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P68181

- KAPCB_MOUSE

UniProt

P68181 - KAPCB_MOUSE

Protein

cAMP-dependent protein kinase catalytic subunit beta

Gene

Prkacb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (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 By similarity.By similarity

    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

    GO - Biological processi

    1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
    2. negative regulation of meiotic cell cycle Source: Ensembl
    3. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
    4. neural tube closure Source: MGI
    5. protein phosphorylation Source: UniProtKB
    6. regulation of protein processing Source: MGI
    7. response to clozapine Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, cAMP, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_203795. DARPP-32 events.
    REACT_213852. PKA-mediated phosphorylation of CREB.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_220108. PKA activation.
    REACT_220758. PKA activation in glucagon signalling.
    REACT_225836. Interleukin-3, 5 and GM-CSF 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: 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

    1. cAMP-dependent protein kinase complex Source: UniProtKB
    2. centrosome Source: Ensembl
    3. ciliary base Source: MGI
    4. cytosol Source: Reactome
    5. nucleus Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: Ensembl
    7. plasma membrane Source: UniProtKB-SubCell

    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

    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

    ArrayExpressiP68181.
    BgeeiP68181.
    CleanExiMM_PRKACB.
    GenevestigatoriP68181.

    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. 5 interactions.
    MINTiMINT-4099395.

    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.
    GeneTreeiENSGT00550000074358.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    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_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 (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. Align

    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

    MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL    50
    GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE 100
    FPFLVRLEYS 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 YEEEEIRVSI TEKCGKEFCE 350
    F 351
    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:
         2-13: Missing.
         14-15: ES → MN

    Show »
    Length:339
    Mass (Da):39,581
    Checksum:i358F1764027B55F5
    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:
         2-12: Missing.
         13-16: VESV → MGLL

    Show »
    Length:340
    Mass (Da):39,651
    Checksum:i3EC91AF8D1418BB7
    GO
    Isoform 4 (identifier: P68181-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-16: GNTAIAKKGSEVESV → MAAHKELSSG...EHTASWDKSM

    Note: No experimental confirmation available.

    Show »
    Length:399
    Mass (Da):46,145
    Checksum:i36FF9CACFDA225BE
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 1615GNTAI…EVESV → MAAHKELSSGQHSGTPTALQ KLEGFASRLFHRHSRGTAQE HRAALEDDGLRASEHTASWD KSM in isoform 4. 1 PublicationVSP_017376Add
    BLAST
    Alternative sequencei2 – 1312Missing in isoform 2. 1 PublicationVSP_017373Add
    BLAST
    Alternative sequencei2 – 1211Missing 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:
    EMBL
    GenBank
    DDBJ
    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]
    PIRiA24596. OKMSCB.
    RefSeqiNP_001157670.1. NM_001164198.1.
    NP_001157671.1. NM_001164199.1.
    NP_001157672.1. NM_001164200.1.
    NP_035230.1. NM_011100.4. [P68181-1]
    UniGeneiMm.16766.

    Genome annotation databases

    EnsembliENSMUST00000005164; ENSMUSP00000005164; ENSMUSG00000005034.
    ENSMUST00000102515; ENSMUSP00000099573; ENSMUSG00000005034. [P68181-1]
    ENSMUST00000106137; ENSMUSP00000101743; ENSMUSG00000005034.
    ENSMUST00000106138; ENSMUSP00000101744; ENSMUSG00000005034.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17906.1. [P68181-1 ]
    PIRi A24596. OKMSCB.
    RefSeqi NP_001157670.1. NM_001164198.1.
    NP_001157671.1. NM_001164199.1.
    NP_001157672.1. NM_001164200.1.
    NP_035230.1. NM_011100.4. [P68181-1 ]
    UniGenei Mm.16766.

    3D structure databases

    ProteinModelPortali P68181.
    SMRi P68181. Positions 15-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202193. 2 interactions.
    IntActi P68181. 5 interactions.
    MINTi MINT-4099395.

    Chemistry

    BindingDBi P68181.

    PTM databases

    PhosphoSitei P68181.

    Proteomic databases

    PaxDbi P68181.
    PRIDEi P68181.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005164 ; ENSMUSP00000005164 ; ENSMUSG00000005034 .
    ENSMUST00000102515 ; ENSMUSP00000099573 ; ENSMUSG00000005034 . [P68181-1 ]
    ENSMUST00000106137 ; ENSMUSP00000101743 ; ENSMUSG00000005034 .
    ENSMUST00000106138 ; ENSMUSP00000101744 ; ENSMUSG00000005034 .
    GeneIDi 18749.
    KEGGi mmu:18749.
    UCSCi uc008rrs.2. mouse. [P68181-2 ]
    uc008rrt.2. mouse. [P68181-3 ]
    uc008rru.1. mouse. [P68181-4 ]
    uc008rrv.2. mouse. [P68181-1 ]

    Organism-specific databases

    CTDi 5567.
    MGIi MGI:97594. Prkacb.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074358.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    KOi K04345.
    OMAi GKEFCEF.
    OrthoDBi EOG7VX8WD.
    PhylomeDBi P68181.
    TreeFami TF313399.

    Enzyme and pathway databases

    Reactomei REACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_203795. DARPP-32 events.
    REACT_213852. PKA-mediated phosphorylation of CREB.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_220108. PKA activation.
    REACT_220758. PKA activation in glucagon signalling.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

    Miscellaneous databases

    NextBioi 294913.
    PROi P68181.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68181.
    Bgeei P68181.
    CleanExi MM_PRKACB.
    Genevestigatori P68181.

    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. "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: October 1, 2014
    This is version 109 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