ARRB2_HUMAN - dbPTM
ARRB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARRB2_HUMAN
UniProt AC P32121
Protein Name Beta-arrestin-2
Gene Name ARRB2
Organism Homo sapiens (Human).
Sequence Length 409
Subcellular Localization Cytoplasm. Nucleus. Cell membrane. Membrane, clathrin-coated pit. Cytoplasmic vesicle. Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs.
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. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. 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) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. 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). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. 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. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. 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. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3..
Protein Sequence MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIATYQAFPPVPNPPRPPTRLQDRLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQLEQDDQVSPSSTFCKVYTITPLLSDNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIPLPRPQSAAPETDVPVDTNLIEFDTNYATDDDIVFEDFARLRLKGMKDDDYDDQLC
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 Orthologous
Protein Cluster
13PhosphorylationGTRVFKKSSPNCKLT
CCEEECCCCCCCEEE
52.17-
14PhosphorylationTRVFKKSSPNCKLTV
CEEECCCCCCCEEEE
29.07-
18AcetylationKKSSPNCKLTVYLGK
CCCCCCCEEEEEECC
54.5625953088
20PhosphorylationSSPNCKLTVYLGKRD
CCCCCEEEEEECCHH
7.81-
25AcetylationKLTVYLGKRDFVDHL
EEEEEECCHHHHHCC
46.3125953088
34UbiquitinationDFVDHLDKVDPVDGV
HHHHCCCCCCCCCCE
55.70-
48PhosphorylationVVLVDPDYLKDRKVF
EEEECHHHHCCCEEE
22.5020090780
48 (in isoform 3)Phosphorylation-22.5025147952
50UbiquitinationLVDPDYLKDRKVFVT
EECHHHHCCCEEEEE
49.62-
75PhosphorylationDLDVLGLSFRKDLFI
CCEEEEEEECCCEEE
22.6224719451
78UbiquitinationVLGLSFRKDLFIATY
EEEEEECCCEEEEEE
57.6921890473
78UbiquitinationVLGLSFRKDLFIATY
EEEEEECCCEEEEEE
57.6921890473
78UbiquitinationVLGLSFRKDLFIATY
EEEEEECCCEEEEEE
57.6921890473
108 (in isoform 3)Ubiquitination-57.87-
108UbiquitinationLQDRLLRKLGQHAHP
HHHHHHHHHHCCCCC
57.87-
153 (in isoform 3)Ubiquitination-57.67-
153UbiquitinationEIRAFCAKSLEEKSH
HHHHHHHHHHHHHCC
57.67-
153AcetylationEIRAFCAKSLEEKSH
HHHHHHHHHHHHHCC
57.6723749302
159PhosphorylationAKSLEEKSHKRNSVR
HHHHHHHCCCCCEEE
37.20-
163 (in isoform 2)Ubiquitination-50.0521890473
164PhosphorylationEKSHKRNSVRLVIRK
HHCCCCCEEEEEEEE
16.7927282143
171 (in isoform 3)Ubiquitination-29.30-
171UbiquitinationSVRLVIRKVQFAPEK
EEEEEEEEEECCCCC
29.30-
176HydroxylationIRKVQFAPEKPGPQP
EEEEECCCCCCCCCC
51.9721255264
178 (in isoform 1)Ubiquitination-54.9721890473
178 (in isoform 3)Ubiquitination-54.9721890473
178UbiquitinationKVQFAPEKPGPQPSA
EEECCCCCCCCCCCH
54.972190698
181HydroxylationFAPEKPGPQPSAETT
CCCCCCCCCCCHHHH
51.9821255264
197PhosphorylationHFLMSDRSLHLEASL
HHHHCCCCEEEEEEC
25.7328348404
230AcetylationNNSTKTVKKIKVSVR
