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Q62074

- KPCI_MOUSE

UniProt

Q62074 - KPCI_MOUSE

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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

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
Complete GO annotation...

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-KW
  7. extracellular vesicular exosome Source: Ensembl
  8. Golgi membrane Source: GOC
  9. intercellular bridge Source: Ensembl
  10. microtubule cytoskeleton Source: Ensembl
  11. nucleus Source: UniProtKB
  12. protein complex Source: Ensembl
  13. Schmidt-Lanterman incisure Source: BHF-UCL
Complete GO annotation...

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

BgeeiQ62074.
CleanExiMM_PRKCI.
ExpressionAtlasiQ62074. baseline and differential.
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 25-587.
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.
GeneTreeiENSGT00760000118891.
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.
IPR002219. PE/DAG-bd.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

        10         20         30         40         50
MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL
60 70 80 90 100
CSEVRDMCSF DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE
110 120 130 140 150
LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR
160 170 180 190 200
RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPPEPM
210 220 230 240 250
MPMDQTMHPD HTQTVIPYNP SSHESLDQVG EEKEAMNTRE SGKASSSLGL
260 270 280 290 300
QDFDLLRVIG RGSYAKVLLV RLKKTDRIYA MKVVKKELVN DDEDIDWVQT
310 320 330 340 350
EKHVFEQASN HPFLVGLHSC FQTESRLFFV IEYVNGGDLM FHMQRQRKLP
360 370 380 390 400
EEHARFYSAE ISLALNYLHE RGIIYRDLKL DNVLLDSEGH IKLTDYGMCK
410 420 430 440 450
EGLRPGDTTS TFCGTPNYIA PEILRGEDYG FSVDWWALGV LMFEMMAGRS
460 470 480 490 500
PFDIVGSSDN PDQNTEDYLF QVILEKQIRI PRSLSVKAAS VLKSFLNKDP
510 520 530 540 550
KERLGCHPQT GFADIQGHPF FRNVDWDMME QKQVVPPFKP NISGEFGLDN
560 570 580 590
FDSQFTNEPV QLTPDDDDIV RKIDQSEFEG FEYINPLLMS AEECV
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 25-587.
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 ENSGT00760000118891.
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

Bgeei Q62074.
CleanExi MM_PRKCI.
ExpressionAtlasi Q62074. baseline and differential.
Genevestigatori Q62074.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR002219. PE/DAG-bd.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 157 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