dbPTM

ARRB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARRB1_HUMAN
UniProt AC	P49407
Protein Name	Beta-arrestin-1
Gene Name	ARRB1
Organism	Homo sapiens (Human).
Sequence Length	418
Subcellular Localization	Cytoplasm. Nucleus. Cell membrane. Membrane, clathrin-coated pit . Cell projection, pseudopodium. Cytoplasmic vesicle. Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located i
Protein Description	Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates to the recruitment of the ubiquitin-protein ligase to the receptor. [PubMed: 23886940]
Protein Sequence	MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPENETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPQLNNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	Phosphorylation	VVLVDPEYLKERRVY EEEECHHHHHHCCEE	28.58	27259358
49 (in isoform 2)	Ubiquitination	-	48.55	-
54	Phosphorylation	YLKERRVYVTLTCAF HHHHCCEEEEEEEEH	5.96	17456469
63	Phosphorylation	TLTCAFRYGREDLDV EEEEEHHHCCCCCEE	17.68	28152594
86	Phosphorylation	LFVANVQSFPPAPED EEEEECCCCCCCCCC	35.12	20044836
144	Phosphorylation	GKACGVDYEVKAFCA CCCCCCCHHHHHHHH	21.88	-
157	Acetylation	CAENLEEKIHKRNSV HHHCHHHHHHHCCCE	40.51	25953088
157	Ubiquitination	CAENLEEKIHKRNSV HHHCHHHHHHHCCCE	40.51	-
163	Phosphorylation	EKIHKRNSVRLVIRK HHHHHCCCEEEEEEE	16.79	27282143
173	Phosphorylation	LVIRKVQYAPERPGP EEEEEEECCCCCCCC	27.41	-
186	Phosphorylation	GPQPTAETTRQFLMS CCCCCHHHHHHHHHC	25.47	22210691
187	Phosphorylation	PQPTAETTRQFLMSD CCCCHHHHHHHHHCC	17.61	22210691
193	Phosphorylation	TTRQFLMSDKPLHLE HHHHHHHCCCCEEEE	44.63	27470641
195	Ubiquitination	RQFLMSDKPLHLEAS HHHHHCCCCEEEEEE	42.02	-
275	Phosphorylation	FCKVYTLTPFLANNR EEEEEECCHHHCCCH	12.28	27251275
330	Phosphorylation	VKVKLVVSRGGLLGD EEEEEEEECCCCHHH	20.09	24719451
350	Phosphorylation	VAVELPFTLMHPKPK EEEECCCEECCCCCC	22.64	-
374	Phosphorylation	ENETPVDTNLIELDT CCCCCCCCCCEECCC	31.96	28102081
381	Phosphorylation	TNLIELDTNDDDIVF CCCEECCCCCCCCHH	53.85	25338102
410	Phosphorylation	KEEEEDGTGSPQLNN CCCCCCCCCCCCCCC	46.97	29255136
412	Phosphorylation	EEEDGTGSPQLNNR- CCCCCCCCCCCCCC-	14.87	29255136

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
54	Y	Phosphorylation	Kinase	SRC	P12931	GPS
54	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
163	S	Phosphorylation	Kinase	PKCA	P17252	PSP
412	S	Phosphorylation	Kinase	GRK5	P34947	Uniprot
412	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
412	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:15456867

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
412	S	Phosphorylation		19661922
Constitutively phosphorylated at Ser-412 in the cytoplasm.

