SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P17676

- CEBPB_HUMAN

UniProt

P17676 - CEBPB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

CCAAT/enhancer-binding protein beta

Gene
CEBPB, TCF5, PP9092
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Plays an important role in adipose tissue differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG) as well as other adipogenesis key player genes.2 Publications
Isoform 3: acts as a dominant negative through heterodimerization with isoform 2.2 Publications

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. protein binding Source: UniProtKB
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  4. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. sequence-specific DNA binding Source: Ensembl
  6. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. acute-phase response Source: ProtInc
  2. brown fat cell differentiation Source: Ensembl
  3. cellular response to amino acid stimulus Source: Ensembl
  4. embryonic placenta development Source: Ensembl
  5. immune response Source: ProtInc
  6. inflammatory response Source: ProtInc
  7. mammary gland epithelial cell differentiation Source: Ensembl
  8. mammary gland epithelial cell proliferation Source: Ensembl
  9. negative regulation of neuron apoptotic process Source: Ensembl
  10. negative regulation of transcription, DNA-templated Source: Ensembl
  11. neuron differentiation Source: Ensembl
  12. positive regulation of fat cell differentiation Source: UniProtKB
  13. positive regulation of osteoblast differentiation Source: Ensembl
  14. regulation of interleukin-6 biosynthetic process Source: Ensembl
  15. regulation of transcription, DNA-templated Source: UniProtKB
  16. regulation of transcription involved in cell fate commitment Source: UniProtKB
  17. response to endoplasmic reticulum stress Source: UniProtKB
  18. response to lipopolysaccharide Source: Ensembl
  19. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP17676.

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein beta
Short name:
C/EBP beta
Alternative name(s):
Liver activator protein
Short name:
LAP
Liver-enriched inhibitory protein
Short name:
LIP
Nuclear factor NF-IL6
Transcription factor 5
Short name:
TCF-5
Gene namesi
Name:CEBPB
Synonyms:TCF5
ORF Names:PP9092
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:1834. CEBPB.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nuclear chromatin Source: Ensembl
  3. nuclear matrix Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345CCAAT/enhancer-binding protein betaPRO_0000076617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki174 – 174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei235 – 2351Phosphothreonine; by RPS6KA11 Publication

Post-translational modificationi

Sumoylated by polymeric chains of SUMO2 or SUMO3.1 Publication
Phosphorylated at Thr-235 by RPS6KA1.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17676.
PaxDbiP17676.
PeptideAtlasiP17676.
PRIDEiP17676.

PTM databases

PhosphoSiteiP17676.

Expressioni

Tissue specificityi

Expressed at low levels in the lung, kidney and spleen.

Inductioni

By ER stress.1 Publication

Gene expression databases

ArrayExpressiP17676.
BgeeiP17676.
CleanExiHS_CEBPB.
GenevestigatoriP17676.

Organism-specific databases

HPAiCAB004213.

Interactioni

Subunit structurei

Binds DNA as a dimer and can form stable heterodimers with CEBPA, CEBPD and CEBPG. Isoform 2 and isoform 3 also form heterodimers. Interacts with TRIM28 and PTGES2. Interacts with PRDM16. Interacts with CCDC85B. Forms a complex with THOC5. Interacts with ZNF638; this interaction increases transcriptional activation. Interacts with CIDEA and CIDEC; these interactions increase transcriptional activation of a subset of CEBPB downstream target genes. Interacts with DDIT3/CHOP.Interacts with EP300; recruits EP300 to chromatin. Interacts with RORA; the interaction disrupts interaction with EP300.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CARM1Q86X552EBI-969696,EBI-2339854
E2P031202EBI-969696,EBI-1779322From a different organism.
E2P031223EBI-969696,EBI-7028618From a different organism.
E2P064224EBI-969696,EBI-7136851From a different organism.
E2P067904EBI-969696,EBI-7010629From a different organism.
TP53P046374EBI-969696,EBI-366083

Protein-protein interaction databases

BioGridi107480. 67 interactions.
DIPiDIP-35345N.
IntActiP17676. 9 interactions.
MINTiMINT-230873.
STRINGi9606.ENSP00000305422.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi269 – 2713
Helixi272 – 32857
Turni329 – 3313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTWX-ray1.85A/B259-336[»]
1GU4X-ray1.80A/B259-336[»]
1GU5X-ray2.10A/B259-336[»]
1H88X-ray2.80A/B259-336[»]
1H89X-ray2.45A/B273-336[»]
1H8AX-ray2.23A/B259-336[»]
1HJBX-ray3.00A/B/D/E259-345[»]
1IO4X-ray3.00A/B259-336[»]
2E42X-ray1.80A/B259-336[»]
2E43X-ray2.10A/B259-336[»]
ProteinModelPortaliP17676.
SMRiP17676. Positions 268-334.

