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Protein

cAMP-dependent protein kinase catalytic subunit beta

Gene

Prkacb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

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

  • ATP binding Source: UniProtKB
  • cAMP-dependent protein kinase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
  • negative regulation of meiotic cell cycle Source: Ensembl
  • negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
  • neural tube closure Source: MGI
  • protein phosphorylation Source: UniProtKB
  • regulation of protein processing Source: MGI
  • response to clozapine Source: Ensembl
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. 3474.
ReactomeiREACT_278699. Hedgehog 'off' state.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_287123. PKA-mediated phosphorylation of key metabolic factors.
REACT_295338. PKA activation in glucagon signalling.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_303391. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_306614. Regulation of insulin secretion.
REACT_307305. Rap1 signalling.
REACT_308431. Gluconeogenesis.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_310977. PKA activation.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_325290. DARPP-32 events.
REACT_336227. PKA-mediated phosphorylation of CREB.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360524. CD209 (DC-SIGN) signaling.

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
Synonyms:Pkacb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:97594. Prkacb.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity
  • Nucleus By similarity

  • Note: Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm.By similarity

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: UniProtKB
  • centrosome Source: MGI
  • ciliary base Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit betaPRO_0000086061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei3 – 31Deamidated asparagineBy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei49 – 491PhosphothreonineBy similarity
Modified residuei69 – 691Phosphotyrosine1 Publication
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 deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP68181.
PaxDbiP68181.
PRIDEiP68181.

PTM databases

PhosphoSiteiP68181.

Expressioni

Tissue specificityi

Isoform 1 is found in all tissues examined, with the highest expression in the brain and very low levels in the testis. Isoform 2 is strongly expressed in the brain, in the prelimbic and insular cortex. Isoform 3 is also found only in the brain, but at very low levels.1 Publication

Gene expression databases

BgeeiP68181.
CleanExiMM_PRKACB.
ExpressionAtlasiP68181. baseline and differential.
GenevisibleiP68181. MM.

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

Protein-protein interaction databases

BioGridi202193. 2 interactions.
IntActiP68181. 6 interactions.
MINTiMINT-4099395.
STRINGi10090.ENSMUSP00000005164.

Structurei

3D structure databases

ProteinModelPortaliP68181.
SMRiP68181. 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.
GeneTreeiENSGT00790000122941.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP68181.
KOiK04345.
OMAiGKEFCEF.
OrthoDBiEOG7VX8WD.
PhylomeDBiP68181.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68181-1) [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

        10         20         30         40         50
MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL
60 70 80 90 100
GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE
110 120 130 140 150
FPFLVRLEYS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ
160 170 180 190 200
IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC
210 220 230 240 250
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK
260 270 280 290 300
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT
310 320 330 340 350
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEEIRVSI TEKCGKEFCE

F
Length:351
Mass (Da):40,708
Last modified:January 23, 2007 - v2
Checksum:iEBAC9B8041DF9F47
GO
Isoform 2 (identifier: P68181-2) [UniParc]FASTAAdd to basket

Also known as: Beta2

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.
     14-15: ES → MN

Show »
Length:338
Mass (Da):39,449
Checksum:i346B9D8B775CA4B6
GO
Isoform 3 (identifier: P68181-3) [UniParc]FASTAAdd to basket

Also known as: Beta3

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
     13-16: VESV → MGLL

Show »
Length:339
Mass (Da):39,520
Checksum:i5018FE723E34AC46
GO
Isoform 4 (identifier: P68181-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MGNTAIAKKGSEVESV → MAAHKELSSG...EHTASWDKSM

Note: No experimental confirmation available.
Show »
Length:398
Mass (Da):46,014
Checksum:iE9C32F84ED1FB98B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616MGNTA…EVESV → MAAHKELSSGQHSGTPTALQ KLEGFASRLFHRHSRGTAQE HRAALEDDGLRASEHTASWD KSM in isoform 4. 1 PublicationVSP_017376Add
BLAST
Alternative sequencei1 – 1313Missing in isoform 2. 1 PublicationVSP_017373Add
BLAST
Alternative sequencei1 – 1212Missing in isoform 3. 1 PublicationVSP_017372Add
BLAST
Alternative sequencei13 – 164VESV → MGLL in isoform 3. 1 PublicationVSP_017375
Alternative sequencei14 – 152ES → MN in isoform 2. 1 PublicationVSP_017374

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02626 mRNA. Translation: AAA39941.1.
AK048319 mRNA. Translation: BAC33301.1.
AK139419 mRNA. Translation: BAE24005.1.
AK148728 mRNA. Translation: BAE28648.1.
AK150122 mRNA. Translation: BAE29323.1.
AK150134 mRNA. Translation: BAE29331.1.
AK163585 mRNA. Translation: BAE37407.1.
BC054533 mRNA. Translation: AAH54533.1.
M21096 Genomic DNA. Translation: AAA39938.1.
AF022239 Genomic DNA. No translation available.
X61434 mRNA. Translation: CAA43676.1.
CCDSiCCDS17906.1. [P68181-1]
CCDS51090.1. [P68181-2]
CCDS51091.1. [P68181-3]
CCDS51092.1. [P68181-4]
PIRiA24596. OKMSCB.
RefSeqiNP_001157670.1. NM_001164198.1. [P68181-2]
NP_001157671.1. NM_001164199.1. [P68181-3]
NP_001157672.1. NM_001164200.1. [P68181-4]
NP_035230.1. NM_011100.4. [P68181-1]
UniGeneiMm.16766.