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 ARRB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT43_HUMAN	ZBTB43	physical	16189514
GNMT_HUMAN	GNMT	physical	16189514
KHK_HUMAN	KHK	physical	17353931
NOLC1_HUMAN	NOLC1	physical	17353931
AP3B1_HUMAN	AP3B1	physical	17353931
TCOF_HUMAN	TCOF1	physical	17353931
CHD1_HUMAN	CHD1	physical	17353931
BOP1_HUMAN	BOP1	physical	17353931
ARRC_HUMAN	ARR3	physical	17353931
PESC_HUMAN	PES1	physical	17353931
DDX27_HUMAN	DDX27	physical	17353931
IMA4_HUMAN	KPNA3	physical	17353931
ZRAB2_HUMAN	ZRANB2	physical	17353931
RL7L_HUMAN	RPL7L1	physical	17353931
CCL14_HUMAN	CCL14	physical	17353931
JAK1_HUMAN	JAK1	physical	17353931
RTF1_HUMAN	RTF1	physical	17353931
HDGR2_HUMAN	HDGFRP2	physical	17353931
CSK21_HUMAN	CSNK2A1	physical	17353931
CMBL_HUMAN	CMBL	physical	17353931
DVL2_HUMAN	DVL2	physical	11742073
DVL1_HUMAN	DVL1	physical	11742073
GNDS_HUMAN	RALGDS	physical	12105416
ARF6_HUMAN	ARF6	physical	11533043
CSK_HUMAN	CSK	physical	10753943
NSF_HUMAN	NSF	physical	10196135
NEDD4_HUMAN	NEDD4	physical	18544533
MDM2_HUMAN	MDM2	physical	18544533
ITCH_HUMAN	ITCH	physical	18544533
PRKN_HUMAN	PARK2	physical	21466165
HGS_HUMAN	HGS	physical	20505072
STAM1_HUMAN	STAM	physical	20505072
SL9A1_HUMAN	SLC9A1	physical	20855896
M3K5_HUMAN	MAP3K5	physical	19306926
CHIP_HUMAN	STUB1	physical	19306926
PDE4D_HUMAN	PDE4D	physical	19372219
IGF1R_HUMAN	IGF1R	physical	15878855
MDM2_HUMAN	MDM2	physical	15878855
ARRB2_HUMAN	ARRB2	physical	17620599
ARRS_HUMAN	SAG	physical	17620599
ARRC_HUMAN	ARR3	physical	17620599
1433B_HUMAN	YWHAB	physical	17620599
1433G_HUMAN	YWHAG	physical	17620599
1433T_HUMAN	YWHAQ	physical	17620599
1433F_HUMAN	YWHAH	physical	17620599
1433E_HUMAN	YWHAE	physical	17620599
1433Z_HUMAN	YWHAZ	physical	17620599
RANB9_HUMAN	RANBP9	physical	17620599
STK38_HUMAN	STK38	physical	17620599
SCYL2_HUMAN	SCYL2	physical	17620599
DGKZ_HUMAN	DGKZ	physical	17620599
DGKE_HUMAN	DGKE	physical	17620599
DGKG_HUMAN	DGKG	physical	17620599
ROCK1_HUMAN	ROCK1	physical	17620599
YES_HUMAN	YES1	physical	17620599
ATR_HUMAN	ATR	physical	17620599
PPM1A_HUMAN	PPM1A	physical	17620599
PPM1B_HUMAN	PPM1B	physical	17620599
CLCA_HUMAN	CLTA	physical	17620599
CLH1_HUMAN	CLTC	physical	17620599
AP3D1_HUMAN	AP3D1	physical	17620599
RFIP5_HUMAN	RAB11FIP5	physical	17620599
LRP4_HUMAN	LRP4	physical	17620599
LRP1B_HUMAN	LRP1B	physical	17620599
DYN1_HUMAN	DNM1	physical	17620599
RGS3_HUMAN	RGS3	physical	17620599
RAB1A_HUMAN	RAB1A	physical	17620599
ANXA2_HUMAN	ANXA2	physical	17620599
PTC2_HUMAN	PTCH2	physical	17620599
SDC3_HUMAN	SDC3	physical	17620599
H12_HUMAN	HIST1H1C	physical	17620599
H2B1O_HUMAN	HIST1H2BO	physical	17620599
H2A2B_HUMAN	HIST2H2AB	physical	17620599
NOLC1_HUMAN	NOLC1	physical	17620599
TCOF_HUMAN	TCOF1	physical	17620599
ANM5_HUMAN	PRMT5	physical	17620599
NPM_HUMAN	NPM1	physical	17620599
RPA1_HUMAN	POLR1A	physical	17620599
RPAC1_HUMAN	POLR1C	physical	17620599
RPA49_HUMAN	POLR1E	physical	17620599
RPA34_HUMAN	CD3EAP	physical	17620599
ZRAB2_HUMAN	ZRANB2	physical	17620599
TR150_HUMAN	THRAP3	physical	17620599
