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Protein Page:
RACK1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RACK1 a G-beta like protein containing 7 WD domains. A presumptive scaffold protein, linking protein kinase C to its substrates. Binds inositol 1,4,5-trisphosphate receptors and regulates Ca2+ release by enhancing inositol 1,4,5-trisphosphate receptor binding affinity for inositol 1,4,5-trisphosphate. An insulin-like growth factor 1 receptor-interacting protein that can regulate IGF-1-mediated Akt activation and protection from cell death. Note: This description may include information from UniProtKB.
Protein type: G protein; G protein, heterotrimeric beta; G protein, heterotrimeric; Motility/polarity/chemotaxis; Nuclear receptor co-regulator; Adaptor/scaffold
Cellular Component: small ribosomal subunit; cytoskeleton; mitochondrion; cell soma; perinuclear region of cytoplasm; cytoplasm; dendrite; perikaryon; midbody; nucleus; cytosol; phagocytic cup
Molecular Function: protein tyrosine kinase inhibitor activity; protein binding; enzyme binding; protein homodimerization activity; protein kinase C binding; protein complex scaffold; SH2 domain binding; caspase activator activity; receptor tyrosine kinase binding; protein phosphatase binding; ion channel inhibitor activity; receptor binding
Biological Process: caspase activation; negative regulation of phagocytosis; negative regulation of protein kinase B signaling cascade; negative regulation of Wnt receptor signaling pathway; viral reproduction; positive regulation of apoptosis; regulation of cell cycle; positive regulation of protein homooligomerization; rhythmic process; gastrulation; cell cycle; regulation of protein localization; positive regulation of mitochondrial depolarization; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of translation; positive regulation of cAMP catabolic process; positive regulation of cyclic-nucleotide phosphodiesterase activity; negative regulation of neuron apoptosis; positive regulation of protein amino acid phosphorylation; negative regulation of cell growth; regulation of cell division; positive regulation of cell migration; positive regulation of GTPase activity
Reference #:  P63244 (UniProtKB)
Alt. Names/Synonyms: Cell proliferation-inducing gene 21 protein; GBLP; Gnb2-rs1; GNB2L1; guanine nucleotide binding protein (G protein), beta polypeptide 2-like 1; Guanine nucleotide-binding protein subunit beta-2-like 1; Guanine nucleotide-binding protein subunit beta-like protein 12.3; H12.3; HLC-7; Human lung cancer oncogene 7 protein; lung cancer oncogene 7; PIG21; proliferation-inducing gene 21; protein homologous to chicken B complex protein, guanine nucleotide binding; RACK1; Receptor for activated C kinase; Receptor for Activated C Kinase 1; Receptor of activated protein kinase C 1
Gene Symbols: GNB2L1
Molecular weight: 35,077 Da
Basal Isoelectric point: 7.6  Predict pI for various phosphorylation states
CST Pathways:  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RACK1

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: Y52‑p
cell growth, altered: Y52‑p, Y302‑p
cell motility, altered: Y52‑p, Y246‑p, Y302‑p
transcription, inhibited: Y246‑p
activity, inhibited: Y246‑p
molecular association, regulation: Y52‑p, Y228‑p, Y246‑p, Y302‑p
phosphorylation: Y246‑p
protein conformation: Y52‑p, S146‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 T2-p ______MtEQMtLRG
0 2 T6-p __MtEQMtLRGtLkG
0 1 T10-p EQMtLRGtLkGHNGW
0 18 K12-ub MtLRGtLkGHNGWVT
0 7 T24-p WVTQIATtPQFPDMI
0 4 K38-ub ILSASRDkTIIMWkL
0 17 K44-ub DkTIIMWkLtRDEtN
0 7 T46-p TIIMWkLtRDEtNyG
0 1 T50-p WkLtRDEtNyGIPQR
2 223 Y52-p LtRDEtNyGIPQRAL
0 1 T93-p TLRLWDLttGtTTRR
0 1 T94-p LRLWDLttGtTTRRF
0 1 T96-p LWDLttGtTTRRFVG
0 91 K106-ub RRFVGHTkDVLsVAF
0 1 S110-p GHTkDVLsVAFSSDN
0 1 T128-p VSGSRDKtIkLWNtL
0 3 K130-ac GSRDKtIkLWNtLGV
0 19 K130-ub GSRDKtIkLWNtLGV
0 1 T134-p KtIkLWNtLGVCkYT
0 52 K139-ub WNtLGVCkYTVQDEs
1 0 S146-p kYTVQDEsHSEWVSC
0 1 S157-p WVSCVRFsPNSsNPI
0 2 S161-p VRFsPNSsNPIIVsC
0 1 S167-p SsNPIIVsCGWDkLV
0 7 K172-ac IVsCGWDkLVkVWNL
0 20 K172-ub IVsCGWDkLVkVWNL
0 39 K175-ub CGWDkLVkVWNLANC
0 1 K183-ac VWNLANCkLkTNHIG
0 36 K183-ub VWNLANCkLkTNHIG
0 1 K183-sc VWNLANCkLkTNHIG
0 12 K185-ub NLANCkLkTNHIGHT
1 0 Y194-p NHIGHTGyLNTVTVS
0 5 K212-ub SLCASGGkDGQAMLW
0 3 K225-ub LWDLNEGkHLyTLDG
3 5 Y228-p LNEGkHLyTLDGGDI
6 2 Y246-p LCFSPNRyWLCAATG
0 1 S255-p LCAATGPsIkIWDLE
0 58 K257-ub AATGPsIkIWDLEGk
0 35 K264-ub kIWDLEGkIIVDELk
0 1 K271 kIIVDELKQEVIsTS
0 79 K271-ub kIIVDELkQEVIsTS
0 1 K271-sc kIIVDELkQEVIsTS
0 1 S276-p ELkQEVIsTSSkAEP
0 5 K280-m1 EVIsTSSkAEPPQCT
0 15 K280-ub EVIsTSSkAEPPQCT
1 0 Y302-p GQTLFAGyTDNLVRV
0 1 T313-p LVRVWQVtIGtR___
0 4 T316-p VWQVtIGtR______
  mouse

