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P22694

- KAPCB_HUMAN

UniProt

P22694 - KAPCB_HUMAN

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
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 – 731ATPPROSITE-ProRule annotation
    Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi50 – 589ATPPROSITE-ProRule annotation

    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

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

    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

    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 – 11RemovedBy similarity
    Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit betaPRO_0000086060Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei3 – 31Deamidated asparagineBy similarity
    Modified residuei11 – 111PhosphoserineBy similarity
    Modified residuei49 – 491PhosphothreonineBy similarity
    Modified residuei69 – 691PhosphotyrosineBy similarity
    Modified residuei140 – 1401PhosphoserineBy similarity
    Modified residuei196 – 1961PhosphothreonineBy similarity
    Modified residuei198 – 1981PhosphothreonineBy similarity
    Modified residuei202 – 2021PhosphothreonineBy similarity
    Modified residuei331 – 3311PhosphotyrosineBy similarity
    Modified residuei339 – 3391PhosphoserineBy 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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801V → G in CAI56774. 1 PublicationCurated
    Sequence conflicti159 – 1591H → N in AAH35058. (PubMed:15489334)Curated
    Sequence conflicti163 – 1631L → I in AAH35058. (PubMed:15489334)Curated
    Sequence conflicti233 – 2331A → V in CAI56774. 1 PublicationCurated
    Sequence conflicti261 – 2611H → N in AAH35058. (PubMed:15489334)Curated

    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. 2 PublicationsVSP_017364Add
    BLAST
    Alternative sequencei2 – 1514GNAAT…SEVES → MSARKSSDASACSSSEISDS F in isoform 6. 2 PublicationsVSP_017365Add
    BLAST
    Alternative sequencei2 – 1514GNAAT…SEVES → MGLSRKSSDASACSSSEISD SF in isoform 9. 1 PublicationVSP_043372Add
    BLAST
    Alternative sequencei2 – 1413GNAAT…GSEVE → MSARKSSDASACSSSEI in isoform 5 and isoform 10. 2 PublicationsVSP_017366Add
    BLAST
    Alternative sequencei2 – 1413GNAAT…GSEVE → MGLSRKSSDASACSSSEI in isoform 7. 1 PublicationVSP_017367Add
    BLAST
    Alternative sequencei2 – 1312Missing in isoform 4. 1 PublicationVSP_017368Add
    BLAST
    Alternative sequencei2 – 1211Missing in isoform 3. 2 PublicationsVSP_017369Add
    BLAST
    Alternative sequencei13 – 164VESV → MGLL in isoform 3. 2 PublicationsVSP_017370
    Alternative sequencei14 – 141E → M in isoform 4. 1 PublicationVSP_017371
    Alternative sequencei79 – 11133Missing in isoform 10. 1 PublicationVSP_046238Add
    BLAST
    Alternative sequencei256 – 2572VR → NF in isoform 8. 1 PublicationVSP_036556
    Alternative sequencei258 – 35194Missing in isoform 8. 1 PublicationVSP_036557Add
    BLAST

    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

    EnsembliENST00000370685; 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 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

    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: October 1, 2014
    This is version 161 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