Search Keyword:


Search option:


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
341
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 101-160
 Evidence NMR Reference
       Region 101-160 disorder
Seq 119-146 Hetero dimer : IID50008Complex
 Evidence NMR 1kdx B Reference
       Region 1kdx B 119-146 order
Seqdisorder 101-118,147-160
 Evidence NMR Reference
       Region 101-118 disorder
       Region 147-160 disorder
SeqProS verified 119-146 Hetero dimer : IID50008Complex
       Region 1kdx B 119-146 order
       Region 101-160 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. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells (By similarity).
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