CCCCCCEEEEEEEHH
54.7520167786
231AcetylationNSTKTVKKIKVSVRQ
CCCCCEEEEEEEHHH
43.3420167786
233AcetylationTKTVKKIKVSVRQYA
CCCEEEEEEEHHHHH
37.0220167786
266PhosphorylationQDDQVSPSSTFCKVY
CCCCCCCCCCEEEEE
34.2130576142
267PhosphorylationDDQVSPSSTFCKVYT
CCCCCCCCCEEEEEE
28.9630576142
273PhosphorylationSSTFCKVYTITPLLS
CCCEEEEEEECCCCC
4.2930576142
276PhosphorylationFCKVYTITPLLSDNR
EEEEEEECCCCCCCH
10.49-
293AcetylationRGLALDGKLKHEDTN
CCEECCCCCCCCCCC
54.7725953088
293SumoylationRGLALDGKLKHEDTN
CCEECCCCCCCCCCC
54.77-
293 (in isoform 3)Ubiquitination-54.77-
293UbiquitinationRGLALDGKLKHEDTN
CCEECCCCCCCCCCC
54.77-
295 (in isoform 3)Ubiquitination-48.73-
295SumoylationLALDGKLKHEDTNLA
EECCCCCCCCCCCCC
48.73-
295UbiquitinationLALDGKLKHEDTNLA
EECCCCCCCCCCCCC
48.73-
295SumoylationLALDGKLKHEDTNLA
EECCCCCCCCCCCCC
48.73-
308UbiquitinationLASSTIVKEGANKEV
CCCCEEEECCCCHHH
46.72-
327AcetylationVSYRVKVKLVVSRGG
EEEEEEEEEEEECCC
29.8225953088
331PhosphorylationVKVKLVVSRGGDVSV
EEEEEEEECCCCEEE
20.0924719451
360PhosphorylationIPLPRPQSAAPETDV
CCCCCCCCCCCCCCC
29.1326074081
382PhosphorylationEFDTNYATDDDIVFE
EEECCCCCCCCCEEH
29.6014702039
397UbiquitinationDFARLRLKGMKDDDY
HHHHHHHCCCCCCCC
50.99-
397SumoylationDFARLRLKGMKDDDY
HHHHHHHCCCCCCCC
50.99-
400SumoylationRLRLKGMKDDDYDDQ
HHHHCCCCCCCCCCC
67.67-
404PhosphorylationKGMKDDDYDDQLC--
CCCCCCCCCCCCC--
28.5428796482
409 (in isoform 3)Ubiquitination-4.33-
425Phosphorylation-----------------------
-----------------------
27642862

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
14SPhosphorylationKinaseMAPK1P28482
GPS
14SPhosphorylationKinaseMAPK3P27361
GPS
276TPhosphorylationKinaseMAPK1P28482
GPS
276TPhosphorylationKinaseMAPK3P27361
GPS
382TPhosphorylationKinaseCSNK2A1P68400
GPS
382TPhosphorylationKinaseCK2-FAMILY-GPS
382TPhosphorylationKinaseCK2_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:12488444

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
382TPhosphorylation

11877451

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 ARRB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNDS_HUMANRALGDSphysical
12105416
NOLC1_HUMANNOLC1physical
17353931
TCOF_HUMANTCOF1physical
17353931
DDX27_HUMANDDX27physical
17353931
AP3B1_HUMANAP3B1physical
17353931
IMA4_HUMANKPNA3physical
17353931
IMA3_HUMANKPNA4physical
17353931
BOP1_HUMANBOP1physical
17353931
ARRB1_HUMANARRB1physical
17353931
RM44_HUMANMRPL44physical
17353931
RM43_HUMANMRPL43physical
17353931
FBRL_HUMANFBLphysical
17353931
PESC_HUMANPES1physical
17353931
RL7L_HUMANRPL7L1physical
17353931
RAB5C_HUMANRAB5Cphysical
17353931
SMRC2_HUMANSMARCC2physical
16169070
MED8_HUMANMED8physical
16169070
STC2_HUMANSTC2physical
16169070
ARF6_HUMANARF6physical
11533043
MDM2_HUMANMDM2physical
12488444
MK03_HUMANMAPK3physical
12473660
AP2B1_HUMANAP2B1physical
10097102
M3K5_HUMANMAP3K5physical
11090355
MP2K4_HUMANMAP2K4physical
11090355
NEDD4_HUMANNEDD4physical
18544533
MDM2_HUMANMDM2physical
18544533
ITCH_HUMANITCHphysical
18544533
