dbPTM

KPCG_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KPCG_RAT
UniProt AC	P63319
Protein Name	Protein kinase C gamma type
Gene Name	Prkcg
Organism	Rattus norvegicus (Rat).
Sequence Length	697
Subcellular Localization	Cytoplasm . Cytoplasm, perinuclear region. Cell membrane Peripheral membrane protein. Cell junction, synapse, synaptosome . Cell projection, dendrite . Translocates to synaptic membranes on stimulation.
Protein Description	Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity)..
Protein Sequence	MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTSDEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTKTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIAPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Ubiquitination	KFTARFFKQPTFCSH CCCHHHHCCCCCHHH	53.29	-
82	O-linked_Glycosylation	RRCHEFVTFECPGAG CCCCEEEEEECCCCC	21.02	12632777
122	Phosphorylation	DHCGSLLYGLVHQGM HHHHHHHHHHHHCCC	17.44	-
148	Phosphorylation	RCVRSVPSLCGVDHT HHHHHCHHHCCCCCC	33.85	25403869
192	Phosphorylation	PMDPNGLSDPYVKLK CCCCCCCCCCCEEEE	37.63	-
195	Phosphorylation	PNGLSDPYVKLKLIP CCCCCCCCEEEEECC	18.40	25403869
197	Ubiquitination	GLSDPYVKLKLIPDP CCCCCCEEEEECCCC	33.78	-
197	Acetylation	GLSDPYVKLKLIPDP CCCCCCEEEEECCCC	33.78	14509517
199	Acetylation	SDPYVKLKLIPDPRN CCCCEEEEECCCCCC	38.36	8264497
208	Phosphorylation	IPDPRNLTKQKTKTV CCCCCCCCCCCCCCE	34.67	18295358
212	Phosphorylation	RNLTKQKTKTVKATL CCCCCCCCCCEEEEE	29.47	18295358
216	Ubiquitination	KQKTKTVKATLNPVW CCCCCCEEEEECCCC	40.67	-
232	Ubiquitination	ETFVFNLKPGDVERR CEEEEECCCCCCEEC	48.32	-
241	Phosphorylation	GDVERRLSVEVWDWD CCCEECEEEEEECCC	17.89	-
250	Phosphorylation	EVWDWDRTSRNDFMG EEECCCCCCCCCHHH	29.57	-
275	Phosphorylation	KAPVDGWYKLLNQEE CCCCCCHHHHHCCCC	9.40	-
285	Phosphorylation	LNQEEGEYYNVPVAD HCCCCCCEECCCCCC	15.93	-
286	Phosphorylation	NQEEGEYYNVPVADA CCCCCCEECCCCCCC	12.84	-
297	Phosphorylation	VADADNCSLLQKFEA CCCCCCCCHHHHHHH	38.07	-
307	Phosphorylation	QKFEACNYPLELYER HHHHHCCCCHHHHHH	14.74	-
312	Phosphorylation	CNYPLELYERVRMGP CCCCHHHHHHHHCCC	7.72	-
320	Phosphorylation	ERVRMGPSSSPIPSP HHHHCCCCCCCCCCC	37.41	28551015
321	Phosphorylation	RVRMGPSSSPIPSPS HHHCCCCCCCCCCCC	43.18	27097102
321	O-linked_Glycosylation	RVRMGPSSSPIPSPS HHHCCCCCCCCCCCC	43.18	12632787
322	Phosphorylation	VRMGPSSSPIPSPSP HHCCCCCCCCCCCCC	31.05	27097102
326	Phosphorylation	PSSSPIPSPSPSPTD CCCCCCCCCCCCCCC	38.44	27097102
326	O-linked_Glycosylation	PSSSPIPSPSPSPTD CCCCCCCCCCCCCCC	38.44	1523493
328	Phosphorylation	SSPIPSPSPSPTDSK CCCCCCCCCCCCCCC	42.20	30411139
328	O-linked_Glycosylation	SSPIPSPSPSPTDSK CCCCCCCCCCCCCCC	42.20	4043341
330	O-linked_Glycosylation	PIPSPSPSPTDSKRC CCCCCCCCCCCCCCC	44.78	181873
330	Phosphorylation	PIPSPSPSPTDSKRC CCCCCCCCCCCCCCC	44.78	30411139
332	Phosphorylation	PSPSPSPTDSKRCFF CCCCCCCCCCCCCCC	58.19	30411139
334	Phosphorylation	PSPSPTDSKRCFFGA CCCCCCCCCCCCCCC	25.20	28551015
335	Ubiquitination	SPSPTDSKRCFFGAS CCCCCCCCCCCCCCC	56.87	-
361	Phosphorylation	LMVLGKGSFGKVMLA EEEECCCCHHHHEEE	34.02	23984901
