KPCZ_MOUSE - dbPTM
KPCZ_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPCZ_MOUSE
UniProt AC Q02956
Protein Name Protein kinase C zeta type
Gene Name Prkcz
Organism Mus musculus (Mouse).
Sequence Length 592
Subcellular Localization Cytoplasm . Endosome . Cell junction . In the retina, localizes in the terminals of the rod bipolar cells. Associated with endosomes. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. Colocalizes with VAMP2 and
Protein Description Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro (By similarity)..
Protein Sequence MPSRTDPKMDRSGGRVRLKAHYGGDILITSVDAMTTFKDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLVCQGRDEVLIIHVFPSIPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRGAYCGQCSERIWGLSRQGYRCINCKLLVHKRCHVLVPLTCRRHMDSVMPSQEPPVDDKNDGVDLPSEETDGIAYISSSRKHDNIKDDSEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSAEESV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MPSRTDPKMDRS
---CCCCCCCCCCCC
62.0820139300
113PhosphorylationPCPGEDKSIYRRGAR
CCCCCCCCHHHHHHH
36.8522817900
155PhosphorylationSERIWGLSRQGYRCI
HHHHHCCCCCCEEEE
20.7222006019
160MethylationGLSRQGYRCINCKLL
CCCCCCEEEECCEEE
22.9716289167
186PhosphorylationTCRRHMDSVMPSQEP
CHHHHHHHCCCCCCC
16.8522817900
217PhosphorylationDGIAYISSSRKHDNI
CCEEEEECCCCCCCC
25.3022817900
218PhosphorylationGIAYISSSRKHDNIK
CEEEEECCCCCCCCC
38.2622817900
262PhosphorylationIRVIGRGSYAKVLLV
EEEECCCCCEEEEEE
22.1325338131
263PhosphorylationRVIGRGSYAKVLLVR
EEECCCCCEEEEEEE
17.1729514104
375MethylationHERGIIYRDLKLDNV
HHCCCCCCCCCCCCE
32.1730988871
407PhosphorylationEGLGPGDTTSTFCGT
CCCCCCCCCCCCCCC
28.6720469934
408PhosphorylationGLGPGDTTSTFCGTP
CCCCCCCCCCCCCCC
30.4321183079
409PhosphorylationLGPGDTTSTFCGTPN
CCCCCCCCCCCCCCC
22.9122322096
410O-linked_GlycosylationGPGDTTSTFCGTPNY
CCCCCCCCCCCCCCE
22.3529249667
410PhosphorylationGPGDTTSTFCGTPNY
CCCCCCCCCCCCCCE
22.3525521595
414PhosphorylationTTSTFCGTPNYIAPE
CCCCCCCCCCEECHH
15.0019060867
417PhosphorylationTFCGTPNYIAPEILR
CCCCCCCEECHHHHC
10.3220469934
513AcetylationQTGFSDIKSHAFFRS
CCCCCHHHHHHHHHH
40.977617797
520PhosphorylationKSHAFFRSIDWDLLE
HHHHHHHHCCHHHHH
21.5322817900
560PhosphorylationTSEPVQLTPDDEDVI
CCCCCCCCCCCHHHH
13.9522817900
573PhosphorylationVIKRIDQSEFEGFEY
HHHHCCHHHCCCCCC
40.2721743459
580PhosphorylationSEFEGFEYINPLLLS
HHCCCCCCCCHHHHH
12.0721743459
587PhosphorylationYINPLLLSAEESV--
CCCHHHHHHHHCC--
33.3421743459
591PhosphorylationLLLSAEESV------
HHHHHHHCC------
25.3221743459

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
113SPhosphorylationKinasePRKCZQ05513
GPS
186SPhosphorylationKinasePRKCZQ05513
GPS
410TPhosphorylationKinasePDPK1Q9Z2A0
Uniprot
410TPhosphorylationKinasePI3K-Uniprot
560TPhosphorylationKinasePRKCZQ05513
GPS
560TPhosphorylationKinasePKCZQ02956
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
410TPhosphorylation

-
410TPhosphorylation

-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KPCZ_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSK3B_MOUSEGsk3bphysical
17053159
MBP_MOUSEMbpphysical
14685273
PAR6A_MOUSEPard6aphysical
14685273
KPYM_MOUSEPkmphysical
14685273
KPCZ_RATPrkczphysical
8694767
PAR6A_MOUSEPard6aphysical
16510873
PARD3_MOUSEPard3physical
16510873
GSK3B_MOUSEGsk3bphysical
16510873
DYST_HUMANDSTphysical
26496610
IFIT1_HUMANIFIT1physical
26496610
LASP1_HUMANLASP1physical
26496610
STX3_HUMANSTX3physical
26496610
SF01_HUMANSF1physical
26496610
MRCKB_HUMANCDC42BPBphysical
26496610
ACTZ_HUMANACTR1Aphysical
26496610
RBP1_HUMANRALBP1physical
26496610
RPC1_HUMANPOLR3Aphysical
26496610
PDS5B_HUMANPDS5Bphysical
26496610
GOLI4_HUMANGOLIM4physical
26496610
CTF8_HUMANCHTF8physical
26496610
ATG3_HUMANATG3physical
26496610
ASPM_HUMANASPMphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KPCZ_MOUSE

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Related Literatures of Post-Translational Modification

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