A8KBH6

SS
Gene name
prkcb (prkcb1)
Protein name
Protein kinase C beta type
Names
PKC-B , PKC-beta , EC 2.7.11.13
Species
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
KEGG Pathway
xtr:100038043
EC number
2.7.11.-: Protein-serine/threonine kinases
Protein Class

Descriptions

Protein kinase C is a multi-module Ser/Thr protein kinase that transduces the abundance of signals resulting in phospholipid hydrolysis. Binding of diacylglycerol allosterically and reversibly activates these enzymes to affect their major role in maintaining cellular homeostasis. This allosteric regulation is precisely controlled by multiple mechanisms that ensure that the enzyme is only active for specific times at specific locations in response to specific signals. <br> PKC consists of a regulatory moiety (pseudosubstrate site, C1A and C1B able to bind phorbol esters and diacylglycerol, and calcium-binding C2 domain) and protein kinase domain. The kinase domain is followed by a C-Tail that is a hallmark regulatory region of AGC kinases and serves as a docking site for regulatory proteins. <br>The pseudosubstrate binds the substrate-binding cavity of the kinase domain and operates as an autoinhibitory segment. While the pseudosubstrate-C1A is the dominant autoinhibitory module and is necessary for the autoinhibition of all PKC family members, all domains in the regulatory module participate in a network of interactions to maintain autoinhibition. <br>

Autoinhibitory domains (AIDs)

33-83 (C1A domain) SS

Target domain

341-583 (Protein kinase domain)

Relief mechanism

Ligand binding

Assay

98-148 (C1B domain) SS

Target domain

341-583 (Protein kinase domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

480-503 (Activation loop from InterPro)

Target domain

338-660 (Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta)

Relief mechanism

Assay

480-503 (Activation loop from InterPro)

Target domain

338-660 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for A8KBH6

Entry ID Method Resolution Chain Position Source
AF-A8KBH6-F1 Predicted AlphaFoldDB

No variants for A8KBH6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8KBH6

No associated diseases with A8KBH6

13 regional properties for A8KBH6

Type Name Position InterPro Accession
domain C2 domain 155 - 274 IPR000008
domain Protein kinase domain 339 - 597 IPR000719
domain AGC-kinase, C-terminal 598 - 668 IPR000961
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 33 - 84 IPR002219-1
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 98 - 150 IPR002219-2
active_site Serine/threonine-protein kinase, active site 459 - 471 IPR008271
binding_site Protein kinase, ATP binding site 345 - 368 IPR017441
domain Protein kinase, C-terminal 624 - 658 IPR017892
domain Diacylglycerol/phorbol-ester binding 31 - 45 IPR020454-1
domain Diacylglycerol/phorbol-ester binding 47 - 56 IPR020454-2
domain Diacylglycerol/phorbol-ester binding 60 - 71 IPR020454-3
domain Diacylglycerol/phorbol-ester binding 137 - 149 IPR020454-4
domain Classical protein kinase C beta, catalytic domain 338 - 660 IPR034664

Functions

Description
EC Number 2.7.11.- Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

9 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
diacylglycerol-dependent serine/threonine kinase activity Catalysis of the reaction
histone binding Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription.
histone H3T6 kinase activity Catalysis of the reaction
nuclear androgen receptor binding Binding to a nuclear androgen receptor.
nuclear receptor coactivator activity A transcription coactivator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound nuclear receptor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.
protein serine kinase activity Catalysis of the reactions
zinc ion binding Binding to a zinc ion (Zn).

9 GO annotations of biological process

Name Definition
adaptive immune response An immune response mediated by cells expressing specific receptors for antigens produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory).
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
B cell activation The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
B cell receptor signaling pathway The series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
positive regulation of canonical NF-kappaB signal transduction Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
post-translational protein modification The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
regulation of transcription by RNA polymerase II Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.

18 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P24583 PKC1 Protein kinase C-like 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P04409 PRKCA Protein kinase C alpha type Bos taurus (Bovine) EV SS
P05128 PRKCG Protein kinase C gamma type Bos taurus (Bovine) SS
P05126 PRKCB Protein kinase C beta type Bos taurus (Bovine) SS
P13677 inaC Protein kinase C, eye isozyme Drosophila melanogaster (Fruit fly) SS
P05130 Pkc53E Protein kinase C, brain isozyme Drosophila melanogaster (Fruit fly) SS
P17252 PRKCA Protein kinase C alpha type Homo sapiens (Human) EV
P05129 PRKCG Protein kinase C gamma type Homo sapiens (Human) SS
P05771 PRKCB Protein kinase C beta type Homo sapiens (Human) SS
P20444 Prkca Protein kinase C alpha type Mus musculus (Mouse) SS
P63318 Prkcg Protein kinase C gamma type Mus musculus (Mouse) SS
P68404 Prkcb Protein kinase C beta type Mus musculus (Mouse) SS
P05696 Prkca Protein kinase C alpha type Rattus norvegicus (Rat) SS
P63319 Prkcg Protein kinase C gamma type Rattus norvegicus (Rat) SS
P68403 Prkcb Protein kinase C beta type Rattus norvegicus (Rat) SS
P90980 pkc-2 Protein kinase C-like 2 Caenorhabditis elegans SS
Q5BKK4 sgk1 Serine/threonine-protein kinase Sgk1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q7SY24 prkcbb Protein kinase C beta type Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MADPAACEPG EDTTTRFARK GALRQKNVHE VKEHKFTARF FKQPTFCSHC TDFIWGFGKQ
70 80 90 100 110 120
GFQCQVCCFV VHKRCHEFVT FSCPGADKGP ASDDPRSKHK FKIHTYSSPT FCDHCGSLLY
130 140 150 160 170 180
GLIHQGMKCE TCMMNVHKRC VMNVPSLCGT DHTERRGRIH IKAEIREEVL TVTVGDARNL
190 200 210 220 230 240
VPMDPNGLSD PYVKLKLIPD PKSESKQKTK TIKCSLNPTW NESFKFQLKE SDKDRRLSVE
250 260 270 280 290 300
IWDWDLTSRN DFMGSLSFGI SELLKAGVDG WFKLLSQEEG EYFNVPVPPE GEEGNEELRQ
310 320 330 340 350 360
KFERAKIGPG TKAVEEKVVN PMPKVDNNET RDRMKVSDFN FLKVLGKGSF GKVILAERKG
370 380 390 400 410 420
TDELYAIKIL KKDVVIQDDD VECTMVEKRV LALSGKPPFL TQLHSCFQTM DRLYFVMEYV
430 440 450 460 470 480
NGGDLMYQIQ QVGRFKEPHA VFYAAEIAIG LLFLHSKGIV YRDLKLDNVM LDSEGHIKIA
490 500 510 520 530 540
DFGMCKENMW DGVTTKTFCG TPDYIAPEII AYQPYAKSVD WWAFGILLYE MLAGQAPFEG
550 560 570 580 590 600
EDEDELFQSI MEHNVAYPKS MSKEAVAICK GLMTKHPGKR LGCGPEGERD IKDHAFFRYI
610 620 630 640 650 660
DWEKLERNEI QPPYKPKACG RNAENFDKFF TRHPPVLTPP DHEVIRNIDQ SEFEGFSYVN
SDFAKEEEKD