373	Phosphorylation	MLAERRGSDELYAIK EEEECCCCCCEEEEE	26.54	18295358
377	Phosphorylation	RRGSDELYAIKILKK CCCCCCEEEEEEECC	12.30	-
396	O-linked_Glycosylation	QDDDVDCTLVEKRVL CCCCCCCEEEEEEEE	29.40	18295358
400	Ubiquitination	VDCTLVEKRVLALGG CCCEEEEEEEECCCC	40.08	-
482	Ubiquitination	GIIYRDLKLDNVMLD CEEECCCCCCCEEEC	59.07	-
503	Ubiquitination	ITDFGMCKENVFPGS ECCCCCCCCCCCCCC	43.35	-
510	Phosphorylation	KENVFPGSTTRTFCG CCCCCCCCCCEEECC	27.18	25403869
511	Phosphorylation	ENVFPGSTTRTFCGT CCCCCCCCCEEECCC	26.64	25403869
514	Phosphorylation	FPGSTTRTFCGTPDY CCCCCCEEECCCCCC	22.61	23991683
518	Phosphorylation	TTRTFCGTPDYIAPE CCEEECCCCCCCCCH	17.73	27097102
521	Phosphorylation	TFCGTPDYIAPEIIA EECCCCCCCCCHHHE	10.53	27097102
529	Phosphorylation	IAPEIIAYQPYGKSV CCCHHHEECCCCCCC	10.30	23991683
532	Phosphorylation	EIIAYQPYGKSVDWW HHHEECCCCCCCCHH	22.97	-
587	Ubiquitination	REAVAICKGFLTKHP HHHHHHHHHHHHCCC	46.73	-
587	Acetylation	REAVAICKGFLTKHP HHHHHHHHHHHHCCC	46.73	166445
591	O-linked_Glycosylation	AICKGFLTKHPGKRL HHHHHHHHCCCCCCC	25.66	18295358
592	Ubiquitination	ICKGFLTKHPGKRLG HHHHHHHCCCCCCCC	50.37	-
596	Ubiquitination	FLTKHPGKRLGSGPD HHHCCCCCCCCCCCC	49.23	-
639	O-linked_Glycosylation	RPRPCGRSGENFDKF CCCCCCCCCCCHHHH	35.42	18295358
645	Ubiquitination	RSGENFDKFFTRAAP CCCCCHHHHHHHCCC	37.94	-
648	Phosphorylation	ENFDKFFTRAAPALT CCHHHHHHHCCCCCC	23.64	-
655	Phosphorylation	TRAAPALTPPDRLVL HHCCCCCCCCCCEEE	34.58	30411139
664	Phosphorylation	PDRLVLASIDQADFQ CCCEEEEECCHHHCC	23.65	22673903
674	Phosphorylation	QADFQGFTYVNPDFV HHHCCCCEEECCCCC	33.13	25403869
675	Phosphorylation	ADFQGFTYVNPDFVH HHCCCCEEECCCCCC	8.93	22673903
687	Phosphorylation	FVHPDARSPTSPVPV CCCCCCCCCCCCCCC	33.96	27097102
689	Phosphorylation	HPDARSPTSPVPVPV CCCCCCCCCCCCCCC	47.08	27097102
689	O-linked_Glycosylation	HPDARSPTSPVPVPV CCCCCCCCCCCCCCC	47.08	1523487
690	Phosphorylation	PDARSPTSPVPVPVM CCCCCCCCCCCCCCC	27.55	27097102
690	O-linked_Glycosylation	PDARSPTSPVPVPVM CCCCCCCCCCCCCCC	27.55	18295358

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
514	T	Phosphorylation	Kinase	PDPK1	O55173	Uniprot
675	Y	Phosphorylation	Kinase	SYK	Q64725	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
674	T	Phosphorylation		-
Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4.

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 KPCG_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HMGB1_RAT	Hmgb1	physical	10617144
GBRR1_HUMAN	GABRR1	physical	12175859
STXB1_RAT	Stxbp1	physical	8631738
PEBP1_RAT	Pebp1	physical	12551925
CD5_HUMAN	CD5	physical	11123317
GBRB1_MOUSE	Gabrb1	physical	1321150
GBRG2_MOUSE	Gabrg2	physical	1321150
CXA1_RAT	Gja1	physical	10871288
NMDE2_MOUSE	Grin2b	physical	11306676
ANXA7_HUMAN	ANXA7	physical	11278415
TAU_BOVIN	MAPT	physical	3111527
H11_BOVIN	HIST1H1A	physical	3111527
H12_BOVIN	HIST1H1C	physical	3111527
BCL2_MOUSE	Bcl2	physical	7929424
XERO2_ARATH	LTI30	physical	21665998

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KPCG_RAT

Related Literatures of Post-Translational Modification

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