 
T2 ______MTEQMTLRG
T6 __MTEQMTLRGTLkG
T10 EQMTLRGTLkGHNGW
K12-ub MTLRGTLkGHNGWVT
T24 WVTQIATTPQFPDMI
K38 ILSASRDKTIIMWKL
K44 DKTIIMWKLTRDETN
T46 TIIMWKLTRDETNyG
T50 WKLTRDETNyGIPQR
Y52-p LTRDETNyGIPQRAL
T93 TLRLWDLTTGTTTRR
T94 LRLWDLTTGTTTRRF
T96 LWDLTTGTTTRRFVG
K106-ub RRFVGHTkDVLSVAF
S110 GHTkDVLSVAFSSDN
T128 VSGSRDKTIkLWNTL
K130-ac GSRDKTIkLWNTLGV
K130-ub GSRDKTIkLWNTLGV
T134 KTIkLWNTLGVCkYT
K139-ub WNTLGVCkYTVQDES
S146 kYTVQDESHSEWVSC
S157 WVSCVRFSPNSsNPI
S161-p VRFSPNSsNPIIVSC
S167 SsNPIIVSCGWDkLV
K172 IVSCGWDKLVkVWNL
K172-ub IVSCGWDkLVkVWNL
K175-ub CGWDkLVkVWNLANC
K183 VWNLANCKLKTNHIG
K183-ub VWNLANCkLKTNHIG
K183 VWNLANCKLKTNHIG
K185 NLANCkLKTNHIGHT
Y194 NHIGHTGYLNTVTVS
K212 SLCASGGKDGQAMLW
K225 LWDLNEGKHLyTLDG
Y228-p LNEGKHLyTLDGGDI
Y246 LCFSPNRYWLCAATG
S255 LCAATGPSIkIWDLE
K257-ub AATGPSIkIWDLEGk
K264-ub kIWDLEGkIIVDELk
K271-ac kIIVDELkQEVISTS
K271-ub kIIVDELkQEVISTS
K271 kIIVDELKQEVISTS
S276 ELkQEVISTSSkAEP
K280 EVISTSSKAEPPQCT
K280-ub EVISTSSkAEPPQCT
Y302 GQTLFAGYTDNLVRV
T313 LVRVWQVTIGtR___
T316-p VWQVTIGtR______
  rat

 
T2 ______MTEQMTLRG
T6 __MTEQMTLRGTLKG
T10 EQMTLRGTLKGHNGW
K12 MTLRGTLKGHNGWVT
T24 WVTQIATTPQFPDMI
K38 ILSASRDKTIIMWKL
K44 DKTIIMWKLTRDETN
T46 TIIMWKLTRDETNyG
T50 WKLTRDETNyGIPQR
Y52-p LTRDETNyGIPQRAL
T93 TLRLWDLTTGTTTRR
T94 LRLWDLTTGTTTRRF
T96 LWDLTTGTTTRRFVG
K106 RRFVGHTKDVLSVAF
S110 GHTKDVLSVAFSSDN
T128 VSGSRDKTIKLWNTL
K130 GSRDKTIKLWNTLGV
K130 GSRDKTIKLWNTLGV
T134 KTIKLWNTLGVCKYT
K139 WNTLGVCKYTVQDES
S146 KYTVQDESHSEWVSC
S157 WVSCVRFSPNSSNPI
S161 VRFSPNSSNPIIVSC
S167 SSNPIIVSCGWDKLV
K172 IVSCGWDKLVKVWNL
K172 IVSCGWDKLVKVWNL
K175 CGWDKLVKVWNLANC
K183 VWNLANCKLKTNHIG
K183 VWNLANCKLKTNHIG
K183 VWNLANCKLKTNHIG
K185 NLANCKLKTNHIGHT
Y194 NHIGHTGYLNTVTVS
K212 SLCASGGKDGQAMLW
K225 LWDLNEGKHLYTLDG
Y228 LNEGKHLYTLDGGDI
Y246 LCFSPNRYWLCAATG
S255 LCAATGPSIKIWDLE
K257 AATGPSIKIWDLEGK
K264 KIWDLEGKIIVDELK
K271 KIIVDELKQEVISTS
K271 KIIVDELKQEVISTS
K271 KIIVDELKQEVISTS
S276 ELKQEVISTSSKAEP
K280 EVISTSSKAEPPQCT
K280 EVISTSSKAEPPQCT
Y302 GQTLFAGYTDNLVRV
T313 LVRVWQVTIGTR___
T316 VWQVTIGTR______
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