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2LQN

Solution structure of CRKL

Functional Information from GO Data
ChainGOidnamespacecontents
A0001784molecular_functionphosphotyrosine residue binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007167biological_processenzyme-linked receptor protein signaling pathway
A0007254biological_processJNK cascade
A0007265biological_processRas protein signal transduction
A0008284biological_processpositive regulation of cell population proliferation
A0010468biological_processregulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0016477biological_processcell migration
A0030334biological_processregulation of cell migration
A0030971molecular_functionreceptor tyrosine kinase binding
A0031594cellular_componentneuromuscular junction
A0032991cellular_componentprotein-containing complex
A0035022biological_processpositive regulation of Rac protein signal transduction
A0035556biological_processintracellular signal transduction
A0035591molecular_functionsignaling adaptor activity
A0042802molecular_functionidentical protein binding
A0045202cellular_componentsynapse
A0045296molecular_functioncadherin binding
A0060392biological_processnegative regulation of SMAD protein signal transduction
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0071363biological_processcellular response to growth factor stimulus
A0071560biological_processcellular response to transforming growth factor beta stimulus
A0098698biological_processpostsynaptic specialization assembly
A0098890cellular_componentextrinsic component of postsynaptic membrane
A1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
A1903977biological_processpositive regulation of glial cell migration
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsDomain: {"description":"SH2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues60
DetailsDomain: {"description":"SH3 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues61
DetailsDomain: {"description":"SH3 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues50
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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