| General information | | DisProt: | DP00682 | | Name: | Cyclic AMP-responsive element-binding protein 1 | | Synonym(s): | CREB1_RAT
cAMP-responsive element-binding protein 1
CREB-1
| | First appeared in release: | Release 5.1 (05/28/2010) | | UniProt: | P15337 | | UniGene: | Mm.466618 | | SwissProt: | CREB1_RAT | | TrEMBL: | | | NCBI (GI): | 12644184 | | Source organism: | Rattus norvegicus (Rat) | | Sequence length: | 341 | | Percent disordered: | 10% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MTMDSGADNQ QSGDAAVTEA ESQQMTVQAQ PQIATLAQVS MPAAHATSSA PTVTLVQLPN - 60
GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT QISTIAESED SQESVDSVTD - 120
SQKRREILSR RPSYRKILND LSSDAPGVPR IEEEKSEEET SAPAITTVTV PTPIYQTSSG - 180
QYIAITQGGA IQLANNGTDG VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV - 240
VVQAASGDVQ TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC - 300
RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D
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| Functional narrative |
This protein binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. CREB stimulates transcription on binding to the CRE. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Implicated in synchronization of circadian rhythmicity
Interacts with PPRC1. Binds DNA as a dimer. Interacts, through the bZIP domain, with the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3 (By similarity). When phosphorylated on Ser-133, binds CREBBP. Interacts with ARRB1 (By similarity). Q4AE70:Carm1; NbExp=1; IntAct=EBI-973322, EBI-973358;
Belongs to the bZIP family.
Contains 1 bZIP domain.
Contains 1 KID (kinase-inducible) domain.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | pKID domain | | Location: | 101 - 120 | | Length: | 20 | | Region sequence: |
QISTIAESEDSQESVDSVTD | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (315 K; Bruker 500 MHz; Bruker 600; Bruker 750; Felix 95 (software))
| References:
- Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE. "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions." Cell. 1997; 91(6): 741-752. PubMed: 9413984
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | pKID domain | | Location: | 146 - 160 | | Length: | 15 | | Region sequence: |
PGVPRIEEEKSEEET | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (315 K; Bruker 500 MHz; Bruker 600 MHz; Bruker 750 MHz; Felix 95 (software))
| References:
- Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE. "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions." Cell. 1997; 91(6): 741-752. PubMed: 9413984
| Comments:
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| Region 3 | | Type: | Ordered | | Name: | pKID domain | | Location: | 119 - 146 | | Length: | 28 | | Region sequence: |
TDSQKRREILSRRPSYRKILNDLSSDAP | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (315 K; Bruker 500 MHz; Bruker 600 MHz; Bruker 750 MHz; Felix 95 (software))
| References:
- Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE. "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions." Cell. 1997; 91(6): 741-752. PubMed: 9413984
| Comments:
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