LAP2A_HUMAN	TMPO	physical	17620599
LAP2B_HUMAN	TMPO	physical	17620599
YBOX1_HUMAN	YBX1	physical	17620599
THOC4_HUMAN	ALYREF	physical	17620599
NOP10_HUMAN	NOP10	physical	17620599
RBM10_HUMAN	RBM10	physical	17620599
SF3B2_HUMAN	SF3B2	physical	17620599
NUCL_HUMAN	NCL	physical	17620599
SMD1_HUMAN	SNRPD1	physical	17620599
SRRM2_HUMAN	SRRM2	physical	17620599
HNRPM_HUMAN	HNRNPM	physical	17620599
HNRPK_HUMAN	HNRNPK	physical	17620599
DKC1_HUMAN	DKC1	physical	17620599
ROA3_HUMAN	HNRNPA3	physical	17620599
IF4B_HUMAN	EIF4B	physical	17620599
EF1A2_HUMAN	EEF1A2	physical	17620599
RL22_HUMAN	RPL22	physical	17620599
RS3A_HUMAN	RPS3A	physical	17620599
RS17_HUMAN	RPS17	physical	17620599
IF2B2_HUMAN	IGF2BP2	physical	17620599
ACTS_HUMAN	ACTA1	physical	17620599
TBA4A_HUMAN	TUBA4A	physical	17620599
TBA3C_HUMAN	TUBA3C	physical	17620599
TBA1C_HUMAN	TUBA1C	physical	17620599
TBB5_HUMAN	TUBB	physical	17620599
VIME_HUMAN	VIM	physical	17620599
TBB2A_HUMAN	TUBB2A	physical	17620599
FLNA_HUMAN	FLNA	physical	17620599
GELS_HUMAN	GSN	physical	17620599
LIMA1_HUMAN	LIMA1	physical	17620599
MPRIP_HUMAN	MPRIP	physical	17620599
CALD1_HUMAN	CALD1	physical	17620599
MAP1B_HUMAN	MAP1B	physical	17620599
SPTN1_HUMAN	SPTAN1	physical	17620599
TPM4_HUMAN	TPM4	physical	17620599
CKAP4_HUMAN	CKAP4	physical	17620599
MYH9_HUMAN	MYH9	physical	17620599
ML12B_HUMAN	MYL12B	physical	17620599
KI26A_HUMAN	KIF26A	physical	17620599
MYH1_HUMAN	MYH1	physical	17620599
FAS_HUMAN	FASN	physical	17620599
KPYM_HUMAN	PKM	physical	17620599
DHRS2_HUMAN	DHRS2	physical	17620599
ATPA_HUMAN	ATP5A1	physical	17620599
ATPB_HUMAN	ATP5B	physical	17620599
F263_HUMAN	PFKFB3	physical	17620599
PDIA1_HUMAN	P4HB	physical	17620599
HSP7C_HUMAN	HSPA8	physical	17620599
HS90A_HUMAN	HSP90AA1	physical	17620599
CNGA3_HUMAN	CNGA3	physical	17620599
GRP78_HUMAN	HSPA5	physical	17620599
APLP1_HUMAN	APLP1	physical	17620599
GRP75_HUMAN	HSPA9	physical	17620599
BCLF1_HUMAN	BCLAF1	physical	17620599
RS27A_HUMAN	RPS27A	physical	17620599
UBB_HUMAN	UBB	physical	17620599
UBC_HUMAN	UBC	physical	17620599
RL40_HUMAN	UBA52	physical	17620599
CBPA1_HUMAN	CPA1	physical	17620599
CASB_HUMAN	CSN2	physical	17620599
MEP50_HUMAN	WDR77	physical	17620599
HDGR2_HUMAN	HDGFRP2	physical	17620599
DGKH_HUMAN	DGKH	physical	17620599
ST38L_HUMAN	STK38L	physical	17620599
M3K1_HUMAN	MAP3K1	physical	17620599
P85B_HUMAN	PIK3R2	physical	17620599
P3C2A_HUMAN	PIK3C2A	physical	17620599
STXB5_HUMAN	STXBP5	physical	17620599
CPNE8_HUMAN	CPNE8	physical	17620599
RHG32_HUMAN	ARHGAP32	physical	17620599
G3BP1_HUMAN	G3BP1	physical	17620599
S10A9_HUMAN	S100A9	physical	17620599
ZYX_HUMAN	ZYX	physical	17620599
H2AX_HUMAN	H2AFX	physical	17620599
H1X_HUMAN	H1FX	physical	17620599
XRCC5_HUMAN	XRCC5	physical	17620599
RPAB1_HUMAN	POLR2E	physical	17620599
BACH2_HUMAN	BACH2	physical	17620599
HNRPU_HUMAN	HNRNPU	physical	17620599
HNRH1_HUMAN	HNRNPH1	physical	17620599
ROA1_HUMAN	HNRNPA1	physical	17620599
RL3_HUMAN	RPL3	physical	17620599
RS2_HUMAN	RPS2	physical	17620599
RS8_HUMAN	RPS8	physical	17620599
RL6_HUMAN	RPL6	physical	17620599
RL7A_HUMAN	RPL7A	physical	17620599
