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7UMB

NanoBRET tracer Tram-bo bound to a KSR2-MEK1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0000165biological_processMAPK cascade
C0000187biological_processobsolete activation of MAPK activity
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004708molecular_functionMAP kinase kinase activity
C0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005078molecular_functionMAP-kinase scaffold activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005769cellular_componentearly endosome
C0005770cellular_componentlate endosome
C0005783cellular_componentendoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0005813cellular_componentcentrosome
C0005816cellular_componentspindle pole body
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006468biological_processprotein phosphorylation
C0006935biological_processchemotaxis
C0007165biological_processsignal transduction
C0007507biological_processheart development
C0008285biological_processnegative regulation of cell population proliferation
C0010628biological_processpositive regulation of gene expression
C0014044biological_processSchwann cell development
C0016020cellular_componentmembrane
C0021697biological_processcerebellar cortex formation
C0030182biological_processneuron differentiation
C0030216biological_processkeratinocyte differentiation
C0030295molecular_functionprotein kinase activator activity
C0030878biological_processthyroid gland development
C0032872biological_processregulation of stress-activated MAPK cascade
C0035987biological_processendodermal cell differentiation
C0038133biological_processERBB2-ERBB3 signaling pathway
C0042552biological_processmyelination
C0043410biological_processpositive regulation of MAPK cascade
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0044342biological_processtype B pancreatic cell proliferation
C0045893biological_processpositive regulation of DNA-templated transcription
C0048009biological_processinsulin-like growth factor receptor signaling pathway
C0048538biological_processthymus development
C0048679biological_processregulation of axon regeneration
C0048870biological_processcell motility
C0050772biological_processpositive regulation of axonogenesis
C0060020biological_processBergmann glial cell differentiation
C0060324biological_processface development
C0060425biological_processlung morphogenesis
C0060440biological_processtrachea formation
C0060502biological_processepithelial cell proliferation involved in lung morphogenesis
C0060674biological_processplacenta blood vessel development
C0060711biological_processlabyrinthine layer development
C0070371biological_processERK1 and ERK2 cascade
C0070374biological_processpositive regulation of ERK1 and ERK2 cascade
C0071902biological_processpositive regulation of protein serine/threonine kinase activity
C0090170biological_processregulation of Golgi inheritance
C0090398biological_processcellular senescence
C0097110molecular_functionscaffold protein binding
C0106310molecular_functionprotein serine kinase activity
C1903226biological_processpositive regulation of endodermal cell differentiation
C2000641biological_processregulation of early endosome to late endosome transport
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK
ChainResidueDetails
CLEU74-LYS97

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHkDLKskNVFY
ChainResidueDetails
BILE782-TYR794
CILE186-VAL198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
CASP190

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613
ChainResidueDetails
CLEU74
CMET143
CSER150
CLYS192
CASP208

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH
ChainResidueDetails
CLYS97
BASP803

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF
ChainResidueDetails
CGLU144
CSER194

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746
ChainResidueDetails
CSER218

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746
ChainResidueDetails
CSER222

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
CTHR286

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986
ChainResidueDetails
CTHR292

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686
ChainResidueDetails
CSER298

223532

PDB entries from 2024-08-07

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