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P17612

- KAPCA_HUMAN

UniProt

P17612 - KAPCA_HUMAN

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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

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 kinase A regulatory subunit binding Source: BHF-UCL
  4. protein kinase binding Source: BHF-UCL
  5. protein serine/threonine/tyrosine kinase activity Source: MGI
  6. 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. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: Ensembl
  23. neural tube closure Source: Ensembl
  24. neurotrophin TRK receptor signaling pathway Source: Reactome
  25. peptidyl-serine phosphorylation Source: BHF-UCL
  26. peptidyl-threonine phosphorylation Source: Ensembl
  27. positive regulation of cell cycle arrest Source: UniProtKB
  28. positive regulation of protein export from nucleus Source: Ensembl
  29. protein autophosphorylation Source: Ensembl
  30. protein phosphorylation Source: UniProtKB
  31. regulation of cardiac muscle contraction Source: BHF-UCL
  32. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  33. regulation of heart rate Source: BHF-UCL
  34. regulation of insulin secretion Source: Reactome
  35. regulation of osteoblast differentiation Source: UniProtKB
  36. regulation of proteasomal protein catabolic process Source: UniProtKB
  37. regulation of protein binding Source: BHF-UCL
  38. regulation of protein processing Source: Ensembl
  39. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  40. regulation of synaptic transmission Source: Ensembl
  41. regulation of tight junction assembly Source: UniProtKB
  42. signal transduction Source: Reactome
  43. small molecule metabolic process Source: Reactome
  44. sperm capacitation Source: UniProtKB
  45. transmembrane transport Source: Reactome
  46. triglyceride catabolic process Source: Reactome
  47. water transport Source: Reactome
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. 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_206597. Degradation of GLI2 by the proteasome.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23898. Rap1 signalling.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_267634. Hedgehog 'off' state.
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. ciliary base Source: Ensembl
  6. cytosol Source: Reactome
  7. extracellular vesicular exosome Source: UniProtKB
  8. mitochondrion Source: UniProtKB-KW
  9. motile cilium Source: UniProtKB-KW
  10. neuromuscular junction Source: Ensembl
  11. nucleus Source: UniProt
  12. plasma membrane Source: UniProtKB-KW
  13. sperm midpiece Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Primary pigmented nodular adrenocortical disease 4 (PPNAD4) [MIM:615830]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061L → R in PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A. 4 Publications
VAR_071707

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

Keywords - Diseasei

Cushing syndrome, Disease mutation

Organism-specific databases

MIMi615830. phenotype.
Orphaneti401920. Fibrolamellar hepatocellular carcinoma.
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 – 491Phosphothreonine1 Publication
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei196 – 1961Phosphothreonine1 Publication
Modified residuei198 – 1981Phosphothreonine; by PDPK17 Publications
Modified residuei202 – 2021Phosphothreonine1 Publication
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei339 – 3391Phosphoserine8 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

BgeeiP17612.
CleanExiHS_PRKACA.
ExpressionAtlasiP17612. baseline and differential.
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. 114 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 – 64Combined 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 – 9813Combined 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
Helixi203 – 2053Combined sources
Helixi208 – 2114Combined sources
Beta strandi212 – 2143Combined sources
Helixi219 – 23416Combined sources
Helixi244 – 25310Combined sources
Helixi264 – 27310Combined sources
Turni278 – 2803Combined sources
Turni282 – 2843Combined sources
Turni286 – 2894Combined sources
Helixi290 – 2934Combined sources
Helixi296 – 2983Combined sources
Helixi303 – 3075Combined sources
Turni345 – 3506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120454.
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.
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

        10         20         30         40         50
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL
60 70 80 90 100
GTGSFGRVML VKHKETGNHY 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):40,590
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:
     1-15: MGNAAAAKKGSEQES → MASNSSD

Show »
Length:343
Mass (Da):39,822
Checksum:i5AD33AECC261EA16
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 varianti206 – 2061L → R in PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A. 4 Publications
VAR_071707
Natural varianti264 – 2641S → C.1 Publication
Corresponds to variant rs35635531 [ dbSNP | Ensembl ].
VAR_040593

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MGNAA…SEQES → MASNSSD in isoform 2. 3 PublicationsVSP_004759Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 114 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.
615830. phenotype.
neXtProti NX_P17612.
Orphaneti 401920. Fibrolamellar hepatocellular carcinoma.
PharmGKBi PA33748.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120454.
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_206597. Degradation of GLI2 by the proteasome.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23898. Rap1 signalling.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_267634. Hedgehog 'off' state.
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

Bgeei P17612.
CleanExi HS_PRKACA.
ExpressionAtlasi P17612. baseline and differential.
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.
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

« Hide 'large scale' publications
  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. Cited for: INVOLVEMENT IN PPNAD4, VARIANT PPNAD4 ARG-206, CHARACTERIZATION OF VARIANT PPNAD4 ARG-206.
  31. "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.
  32. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND SER-339, ENZYME REGULATION.
  33. Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND SER-339, ENZYME REGULATION.
  34. "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.
  35. "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.
  36. "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.
  37. "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).
  38. "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.
  39. Cited for: VARIANT PPNAD4 ARG-206, CHARACTERIZATION OF VARIANT PPNAD4 ARG-206.
  40. Cited for: VARIANT PPNAD4 ARG-206, CHARACTERIZATION OF VARIANT PPNAD4 ARG-206.
  41. Cited for: VARIANT PPNAD4 ARG-206, CHARACTERIZATION OF VARIANT PPNAD4 ARG-206.

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: November 26, 2014
This is version 173 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