RACK1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RACK1_RAT
• UniProt AC: P63245
• Protein Name: Receptor of activated protein C kinase 1
• Gene Name: Rack1 {ECO:0000312|RGD:69229}
• Organism: Rattus norvegicus (Rat).
• 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. Also asso
• 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. [PubMed: 15340087 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.]
• 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	Acetylation	------MTEQMTLRG ------CCCEEEECE		-
2	Phosphorylation	------MTEQMTLRG ------CCCEEEECE		23984901
6	Phosphorylation	--MTEQMTLRGTLKG --CCCEEEECEEEEC		23984901
10	Phosphorylation	EQMTLRGTLKGHNGW CEEEECEEEECCCCC		25575281
52	Phosphorylation	LTRDETNYGIPQRAL ECCCCCCCCCCHHHH		-
93	Phosphorylation	TLRLWDLTTGTTTRR EEEEEECCCCCCEEE		23984901
94	Phosphorylation	LRLWDLTTGTTTRRF EEEEECCCCCCEEEE		23984901
96	Phosphorylation	LWDLTTGTTTRRFVG EEECCCCCCEEEECC		23984901
97	Phosphorylation	WDLTTGTTTRRFVGH EECCCCCCEEEECCC		23984901
98	Phosphorylation	DLTTGTTTRRFVGHT ECCCCCCEEEECCCC		23984901
130	Acetylation	GSRDKTIKLWNTLGV CCCCHHEEHHHHCCC		25786129
134	Phosphorylation	KTIKLWNTLGVCKYT HHEEHHHHCCCCEEE		23984901
157	Phosphorylation	WVSCVRFSPNSSNPI CEEEEEECCCCCCCE		23984901
160	Phosphorylation	CVRFSPNSSNPIIVS EEEECCCCCCCEEEE		23984901
161	Phosphorylation	VRFSPNSSNPIIVSC EEECCCCCCCEEEEE		23984901
183	Acetylation	VWNLANCKLKTNHIG HHHHCCCEEECCCCC		-
201	Phosphorylation	YLNTVTVSPDGSLCA EEEEEEECCCCCCCC		23984901
205	Phosphorylation	VTVSPDGSLCASGGK EEECCCCCCCCCCCC		23984901
209	Phosphorylation	PDGSLCASGGKDGQA CCCCCCCCCCCCCCE		23984901
228	Phosphorylation	LNEGKHLYTLDGGDI CCCCCEEEEECCCCC		23984901
229	Phosphorylation	NEGKHLYTLDGGDII CCCCEEEEECCCCCE		23984901
271	Acetylation	KIIVDELKQEVISTS CEEHHHHHHHHHCCC		22902405
271	Ubiquitination	KIIVDELKQEVISTS CEEHHHHHHHHHCCC		-
276	Phosphorylation	ELKQEVISTSSKAEP HHHHHHHCCCCCCCC		28432305
277	Phosphorylation	LKQEVISTSSKAEPP HHHHHHCCCCCCCCC		28432305
278	Phosphorylation	KQEVISTSSKAEPPQ HHHHHCCCCCCCCCC		28432305
279	Phosphorylation	QEVISTSSKAEPPQC HHHHCCCCCCCCCCC		28432305
313	Phosphorylation	LVRVWQVTIGTR--- EEEEEEEEECCC---		23984901
316	Phosphorylation	VWQVTIGTR------ EEEEEECCC------		23984901

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	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RACK1_RAT !!

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RACK1_RAT !!

Drug and Disease Associations

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