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P22694 (KAPCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase catalytic subunit beta

Short name=PKA C-beta
EC=2.7.11.11
Gene names
Name:PRKACB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Activated by cAMP.

Subunit structure

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.

Subcellular location

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. Ref.13

Tissue specificity

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. Ref.9

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
cAMP
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase C activity

Traceable author statement. Source: Reactome

activation of protein kinase A activity

Traceable author statement. Source: Reactome

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement Ref.10. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to glucagon stimulus

Traceable author statement. Source: Reactome

energy reserve metabolic process

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Traceable author statement. Source: Reactome

negative regulation of meiotic cell cycle

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

protein phosphorylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of insulin secretion

Traceable author statement. Source: Reactome

response to clozapine

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

triglyceride catabolic process

Traceable author statement. Source: Reactome

water transport

Traceable author statement. Source: Reactome

   Cellular_componentcAMP-dependent protein kinase complex

Traceable author statement Ref.10. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.10. Source: UniProtKB

cAMP-dependent protein kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22939624PubMed 23455922PubMed 21880142. Source: IntAct

ubiquitin protein ligase binding

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GPKOWQ929174EBI-5258763,EBI-746309
HSP90AB1P082382EBI-2679622,EBI-352572

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22694-1)

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.
Isoform 2 (identifier: P22694-2)

Also known as: Beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     2-16: GNAATAKKGSEVESV → MAAYREPPCN...EHTALWDRSM
Isoform 3 (identifier: P22694-3)

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.
Isoform 4 (identifier: P22694-4)

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.
Isoform 5 (identifier: P22694-5)

Also known as: Beta4ab;

The sequence of this isoform differs from the canonical sequence as follows:
     2-14: GNAATAKKGSEVE → MSARKSSDASACSSSEI
Note: Incomplete sequence.
Isoform 6 (identifier: P22694-6)

Also known as: Beta4abc;

The sequence of this isoform differs from the canonical sequence as follows:
     2-15: GNAATAKKGSEVES → MSARKSSDASACSSSEISDSF
Isoform 7 (identifier: P22694-7)

The sequence of this isoform differs from the canonical sequence as follows:
     2-14: GNAATAKKGSEVE → MGLSRKSSDASACSSSEI
Note: No experimental confirmation available.
Isoform 8 (identifier: P22694-8)

The sequence of this isoform differs from the canonical sequence as follows:
     256-257: VR → NF
     258-351: Missing.
Isoform 9 (identifier: P22694-9)

The sequence of this isoform differs from the canonical sequence as follows:
     2-15: GNAATAKKGSEVES → MGLSRKSSDASACSSSEISDSF
Note: No experimental confirmation available.
Isoform 10 (identifier: P22694-10)

The sequence of this isoform differs from the canonical sequence as follows:
     2-14: GNAATAKKGSEVE → MSARKSSDASACSSSEI
     79-111: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 351350cAMP-dependent protein kinase catalytic subunit beta
PRO_0000086060

Regions

Domain44 – 298255Protein kinase
Domain299 – 35153AGC-kinase C-terminal
Nucleotide binding50 – 589ATP By similarity

Sites

Active site1671Proton acceptor By similarity
Binding site731ATP By similarity

Amino acid modifications

Modified residue31Deamidated asparagine By similarity
Modified residue111Phosphoserine By similarity
Modified residue491Phosphothreonine By similarity
Modified residue691Phosphotyrosine By similarity
Modified residue1401Phosphoserine By similarity
Modified residue1961Phosphothreonine By similarity
Modified residue1981Phosphothreonine By similarity
Modified residue2021Phosphothreonine By similarity
Modified residue3311Phosphotyrosine By similarity
Modified residue3391Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence2 – 1615GNAAT…EVESV → MAAYREPPCNQYTGTTTALQ KLEGFASRLFHRHSKGTAHD QKTALENDSLHFSEHTALWD RSM in isoform 2.
VSP_017364
Alternative sequence2 – 1514GNAAT…SEVES → MSARKSSDASACSSSEISDS F in isoform 6.
VSP_017365
Alternative sequence2 – 1514GNAAT…SEVES → MGLSRKSSDASACSSSEISD SF in isoform 9.
VSP_043372
Alternative sequence2 – 1413GNAAT…GSEVE → MSARKSSDASACSSSEI in isoform 5 and isoform 10.
VSP_017366
Alternative sequence2 – 1413GNAAT…GSEVE → MGLSRKSSDASACSSSEI in isoform 7.
VSP_017367
Alternative sequence2 – 1312Missing in isoform 4.
VSP_017368
Alternative sequence2 – 1211Missing in isoform 3.
VSP_017369
Alternative sequence13 – 164VESV → MGLL in isoform 3.
VSP_017370
Alternative sequence141E → M in isoform 4.
VSP_017371
Alternative sequence79 – 11133Missing in isoform 10.
VSP_046238
Alternative sequence256 – 2572VR → NF in isoform 8.
VSP_036556
Alternative sequence258 – 35194Missing in isoform 8.
VSP_036557
Natural variant1061R → Q. Ref.14
Corresponds to variant rs36117118 [ dbSNP | Ensembl ].
VAR_040594

