CREB1
entrez
1385
canonical
uniprot
P16220
canonical
ensembl
ENSG00000118260
resolver
ensp
ENSP00000236995
resolver
ensp
ENSP00000387699
resolver
ensp
ENSP00000405539
resolver
ensp
ENSP00000405711
resolver
ensp
ENSP00000407227
resolver
ensp
ENSP00000631950
resolver
ensp
ENSP00000673615
resolver
ensp
ENSP00000673616
resolver
ensp
ENSP00000732879
resolver
ensp
ENSP00000760642
resolver
ensp
ENSP00000777816
resolver
ensp
ENSP00000787509
resolver
ensp
ENSP00000787510
resolver
genesymbol
CREB1
resolver
hgnc
HGNC:2345
resolver
uniprot
A0A024R401
resolver
uniprot
A0A024R437
resolver
uniprot
B7Z5C6
resolver
uniprot
P21934
resolver
uniprot
Q53X93
resolver
uniprot
Q5U0J5
resolver
uniprot
Q6V963
resolver
uniprot
Q9UMA7
resolver
uniprot_entry
B7Z5C6_HUMAN
resolver
uniprot_entry
CREB1_HUMAN
resolver
uniprot_entry
Q53X93_HUMAN
resolver
uniprot_entry
Q5U0J5_HUMAN
resolver
uniprot_sec
A0A024R401
resolver
uniprot_sec
A0A024R437
resolver
uniprot_sec
P21934
resolver
uniprot_sec
Q6V963
resolver
uniprot_sec
Q9UMA7
resolver
amino_acid_sequence
MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD
uniprot
proteins
disease_involvement
DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving CREB1 is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type.; DISEASE: Note=A CREB1 mutation has been found in a patient with multiple congenital anomalies consisting of agenesis of the corpus callosum, cerebellar hypoplasia, severe neonatal respiratory distress refractory to surfactant, thymus hypoplasia, and thyroid follicular hypoplasia. {ECO:0000269|PubMed:22267179}.
uniprot
proteins
function
FUNCTION: 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 (PubMed:14536081). 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 (By similarity). {ECO:0000250|UniProtKB:P27925, ECO:0000250|UniProtKB:Q01147, ECO:0000269|PubMed:14536081}.
uniprot
proteins
mass_dalton
35136
uniprot
proteins
mutagenesis
MUTAGEN 119; /note="S->A: Does not interact with TOX3 and inhibits induction of transcription by TOX3. Loss of phosphorylation by CaMK4. Loss of phosphorylation by TSSK4."; /evidence="ECO:0000269|PubMed:15964553, ECO:0000269|PubMed:21172805, ECO:0000269|PubMed:8065343"; MUTAGEN 141; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:12552083"; MUTAGEN 257; /note="S->A: Impaired phosphorylation by HIPK2 and subsequent transactivation."; /evidence="ECO:0000269|PubMed:20573984"; MUTAGEN 257; /note="S->E: Potentiated transactivation."; /evidence="ECO:0000269|PubMed:20573984"; MUTAGEN 271; /note="K->R: Decreased sumoylation, in vivo and in vitro."; /evidence="ECO:0000269|PubMed:12552083"; MUTAGEN 290; /note="K->R: Decreased sumoylation, in vivo and in vitro. Loss of nuclear localization."; /evidence="ECO:0000269|PubMed:12552083
uniprot
proteins
post_translational_modification
PTM: Stimulated by phosphorylation. Phosphorylation of both Ser-119 and Ser-128 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. Phosphorylation of Ser-119 allows CREBBP binding. In liver, phosphorylation is induced by fasting or glucagon in a circadian fashion (By similarity). CREBL2 positively regulates phosphorylation at Ser-119 thereby stimulating CREB1 transcriptional activity (By similarity). Phosphorylated upon calcium influx by CaMK4 and CaMK2 on Ser-119. CaMK4 is much more potent than CaMK2 in activating CREB. Phosphorylated by CaMK2 on Ser-128. Phosphorylation of Ser-128 blocks CREB-mediated transcription even when Ser-119 is phosphorylated. Phosphorylated by CaMK1 (By similarity). Phosphorylation of Ser-257 by HIPK2 in response to genotoxic stress promotes CREB1 activity, facilitating the recruitment of the coactivator CBP. Phosphorylated at Ser-119 by RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. Phosphorylated by TSSK4 on Ser-119 (PubMed:15964553). {ECO:0000250, ECO:0000269|PubMed:15733869, ECO:0000269|PubMed:15964553, ECO:0000269|PubMed:20573984, ECO:0000269|PubMed:7608156, ECO:0000269|PubMed:8065343, ECO:0000269|PubMed:9770464, ECO:0000269|PubMed:9829964}.; PTM: Sumoylated with SUMO1. Sumoylation on Lys-290, but not on Lys-271, is required for nuclear localization of this protein. Sumoylation is enhanced under hypoxia, promoting nuclear localization and stabilization. {ECO:0000269|PubMed:12552083}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
pubmed
12552083
uniprot
proteins
pubmed
1386673
uniprot
proteins
pubmed
14506290
uniprot
proteins
pubmed
14536081
uniprot
proteins
pubmed
15454081
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15579595
uniprot
proteins
pubmed
15733869
uniprot
proteins
pubmed
15964553
uniprot
proteins
pubmed
16325578
uniprot
proteins
pubmed
16908542
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17724745
uniprot
proteins
pubmed
18160048
uniprot
proteins
pubmed
1827531
uniprot
proteins
pubmed
1831258
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1966745
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20573984
uniprot
proteins
pubmed
21172805
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
2142528
uniprot
proteins
pubmed
2196176
uniprot
proteins
pubmed
22267179
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23651431
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
2974179
uniprot
proteins
pubmed
7608156
uniprot
proteins
pubmed
8065343
uniprot
proteins
pubmed
8381074
uniprot
proteins
pubmed
9770464
uniprot
proteins
pubmed
9829964
uniprot
proteins
sequence_length
327
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:12552083}.
uniprot
proteins