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IID50004
 UniprotP15337
ProteinCyclic AMP-responsive element-binding protein 1
GeneCreb1
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
327
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 87-146
 Evidence NMR The NMR spectra of free pKID have the characteristics of an unstructured peptide (PMID: 9413984) Reference
       Region 87-146 disorder
Seq 87-146 Hetero dimer : IID50008Complex
 Evidence NMR 1kdx B Even in the KIX complex, residues 101-120 and 146-160 of pKID exhibit resonances that are sharp and have chemical shifts close to random coil values, indicating that these regions remain largely unstructured and flexible. (PMID: 9413984, Note: In this article, the amino acid residues are numbered based on the sequence P15337-1). Reference
       Region 1kdx B 87-106 disorder
       Region 1kdx B 105-132 order
       Region 1kdx B 132-146 disorder
SeqProS verified 107-131 Hetero dimer : IID50008Complex
       Region 1kdx B 105-132 order
       Region 87-146 disorder
Seqphosphorylation
    128-128 Phosphoserine; by CaMK2
    257-257 Phosphoserine; by HIPK2
    119-119 Phosphoserine; by CaMK1
 
Prediction
NeProc
Disorder 1-276
Order 277-327
ProS 65-69,78-91,120-138,164-177,205-209,218-222,227-232,270-276
AlphaFold
Disorder 1-103,130-158,173-173,176-176,181-214,216-219,221-230,233-233,240-263,326-327
Order 104-129,159-172,174-175,177-180,215-215,220-220,231-232,234-239,264-325
Pfam Hmmer
PF02173 99-139 8.8e-23
PF00170 267-327 1e-21
SEG 93-108 ,138-145 ,148-160 ,278-292
Function
Function in SwissProt
Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters (By similarity). Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation (By similarity). Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells (By similarity). Regulates the expression of apoptotic and inflammatory response factors in cardiomyocytes in response to ERFE-mediated activation of AKT signaling (PubMed:30566056).
Biological Process
Diagram with PDB data
Creb1/CrebbpKIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEX WITH PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RAT CREB (CYCLIC AMP RESPONSE ELEMENT BINDING PROTEIN), NMR 17 STRUCTURES