    Prkar2bP123692EBI-476586,EBI-6096160From a different organism.

    Protein-protein interaction databases

    BioGridi111553. 113 interactions.
    DIPiDIP-33878N.
    IntActiP17612. 58 interactions.
    MINTiMINT-95365.
    STRINGi9606.ENSP00000309591.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Helixi16 – 3217
    Helixi41 – 433
    Beta strandi44 – 5310
    Beta strandi56 – 638
    Turni64 – 663
    Beta strandi69 – 768
    Helixi77 – 826
    Helixi86 – 9813
    Beta strandi107 – 1126
    Beta strandi114 – 1229
    Helixi129 – 1368
    Helixi141 – 16020
    Helixi170 – 1723
    Beta strandi173 – 1753
    Beta strandi181 – 1833
    Helixi203 – 2053
    Helixi208 – 2114
    Beta strandi212 – 2143
    Helixi219 – 23416
    Helixi244 – 25310
    Helixi264 – 27310
    Turni278 – 2803
    Turni282 – 2843
    Turni286 – 2894
    Helixi290 – 2934
    Helixi296 – 2983
    Helixi303 – 3075
    Turni345 – 3506

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GU8X-ray2.20A15-351[»]
    3AGLX-ray2.10A/B1-351[»]
    3AGMX-ray2.00A1-351[»]
    3AMAX-ray1.75A1-351[»]
    3AMBX-ray2.25A1-351[»]
    3L9LX-ray2.00A/B1-351[»]
    3L9MX-ray1.90A/B1-351[»]
    3L9NX-ray2.00A1-351[»]
    3MVJX-ray2.49A/B/E1-351[»]
    3NX8X-ray2.00A1-351[»]
    3OOGX-ray2.00A1-351[»]
    3OVVX-ray1.58A1-351[»]
    3OWPX-ray1.88A1-351[»]
    3OXTX-ray2.20A1-351[»]
    3P0MX-ray2.03A1-351[»]
    3POOX-ray1.60A1-351[»]
    3VQHX-ray1.95A1-351[»]
    4AE6X-ray2.10A/B16-351[»]
    4AE9X-ray2.30A/B16-351[»]
    ProteinModelPortaliP17612.
    SMRiP17612. Positions 15-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17612.

    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.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiP17612.
    KOiK04345.
    OMAiGQHFAMK.
    OrthoDBiEOG7VX8WD.
    PhylomeDBiP17612.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17612-1) [UniParc]FASTAAdd to Basket

    Also known as: C-alpha-1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL    50
    GTGSFGRVML VKHKETGNHY 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):40,590
    Last modified:January 23, 2007 - v2
    Checksum:iBF6D3ECD2614E5AB
    GO
    Isoform 2 (identifier: P17612-2) [UniParc]FASTAAdd to Basket

    Also known as: C-alpha-2, C-alpha-S, C(s)

    The sequence of this isoform differs from the canonical sequence as follows:
         2-15: GNAAAAKKGSEQES → MASNSSD

    Show »
    Length:344
    Mass (Da):39,953
    Checksum:iD10578641CB00E9C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411L → V.1 Publication
    Corresponds to variant rs56029020 [ dbSNP | Ensembl ].
    VAR_040591
    Natural varianti46 – 461R → Q.1 Publication
    Corresponds to variant rs56085217 [ dbSNP | Ensembl ].
    VAR_040592
    Natural varianti264 – 2641S → C.1 Publication
    Corresponds to variant rs35635531 [ dbSNP | Ensembl ].
    VAR_040593

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 1514GNAAA…SEQES → MASNSSD in isoform 2. 3 PublicationsVSP_004759Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07767 mRNA. Translation: CAA30597.1.
    AK290147 mRNA. Translation: BAF82836.1.
    DQ667173 Genomic DNA. Translation: ABG25918.1.
    CH471106 Genomic DNA. Translation: EAW84399.1.
    BC039846 mRNA. Translation: AAH39846.1.
    BC108259 mRNA. Translation: AAI08260.1.
    AF208004 mRNA. Translation: AAG35720.1.
    AF239744 mRNA. Translation: AAF76426.1.
    AF224718 mRNA. Translation: AAF75622.1.
    CCDSiCCDS12304.1. [P17612-1]
    PIRiS01404. OKHU2C.
    RefSeqiNP_002721.1. NM_002730.3. [P17612-1]
    NP_997401.1. NM_207518.1.
    UniGeneiHs.631630.