EIF3I_HUMAN	EIF3I	physical	17620599
TMOD3_HUMAN	TMOD3	physical	17620599
COF1_HUMAN	CFL1	physical	17620599
SRC8_HUMAN	CTTN	physical	17620599
ARPC5_HUMAN	ARPC5	physical	17620599
KTN1_HUMAN	KTN1	physical	17620599
TITIN_HUMAN	TTN	physical	17620599
AINX_HUMAN	INA	physical	17620599
DMD_HUMAN	DMD	physical	17620599
MYO1C_HUMAN	MYO1C	physical	17620599
MYL6_HUMAN	MYL6	physical	17620599
KIF2C_HUMAN	KIF2C	physical	17620599
KIF3A_HUMAN	KIF3A	physical	17620599
DYH3_HUMAN	DNAH3	physical	17620599
ACACA_HUMAN	ACACA	physical	17620599
KCTD3_HUMAN	KCTD3	physical	17620599
UBP24_HUMAN	USP24	physical	17620599
SPIN1_HUMAN	SPIN1	physical	17620599
VIGLN_HUMAN	HDLBP	physical	17620599
DPY30_HUMAN	DPY30	physical	17620599
PRP4_HUMAN	PRPF4	physical	17620599
TRAF6_HUMAN	TRAF6	physical	16378096
GBB1_HUMAN	GNB1	physical	18729826
IKBA_HUMAN	NFKBIA	physical	15173580
IKBA_HUMAN	NFKBIA	physical	15125834
EDNRA_HUMAN	EDNRA	physical	19202075
SRC_HUMAN	SRC	physical	19202075
AXIN1_HUMAN	AXIN1	physical	19202075
M3K5_HUMAN	MAP3K5	physical	19782076
MP2K4_HUMAN	MAP2K4	physical	19782076
AKT1_HUMAN	AKT1	physical	19262695
CSK_HUMAN	CSK	physical	19262695
PLPP_HUMAN	PDXP	physical	17500066
LIMK1_HUMAN	LIMK1	physical	17500066
CLH1_HUMAN	CLTC	physical	16709866
PTAFR_HUMAN	PTAFR	physical	16709866
AP2A1_HUMAN	AP2A1	physical	16709866
MP2K3_HUMAN	MAP2K3	physical	16709866
MK14_HUMAN	MAPK14	physical	16709866
ARRD1_HUMAN	ARRDC1	physical	23886940
NOTC1_HUMAN	NOTCH1	physical	23886940
GNMT_HUMAN	GNMT	physical	21988832
RL15_HUMAN	RPL15	physical	21988832
BAG1_HUMAN	BAG1	physical	21988832
NEK6_HUMAN	NEK6	physical	21988832
BTK_HUMAN	BTK	physical	21988832
P85B_HUMAN	PIK3R2	physical	21988832
MK09_HUMAN	MAPK9	physical	21988832
PE2R4_HUMAN	PTGER4	physical	16432186
SRC_HUMAN	SRC	physical	16432186
UBP33_HUMAN	USP33	physical	19363159
MK09_HUMAN	MAPK9	physical	25416956
HGS_HUMAN	HGS	physical	23208550
MDM2_HUMAN	MDM2	physical	21466165
DRD4_HUMAN	DRD4	physical	27155323
KLH12_HUMAN	KLHL12	physical	27155323
CUL3_HUMAN	CUL3	physical	27155323
ARRS_HUMAN	SAG	physical	28514442
BRPF1_HUMAN	BRPF1	physical	28514442
RTF1_HUMAN	RTF1	physical	28514442
NOLC1_HUMAN	NOLC1	physical	28514442
DOCK4_HUMAN	DOCK4	physical	28514442
AL4A1_HUMAN	ALDH4A1	physical	28514442
LYRM7_HUMAN	LYRM7	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
HDGR2_HUMAN	HDGFRP2	physical	28514442
DCAF5_HUMAN	DCAF5	physical	28514442
ELMO2_HUMAN	ELMO2	physical	28514442
TCOF_HUMAN	TCOF1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of ARRB1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Beta-arrestin1 phosphorylation by GRK5 regulates G protein-independent 5-HT4 receptor signalling."; Barthet G., Carrat G., Cassier E., Barker B., Gaven F., Pillot M.,Framery B., Pellissier L.P., Augier J., Kang D.S., Claeysen S.,Reiter E., Baneres J.L., Benovic J.L., Marin P., Bockaert J.,Dumuis A.; EMBO J. 28:2706-2718(2009). Cited for: PHOSPHORYLATION AT SER-412.	19661922 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASSSPECTROMETRY.	19413330 [Abstract]

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