RACK1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RACK1_MOUSE
• UniProt AC: P68040
• Protein Name: Receptor of activated protein C kinase 1
• Gene Name: Rack1 {ECO:0000312|MGI:MGI:101849}
• Organism: Mus musculus (Mouse).
• Sequence Length: 317
• Subcellular Localization: Cell membrane ; Peripheral membrane protein . Cytoplasm . Cytoplasm, perinuclear region . Nucleus . Perikaryon . Cell projection, dendrite . Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. PKC activ
• Protein Description: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity)..
• Protein Sequence: MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR

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
1	Acetylation	-------MTEQMTLR -------CCCEEEEC		-
2	Phosphorylation	------MTEQMTLRG ------CCCEEEECE		29176673
2	Acetylation	------MTEQMTLRG ------CCCEEEECE		-
6	Phosphorylation	--MTEQMTLRGTLKG --CCCEEEECEEEEC		29176673
10	Phosphorylation	EQMTLRGTLKGHNGW CEEEECEEEECCCCC		28576409
12	Ubiquitination	MTLRGTLKGHNGWVT EEECEEEECCCCCEE		22790023
52	Phosphorylation	LTRDETNYGIPQRAL ECCCCCCCCCCHHHH		29514104
93	Phosphorylation	TLRLWDLTTGTTTRR EEEEEECCCCCCEEE		24759943
94	Phosphorylation	LRLWDLTTGTTTRRF EEEEECCCCCCEEEE		22006019
96	Phosphorylation	LWDLTTGTTTRRFVG EEECCCCCCEEEECC		29514104
106	Ubiquitination	RRFVGHTKDVLSVAF EEECCCCCCEEEEEE		22790023
115	Phosphorylation	VLSVAFSSDNRQIVS EEEEEECCCCCEEEC		24899341
130	Malonylation	GSRDKTIKLWNTLGV CCCCHHEEHHHHCCC		26320211
130	Acetylation	GSRDKTIKLWNTLGV CCCCHHEEHHHHCCC		23806337
130	Ubiquitination	GSRDKTIKLWNTLGV CCCCHHEEHHHHCCC		-
134	Phosphorylation	KTIKLWNTLGVCKYT HHEEHHHHCCCCEEE		22006019
138	S-palmitoylation	LWNTLGVCKYTVQDE HHHHCCCCEEEECCC		28526873
138	S-nitrosocysteine	LWNTLGVCKYTVQDE HHHHCCCCEEEECCC		-
139	Malonylation	WNTLGVCKYTVQDES HHHCCCCEEEECCCC		26320211
139	Ubiquitination	WNTLGVCKYTVQDES HHHCCCCEEEECCCC		-
153	S-palmitoylation	SHSEWVSCVRFSPNS CCCCCEEEEEECCCC		28526873
153	S-nitrosocysteine	SHSEWVSCVRFSPNS CCCCCEEEEEECCCC		-
157	Phosphorylation	WVSCVRFSPNSSNPI CEEEEEECCCCCCCE		26060331
160	Phosphorylation	CVRFSPNSSNPIIVS EEEECCCCCCCEEEE		26060331
161	Phosphorylation	VRFSPNSSNPIIVSC EEECCCCCCCEEEEE		26745281
168	S-nitrosocysteine	SNPIIVSCGWDKLVK CCCEEEEECHHHHHH		-
168	S-palmitoylation	SNPIIVSCGWDKLVK CCCEEEEECHHHHHH		28526873
172	Ubiquitination	IVSCGWDKLVKVWNL EEEECHHHHHHHHHH		22790023
175	Ubiquitination	CGWDKLVKVWNLANC ECHHHHHHHHHHCCC		-
175	Succinylation	CGWDKLVKVWNLANC ECHHHHHHHHHHCCC		23806337
175	Acetylation	CGWDKLVKVWNLANC ECHHHHHHHHHHCCC		23806337
182	S-nitrosocysteine	KVWNLANCKLKTNHI HHHHHCCCEEECCCC		-
182	S-palmitoylation	KVWNLANCKLKTNHI HHHHHCCCEEECCCC		28526873
183	Malonylation	VWNLANCKLKTNHIG HHHHCCCEEECCCCC		26320211
183	Succinylation	VWNLANCKLKTNHIG HHHHCCCEEECCCCC		-
183	Acetylation	VWNLANCKLKTNHIG HHHHCCCEEECCCCC		23806337
183	Ubiquitination	VWNLANCKLKTNHIG HHHHCCCEEECCCCC		-
207	S-palmitoylation	VSPDGSLCASGGKDG ECCCCCCCCCCCCCC		28526873
207	S-nitrosocysteine	VSPDGSLCASGGKDG ECCCCCCCCCCCCCC		-
228	Phosphorylation	LNEGKHLYTLDGGDI CCCCCEEEEECCCCC		18563927
240	S-palmitoylation	GDIINALCFSPNRYW CCCEEEEEECCCCEE		28526873
240	S-nitrosocysteine	GDIINALCFSPNRYW CCCEEEEEECCCCEE		-
249	S-nitrosocysteine	SPNRYWLCAATGPSI CCCCEEEEEECCCEE		-
249	S-palmitoylation	SPNRYWLCAATGPSI CCCCEEEEEECCCEE		28526873
255	Phosphorylation	LCAATGPSIKIWDLE EEEECCCEEEEEECC		22006019
257	Ubiquitination	AATGPSIKIWDLEGK EECCCEEEEEECCCC		22790023
264	Ubiquitination	KIWDLEGKIIVDELK EEEECCCCEEHHHHH		-
271	Acetylation	KIIVDELKQEVISTS CEEHHHHHHHHHCCC		22826441
271	Ubiquitination	KIIVDELKQEVISTS CEEHHHHHHHHHCCC		22790023
276	Phosphorylation	ELKQEVISTSSKAEP HHHHHHHCCCCCCCC		26824392
277	Phosphorylation	LKQEVISTSSKAEPP HHHHHHCCCCCCCCC		23984901
278	Phosphorylation	KQEVISTSSKAEPPQ HHHHHCCCCCCCCCC		23984901
279	Phosphorylation	QEVISTSSKAEPPQC HHHHCCCCCCCCCCC		23984901
280	Ubiquitination	EVISTSSKAEPPQCT HHHCCCCCCCCCCCC		-
286	S-palmitoylation	SKAEPPQCTSLAWSA CCCCCCCCCEEEEEC		28526873
313	Phosphorylation	LVRVWQVTIGTR--- EEEEEEEEECCC---		28066266
316	Phosphorylation	VWQVTIGTR------ EEEEEECCC------		21082442

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
52	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RACK1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RACK1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RACK1_MOUSE !!

Drug and Disease Associations

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