Miscellaneous databases

EvolutionaryTraceiP17676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 33464bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2424Required for Lys-174 sumoylationAdd
BLAST
Regioni275 – 29521Basic motif By similarityAdd
BLAST
Regioni297 – 3048Leucine-zipper By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi116 – 12499aaTAD

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi162 – 1709Poly-Pro

Domaini

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

Sequence similaritiesi

Belongs to the bZIP family. C/EBP subfamily.

Phylogenomic databases

eggNOGiNOG299311.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP17676.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiP17676.
TreeFamiTF105008.

Family and domain databases

InterProiIPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P17676-1) [UniParc]FASTAAdd to Basket

Also known as: C/EBPbeta-FL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MQRLVAWDPA CLPLPPPPPA FKSMEVANFY YEADCLAAAY GGKAAPAAPP    50
AARPGPRPPA GELGSIGDHE RAIDFSPYLE PLGAPQAPAP ATATDTFEAA 100
PPAPAPAPAS SGQHHDFLSD LFSDDYGGKN CKKPAEYGYV SLGRLGAAKG 150
ALHPGCFAPL HPPPPPPPPP AELKAEPGFE PADCKRKEEA GAPGGGAGMA 200
AGFPYALRAY LGYQAVPSGS SGSLSTSSSS SPPGTPSPAD AKAPPTACYA 250
GAAPAPSQVK SKAKKTVDKH SDEYKIRRER NNIAVRKSRD KAKMRNLETQ 300
HKVLELTAEN ERLQKKVEQL SRELSTLRNL FKQLPEPLLA SSGHC 345
Length:345
Mass (Da):36,106
Last modified:August 22, 2003 - v2
Checksum:i9B725BD6CCAA771D
GO
Isoform 2 (identifier: P17676-2) [UniParc]FASTAAdd to Basket

Also known as: C/EBPbeta-LAP

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Show »
Length:322
Mass (Da):33,592
Checksum:i842B381C36DFA8CE
GO
Isoform 3 (identifier: P17676-3) [UniParc]FASTAAdd to Basket

Also known as: C/EBPbeta-LIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-198: Missing.

Show »
Length:147
Mass (Da):15,938
Checksum:i3D75D9D752E47B88
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti195 – 1951G → S.1 Publication
Corresponds to variant rs4253440 [ dbSNP | Ensembl ].
VAR_016300

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 198198Missing in isoform 3. VSP_053313Add
BLAST
Alternative sequencei1 – 2323Missing in isoform 2. VSP_053314Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411A → P no nucleotide entry 1 Publication
Sequence conflicti253 – 2531A → G in CAA36794. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52560 Genomic DNA. Translation: CAA36794.1.
AF289608 mRNA. Translation: AAL55792.1.
AY193834 Genomic DNA. Translation: AAN86350.1.
AK291536 mRNA. Translation: BAF84225.1.
AL161937 Genomic DNA. Translation: CAC14276.1.
CH471077 Genomic DNA. Translation: EAW75629.1.
BC007538 mRNA. Translation: AAH07538.1.
BC021931 mRNA. Translation: AAH21931.1.
CCDSiCCDS13429.1. [P17676-1]
PIRiS12788.
S66246.
RefSeqiNP_001272807.1. NM_001285878.1. [P17676-2]
NP_001272808.1. NM_001285879.1. [P17676-3]
NP_005185.2. NM_005194.3. [P17676-1]
UniGeneiHs.517106.
Hs.719041.
Hs.720603.

Genome annotation databases

EnsembliENST00000303004; ENSP00000305422; ENSG00000172216. [P17676-1]
GeneIDi1051.
KEGGihsa:1051.
UCSCiuc002xvi.2. human. [P17676-1]

