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HUMAN:Q4LE28

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) CREBBP variant protein (synonyms: CREBBP)
Protein Name(s) CREB binding protein

CREBBP variant protein

External Links
UniProt Q4LE28
EMBL AC004509
AC004651
AC006111
AC007151
AB210043
IPI IPI01009314
RefSeq NP_001073315.1
NP_004371.2
UniGene Hs.459759
ProteinModelPortal Q4LE28
SMR Q4LE28
STRING Q4LE28
Ensembl ENST00000543883
GeneID 1387
KEGG hsa:1387
UCSC uc002cvw.3
CTD 1387
HGNC HGNC:2348
PharmGKB PA26866
GeneTree ENSGT00550000074306
HOVERGEN HBG000185
KO K04498
NextBio 5635
ArrayExpress Q4LE28
Bgee Q4LE28
GO GO:0000123
GO:0004402
GO:0003713
GO:0008270
GO:0006355
InterPro IPR001487
IPR018359
IPR010303
IPR013178
IPR003101
IPR009110
IPR014744
IPR000197
IPR000433
Gene3D G3DSA:1.20.920.10
G3DSA:1.10.246.20
G3DSA:1.10.1630.10
G3DSA:1.20.1020.10
Pfam PF00439
PF09030
PF06001
PF08214
PF02172
PF02135
PF00569
PRINTS PR00503
SMART SM00297
SM00551
SM00291
SUPFAM SSF47370
SSF47040
SSF69125
SSF57933
PROSITE PS00633
PS50014
PS50952
PS50134
PS01357
PS50135

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0030511

positive regulation of transforming growth factor beta receptor signaling pathway

PMID:25514493[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016407

acetyltransferase activity

PMID:15273251[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006473

protein acetylation

PMID:15273251[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034644

cellular response to UV

PMID:24939902[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003682

chromatin binding

PMID:24939902[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003684

damaged DNA binding

PMID:24939902[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016407

acetyltransferase activity

PMID:24939902[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006473

protein acetylation

PMID:24939902[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031648

protein destabilization

PMID:24939902[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0001085

RNA polymerase II transcription factor binding

PMID:21539536[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O43474

F

Seeded From UniProt

complete

enables

GO:0003714

transcription corepressor activity

PMID:21539536[4]

ECO:0000314

direct assay evidence used in manual assertion

F

occurs_at:(SO:0001952)

Seeded From UniProt

complete

enables

GO:0000987

proximal promoter sequence-specific DNA binding

PMID:21539536[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000790

nuclear chromatin

PMID:21539536[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000122

negative regulation of transcription by RNA polymerase II

PMID:21539536[4]

ECO:0000314

direct assay evidence used in manual assertion

P

occurs_at:(SO:0001952)

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

PMID:12169688[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:12169688[5]

ECO:0000305

curator inference used in manual assertion

GO:0003713

C

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:12169688[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

PMID:11742995[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P45481

P

Seeded From UniProt

complete

enables

GO:0043426

MRF binding

PMID:8621548[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0042592

homeostatic process

PMID:15261140[8]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0018076

N-terminal peptidyl-lysine acetylation

PMID:12435739[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016604

nuclear body

PMID:15488321[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016573

histone acetylation

PMID:11742995[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016407

acetyltransferase activity

PMID:11742995[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008134

transcription factor binding

PMID:15509593[11]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P35680-1

F

Seeded From UniProt

complete

involved_in

GO:0007165

signal transduction

PMID:15261140[8]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:12929931[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:12929931[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004402

histone acetyltransferase activity

PMID:11742995[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:8684459[13]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q92793

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:14645221[14]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:12929931[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:12586840[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:12435739[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0002039

p53 binding

PMID:9194565[16]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04637

F

Seeded From UniProt

complete

enables

GO:0016407

acetyltransferase activity

PMID:16135789[17]