    Genome annotation databases

    EnsembliENST00000308677; ENSP00000309591; ENSG00000072062. [P17612-1]
    GeneIDi5566.
    KEGGihsa:5566.
    UCSCiuc002myb.3. human. [P17612-2]
    uc002myc.3. human. [P17612-1]

    Polymorphism databases

    DMDMi125205.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07767 mRNA. Translation: CAA30597.1 .
    AK290147 mRNA. Translation: BAF82836.1 .
    DQ667173 Genomic DNA. Translation: ABG25918.1 .
    CH471106 Genomic DNA. Translation: EAW84399.1 .
    BC039846 mRNA. Translation: AAH39846.1 .
    BC108259 mRNA. Translation: AAI08260.1 .
    AF208004 mRNA. Translation: AAG35720.1 .
    AF239744 mRNA. Translation: AAF76426.1 .
    AF224718 mRNA. Translation: AAF75622.1 .
    CCDSi CCDS12304.1. [P17612-1 ]
    PIRi S01404. OKHU2C.
    RefSeqi NP_002721.1. NM_002730.3. [P17612-1 ]
    NP_997401.1. NM_207518.1.
    UniGenei Hs.631630.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GU8 X-ray 2.20 A 15-351 [» ]
    3AGL X-ray 2.10 A/B 1-351 [» ]
    3AGM X-ray 2.00 A 1-351 [» ]
    3AMA X-ray 1.75 A 1-351 [» ]
    3AMB X-ray 2.25 A 1-351 [» ]
    3L9L X-ray 2.00 A/B 1-351 [» ]
    3L9M X-ray 1.90 A/B 1-351 [» ]
    3L9N X-ray 2.00 A 1-351 [» ]
    3MVJ X-ray 2.49 A/B/E 1-351 [» ]
    3NX8 X-ray 2.00 A 1-351 [» ]
    3OOG X-ray 2.00 A 1-351 [» ]
    3OVV X-ray 1.58 A 1-351 [» ]
    3OWP X-ray 1.88 A 1-351 [» ]
    3OXT X-ray 2.20 A 1-351 [» ]
    3P0M X-ray 2.03 A 1-351 [» ]
    3POO X-ray 1.60 A 1-351 [» ]
    3VQH X-ray 1.95 A 1-351 [» ]
    4AE6 X-ray 2.10 A/B 16-351 [» ]
    4AE9 X-ray 2.30 A/B 16-351 [» ]
    ProteinModelPortali P17612.
    SMRi P17612. Positions 15-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111553. 113 interactions.
    DIPi DIP-33878N.
    IntActi P17612. 58 interactions.
    MINTi MINT-95365.
    STRINGi 9606.ENSP00000309591.

    Chemistry

    BindingDBi P17612.
    ChEMBLi CHEMBL2094138.
    GuidetoPHARMACOLOGYi 1476.

    PTM databases

    PhosphoSitei P17612.

    Polymorphism databases

    DMDMi 125205.

    Proteomic databases

    MaxQBi P17612.
    PaxDbi P17612.
    PRIDEi P17612.

    Protocols and materials databases

    DNASUi 5566.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308677 ; ENSP00000309591 ; ENSG00000072062 . [P17612-1 ]
    GeneIDi 5566.
    KEGGi hsa:5566.
    UCSCi uc002myb.3. human. [P17612-2 ]
    uc002myc.3. human. [P17612-1 ]

    Organism-specific databases

    CTDi 5566.
    GeneCardsi GC19M014202.
    HGNCi HGNC:9380. PRKACA.
    HPAi CAB010361.
    MIMi 601639. gene.
    neXtProti NX_P17612.
    PharmGKBi PA33748.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi P17612.
    KOi K04345.
    OMAi GQHFAMK.
    OrthoDBi EOG7VX8WD.
    PhylomeDBi P17612.
    TreeFami TF313399.