Genome annotation databases

EnsembliENSMUST00000005164; ENSMUSP00000005164; ENSMUSG00000005034. [P68181-4]
ENSMUST00000102515; ENSMUSP00000099573; ENSMUSG00000005034. [P68181-1]
ENSMUST00000106137; ENSMUSP00000101743; ENSMUSG00000005034. [P68181-2]
ENSMUST00000106138; ENSMUSP00000101744; ENSMUSG00000005034. [P68181-3]
GeneIDi18749.
KEGGimmu:18749.
UCSCiuc008rrs.2. mouse. [P68181-2]
uc008rrt.2. mouse. [P68181-3]
uc008rru.1. mouse. [P68181-4]
uc008rrv.2. mouse. [P68181-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02626 mRNA. Translation: AAA39941.1.
AK048319 mRNA. Translation: BAC33301.1.
AK139419 mRNA. Translation: BAE24005.1.
AK148728 mRNA. Translation: BAE28648.1.
AK150122 mRNA. Translation: BAE29323.1.
AK150134 mRNA. Translation: BAE29331.1.
AK163585 mRNA. Translation: BAE37407.1.
BC054533 mRNA. Translation: AAH54533.1.
M21096 Genomic DNA. Translation: AAA39938.1.
AF022239 Genomic DNA. No translation available.
X61434 mRNA. Translation: CAA43676.1.
CCDSiCCDS17906.1. [P68181-1]
CCDS51090.1. [P68181-2]
CCDS51091.1. [P68181-3]
CCDS51092.1. [P68181-4]
PIRiA24596. OKMSCB.
RefSeqiNP_001157670.1. NM_001164198.1. [P68181-2]
NP_001157671.1. NM_001164199.1. [P68181-3]
NP_001157672.1. NM_001164200.1. [P68181-4]
NP_035230.1. NM_011100.4. [P68181-1]
UniGeneiMm.16766.

3D structure databases

ProteinModelPortaliP68181.
SMRiP68181. Positions 15-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202193. 2 interactions.
IntActiP68181. 6 interactions.
MINTiMINT-4099395.
STRINGi10090.ENSMUSP00000005164.

Chemistry

BindingDBiP68181.

PTM databases

PhosphoSiteiP68181.

Proteomic databases

MaxQBiP68181.
PaxDbiP68181.
PRIDEiP68181.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005164; ENSMUSP00000005164; ENSMUSG00000005034. [P68181-4]
ENSMUST00000102515; ENSMUSP00000099573; ENSMUSG00000005034. [P68181-1]
ENSMUST00000106137; ENSMUSP00000101743; ENSMUSG00000005034. [P68181-2]
ENSMUST00000106138; ENSMUSP00000101744; ENSMUSG00000005034. [P68181-3]
GeneIDi18749.
KEGGimmu:18749.
UCSCiuc008rrs.2. mouse. [P68181-2]
uc008rrt.2. mouse. [P68181-3]
uc008rru.1. mouse. [P68181-4]
uc008rrv.2. mouse. [P68181-1]

Organism-specific databases

CTDi5567.
MGIiMGI:97594. Prkacb.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122941.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP68181.
KOiK04345.
OMAiGKEFCEF.
OrthoDBiEOG7VX8WD.
PhylomeDBiP68181.
TreeFamiTF313399.

Enzyme and pathway databases

BRENDAi2.7.11.11. 3474.
ReactomeiREACT_278699. Hedgehog 'off' state.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_287123. PKA-mediated phosphorylation of key metabolic factors.
REACT_295338. PKA activation in glucagon signalling.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_303391. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_306614. Regulation of insulin secretion.
REACT_307305. Rap1 signalling.
REACT_308431. Gluconeogenesis.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_310977. PKA activation.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_325290. DARPP-32 events.
REACT_336227. PKA-mediated phosphorylation of CREB.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360524. CD209 (DC-SIGN) signaling.

Miscellaneous databases

NextBioi294913.
PROiP68181.
SOURCEiSearch...

Gene expression databases

BgeeiP68181.
CleanExiMM_PRKACB.
ExpressionAtlasiP68181. baseline and differential.
GenevisibleiP68181. MM.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for a second isoform of the catalytic subunit of cAMP-dependent protein kinase."
    Uhler M.D., Chrivia J.C., McKnight G.S.
    J. Biol. Chem. 261:15360-15363(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Adrenal gland and Head.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Characterization of genomic clones coding for the C alpha and C beta subunits of mouse cAMP-dependent protein kinase."
    Chrivia J.C., Uhler M.D., McKnight G.S.
    J. Biol. Chem. 263:5739-5744(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15 (ISOFORM 1).
  5. "Two novel brain-specific splice variants of the murine Cbeta gene of cAMP-dependent protein kinase."
    Guthrie C.R., Skalhegg B.S., McKnight G.S.
    J. Biol. Chem. 272:29560-29565(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7 (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 (ISOFORM 3), FUNCTION, MYRISTOYLATION AT GLY-2, TISSUE SPECIFICITY.
  6. "A collection of cDNA clones with specific expression patterns in mouse brain."
    Kato K.
    Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-351.
    Strain: BALB/c.
    Tissue: Brain.
  7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKAPCB_MOUSE
AccessioniPrimary (citable) accession number: P68181
Secondary accession number(s): P05206
, Q3TQH5, Q3UDD0, Q3UTH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.