ECO:0000269

experimental evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016407

acetyltransferase activity

PMID:12456660[18]

ECO:0000269

experimental evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016604

nuclear body

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000123

histone acetyltransferase complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014744

C

Seeded From UniProt

complete

enables

GO:0003712

transcription coregulator activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000197
InterPro:IPR003101
InterPro:IPR036529

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014744

F

Seeded From UniProt

complete

enables

GO:0004402

histone acetyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000197
InterPro:IPR013178
InterPro:IPR014744

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000197
InterPro:IPR014744

C

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000197
InterPro:IPR003101
InterPro:IPR013178
InterPro:IPR014744
InterPro:IPR036529

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000197
InterPro:IPR000433

F

Seeded From UniProt

complete

involved_in

GO:0016573

histone acetylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013178
InterPro:IPR014744

P

Seeded From UniProt

complete

enables

GO:0004402

histone acetyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.48

F

Seeded From UniProt

complete

enables

GO:0004402

histone acetyltransferase activity

PMID:10362258[19]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:10362258[19]
PMID:10893273[20]
PMID:11001584[21]

ECO:0000304

author statement supported by traceable reference used in manual assertion



F

Seeded From UniProt

complete

involved_in

GO:0006473

protein acetylation

PMID:28386764[22]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

has_input:(UniProtKB:P10636)

Seeded From UniProt

complete

involved_in

GO:0007165

signal transduction

PMID:7913207[23]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0065003

protein-containing complex assembly

PMID:7913207[23]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

PMID:7913207[23]
PMID:15261140[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion


P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:7913207[23]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:7913207[23]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0042733

embryonic digit morphogenesis

PMID:11001584[21]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008589

regulation of smoothened signaling pathway

PMID:11001584[21]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0001102

RNA polymerase II activating transcription factor binding

PMID:11001584[21]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0001666

response to hypoxia

PMID:15261140[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904837

beta-catenin-TCF complex assembly

Reactome:R-HSA-201722

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1900034

regulation of cellular response to heat

Reactome:R-HSA-3371571

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0061418

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Reactome:R-HSA-1234174

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045944

positive regulation of transcription by RNA polymerase II

Reactome:R-HSA-8866907

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045747

positive regulation of Notch signaling pathway

Reactome:R-HSA-9017835

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045637

regulation of myeloid cell differentiation

Reactome:R-HSA-8939246

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042981

regulation of apoptotic process

Reactome:R-HSA-5633008

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032481

positive regulation of type I interferon production

Reactome:R-HSA-1834949

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019216

regulation of lipid metabolic process

Reactome:R-HSA-400206

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007221

positive regulation of transcription of Notch receptor target

Reactome:R-HSA-9021451

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007219

Notch signaling pathway

Reactome:R-HSA-1980143

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006367

transcription initiation from RNA polymerase II promoter

Reactome:R-HSA-350054

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-9626928
Reactome:R-HSA-933536
Reactome:R-HSA-9038052
Reactome:R-HSA-9021451
Reactome:R-HSA-9017835
Reactome:R-HSA-8938231
Reactome:R-HSA-8938228
Reactome:R-HSA-8878237
Reactome:R-HSA-8878220
Reactome:R-HSA-8864307
Reactome:R-HSA-6797993
Reactome:R-HSA-5660666
Reactome:R-HSA-5660660
Reactome:R-HSA-4396402
Reactome:R-HSA-4396401
Reactome:R-HSA-4396393
Reactome:R-HSA-4396392
Reactome:R-HSA-4396379
Reactome:R-HSA-4396371
Reactome:R-HSA-400143
Reactome:R-HSA-3371554
Reactome:R-HSA-3322427
Reactome:R-HSA-3134883
Reactome:R-HSA-2220971
Reactome:R-HSA-2220964
Reactome:R-HSA-2220957
Reactome:R-HSA-212356
Reactome:R-HSA-1912394
Reactome:R-HSA-1234167
Reactome:R-HSA-1028820
Reactome:R-HSA-1028819
Reactome:R-HSA-1028817
Reactome:R-HSA-1028815

ECO:0000304

author statement supported by traceable reference used in manual assertion

































C

Seeded From UniProt

complete

involved_in

GO:0002223

stimulatory C-type lectin receptor signaling pathway

Reactome:R-HSA-5621481

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0048511

rhythmic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0090

P

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Yang, Y et al. (2015) Pokemon (FBI-1) interacts with Smad4 to repress TGF-β-induced transcriptional responses. Biochim. Biophys. Acta 1849 270-81 PubMed GONUTS page
  2. 2.0 2.1 Zhao, Q et al. (2004) Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1. J. Biol. Chem. 279 41477-86 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 Cazzalini, O et al. (2014) CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis. Nucleic Acids Res. 42 8433-48 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 Kalra, IS et al. (2011) Krüppel-like Factor 4 activates HBG gene expression in primary erythroid cells. Br. J. Haematol. 154 248-59 PubMed GONUTS page
  5. 5.0 5.1 5.2 Uchida, C et al. (2002) The role of Sp1 and AP-2 in basal and protein kinase A--induced expression of mitochondrial serine:pyruvate aminotransferase in hepatocytes. J. Biol. Chem. 277 39082-92 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 Kitabayashi, I et al. (2001) Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. EMBO J. 20 7184-96 PubMed GONUTS page
  7. Yuan, W et al. (1996) Human p300 protein is a coactivator for the transcription factor MyoD. J. Biol. Chem. 271 9009-13 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 Kung, AL et al. (2004) Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway. Cancer Cell 6 33-43 PubMed GONUTS page
  9. 9.0 9.1 Bradney, C et al. (2003) Regulation of E2A activities by histone acetyltransferases in B lymphocyte development. J. Biol. Chem. 278 2370-6 PubMed GONUTS page
  10. Pradhan, A & Liu, Y (2004) The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies. Neurosci. Lett. 370 191-5 PubMed GONUTS page
  11. Barbacci, E et al. (2004) HNF1beta/TCF2 mutations impair transactivation potential through altered co-regulator recruitment. Hum. Mol. Genet. 13 3139-49 PubMed GONUTS page
  12. 12.0 12.1 12.2 Iioka, T et al. (2003) P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain. J. Bone Miner. Res. 18 1419-29 PubMed GONUTS page
  13. Yang, XJ et al. (1996) A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 319-24 PubMed GONUTS page
  14. Curtis, AM et al. (2004) Histone acetyltransferase-dependent chromatin remodeling and the vascular clock. J. Biol. Chem. 279 7091-7 PubMed GONUTS page
  15. Bragança, J et al. (2003) Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2. J. Biol. Chem. 278 16021-9 PubMed GONUTS page
  16. Lill, NL et al. (1997) Binding and modulation of p53 by p300/CBP coactivators. Nature 387 823-7 PubMed GONUTS page
  17. Chen, LF et al. (2005) NF-kappaB RelA phosphorylation regulates RelA acetylation. Mol. Cell. Biol. 25 7966-75 PubMed GONUTS page
  18. Chen, LF et al. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J. 21 6539-48 PubMed GONUTS page
  19. 19.0 19.1 Billon, N et al. (1999) Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation. Oncogene 18 2872-82 PubMed GONUTS page
  20. von Mikecz, A et al. (2000) CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus. J. Cell Biol. 150 265-73 PubMed GONUTS page
  21. 21.0 21.1 21.2 21.3 Villavicencio, EH et al. (2000) The sonic hedgehog-patched-gli pathway in human development and disease. Am. J. Hum. Genet. 67 1047-54 PubMed GONUTS page
  22. Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page
  23. 23.0 23.1 23.2 23.3 23.4 Kwok, RP et al. (1994) Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370 223-6 PubMed GONUTS page