Polymorphism databases

DMDMi34223718.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52560 Genomic DNA. Translation: CAA36794.1 .
AF289608 mRNA. Translation: AAL55792.1 .
AY193834 Genomic DNA. Translation: AAN86350.1 .
AK291536 mRNA. Translation: BAF84225.1 .
AL161937 Genomic DNA. Translation: CAC14276.1 .
CH471077 Genomic DNA. Translation: EAW75629.1 .
BC007538 mRNA. Translation: AAH07538.1 .
BC021931 mRNA. Translation: AAH21931.1 .
CCDSi CCDS13429.1. [P17676-1 ]
PIRi S12788.
S66246.
RefSeqi NP_001272807.1. NM_001285878.1. [P17676-2 ]
NP_001272808.1. NM_001285879.1. [P17676-3 ]
NP_005185.2. NM_005194.3. [P17676-1 ]
UniGenei Hs.517106.
Hs.719041.
Hs.720603.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GTW X-ray 1.85 A/B 259-336 [» ]
1GU4 X-ray 1.80 A/B 259-336 [» ]
1GU5 X-ray 2.10 A/B 259-336 [» ]
1H88 X-ray 2.80 A/B 259-336 [» ]
1H89 X-ray 2.45 A/B 273-336 [» ]
1H8A X-ray 2.23 A/B 259-336 [» ]
1HJB X-ray 3.00 A/B/D/E 259-345 [» ]
1IO4 X-ray 3.00 A/B 259-336 [» ]
2E42 X-ray 1.80 A/B 259-336 [» ]
2E43 X-ray 2.10 A/B 259-336 [» ]
ProteinModelPortali P17676.
SMRi P17676. Positions 268-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107480. 67 interactions.
DIPi DIP-35345N.
IntActi P17676. 9 interactions.
MINTi MINT-230873.
STRINGi 9606.ENSP00000305422.

PTM databases

PhosphoSitei P17676.

Polymorphism databases

DMDMi 34223718.

Proteomic databases

MaxQBi P17676.
PaxDbi P17676.
PeptideAtlasi P17676.
PRIDEi P17676.

Protocols and materials databases

DNASUi 1051.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303004 ; ENSP00000305422 ; ENSG00000172216 . [P17676-1 ]
GeneIDi 1051.
KEGGi hsa:1051.
UCSCi uc002xvi.2. human. [P17676-1 ]

Organism-specific databases

CTDi 1051.
GeneCardsi GC20P048807.
H-InvDB HIX0174729.
HGNCi HGNC:1834. CEBPB.
HPAi CAB004213.
MIMi 189965. gene.
neXtProti NX_P17676.
PharmGKBi PA26377.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG299311.
HOGENOMi HOG000013112.
HOVERGENi HBG050879.
InParanoidi P17676.
KOi K10048.
OMAi CKKPAEY.
OrthoDBi EOG7R56TQ.
PhylomeDBi P17676.
TreeFami TF105008.

Enzyme and pathway databases

Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki P17676.

Miscellaneous databases

EvolutionaryTracei P17676.
GeneWikii CEBPB.
GenomeRNAii 1051.
NextBioi 4401.
PROi P17676.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17676.
Bgeei P17676.
CleanExi HS_CEBPB.
Genevestigatori P17676.

Family and domain databases

InterProi IPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view ]
Pfami PF07716. bZIP_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A nuclear factor for IL-6 expression (NF-IL6) is a member of a C/EBP family."
    Akira S., Isshiki H., Sugita T., Tanabe O., Kinoshita S., Nishio Y., Nakajima T., Hirano T., Kishimoto T.
    EMBO J. 9:1897-1906(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. SeattleSNPs variation discovery resource
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-195.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle and Skin.
  8. "Identification of a transcriptional regulatory factor for human aromatase cytochrome P450 gene expression as nuclear factor interleukin-6 (NF-IL6), a member of the CCAAT/enhancer-binding protein family."
    Toda K., Akira S., Kishimoto T., Sasaki H., Hashimoto K., Yamamoto Y., Sagara Y., Shizuta Y.
    Eur. J. Biochem. 231:292-299(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-323 (ISOFORMS 1/2/3).
  9. "C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival."
    Buck M., Poli V., Hunter T., Chojkier M.
    Mol. Cell 8:807-816(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-235.
  10. "Dynamic regulation of cyclooxygenase-2 promoter activity by isoforms of CCAAT/enhancer-binding proteins."
    Zhu Y., Saunders M.A., Yeh H., Deng W.G., Wu K.K.
    J. Biol. Chem. 277:6923-6928(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), DNA-BINDING.
  11. "Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3."
    Eaton E.M., Sealy L.
    J. Biol. Chem. 278:33416-33421(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-174.
  12. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
    Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
    Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma."
    Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.
    J. Biol. Chem. 285:35330-35339(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDIT3, SUBCELLULAR LOCATION, INDUCTION.
  15. "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta."
    Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M., Kimura K., Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S., Ogata K.
    Cell 104:755-767(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 259-336 IN COMPLEX WITH RUNX1; CBFB AND DNA.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 259-345 IN COMPLEX WITH MOUSE MYB.

Entry informationi

Entry nameiCEBPB_HUMAN
AccessioniPrimary (citable) accession number: P17676
Secondary accession number(s): A8K671, Q96IH2, Q9H4Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 22, 2003
Last modified: September 3, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi