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P22694

- KAPCB_HUMAN

UniProt

P22694 - KAPCB_HUMAN

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Protein

cAMP-dependent protein kinase catalytic subunit beta

Gene
PRKACB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. 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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Activated by cAMP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATP By similarity
Active sitei167 – 1671Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. cAMP-dependent protein kinase activity Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. 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. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
  4. blood coagulation Source: Reactome
  5. carbohydrate metabolic process Source: Reactome
  6. cellular response to glucagon stimulus Source: Reactome
  7. energy reserve metabolic process Source: Reactome
  8. epidermal growth factor receptor signaling pathway Source: Reactome
  9. fibroblast growth factor receptor signaling pathway Source: Reactome
  10. gluconeogenesis Source: Reactome
  11. glucose metabolic process Source: Reactome
  12. innate immune response Source: Reactome
  13. intracellular signal transduction Source: Reactome
  14. negative regulation of meiotic cell cycle Source: Ensembl
  15. neurotrophin TRK receptor signaling pathway Source: Reactome
  16. protein phosphorylation Source: UniProtKB
  17. regulation of insulin secretion Source: Reactome
  18. response to clozapine Source: Ensembl
  19. signal transduction Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. synaptic transmission Source: Reactome
  22. transmembrane transport Source: Reactome
  23. triglyceride catabolic process Source: Reactome
  24. 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_15334. DARPP-32 events.
REACT_15497. PKA-mediated phosphorylation of CREB.
REACT_15530. PKA activation.
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.
SignaLinkiP22694.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit beta (EC:2.7.11.11)
Short name:
PKA C-beta
Gene namesi
Name:PRKACB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9381. PRKACB.

Subcellular locationi

Cytoplasm. Cell membrane. Nucleus By similarity
Note: Translocates into the nucleus (monomeric catalytic subunit) By similarity. The inactive holoenzyme is found in the cytoplasm By similarity.1 Publication

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. nucleoplasm Source: Reactome
  6. perinuclear region of cytoplasm Source: Ensembl
  7. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit betaPRO_0000086060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Modified residuei3 – 31Deamidated asparagine By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei49 – 491Phosphothreonine By similarity
Modified residuei69 – 691Phosphotyrosine By similarity
Modified residuei140 – 1401Phosphoserine By similarity
Modified residuei196 – 1961Phosphothreonine By similarity
Modified residuei198 – 1981Phosphothreonine By similarity
Modified residuei202 – 2021Phosphothreonine By similarity
Modified residuei331 – 3311Phosphotyrosine By similarity
Modified residuei339 – 3391Phosphoserine By similarity

Post-translational modificationi

Asn-3 is partially deaminated to Asp giving rise to 2 major isoelectric variants, called CB and CA respectively By similarity.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP22694.
PaxDbiP22694.
PRIDEiP22694.

PTM databases

PhosphoSiteiP22694.

Expressioni

Tissue specificityi

Isoform 1 is most abundant in the brain, with low level expression in kidney. Isoform 2 is predominantly expressed in thymus, spleen and kidney. Isoform 3 and isoform 4 are only expressed in the brain.1 Publication

Gene expression databases

ArrayExpressiP22694.
BgeeiP22694.
GenevestigatoriP22694.

Organism-specific databases

HPAiCAB010363.
HPA029754.

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 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
GPKOWQ929174EBI-5258763,EBI-746309
HSP90AB1P082382EBI-2679622,EBI-352572

Protein-protein interaction databases

BioGridi111554. 43 interactions.
IntActiP22694. 31 interactions.
MINTiMINT-1178341.

Structurei

3D structure databases

ProteinModelPortaliP22694.
SMRiP22694. Positions 15-351.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
KOiK04345.
OMAiGKEFCEF.
OrthoDBiEOG7VX8WD.
PhylomeDBiP22694.
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 (10)i

Sequence statusi: Complete.

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

This entry describes 10 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P22694-1) [UniParc]FASTAAdd to Basket

Also known as: Beta1

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

MGNAATAKKG SEVESVKEFL AKAKEDFLKK WENPTQNNAG LEDFERKKTL    50
GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN 100
FPFLVRLEYA FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ 150
IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC 200
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK 250
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT 300
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCAKEFGE 350
F 351
Length:351
Mass (Da):40,623
Last modified:January 23, 2007 - v2
Checksum:i5C7443FBBA1C9BEC
GO
Isoform 2 (identifier: P22694-2) [UniParc]FASTAAdd to Basket

Also known as: Beta2

The sequence of this isoform differs from the canonical sequence as follows:
     2-16: GNAATAKKGSEVESV → MAAYREPPCN...EHTALWDRSM

Show »
Length:399
Mass (Da):46,367
Checksum:i96D31C1652D9F4C9
GO
Isoform 3 (identifier: P22694-3) [UniParc]FASTAAdd to Basket

Also known as: Beta3

The sequence of this isoform differs from the canonical sequence as follows:
     2-12: Missing.
     13-16: VESV → MGLL

Note: Incomplete sequence.

Show »
Length:340
Mass (Da):39,608
Checksum:iC3DCB03C01C532F0
GO
Isoform 4 (identifier: P22694-4) [UniParc]FASTAAdd to Basket

Also known as: Beta4

The sequence of this isoform differs from the canonical sequence as follows:
     2-13: Missing.
     14-14: E → M

Note: Incomplete sequence.

Show »
Length:339
Mass (Da):39,511
Checksum:iCE57849B1AF7D4B6
GO
Isoform 5 (identifier: P22694-5) [UniParc]FASTAAdd to Basket

Also known as: Beta4ab

The sequence of this isoform differs from the canonical sequence as follows:
     2-14: GNAATAKKGSEVE → MSARKSSDASACSSSEI

Note: Incomplete sequence.

Show »
Length:355
Mass (Da):41,078
Checksum:iABBF3A14632A0593
GO
Isoform 6 (identifier: P22694-6) [UniParc]FASTAAdd to Basket

Also known as: Beta4abc

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

Show »
Length:358
Mass (Da):41,428
Checksum:i41F071991FB5619C
GO
Isoform 7 (identifier: P22694-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-14: GNAATAKKGSEVE → MGLSRKSSDASACSSSEI

Note: No experimental confirmation available.

Show »
Length:356
Mass (Da):41,177
Checksum:i3015C1F5B0611244
GO
Isoform 8 (identifier: P22694-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     256-257: VR → NF
     258-351: Missing.

Show »
Length:257
Mass (Da):29,696
Checksum:i38FCBB18E1BF2761
GO
Isoform 9 (identifier: P22694-9) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:359
Mass (Da):41,527
Checksum:i22BFCA12B54E804F
GO
Isoform 10 (identifier: P22694-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-14: GNAATAKKGSEVE → MSARKSSDASACSSSEI
     79-111: Missing.

Note: No experimental confirmation available.

Show »
Length:322
Mass (Da):37,110
Checksum:i5E440A66F910EF71
GO

Sequence cautioni

The sequence BAD92426.1 differs from that shown. Reason: Frameshift at position 322.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061R → Q.1 Publication
Corresponds to variant rs36117118 [ dbSNP | Ensembl ].
VAR_040594

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 1615GNAAT…EVESV → MAAYREPPCNQYTGTTTALQ KLEGFASRLFHRHSKGTAHD QKTALENDSLHFSEHTALWD RSM in isoform 2. VSP_017364Add
BLAST
Alternative sequencei2 – 1514GNAAT…SEVES → MSARKSSDASACSSSEISDS F in isoform 6. VSP_017365Add
BLAST
Alternative sequencei2 – 1514GNAAT…SEVES → MGLSRKSSDASACSSSEISD SF in isoform 9. VSP_043372Add
BLAST
Alternative sequencei2 – 1413GNAAT…GSEVE → MSARKSSDASACSSSEI in isoform 5 and isoform 10. VSP_017366Add
BLAST
Alternative sequencei2 – 1413GNAAT…GSEVE → MGLSRKSSDASACSSSEI in isoform 7. VSP_017367Add
BLAST
Alternative sequencei2 – 1312Missing in isoform 4. VSP_017368Add
BLAST
Alternative sequencei2 – 1211Missing in isoform 3. VSP_017369Add
BLAST
Alternative sequencei13 – 164VESV → MGLL in isoform 3. VSP_017370
Alternative sequencei14 – 141E → M in isoform 4. VSP_017371
Alternative sequencei79 – 11133Missing in isoform 10. VSP_046238Add
BLAST
Alternative sequencei256 – 2572VR → NF in isoform 8. VSP_036556
Alternative sequencei258 – 35194Missing in isoform 8. VSP_036557Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801V → G in CAI56774. 1 Publication
Sequence conflicti159 – 1591H → N in AAH35058. 1 Publication
Sequence conflicti163 – 1631L → I in AAH35058. 1 Publication
Sequence conflicti233 – 2331A → V in CAI56774. 1 Publication
Sequence conflicti261 – 2611H → N in AAH35058. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34181 mRNA. Translation: AAA60170.1.
BX537705 mRNA. Translation: CAD97818.1.
BX641026 mRNA. Translation: CAE46017.1.
AB209189 mRNA. Translation: BAD92426.1. Sequence problems.
CR936631 mRNA. Translation: CAI56774.1.
AK091420 mRNA. Translation: BAG52356.1.
AK296482 mRNA. Translation: BAG59122.1.
AK304375 mRNA. Translation: BAG65213.1.
DQ667174 Genomic DNA. Translation: ABG25919.1.
AL359504, AL450063 Genomic DNA. Translation: CAI14540.1.
AL359504, AL450063 Genomic DNA. Translation: CAI14541.1.
AL450063, AL359504 Genomic DNA. Translation: CAI16844.1.
AL450063, AL359504 Genomic DNA. Translation: CAI16845.1.
AL450063 Genomic DNA. Translation: CAI16846.1.
CH471097 Genomic DNA. Translation: EAW73248.1.
BC016285 mRNA. Translation: AAH16285.1.
BC035058 mRNA. Translation: AAH35058.1.
AY927364 mRNA. Translation: AAX19487.1.
AY927365 mRNA. Translation: AAX19488.1.
AY927366 mRNA. Translation: AAX19489.1.
AY927367 mRNA. Translation: AAX19490.1.
AY927368 mRNA. Translation: AAX19491.1.
AF538872 Genomic DNA. Translation: AAN16454.1.
CCDSiCCDS691.1. [P22694-1]
CCDS692.1. [P22694-8]
PIRiA34724. OKHUCB.
RefSeqiNP_001229786.1. NM_001242857.1.
NP_001229787.1. NM_001242858.1.
NP_001229788.1. NM_001242859.1.
NP_001229789.1. NM_001242860.1.
NP_001229790.1. NM_001242861.1.
NP_001229791.1. NM_001242862.1.
NP_002722.1. NM_002731.2. [P22694-1]
NP_891993.1. NM_182948.2.
NP_997461.1. NM_207578.1. [P22694-8]
UniGeneiHs.487325.

Genome annotation databases

EnsembliENST00000370682; ENSP00000359716; ENSG00000142875. [P22694-7]
ENST00000370685; ENSP00000359719; ENSG00000142875. [P22694-2]
ENST00000370688; ENSP00000359722; ENSG00000142875. [P22694-8]
ENST00000370689; ENSP00000359723; ENSG00000142875. [P22694-1]
ENST00000394838; ENSP00000378314; ENSG00000142875. [P22694-9]
ENST00000394839; ENSP00000378315; ENSG00000142875. [P22694-10]
GeneIDi5567.
KEGGihsa:5567.
UCSCiuc001dji.3. human. [P22694-8]
uc001djj.3. human. [P22694-1]
uc001djl.3. human. [P22694-2]
uc001djn.3. human. [P22694-7]
uc001djp.3. human. [P22694-6]
uc001djq.3. human.
uc010ort.2. human. [P22694-9]
uc010oru.2. human. [P22694-3]

Polymorphism databases

DMDMi125210.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34181 mRNA. Translation: AAA60170.1 .
BX537705 mRNA. Translation: CAD97818.1 .
BX641026 mRNA. Translation: CAE46017.1 .
AB209189 mRNA. Translation: BAD92426.1 . Sequence problems.
CR936631 mRNA. Translation: CAI56774.1 .
AK091420 mRNA. Translation: BAG52356.1 .
AK296482 mRNA. Translation: BAG59122.1 .
AK304375 mRNA. Translation: BAG65213.1 .
DQ667174 Genomic DNA. Translation: ABG25919.1 .
AL359504 , AL450063 Genomic DNA. Translation: CAI14540.1 .
AL359504 , AL450063 Genomic DNA. Translation: CAI14541.1 .
AL450063 , AL359504 Genomic DNA. Translation: CAI16844.1 .
AL450063 , AL359504 Genomic DNA. Translation: CAI16845.1 .
AL450063 Genomic DNA. Translation: CAI16846.1 .
CH471097 Genomic DNA. Translation: EAW73248.1 .
BC016285 mRNA. Translation: AAH16285.1 .
BC035058 mRNA. Translation: AAH35058.1 .
AY927364 mRNA. Translation: AAX19487.1 .
AY927365 mRNA. Translation: AAX19488.1 .
AY927366 mRNA. Translation: AAX19489.1 .
AY927367 mRNA. Translation: AAX19490.1 .
AY927368 mRNA. Translation: AAX19491.1 .
AF538872 Genomic DNA. Translation: AAN16454.1 .
CCDSi CCDS691.1. [P22694-1 ]
CCDS692.1. [P22694-8 ]
PIRi A34724. OKHUCB.
RefSeqi NP_001229786.1. NM_001242857.1.
NP_001229787.1. NM_001242858.1.
NP_001229788.1. NM_001242859.1.
NP_001229789.1. NM_001242860.1.
NP_001229790.1. NM_001242861.1.
NP_001229791.1. NM_001242862.1.
NP_002722.1. NM_002731.2. [P22694-1 ]
NP_891993.1. NM_182948.2.
NP_997461.1. NM_207578.1. [P22694-8 ]
UniGenei Hs.487325.

3D structure databases

ProteinModelPortali P22694.
SMRi P22694. Positions 15-351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111554. 43 interactions.
IntActi P22694. 31 interactions.
MINTi MINT-1178341.

Chemistry

BindingDBi P22694.
ChEMBLi CHEMBL2918.
GuidetoPHARMACOLOGYi 1477.

PTM databases

PhosphoSitei P22694.

Polymorphism databases

DMDMi 125210.

Proteomic databases

MaxQBi P22694.
PaxDbi P22694.
PRIDEi P22694.

Protocols and materials databases

DNASUi 5567.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370682 ; ENSP00000359716 ; ENSG00000142875 . [P22694-7 ]
ENST00000370685 ; ENSP00000359719 ; ENSG00000142875 . [P22694-2 ]
ENST00000370688 ; ENSP00000359722 ; ENSG00000142875 . [P22694-8 ]
ENST00000370689 ; ENSP00000359723 ; ENSG00000142875 . [P22694-1 ]
ENST00000394838 ; ENSP00000378314 ; ENSG00000142875 . [P22694-9 ]
ENST00000394839 ; ENSP00000378315 ; ENSG00000142875 . [P22694-10 ]
GeneIDi 5567.
KEGGi hsa:5567.
UCSCi uc001dji.3. human. [P22694-8 ]
uc001djj.3. human. [P22694-1 ]
uc001djl.3. human. [P22694-2 ]
uc001djn.3. human. [P22694-7 ]
uc001djp.3. human. [P22694-6 ]
uc001djq.3. human.
uc010ort.2. human. [P22694-9 ]
uc010oru.2. human. [P22694-3 ]

Organism-specific databases

CTDi 5567.
GeneCardsi GC01P084543.
HGNCi HGNC:9381. PRKACB.
HPAi CAB010363.
HPA029754.
MIMi 176892. gene.
neXtProti NX_P22694.
PharmGKBi PA33749.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
KOi K04345.
OMAi GKEFCEF.
OrthoDBi EOG7VX8WD.
PhylomeDBi P22694.
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_15334. DARPP-32 events.
REACT_15497. PKA-mediated phosphorylation of CREB.
REACT_15530. PKA activation.
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 P22694.

Miscellaneous databases

ChiTaRSi PRKACB. human.
GeneWikii PRKACB.
GenomeRNAii 5567.
NextBioi 21570.
PROi P22694.
SOURCEi Search...

Gene expression databases

ArrayExpressi P22694.
Bgeei P22694.
Genevestigatori P22694.

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

« Hide 'large scale' publications
  1. "Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis -- representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase."
    Beebe S.J., Oyen O., Sandberg M., Froysa A., Hansson V., Jahnsen T.
    Mol. Endocrinol. 4:465-475(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
    Tissue: Retina and Salivary gland.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Brain.
  4. "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] (ISOFORMS 3; 9 AND 10).
    Tissue: Brain, Thalamus and Trachea.
  5. SeattleSNPs variation discovery resource
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORMS 1 AND 8).
    Tissue: Brain.
  9. "Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase."
    Orstavik S., Reinton N., Frengen E., Langeland B.T., Jahnsen T., Skalhegg B.S.
    Eur. J. Biochem. 268:5066-5073(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-30 (ISOFORMS 2; 5 AND 6), NUCLEOTIDE SEQUENCE [MRNA] OF 1-16 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 4), TISSUE SPECIFICITY.
  10. "c-MYC activates protein kinase A (PKA) by direct transcriptional activation of the PKA catalytic subunit beta (PKA-CB) gene."
    Wu K.-J., Mattioli M., Morse H.C., Dalla-Favera R.
    Oncogene 21:7872-7882(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-15 (ISOFORM 1), FUNCTION.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PJA2.
  14. "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: VARIANT [LARGE SCALE ANALYSIS] GLN-106.

Entry informationi

Entry nameiKAPCB_HUMAN
AccessioniPrimary (citable) accession number: P22694
Secondary accession number(s): B1APG4
, B4DKB0, B4E2Q1, Q14VH1, Q59GC0, Q5BNE9, Q5BNF0, Q5BNF1, Q5BNF2, Q5BNF3, Q5CZ92, Q5T1K3, Q7Z3M1, Q8IYR5, Q8IZQ0, Q96B09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 160 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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