Experimental info

Sequence conflict801V → G in CAI56774. Ref.3
Sequence conflict1591H → N in AAH35058. Ref.8
Sequence conflict1631L → I in AAH35058. Ref.8
Sequence conflict2331A → V in CAI56774. Ref.3
Sequence conflict2611H → N in AAH35058. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta1) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5C7443FBBA1C9BEC

FASTA35140,623
        10         20         30         40         50         60 
MGNAATAKKG SEVESVKEFL AKAKEDFLKK WENPTQNNAG LEDFERKKTL GTGSFGRVML 

        70         80         90        100        110        120 
VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEYA FKDNSNLYMV 

       130        140        150        160        170        180 
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY 

       190        200        210        220        230        240 
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF 

       250        260        270        280        290        300 
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT 

       310        320        330        340        350 
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCAKEFGE F 

« Hide

Isoform 2 (Beta2) [UniParc].

Checksum: 96D31C1652D9F4C9
Show »

FASTA39946,367
Isoform 3 (Beta3) [UniParc].

Checksum: C3DCB03C01C532F0
Show »

FASTA34039,608
Isoform 4 (Beta4) [UniParc].

Checksum: CE57849B1AF7D4B6
Show »

FASTA33939,511
Isoform 5 (Beta4ab) [UniParc].

Checksum: ABBF3A14632A0593
Show »

FASTA35541,078
Isoform 6 (Beta4abc) [UniParc].

Checksum: 41F071991FB5619C
Show »

FASTA35841,428
Isoform 7 [UniParc].

Checksum: 3015C1F5B0611244
Show »

FASTA35641,177
Isoform 8 [UniParc].

Checksum: 38FCBB18E1BF2761
Show »

FASTA25729,696
Isoform 9 [UniParc].

Checksum: 22BFCA12B54E804F
Show »

FASTA35941,527
Isoform 10 [UniParc].

Checksum: 5E440A66F910EF71
Show »

FASTA32237,110

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Control of PKA stability and signalling by the RING ligase praja2."
Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R., Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.
Nat. Cell Biol. 13:412-422(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS55609.1. [P22694-9]
CCDS55610.1. [P22694-7]
CCDS55611.1. [P22694-10]
CCDS691.1. [P22694-1]
CCDS692.1. [P22694-8]
CCDS693.1. [P22694-2]
PIROKHUCB. A34724.
RefSeqNP_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]
UniGeneHs.487325.

3D structure databases

ProteinModelPortalP22694.
SMRP22694. Positions 15-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111554. 132 interactions.
IntActP22694. 31 interactions.
MINTMINT-1178341.

Chemistry

BindingDBP22694.
ChEMBLCHEMBL2918.
GuidetoPHARMACOLOGY1477.

PTM databases

PhosphoSiteP22694.

Polymorphism databases

DMDM125210.

Proteomic databases

MaxQBP22694.
PaxDbP22694.
PRIDEP22694.

Protocols and materials databases

DNASU5567.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370682; 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]
GeneID5567.
KEGGhsa:5567.
UCSCuc001dji.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

CTD5567.
GeneCardsGC01P084543.
HGNCHGNC:9381. PRKACB.
HPACAB010363.
HPA029754.
MIM176892. gene.
neXtProtNX_P22694.
PharmGKBPA33749.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG108317.
KOK04345.
OMAGKEFCEF.
OrthoDBEOG7VX8WD.
PhylomeDBP22694.
TreeFamTF313399.

Enzyme and pathway databases

BRENDA2.7.11.11. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP22694.

Gene expression databases

ArrayExpressP22694.
BgeeP22694.
GenevestigatorP22694.

Family and domain databases

InterProIPR000961. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSPRKACB. human.
GeneWikiPRKACB.
GenomeRNAi5567.
NextBio21570.
PROP22694.
SOURCESearch...

Entry information

Entry nameKAPCB_HUMAN
AccessionPrimary (citable) accession number: P22694
Secondary accession number(s): B1APG4 expand/collapse secondary AC list , B4DKB0, B4E2Q1, Q14VH1, Q59GC0, Q5BNE9, Q5BNF0, Q5BNF1, Q5BNF2, Q5BNF3, Q5CZ92, Q5T1K3, Q7Z3M1, Q8IYR5, Q8IZQ0, Q96B09
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM