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8CPD

Cryo-EM structure of CRaf dimer with 14:3:3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0001678biological_processintracellular glucose homeostasis
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004709molecular_functionMAP kinase kinase kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0008270molecular_functionzinc ion binding
A0008285biological_processnegative regulation of cell population proliferation
A0008286biological_processinsulin receptor signaling pathway
A0008625biological_processextrinsic apoptotic signaling pathway via death domain receptors
A0010856molecular_functionadenylate cyclase activator activity
A0014044biological_processSchwann cell development
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019899molecular_functionenzyme binding
A0030154biological_processcell differentiation
A0030878biological_processthyroid gland development
A0031143cellular_componentpseudopodium
A0031267molecular_functionsmall GTPase binding
A0031333biological_processnegative regulation of protein-containing complex assembly
A0033138biological_processpositive regulation of peptidyl-serine phosphorylation
A0035019biological_processsomatic stem cell population maintenance
A0035023biological_processregulation of Rho protein signal transduction
A0035773biological_processinsulin secretion involved in cellular response to glucose stimulus
A0035994biological_processresponse to muscle stretch
A0038133biological_processERBB2-ERBB3 signaling pathway
A0042060biological_processwound healing
A0042552biological_processmyelination
A0042802molecular_functionidentical protein binding
A0042981biological_processregulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0043410biological_processpositive regulation of MAPK cascade
A0044342biological_processtype B pancreatic cell proliferation
A0045104biological_processintermediate filament cytoskeleton organization
A0045595biological_processregulation of cell differentiation
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0048009biological_processinsulin-like growth factor receptor signaling pathway
A0048011biological_processneurotrophin TRK receptor signaling pathway
A0048538biological_processthymus development
A0060324biological_processface development
A0060333biological_processtype II interferon-mediated signaling pathway
A0071550biological_processdeath-inducing signaling complex assembly
A0106310molecular_functionprotein serine kinase activity
A1902042biological_processnegative regulation of extrinsic apoptotic signaling pathway via death domain receptors
B0000165biological_processMAPK cascade
B0000166molecular_functionnucleotide binding
B0001678biological_processintracellular glucose homeostasis
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004709molecular_functionMAP kinase kinase kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0007165biological_processsignal transduction
B0008270molecular_functionzinc ion binding
B0008285biological_processnegative regulation of cell population proliferation
B0008286biological_processinsulin receptor signaling pathway
B0008625biological_processextrinsic apoptotic signaling pathway via death domain receptors
B0010856molecular_functionadenylate cyclase activator activity
B0014044biological_processSchwann cell development
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0019899molecular_functionenzyme binding
B0030154biological_processcell differentiation
B0030878biological_processthyroid gland development
B0031143cellular_componentpseudopodium
B0031267molecular_functionsmall GTPase binding
B0031333biological_processnegative regulation of protein-containing complex assembly
B0033138biological_processpositive regulation of peptidyl-serine phosphorylation
B0035019biological_processsomatic stem cell population maintenance
B0035023biological_processregulation of Rho protein signal transduction
B0035773biological_processinsulin secretion involved in cellular response to glucose stimulus
B0035994biological_processresponse to muscle stretch
B0038133biological_processERBB2-ERBB3 signaling pathway
B0042060biological_processwound healing
B0042552biological_processmyelination
B0042802molecular_functionidentical protein binding
B0042981biological_processregulation of apoptotic process
B0043066biological_processnegative regulation of apoptotic process
B0043410biological_processpositive regulation of MAPK cascade
B0044342biological_processtype B pancreatic cell proliferation
B0045104biological_processintermediate filament cytoskeleton organization
B0045595biological_processregulation of cell differentiation
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0048009biological_processinsulin-like growth factor receptor signaling pathway
B0048011biological_processneurotrophin TRK receptor signaling pathway
B0048538biological_processthymus development
B0060324biological_processface development
B0060333biological_processtype II interferon-mediated signaling pathway
B0071550biological_processdeath-inducing signaling complex assembly
B0106310molecular_functionprotein serine kinase activity
B1902042biological_processnegative regulation of extrinsic apoptotic signaling pathway via death domain receptors
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
AILE355-LYS375

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKsnNIFL
ChainResidueDetails
AILE464-LEU476

site_idPS00479
Number of Residues46
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFarktflklaf.CdiCqkfLlngfr.....CqtCgykfHehCstkvptm..C
ChainResidueDetails
AHIS139-CYS184

site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
CARG44-VAL54

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
CTYR217-SER236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues92
DetailsZN_FING: Phorbol-ester/DAG-type => ECO:0000255|PROSITE-ProRule:PRU00226
ChainResidueDetails
ATHR138-CYS184
BTHR138-CYS184

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP468
BASP468

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AHIS139
BCYS152
BCYS155
BCYS165
BCYS168
BHIS173
BCYS176
BCYS184
ACYS152
ACYS155
ACYS165
ACYS168
AHIS173
ACYS176
ACYS184
BHIS139

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE355
ALYS375
BILE355
BLYS375

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0000250|UniProtKB:Q99N57
ChainResidueDetails
ASER29
BSER29

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA and MAPK1 => ECO:0000269|PubMed:8349614
ChainResidueDetails
ASER43
BSER43

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ASER252
BSER252

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA, PKC and PKB/AKT1 => ECO:0000269|PubMed:10576742, ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:11756411, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:8349614
ChainResidueDetails
ASER259
BSER259

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8349614
ChainResidueDetails
ATHR268
BTHR268

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:7477354
ChainResidueDetails
ATHR269
BTHR269

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0000269|PubMed:21917714, ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER289
BSER289

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER296
BSER296

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0000269|PubMed:21917714, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER301
BSER301

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK1, PAK2, PAK3 and PAK5 => ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:18465753, ECO:0000269|PubMed:21917714
ChainResidueDetails
ASER338
BSER338

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK1, PAK2 and PAK3 => ECO:0000269|PubMed:15849194
ChainResidueDetails
ASER339
BSER339

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:16892053
ChainResidueDetails
ATYR340
AASP341
BTYR340
BASP341

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16093354
ChainResidueDetails
ASER471
BSER471

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11447113
ChainResidueDetails
ATHR491
BTHR491

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11447113
ChainResidueDetails
ASER494
BSER494

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8349614
ChainResidueDetails
ASER499
BSER499

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:21917714
ChainResidueDetails
AARG563
BARG563

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:8349614
ChainResidueDetails
ASEP621
BSEP621

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER642
BSER642

237735

PDB entries from 2025-06-18

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