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P17676 (CEBPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CEBPB
Synonyms:TCF5
ORF Names:PP9092
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.14

Isoform 3:acts as a dominant negative through heterodimerization with isoform 2. Ref.10 Ref.14

Subunit structure

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. Ref.14

Subcellular location

Nucleus Ref.14.

Tissue specificity

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

Induction

By ER stress. Ref.14

Domain

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.12

Post-translational modification

Sumoylated by polymeric chains of SUMO2 or SUMO3. Ref.11

Phosphorylated at Thr-235 by RPS6KA1. Ref.9

Sequence similarities

Belongs to the bZIP family. C/EBP subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Traceable author statement Ref.1. Source: ProtInc

brown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement Ref.1. Source: ProtInc

inflammatory response

Traceable author statement Ref.1. Source: ProtInc

mammary gland epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of interleukin-6 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from direct assay Ref.14. Source: UniProtKB

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 10821850. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 10821850. Source: ProtInc

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Non-traceable author statement PubMed 10821850. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P17676-1)

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.
Isoform 2 (identifier: P17676-2)

Also known as: C/EBPbeta-LAP;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Isoform 3 (identifier: P17676-3)

Also known as: C/EBPbeta-LIP;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345CCAAT/enhancer-binding protein beta
PRO_0000076617

Regions

Domain271 – 33464bZIP
Region1 – 2424Required for Lys-174 sumoylation
Region275 – 29521Basic motif By similarity
Region297 – 3048Leucine-zipper By similarity
Motif116 – 12499aaTAD
Compositional bias162 – 1709Poly-Pro

Amino acid modifications

Modified residue2351Phosphothreonine; by RPS6KA1 Ref.9
Cross-link174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Alternative sequence1 – 198198Missing in isoform 3.
VSP_053313
Alternative sequence1 – 2323Missing in isoform 2.
VSP_053314
Natural variant1951G → S. Ref.3
Corresponds to variant rs4253440 [ dbSNP | Ensembl ].
VAR_016300

Experimental info

Sequence conflict2411A → P no nucleotide entry Ref.8
Sequence conflict2531A → G in CAA36794. Ref.1

Secondary structure

..... 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (C/EBPbeta-FL) [UniParc].

Last modified August 22, 2003. Version 2.
Checksum: 9B725BD6CCAA771D

FASTA34536,106
        10         20         30         40         50         60 
MQRLVAWDPA CLPLPPPPPA FKSMEVANFY YEADCLAAAY GGKAAPAAPP AARPGPRPPA 

        70         80         90        100        110        120 
GELGSIGDHE RAIDFSPYLE PLGAPQAPAP ATATDTFEAA PPAPAPAPAS SGQHHDFLSD 

       130        140        150        160        170        180 
LFSDDYGGKN CKKPAEYGYV SLGRLGAAKG ALHPGCFAPL HPPPPPPPPP AELKAEPGFE 

       190        200        210        220        230        240 
PADCKRKEEA GAPGGGAGMA AGFPYALRAY LGYQAVPSGS SGSLSTSSSS SPPGTPSPAD 

       250        260        270        280        290        300 
AKAPPTACYA GAAPAPSQVK SKAKKTVDKH SDEYKIRRER NNIAVRKSRD KAKMRNLETQ 

       310        320        330        340 
HKVLELTAEN ERLQKKVEQL SRELSTLRNL FKQLPEPLLA SSGHC 

« Hide

Isoform 2 (C/EBPbeta-LAP) [UniParc].

Checksum: 842B381C36DFA8CE
Show »

FASTA32233,592
Isoform 3 (C/EBPbeta-LIP) [UniParc].

Checksum: 3D75D9D752E47B88
Show »

FASTA14715,938

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a promoter."
Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T., Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T., Yamamoto M., Ishii S., Ogata K.
Cell 108:57-70(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 259-345 IN COMPLEX WITH MOUSE MYB.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS12788.
S66246.
RefSeqNP_001272807.1. NM_001285878.1.
NP_001272808.1. NM_001285879.1.
NP_005185.2. NM_005194.3.
UniGeneHs.517106.
Hs.719041.
Hs.720603.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP17676.
SMRP17676. Positions 268-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107480. 67 interactions.
DIPDIP-35345N.
IntActP17676. 8 interactions.
MINTMINT-230873.
STRING9606.ENSP00000305422.

PTM databases

PhosphoSiteP17676.

Polymorphism databases

DMDM34223718.

Proteomic databases

PaxDbP17676.
PeptideAtlasP17676.
PRIDEP17676.

Protocols and materials databases

DNASU1051.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303004; ENSP00000305422; ENSG00000172216. [P17676-1]
GeneID1051.
KEGGhsa:1051.
UCSCuc002xvi.2. human. [P17676-1]

Organism-specific databases

CTD1051.
GeneCardsGC20P048807.
H-InvDBHIX0174729.
HGNCHGNC:1834. CEBPB.
HPACAB004213.
MIM189965. gene.
neXtProtNX_P17676.
PharmGKBPA26377.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299311.
HOGENOMHOG000013112.
HOVERGENHBG050879.
InParanoidP17676.
KOK10048.
OMACKKPAEY.
OrthoDBEOG7R56TQ.
PhylomeDBP17676.
TreeFamTF105008.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_120956. Cellular responses to stress.
SignaLinkP17676.

Gene expression databases

ArrayExpressP17676.
BgeeP17676.
CleanExHS_CEBPB.
GenevestigatorP17676.

Family and domain databases

InterProIPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view]
PfamPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17676.
GeneWikiCEBPB.
GenomeRNAi1051.
NextBio4401.
PROP17676.
SOURCESearch...

Entry information

Entry nameCEBPB_HUMAN
AccessionPrimary (citable) accession number: P17676
Secondary accession number(s): A8K671, Q96IH2, Q9H4Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 22, 2003
Last modified: April 16, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM