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Q62074

- KPCI_MOUSE

UniProt

Q62074 - KPCI_MOUSE

Protein

Protein kinase C iota type

Gene

Prkci

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis By similarity. Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity.By similarity5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-411 (activation loop of the kinase domain) and Thr-563 (turn motif), need to be phosphorylated for its full activation By similarity. Might also be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei282 – 2821ATPPROSITE-ProRule annotation
    Active sitei377 – 3771Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri140 – 19051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi259 – 2679ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phospholipid binding Source: UniProtKB
    3. protein kinase activity Source: UniProtKB
    4. protein kinase C activity Source: BHF-UCL
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament organization Source: MGI
    2. cell-cell junction organization Source: UniProtKB
    3. cell migration Source: Ensembl
    4. cellular protein localization Source: Ensembl
    5. cellular response to insulin stimulus Source: BHF-UCL
    6. establishment of apical/basal cell polarity Source: MGI
    7. eye photoreceptor cell development Source: MGI
    8. Golgi vesicle budding Source: Ensembl
    9. intracellular signal transduction Source: InterPro
    10. negative regulation of glial cell apoptotic process Source: UniProtKB
    11. negative regulation of neuron apoptotic process Source: UniProtKB
    12. positive regulation of endothelial cell apoptotic process Source: UniProtKB
    13. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    14. positive regulation of glial cell proliferation Source: UniProtKB
    15. positive regulation of glucose import Source: BHF-UCL
    16. positive regulation of neuron projection development Source: UniProtKB
    17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    18. protein phosphorylation Source: BHF-UCL
    19. response to interleukin-1 Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 3474.
    ReactomeiREACT_214670. p75NTR recruits signalling complexes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C iota type (EC:2.7.11.13)
    Alternative name(s):
    Atypical protein kinase C-lambda/iota
    Short name:
    aPKC-lambda/iota
    nPKC-iota
    Gene namesi
    Name:Prkci
    Synonyms:Pkcl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:99260. Prkci.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity. Endosome By similarity. Nucleus By similarity
    Note: Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A By similarity.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. apical plasma membrane Source: MGI
    3. cell leading edge Source: Ensembl
    4. cytoplasm Source: MGI
    5. cytosol Source: UniProtKB
    6. endosome Source: UniProtKB-SubCell
    7. Golgi membrane Source: GOC
    8. nucleus Source: UniProtKB
    9. protein complex Source: Ensembl
    10. Schmidt-Lanterman incisure Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic lethal at 9.5 dpc.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 271R → A: No effect on interaction with SQSTM1. 1 Publication
    Mutagenesisi28 – 281V → A: No effect on interaction with SQSTM1; when associated with A-29. 1 Publication
    Mutagenesisi29 – 291K → A: No effect on interaction with SQSTM1; when associated with A-118. 1 Publication
    Mutagenesisi70 – 701W → A: Loss of interaction with SQSTM1. 1 Publication
    Mutagenesisi72 – 721D → A: Loss of interaction with SQSTM1. 1 Publication
    Mutagenesisi74 – 741E → A: Loss of interaction with SQSTM1. 1 Publication
    Mutagenesisi76 – 761D → A: Loss of interaction with SQSTM1. 1 Publication
    Mutagenesisi83 – 831Q → A: No effect on interaction with SQSTM1. 1 Publication
    Mutagenesisi85 – 851E → A: Loss of interaction with SQSTM1. 1 Publication

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 595594Protein kinase C iota typePRO_0000055711Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei3 – 31PhosphothreonineBy similarity
    Modified residuei7 – 71PhosphoserineBy similarity
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei9 – 91PhosphothreonineBy similarity
    Modified residuei264 – 2641Phosphotyrosine; by SRCBy similarity
    Modified residuei279 – 2791Phosphotyrosine; by SRCBy similarity
    Modified residuei333 – 3331Phosphotyrosine; by SRCBy similarity
    Modified residuei411 – 4111Phosphothreonine; alternate1 Publication
    Modified residuei411 – 4111Phosphothreonine; by PDPK1; alternateBy similarity
    Modified residuei563 – 5631Phosphothreonine1 Publication

    Post-translational modificationi

    Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-264, Tyr-279 and Tyr-333. Phosphorylation on Tyr-264 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus. Phosphorylation on Tyr-333 is important for NF-kappa-B stimulation By similarity. Phosphorylation at Thr-411 in the activation loop is not mandatory for activation.By similarity2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ62074.
    PaxDbiQ62074.
    PRIDEiQ62074.

    PTM databases

    PhosphoSiteiQ62074.

    Expressioni

    Gene expression databases

    ArrayExpressiQ62074.
    BgeeiQ62074.
    CleanExiMM_PRKCI.
    GenevestigatoriQ62074.

    Interactioni

    Subunit structurei

    Forms a complex with SQSTM1 and MP2K5 By similarity. Interacts directly with SQSTM1 Probable. Interacts with IKBKB. Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs). Interacts with ECT2 ('Thr-359' phosphorylated form) By similarity.By similarityCurated

    Protein-protein interaction databases

    BioGridi202200. 2 interactions.
    DIPiDIP-32555N.
    IntActiQ62074. 2 interactions.
    MINTiMINT-4100000.

    Structurei

    Secondary structure

    1
    595
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi250 – 2523
    Beta strandi253 – 2619
    Beta strandi263 – 27210
    Turni273 – 2753
    Beta strandi278 – 2858
    Helixi286 – 2883
    Helixi297 – 30812
    Beta strandi317 – 3226
    Beta strandi324 – 3329
    Helixi339 – 3468
    Helixi351 – 37020
    Helixi380 – 3823
    Beta strandi383 – 3853
    Beta strandi391 – 3933
    Helixi416 – 4183
    Helixi421 – 4244
    Helixi432 – 44716
    Turni453 – 4564
    Helixi466 – 47510
    Helixi486 – 49510
    Turni500 – 5023
    Turni508 – 5103
    Helixi511 – 5177
    Turni519 – 5235
    Helixi526 – 5305
    Helixi548 – 5503
    Helixi553 – 5564
    Helixi567 – 5704
    Helixi575 – 5784

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DC2X-ray2.40A231-595[»]
    ProteinModelPortaliQ62074.
    SMRiQ62074. Positions 25-192, 248-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 10884OPRAdd
    BLAST
    Domaini253 – 521269Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini522 – 59574AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 252251Regulatory domainBy similarityAdd
    BLAST
    Regioni2 – 2827Required for interaction with RAB2By similarityAdd
    BLAST
    Regioni72 – 9120Interaction with PARD6ABy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi125 – 13410Pseudosubstrate

    Domaini

    The OPR domain mediates interaction with SQSTM1.
    The C1 zinc finger does not bind diacylglycerol (DAG).By similarity
    The pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins, except the presence of a non-phosphorylatable residue in place of Ser, it modulates activity by competing with substrates.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 OPR domain.Curated
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri140 – 19051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117322.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ62074.
    KOiK06069.
    OMAiFEPSISY.
    OrthoDBiEOG7HF1J3.
    TreeFamiTF102004.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR012233. PKC_zeta.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24357:SF60. PTHR24357:SF60. 1 hit.
    PfamiPF00130. C1_1. 1 hit.
    PF00564. PB1. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000554. PKC_zeta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 1 hit.
    SM00666. PB1. 1 hit.
    SM00133. 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.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q62074-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL    50
    CSEVRDMCSF DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE 100
    LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR 150
    RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPPEPM 200
    MPMDQTMHPD HTQTVIPYNP SSHESLDQVG EEKEAMNTRE SGKASSSLGL 250
    QDFDLLRVIG RGSYAKVLLV RLKKTDRIYA MKVVKKELVN DDEDIDWVQT 300
    EKHVFEQASN HPFLVGLHSC FQTESRLFFV IEYVNGGDLM FHMQRQRKLP 350
    EEHARFYSAE ISLALNYLHE RGIIYRDLKL DNVLLDSEGH IKLTDYGMCK 400
    EGLRPGDTTS TFCGTPNYIA PEILRGEDYG FSVDWWALGV LMFEMMAGRS 450
    PFDIVGSSDN PDQNTEDYLF QVILEKQIRI PRSLSVKAAS VLKSFLNKDP 500
    KERLGCHPQT GFADIQGHPF FRNVDWDMME QKQVVPPFKP NISGEFGLDN 550
    FDSQFTNEPV QLTPDDDDIV RKIDQSEFEG FEYINPLLMS AEECV 595
    Length:595
    Mass (Da):68,203
    Last modified:June 16, 2009 - v3
    Checksum:i6AC612D1E9264825
    GO

    Sequence cautioni

    The sequence AAH21630.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA32499.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28577 mRNA. Translation: BAA32499.1. Different initiation.
    BC021630 mRNA. Translation: AAH21630.1. Different initiation.
    CCDSiCCDS17289.2.
    PIRiA53758.
    RefSeqiNP_032883.2. NM_008857.3.
    UniGeneiMm.291554.

