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6PWC

A complex structure of arrestin-2 bound to neurotensin receptor 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000785cellular_componentchromatin
A0001664molecular_functionG protein-coupled receptor binding
A0001934biological_processpositive regulation of protein phosphorylation
A0002031biological_processG protein-coupled receptor internalization
A0002092biological_processpositive regulation of receptor internalization
A0003713molecular_functiontranscription coactivator activity
A0004402molecular_functionhistone acetyltransferase activity
A0004857molecular_functionenzyme inhibitor activity
A0005096molecular_functionGTPase activator activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005905cellular_componentclathrin-coated pit
A0006357biological_processregulation of transcription by RNA polymerase II
A0006511biological_processubiquitin-dependent protein catabolic process
A0007165biological_processsignal transduction
A0007601biological_processvisual perception
A0009968biological_processnegative regulation of signal transduction
A0015031biological_processprotein transport
A0016567biological_processprotein ubiquitination
A0016604cellular_componentnuclear body
A0030659cellular_componentcytoplasmic vesicle membrane
A0030666cellular_componentendocytic vesicle membrane
A0031143cellular_componentpseudopodium
A0031397biological_processnegative regulation of protein ubiquitination
A0031410cellular_componentcytoplasmic vesicle
A0031625molecular_functionubiquitin protein ligase binding
A0031701molecular_functionangiotensin receptor binding
A0032088biological_processnegative regulation of NF-kappaB transcription factor activity
A0032715biological_processnegative regulation of interleukin-6 production
A0032717biological_processnegative regulation of interleukin-8 production
A0035025biological_processpositive regulation of Rho protein signal transduction
A0042995cellular_componentcell projection
A0043149biological_processstress fiber assembly
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045746biological_processnegative regulation of Notch signaling pathway
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A1990763molecular_functionarrestin family protein binding
R0004930molecular_functionG protein-coupled receptor activity
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0016492molecular_functionG protein-coupled neurotensin receptor activity
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ATAlNVASLSVERYLaI
ChainResidueDetails
RALA154-ILE170

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
HTYR204-HIS210
LTYR193-HIS199

site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
APHE61-LEU79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS250
AMET255
ALYS324
ALYS326

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8BWG8
ChainResidueDetails
ATYR47
RGLU165-ARG184
RALA260-ARG303
RASN365-TYR418

site_idSWS_FT_FI3
Number of Residues19
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RTYR103-VAL122

site_idSWS_FT_FI4
Number of Residues64
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RGLU123-ARG142
RTHR206-LYS234
RPHE326-HIS343

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RGLY143-VAL164

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RTHR185-PHE205

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RVAL235-ILE259

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RVAL304-MET325

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P20789
ChainResidueDetails
RTYR344-TYR364

site_idSWS_FT_FI10
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:21725197
ChainResidueDetails
RCYS381
RCYS383

226707

PDB entries from 2024-10-30

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