    Enzyme and pathway databases

    BRENDAi 2.7.11.11. 2681.
    Reactomei REACT_1520. Gluconeogenesis.
    REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15334. DARPP-32 events.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15497. PKA-mediated phosphorylation of CREB.
    REACT_15530. PKA activation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18325. Regulation of insulin secretion.
    REACT_1946. PKA activation in glucagon signalling.
    REACT_20625. CREB phosphorylation through the activation of Adenylate Cyclase.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23898. Rap1 signalling.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    SignaLinki P17612.

    Miscellaneous databases

    ChiTaRSi PRKACA. human.
    EvolutionaryTracei P17612.
    GeneWikii PRKACA.
    GenomeRNAii 5566.
    NextBioi 21564.
    PROi P17612.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17612.
    Bgeei P17612.
    CleanExi HS_PRKACA.
    Genevestigatori P17612.

    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. "A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha."
      Maldonado F., Hanks S.K.
      Nucleic Acids Res. 16:8189-8190(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Thalamus.
    3. SeattleSNPs variation discovery resource
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Eye and Testis.
    6. "A novel isoform of human cyclic 3',5'-adenosine monophosphate-dependent protein kinase, c alpha-s, localizes to sperm midpiece."
      Reinton N., Orstavik S., Haugen T.B., Jahnsen T., Tasken K., Skalhegg B.S.
      Biol. Reprod. 63:607-611(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-189 (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative C-alpha mRNA expressed specifically in spermatogenic cells."
      San Agustin J.T., Wilkerson C.G., Witman G.B.
      Mol. Biol. Cell 11:3031-3044(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-152 (ISOFORM 2).
      Tissue: Testis.
    8. "Expression of a nonmyristylated variant of the catalytic subunit of protein kinase A during male germ-cell development."
      Desseyn J.-L., Burton K.A., McKnight G.S.
      Proc. Natl. Acad. Sci. U.S.A. 97:6433-6438(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-39 (ISOFORM 2).
      Tissue: Testis.
    9. "Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1."
      Moore M.J., Kanter J.R., Jones K.C., Taylor S.S.
      J. Biol. Chem. 277:47878-47884(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-196, PHOSPHORYLATION AT THR-198 BY PDK1, MUTAGENESIS OF ARG-195; GLY-201 AND THR-202.
    10. "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.
    11. "DNA binding of repressor nuclear factor-kappaB p50/p50 depends on phosphorylation of Ser337 by the protein kinase A catalytic subunit."
      Guan H., Hou S., Ricciardi R.P.
      J. Biol. Chem. 280:9957-9962(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS NFKB1 KINASE.
    12. "Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells."
      D'Souza T., Agarwal R., Morin P.J.
      J. Biol. Chem. 280:26233-26240(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CLDN3 KINASE.
    13. "PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells."
      Pasqualucci L., Kitaura Y., Gu H., Dalla-Favera R.
      Proc. Natl. Acad. Sci. U.S.A. 103:395-400(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AICDA.
    14. "Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6."
      Zhang F., Hu Y., Huang P., Toleman C.A., Paterson A.J., Kudlow J.E.
      J. Biol. Chem. 282:22460-22471(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEASOME REGULATION, FUNCTION AS PSMC5/RPT6 KINASE.
    15. "Functional consequence of protein kinase A-dependent phosphorylation of the cardiac ryanodine receptor: sensitization of store overload-induced Ca2+ release."
      Xiao B., Tian X., Xie W., Jones P.P., Cai S., Wang X., Jiang D., Kong H., Zhang L., Chen K., Walsh M.P., Cheng H., Chen S.R.W.
      J. Biol. Chem. 282:30256-30264(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RYR2 KINASE.
    16. "Vitamin K2 induces phosphorylation of protein kinase A and expression of novel target genes in osteoblastic cells."
      Ichikawa T., Horie-Inoue K., Ikeda K., Blumberg B., Inoue S.
      J. Mol. Endocrinol. 39:239-247(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, ENZYME REGULATION.
