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2L7W

Solution structure of the human Raf-1 kinase inhibitor protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0008429molecular_functionphosphatidylethanolamine binding
A0019899molecular_functionenzyme binding
A0019901molecular_functionprotein kinase binding
A0043409biological_processnegative regulation of MAPK cascade
A0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS01220
Number of Residues23
DetailsPBP Phosphatidylethanolamine-binding protein family signature. YtLVlTDPDaPSrkdpkyrewhH
ChainResidueDetails
ATYR64-HIS86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER6
ASER98
ASER153

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P31044
ChainResidueDetails
ASER13

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR42

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER52

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER54

221051

PDB entries from 2024-06-12

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