MK01_HUMANMAPK1physical
15699045
UBP33_HUMANUSP33physical
19424180
AGRG1_HUMANGPR56physical
21708946
UBP33_HUMANUSP33physical
19363159
PRKN_HUMANPARK2physical
21466165
MDM2_HUMANMDM2physical
21466165
M3K5_HUMANMAP3K5physical
19306926
CHIP_HUMANSTUB1physical
19306926
MP2K1_HUMANMAP2K1physical
11226259
MK01_HUMANMAPK1physical
11226259
AKT1_HUMANAKT1physical
18191226
MDM2_HUMANMDM2physical
21389118
PTPA_HUMANPPP2R4physical
21502318
TEBP_HUMANPTGES3physical
21502318
IGF1R_HUMANIGF1Rphysical
15878855
MDM2_HUMANMDM2physical
15878855
ARRB1_HUMANARRB1physical
17620599
ARRS_HUMANSAGphysical
17620599
ARRC_HUMANARR3physical
17620599
1433B_HUMANYWHABphysical
17620599
1433G_HUMANYWHAGphysical
17620599
1433T_HUMANYWHAQphysical
17620599
1433F_HUMANYWHAHphysical
17620599
1433E_HUMANYWHAEphysical
17620599
STK38_HUMANSTK38physical
17620599
SCYL2_HUMANSCYL2physical
17620599
DGKZ_HUMANDGKZphysical
17620599
DGKE_HUMANDGKEphysical
17620599
CSK21_HUMANCSNK2A1physical
17620599
MK01_HUMANMAPK1physical
17620599
KCC2D_HUMANCAMK2Dphysical
17620599
CDK13_HUMANCDK13physical
17620599
CDK3_HUMANCDK3physical
17620599
CDK7_HUMANCDK7physical
17620599
KC1AL_HUMANCSNK1A1Lphysical
17620599
E2AK4_HUMANEIF2AK4physical
17620599
PPM1A_HUMANPPM1Aphysical
17620599
PPM1B_HUMANPPM1Bphysical
17620599
2AAA_HUMANPPP2R1Aphysical
17620599
MYPT1_HUMANPPP1R12Aphysical
17620599
CLCA_HUMANCLTAphysical
17620599
CLCB_HUMANCLTBphysical
17620599
AP2A1_HUMANAP2A1physical
17620599
AP2B1_HUMANAP2B1physical
17620599
RFIP5_HUMANRAB11FIP5physical
17620599
VPS35_HUMANVPS35physical
17620599
CPNE1_HUMANCPNE1physical
17620599
AP3D1_HUMANAP3D1physical
17620599
ARHG6_HUMANARHGEF6physical
17620599
RAGP1_HUMANRANGAP1physical
17620599
RHG21_HUMANARHGAP21physical
17620599
G3BP2_HUMANG3BP2physical
17620599
ANXA2_HUMANANXA2physical
17620599
TAB1_HUMANTAB1physical
17620599
IKKA_HUMANCHUKphysical
17620599
CTNA1_HUMANCTNNA1physical
17620599
CTND1_HUMANCTNND1physical
17620599
SDC3_HUMANSDC3physical
17620599
ANM1_HUMANPRMT1physical
17620599
WDR26_HUMANWDR26physical
17620599
H11_HUMANHIST1H1Aphysical
17620599
H1X_HUMANH1FXphysical
17620599
H2A2B_HUMANHIST2H2ABphysical
17620599
XRCC6_HUMANXRCC6physical
17620599
HDAC2_HUMANHDAC2physical
17620599
H2B1O_HUMANHIST1H2BOphysical
17620599
XRCC5_HUMANXRCC5physical
17620599
LBR_HUMANLBRphysical
17620599
MCM3_HUMANMCM3physical
17620599
NOLC1_HUMANNOLC1physical
17620599
TCOF_HUMANTCOF1physical
17620599
ANM5_HUMANPRMT5physical
17620599
NPM_HUMANNPM1physical
17620599
ERH_HUMANERHphysical
17620599
TIF1B_HUMANTRIM28physical
17620599
YBOX1_HUMANYBX1physical
17620599
LEO1_HUMANLEO1physical
17620599
THOC4_HUMANALYREFphysical
17620599
ZRAB2_HUMANZRANB2physical
17620599
TR150_HUMANTHRAP3physical
17620599
HTSF1_HUMANHTATSF1physical
17620599
RPA1_HUMANPOLR1Aphysical
17620599
RPA2_HUMANPOLR1Bphysical
17620599
ILF3_HUMANILF3physical
17620599
RPA43_HUMANTWISTNBphysical
17620599
NP1L1_HUMANNAP1L1physical
17620599
YBOX3_HUMANYBX3physical