    17. "Activation of protein kinase A (PKA) signaling mitigates the antiproliferative and antiinvasive effects of alpha-difluoromethylornithine in breast cancer cells."
      Xu H., Washington S., Verderame M.F., Manni A.
      Breast Cancer Res. Treat. 107:63-70(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ALPHA-DIFLUOROMETHYLORNITHINE ANTAGONIST.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif."
      Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M., Io K., Sato T., Sato H., Uchiyama T.
      Nat. Struct. Mol. Biol. 15:1184-1191(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APOBEC3G.
    20. Cited for: ENZYME REGULATION, MUTAGENESIS OF TYR-205.
    21. "Gravin dynamics regulates the subcellular distribution of PKA."
      Yan X., Walkiewicz M., Carlson J., Leiphon L., Grove B.
      Exp. Cell Res. 315:1247-1259(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex."
      Gambaryan S., Kobsar A., Rukoyatkina N., Herterich S., Geiger J., Smolenski A., Lohmann S.M., Walter U.
      J. Biol. Chem. 285:18352-18363(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PLATELETS, FUNCTION AS VASP KINASE, INTERACTION WITH NFKB1; NFKB2 AND NFKBIA.
    25. "High glucose stimulates adipogenic and inhibits osteogenic differentiation in MG-63 cells through cAMP/protein kinase A/extracellular signal-regulated kinase pathway."
      Wang W., Zhang X., Zheng J., Yang J.
      Mol. Cell. Biochem. 338:115-122(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION, ENZYME REGULATION.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Protein kinase A activates and phosphorylates ROR?4 in vitro and takes part in ROR? activation by CaMK-IV."
      Ermisch M., Firla B., Steinhilber D.
      Biochem. Biophys. Res. Commun. 408:442-446(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RORA KINASE.
    28. "The testis-specific C?2 subunit of PKA is kinetically indistinguishable from the common C?1 subunit of PKA."
      Vetter M.M., Zenn H.-M., Mendez E., van den Boom H., Herberg F.W., Skaalhegg B.S.
      BMC Biochem. 12:40-40(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS KINASE, TISSUE SPECIFICITY, INTERACTION WITH PRKAR1A/PKR1 AND PRKAR2A/PKR2.
    29. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    30. "Discovery of 2-pyrimidyl-5-amidothiophenes as potent inhibitors for AKT: synthesis and SAR studies."
      Lin X., Murray J.M., Rico A.C., Wang M.X., Chu D.T., Zhou Y., Del Rosario M., Kaufman S., Ma S., Fang E., Crawford K., Jefferson A.B.
      Bioorg. Med. Chem. Lett. 16:4163-4168(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 15-351, PHOSPHORYLATION AT THR-198 AND SER-339.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND SER-339, ENZYME REGULATION.
    32. Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND SER-339, ENZYME REGULATION.
    33. "Diversity of bisubstrate binding modes of adenosine analogue-oligoarginine conjugates in protein kinase a and implications for protein substrate interactions."
      Pflug A., Rogozina J., Lavogina D., Enkvist E., Uri A., Engh R.A., Bossemeyer D.
      J. Mol. Biol. 403:66-77(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOG, PHOSPHORYLATION AT SER-11; THR-198 AND SER-339, ENZYME REGULATION.
    34. "Mutants of protein kinase A that mimic the ATP-binding site of Aurora kinase."
      Pflug A., de Oliveira T.M., Bossemeyer D., Engh R.A.
      Biochem. J. 440:85-93(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH AURORA KINASE INHIBITORS, PHOSPHORYLATION AT SER-11; THR-198 AND SER-339, MUTAGENESIS OF LYS-48; LEU-96; MET-121; VAL-124; GLN-182 AND THR-184.
    35. "Experimental active site mapping as a starting point to fragment-based lead discovery."
      Behnen J., Koester H., Ritschel T., Neudert G., Heine A., Klebe G.
      Submitted (JUL-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND SER-339.
    36. "Fragment based drug design on PKA."
      Koester H., Craan T., Brass S., Heine A., Klebe G.
      Submitted (SEP-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
    37. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-41; GLN-46 AND CYS-264.

    Entry informationi

    Entry nameiKAPCA_HUMAN
    AccessioniPrimary (citable) accession number: P17612
    Secondary accession number(s): Q32P54
    , Q9H2Y0, Q9NRB4, Q9NRH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 171 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3