    Genome annotation databases

    EnsembliENSMUST00000108249; ENSMUSP00000103884; ENSMUSG00000037643.
    GeneIDi18759.
    KEGGimmu:18759.
    UCSCiuc008ovs.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28577 mRNA. Translation: BAA32499.1 . Different initiation.
    BC021630 mRNA. Translation: AAH21630.1 . Different initiation.
    CCDSi CCDS17289.2.
    PIRi A53758.
    RefSeqi NP_032883.2. NM_008857.3.
    UniGenei Mm.291554.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DC2 X-ray 2.40 A 231-595 [» ]
    ProteinModelPortali Q62074.
    SMRi Q62074. Positions 25-192, 248-587.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202200. 2 interactions.
    DIPi DIP-32555N.
    IntActi Q62074. 2 interactions.
    MINTi MINT-4100000.

    PTM databases

    PhosphoSitei Q62074.

    Proteomic databases

    MaxQBi Q62074.
    PaxDbi Q62074.
    PRIDEi Q62074.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000108249 ; ENSMUSP00000103884 ; ENSMUSG00000037643 .
    GeneIDi 18759.
    KEGGi mmu:18759.
    UCSCi uc008ovs.1. mouse.

    Organism-specific databases

    CTDi 5584.
    MGIi MGI:99260. Prkci.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117322.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q62074.
    KOi K06069.
    OMAi FEPSISY.
    OrthoDBi EOG7HF1J3.
    TreeFami TF102004.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 3474.
    Reactomei REACT_214670. p75NTR recruits signalling complexes.

    Miscellaneous databases

    NextBioi 294941.
    PROi Q62074.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62074.
    Bgeei Q62074.
    CleanExi MM_PRKCI.
    Genevestigatori Q62074.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR012233. PKC_zeta.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24357:SF60. PTHR24357:SF60. 1 hit.
    Pfami PF00130. C1_1. 1 hit.
    PF00564. PB1. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000554. PKC_zeta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 1 hit.
    SM00666. PB1. 1 hit.
    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.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new member of the third class in the protein kinase C family, PKC lambda, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells."
      Akimoto K., Mizuno K., Osada S., Hirai S., Tanuma S., Suzuki K., Ohno S.
      J. Biol. Chem. 269:12677-12683(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    3. "Evidence that atypical protein kinase C-lambda and atypical protein kinase C-zeta participate in Ras-mediated reorganization of the F-actin cytoskeleton."
      Uberall F., Hellbert K., Kampfer S., Maly K., Villunger A., Spitaler M., Mwanjewe J., Baier-Bitterlich G., Baier G., Grunicke H.H.
      J. Cell Biol. 144:413-425(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
      Joberty G., Petersen C., Gao L., Macara I.G.
      Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND CDC42.
    5. "Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins."
      Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., Michaelsen E., Bjoerkoey G., Johansen T.
      J. Biol. Chem. 278:34568-34581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1 AND MAP2K5, MUTAGENESIS OF ARG-27; VAL-28; LYS-29; TRP-70; ASP-72; GLU-74; ASP-76; GLN-83 AND GLU-85.
    6. "Insulin-induced GLUT4 translocation involves protein kinase C-lambda-mediated functional coupling between Rab4 and the motor protein kinesin."
      Imamura T., Huang J., Usui I., Satoh H., Bever J., Olefsky J.M.
      Mol. Cell. Biol. 23:4892-4900(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Targeted deletion of protein kinase C lambda reveals a distribution of functions between the two atypical protein kinase C isoforms."
      Soloff R.S., Katayama C., Lin M.Y., Feramisco J.R., Hedrick S.M.
      J. Immunol. 173:3250-3260(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Protein kinase C-lambda knockout in embryonic stem cells and adipocytes impairs insulin-stimulated glucose transport."
      Bandyopadhyay G., Standaert M.L., Sajan M.P., Kanoh Y., Miura A., Braun U., Kruse F., Leitges M., Farese R.V.
      Mol. Endocrinol. 18:373-383(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Function of atypical protein kinase C lambda in differentiating photoreceptors is required for proper lamination of mouse retina."
      Koike C., Nishida A., Akimoto K., Nakaya M.A., Noda T., Ohno S., Furukawa T.
      J. Neurosci. 25:10290-10298(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Substrate recognition mechanism of atypical protein kinase Cs revealed by the structure of PKCiota in complex with a substrate peptide from Par-3."
      Wang C., Shang Y., Yu J., Zhang M.
      Structure 20:791-801(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 231-595 IN COMPLEX WITH RAT PARD3 PEPTIDE, PHOSPHORYLATION AT THR-563, PSEUDOSUBSTRATE MOTIF.

    Entry informationi

    Entry nameiKPCI_MOUSE
    AccessioniPrimary (citable) accession number: Q62074
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3