17620599
NOP10_HUMANNOP10physical
17620599
RBM10_HUMANRBM10physical
17620599
NUCL_HUMANNCLphysical
17620599
NOP56_HUMANNOP56physical
17620599
SF3B1_HUMANSF3B1physical
17620599
SF3B2_HUMANSF3B2physical
17620599
SFPQ_HUMANSFPQphysical
17620599
NONO_HUMANNONOphysical
17620599
DDX3X_HUMANDDX3Xphysical
17620599
DHX15_HUMANDHX15physical
17620599
SRRM2_HUMANSRRM2physical
17620599
SMD1_HUMANSNRPD1physical
17620599
SMD2_HUMANSNRPD2physical
17620599
ROA1_HUMANHNRNPA1physical
17620599
ROA2_HUMANHNRNPA2B1physical
17620599
HNRPD_HUMANHNRNPDphysical
17620599
HNRH1_HUMANHNRNPH1physical
17620599
HNRPK_HUMANHNRNPKphysical
17620599
HNRPM_HUMANHNRNPMphysical
17620599
HNRPU_HUMANHNRNPUphysical
17620599
ROA0_HUMANHNRNPA0physical
17620599
HNRPC_HUMANHNRNPCphysical
17620599
HNRPF_HUMANHNRNPFphysical
17620599
HNRH2_HUMANHNRNPH2physical
17620599
PTBP1_HUMANPTBP1physical
17620599
HNRPR_HUMANHNRNPRphysical
17620599
SF3B3_HUMANSF3B3physical
17620599
DKC1_HUMANDKC1physical
17620599
FBRL_HUMANFBLphysical
17620599
U5S1_HUMANEFTUD2physical
17620599
PABP3_HUMANPABPC3physical
17620599
PABP4_HUMANPABPC4physical
17620599
PAIRB_HUMANSERBP1physical
17620599
IF4B_HUMANEIF4Bphysical
17620599
EF1A2_HUMANEEF1A2physical
17620599
PABP1_HUMANPABPC1physical
17620599
IF2B1_HUMANIGF2BP1physical
17620599
RS3A_HUMANRPS3Aphysical
17620599
RS3_HUMANRPS3physical
17620599
RS17_HUMANRPS17physical
17620599
RS19_HUMANRPS19physical
17620599
RL7A_HUMANRPL7Aphysical
17620599
RL7_HUMANRPL7physical
17620599
RL12_HUMANRPL12physical
17620599
RL18_HUMANRPL18physical
17620599
RL21_HUMANRPL21physical
17620599
RL22_HUMANRPL22physical
17620599
RL31_HUMANRPL31physical
17620599
RLA0_HUMANRPLP0physical
17620599
RLA1_HUMANRPLP1physical
17620599
RLA2_HUMANRPLP2physical
17620599
RS6_HUMANRPS6physical
17620599
RS7_HUMANRPS7physical
17620599
RS8_HUMANRPS8physical
17620599
RS13_HUMANRPS13physical
17620599
RL3_HUMANRPL3physical
17620599
RL6_HUMANRPL6physical
17620599
RL14_HUMANRPL14physical
17620599
RL15_HUMANRPL15physical
17620599
RL28_HUMANRPL28physical
17620599
EF2_HUMANEEF2physical
17620599
ACTB_HUMANACTBphysical
17620599
TBA4A_HUMANTUBA4Aphysical
17620599
TBA3C_HUMANTUBA3Cphysical
17620599
TBA1C_HUMANTUBA1Cphysical
17620599
TBB2A_HUMANTUBB2Aphysical
17620599
TBB4B_HUMANTUBB4Bphysical
17620599
TBB3_HUMANTUBB3physical
17620599
VIME_HUMANVIMphysical
17620599
ACTH_HUMANACTG2physical
17620599
TBB4A_HUMANTUBB4Aphysical
17620599
TBA1A_HUMANTUBA1Aphysical
17620599
COF1_HUMANCFL1physical
17620599
FLNA_HUMANFLNAphysical
17620599
GELS_HUMANGSNphysical
17620599
TMOD3_HUMANTMOD3physical
17620599
SPTN1_HUMANSPTAN1physical
17620599
ARP5L_HUMANARPC5Lphysical
17620599
SPTB2_HUMANSPTBN1physical
17620599
LIMA1_HUMANLIMA1physical
17620599
MAP1B_HUMANMAP1Bphysical
17620599
CAZA1_HUMANCAPZA1physical
17620599
CAZA2_HUMANCAPZA2physical
17620599
SRC8_HUMANCTTNphysical
17620599
DREB_HUMANDBN1physical
17620599
MYH9_HUMANMYH9physical
17620599
MYO1C_HUMANMYO1Cphysical
17620599
