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2R6M

Crystal structure of rat CK2-beta subunit

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003682molecular_functionchromatin binding
A0004674molecular_functionprotein serine/threonine kinase activity
A0005102molecular_functionsignaling receptor binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005956cellular_componentprotein kinase CK2 complex
A0016055biological_processWnt signaling pathway
A0016363cellular_componentnuclear matrix
A0016605cellular_componentPML body
A0019887molecular_functionprotein kinase regulator activity
A0019904molecular_functionprotein domain specific binding
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031519cellular_componentPcG protein complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032927biological_processpositive regulation of activin receptor signaling pathway
A0033211biological_processadiponectin-activated signaling pathway
A0033574biological_processresponse to testosterone
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0043021molecular_functionribonucleoprotein complex binding
A0043537biological_processnegative regulation of blood vessel endothelial cell migration
A0046872molecular_functionmetal ion binding
A0060391biological_processpositive regulation of SMAD protein signal transduction
A0061154biological_processendothelial tube morphogenesis
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0075342biological_processsymbiont-mediated disruption of host cell PML body
A0097421biological_processliver regeneration
A1903901biological_processnegative regulation of viral life cycle
B0000785cellular_componentchromatin
B0003682molecular_functionchromatin binding
B0004674molecular_functionprotein serine/threonine kinase activity
B0005102molecular_functionsignaling receptor binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0005956cellular_componentprotein kinase CK2 complex
B0016055biological_processWnt signaling pathway
B0016363cellular_componentnuclear matrix
B0016605cellular_componentPML body
B0019887molecular_functionprotein kinase regulator activity
B0019904molecular_functionprotein domain specific binding
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031519cellular_componentPcG protein complex
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032927biological_processpositive regulation of activin receptor signaling pathway
B0033211biological_processadiponectin-activated signaling pathway
B0033574biological_processresponse to testosterone
B0042802molecular_functionidentical protein binding
B0042995cellular_componentcell projection
B0043021molecular_functionribonucleoprotein complex binding
B0043537biological_processnegative regulation of blood vessel endothelial cell migration
B0046872molecular_functionmetal ion binding
B0060391biological_processpositive regulation of SMAD protein signal transduction
B0061154biological_processendothelial tube morphogenesis
B0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
B0075342biological_processsymbiont-mediated disruption of host cell PML body
B0097421biological_processliver regeneration
B1903901biological_processnegative regulation of viral life cycle
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 216
ChainResidue
ACYS109
ACYS114
ACYS137
ACYS140

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 216
ChainResidue
BCYS109
BCYS114
BCYS137
BCYS140

Functional Information from PROSITE/UniProt
site_idPS01101
Number of Residues32
DetailsCK2_BETA Casein kinase II regulatory subunit signature. CPrVyCenqpmLPIGlsdipgeamVKlyCPkC
ChainResidueDetails
ACYS109-CYS140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ACYS109
ACYS114
ACYS137
ACYS140
BCYS109
BCYS114
BCYS137
BCYS140

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P67870, ECO:0000305
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P67870
ChainResidueDetails
ASER3
BSER3

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P67870
ChainResidueDetails
ASER8
ASER69
ASER209
BSER8
BSER69
BSER209

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P67870
ChainResidueDetails
ATHR37
BTHR37

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P67870
ChainResidueDetails
ALYS212
BLYS212

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P67870
ChainResidueDetails
ALYS212
BLYS212

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PDB entries from 2024-07-17

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