MYL6_HUMANMYL6physical
17620599
DYHC1_HUMANDYNC1H1physical
17620599
MYH10_HUMANMYH10physical
17620599
KPYM_HUMANPKMphysical
17620599
G3P_HUMANGAPDHphysical
17620599
FAS_HUMANFASNphysical
17620599
F263_HUMANPFKFB3physical
17620599
PDIA1_HUMANP4HBphysical
17620599
SDHA_HUMANSDHAphysical
17620599
RPN2_HUMANRPN2physical
17620599
NAA10_HUMANNAA10physical
17620599
PYRG1_HUMANCTPS1physical
17620599
DDX1_HUMANDDX1physical
17620599
HSP7C_HUMANHSPA8physical
17620599
HS71L_HUMANHSPA1Lphysical
17620599
HS90B_HUMANHSP90AB1physical
17620599
TCPZ_HUMANCCT6Aphysical
17620599
ICLN_HUMANCLNS1Aphysical
17620599
KCAB1_HUMANKCNAB1physical
17620599
TRPV4_HUMANTRPV4physical
17620599
CLIC1_HUMANCLIC1physical
17620599
BCLF1_HUMANBCLAF1physical
17620599
GRP78_HUMANHSPA5physical
17620599
RS27A_HUMANRPS27Aphysical
17620599
UBB_HUMANUBBphysical
17620599
UBC_HUMANUBCphysical
17620599
CAN1_HUMANCAPN1physical
17620599
RL40_HUMANUBA52physical
17620599
UBR5_HUMANUBR5physical
17620599
SPIN1_HUMANSPIN1physical
17620599
SPIN3_HUMANSPIN3physical
17620599
NKTR_HUMANNKTRphysical
17620599
DCD_HUMANDCDphysical
17620599
C1QBP_HUMANC1QBPphysical
17620599
MEP50_HUMANWDR77physical
17620599
HDGR2_HUMANHDGFRP2physical
17620599
BOLA2_HUMANBOLA2physical
17620599
MOB1A_HUMANMOB1Aphysical
17620599
COPRS_HUMANCOPRSphysical
17620599
PAK5_HUMANPAK7physical
17620599
M3K1_HUMANMAP3K1physical
17620599
M3K14_HUMANMAP3K14physical
17620599
WEE1_HUMANWEE1physical
17620599
CDK4_HUMANCDK4physical
17620599
PRP4B_HUMANPRPF4Bphysical
17620599
P3C2A_HUMANPIK3C2Aphysical
17620599
SRPK2_HUMANSRPK2physical
17620599
M3K7_HUMANMAP3K7physical
17620599
KPB2_HUMANPHKA2physical
17620599
AP2A2_HUMANAP2A2physical
17620599
AP3B2_HUMANAP3B2physical
17620599
LRP11_HUMANLRP11physical
17620599
RHG17_HUMANARHGAP17physical
17620599
ARHGB_HUMANARHGEF11physical
17620599
ARHGC_HUMANARHGEF12physical
17620599
PDE4D_HUMANPDE4Dphysical
17620599
AFAD_HUMANMLLT4physical
17620599
S10A9_HUMANS100A9physical
17620599
H12_HUMANHIST1H1Cphysical
17620599
H2AX_HUMANH2AFXphysical
17620599
RFA1_HUMANRPA1physical
17620599
RPAC1_HUMANPOLR1Cphysical
17620599
RPAB1_HUMANPOLR2Ephysical
17620599
STAT1_HUMANSTAT1physical
17620599
MYCD_HUMANMYOCDphysical
17620599
CENPF_HUMANCENPFphysical
17620599
DDX5_HUMANDDX5physical
17620599
RS4X_HUMANRPS4Xphysical
17620599
RL4_HUMANRPL4physical
17620599
RL11_HUMANRPL11physical
17620599
RL19_HUMANRPL19physical
17620599
RL30_HUMANRPL30physical
17620599
RL26_HUMANRPL26physical
17620599
RL35A_HUMANRPL35Aphysical
17620599
RL35_HUMANRPL35physical
17620599
RL36_HUMANRPL36physical
17620599
EF1A1_HUMANEEF1A1physical
17620599
ACTC_HUMANACTC1physical
17620599
LAP2A_HUMANTMPOphysical
17620599
LAP2B_HUMANTMPOphysical
17620599
E41L3_HUMANEPB41L3physical
17620599
BSN_HUMANBSNphysical
17620599
PPIA_HUMANPPIAphysical
17620599
HSP76_HUMANHSPA6physical
17620599
CUL5_HUMANCUL5physical
17620599
CASB_HUMANCSN2physical
17620599
IMB1_HUMANKPNB1physical
17620599
TERA_HUMANVCPphysical
17620599
NSUN2_HUMANNSUN2physical
17620599
PRP4_HUMANPRPF4physical
17620599
MDM2_HUMANMDM2physical
21081496
TRAF6_HUMANTRAF6physical
16378096
UBC_HUMANUBCphysical
21378163
MDM2_HUMANMDM2physical
17984062
AP2M1_HUMANAP2M1physical
17984062
FLNA_HUMANFLNAphysical
17984062
SL9A5_HUMANSLC9A5physical
15699339
IKBA_HUMANNFKBIAphysical
15173580
IGF1R_HUMANIGF1Rphysical
23188799
IKBA_HUMANNFKBIAphysical
15125834
EDNRA_HUMANEDNRAphysical
19202075
SRC_HUMANSRCphysical
19202075
GLUC_HUMANGCGphysical
18445652
MP2K4_HUMANMAP2K4physical
19782076
AKT1_HUMANAKT1physical
19262695
CSK_HUMANCSKphysical
19262695
LIMK1_HUMANLIMK1physical
17500066
AGRB1_HUMANBAI1physical
23782696
MDM2_HUMANMDM2physical
21988832
PTGDS_HUMANPTGDSphysical
21112970
UBP33_HUMANUSP33physical
24377933
MK09_HUMANMAPK9physical
25416956
HGS_HUMANHGSphysical
23208550
NEDD4_HUMANNEDD4physical
23208550
ARRD3_HUMANARRDC3physical
23208550
TRAF6_HUMANTRAF6physical
25425640
ALS_HUMANIGFALSphysical
26344197
AP2B1_HUMANAP2B1physical
21118812
HGS_HUMANHGSphysical
20505072
OPSD_HUMANRHOphysical
9852134
SRC_HUMANSRCphysical
11877451
AP3B2_HUMANAP3B2physical
11877451
AP1B1_HUMANAP1B1physical
11877451
RAF1_HUMANRAF1physical
11226259
SYNE2_HUMANSYNE2physical
26496610
ANR11_HUMANANKRD11physical
26496610
PPM1B_HUMANPPM1Bphysical
25241761
M3K1_HUMANMAP3K1physical
25241761
SRC8_HUMANCTTNphysical
25241761
CTNA1_HUMANCTNNA1physical
25241761
MK01_HUMANMAPK1physical
25241761
IKKA_HUMANCHUKphysical
25241761
TAB2_HUMANTAB2physical
25241761
KPCB_HUMANPRKCBphysical
26545496
DRD2_HUMANDRD2physical
25162404
DRD4_HUMANDRD4physical
27155323
KLH12_HUMANKLHL12physical
27155323
CUL3_HUMANCUL3physical
27155323
PE2R2_HUMANPTGER2physical
11418617
PE2R4_HUMANPTGER4physical
11418617
ARRB1_HUMANARRB1physical
28514442
ARRC_HUMANARR3physical
28514442
KANK1_HUMANKANK1physical
28514442
BRPF1_HUMANBRPF1physical
28514442
DIEXF_HUMANDIEXFphysical
28514442
NAA15_HUMANNAA15physical
28514442
RTF1_HUMANRTF1physical
28514442
RFX1_HUMANRFX1physical
28514442
WDR70_HUMANWDR70physical
28514442
CR025_HUMANC18orf25physical
28514442
RAD18_HUMANRAD18physical
28514442
NOLC1_HUMANNOLC1physical
28514442
SAHH3_HUMANAHCYL2physical
28514442
FLNB_HUMANFLNBphysical
28514442
AFF4_HUMANAFF4physical
28514442
ENL_HUMANMLLT1physical
28514442
AF9_HUMANMLLT3physical
28514442
IKBL1_HUMANNFKBIL1physical
28514442
CENPB_HUMANCENPBphysical
28514442
JPH1_HUMANJPH1physical
28514442
E41L5_HUMANEPB41L5physical
28514442
SAHH2_HUMANAHCYL1physical
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 ARRB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of arrestin-3 phosphorylation by casein kinase II.";
Kim Y.-M., Barak L.S., Caron M.G., Benovic J.L.;
J. Biol. Chem. 277:16837-16846(2002).
Cited for: FUNCTION IN INTERNALIZATION OF ADBR2, PHOSPHORYLATION AT THR-382,INTERACTION WITH AP2B1; CLATHRIN AND SRC, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF THR-382.

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