Cebpa

Functionⁱ

Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:8367486, PubMed:11672531, PubMed:16735515, PubMed:20176812). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (By similarity). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:11672531). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:11672531). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters (PubMed:11672531). Proliferation arrest also depends on a functional binding to SWI/SNF complex (By similarity). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity).By similarity4 Publications

Isoform 3: Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation.By similarity1 Publication

Isoform 4: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation.By similarity

Miscellaneous

The V296A substitution has little effect on the binding of CEBPA to its consensus site (5'-GCAAT-3'), while greatly increasing affinity for cAMP response element (CRE) sites (5'-GTCAT-3').1 Publication

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
DNA bindingⁱ	285 – 300	1 PublicationAdd BLAST		16

GO - Molecular functionⁱ

DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 1377818
- 8367486
histone deacetylase binding
Source: RGD
Inferred from physical interactionⁱ
- 23639777
HMG box domain binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16582099
protein-containing complex binding
Source: RGD
Inferred from direct assayⁱ
- 16172914
protein domain specific binding
Source: RGD
Inferred from physical interactionⁱ
- 11356826
protein heterodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 1377818
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 2171780
proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific
Source: NTNU_SB
Inferred from direct assayⁱ
- 8572170
RNA polymerase II proximal promoter sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 8572170
RNA polymerase I regulatory region DNA binding Source: UniProtKB
sequence-specific DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20176812
transcription coactivator activity Source: UniProtKB
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20176812

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

acute-phase response
Source: RGD
Inferred from expression patternⁱ
- 16172914
animal organ regeneration
Source: RGD
Inferred from expression patternⁱ
- 17047332
cell differentiation
Source: RGD
Inferred from expression patternⁱ
- 16735515
cellular response to drug
Source: RGD
Inferred from expression patternⁱ
- 1377818
fat cell differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 11672531
glucose homeostasis Source: UniProtKB
granulocyte differentiation Source: UniProtKB
lipid homeostasis Source: UniProtKB
liver development
Source: RGD
Inferred from expression patternⁱ
- 16172914
lung development Source: UniProtKB
memory
Source: RGD
Inferred from expression patternⁱ
- 17512093
negative regulation of cell proliferation
Source: UniProtKB
Inferred from direct assayⁱ
- 11672531
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 11672531
osteoblast development
Source: RGD
Inferred from expression patternⁱ
- 1377818
positive regulation of fat cell differentiation
Source: RGD
Inferred from mutant phenotypeⁱ
- 11731483
positive regulation of transcription by RNA polymerase II
Source: NTNU_SB
Inferred from direct assayⁱ
- 8572170
regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 20176812
response to dexamethasone
Source: RGD
Inferred from expression patternⁱ
- 12753899
response to nutrient
Source: RGD
Inferred from expression patternⁱ
- 16856317
response to phenylpropanoid
Source: RGD
Inferred from expression patternⁱ
- 23238999
response to vitamin B2
Source: RGD
Inferred from expression patternⁱ
- 16856317
transcription by RNA polymerase I Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, Developmental protein, DNA-binding
Biological process	Transcription, Transcription regulation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: CCAAT/enhancer-binding protein alphaImported Short name: C/EBP alpha
Gene namesⁱ	Name:CebpaImported
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	2326 Cebpa

RGDⁱ

2326 Cebpa

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	159	K → A or R: Not sumoylated. No effect of sumoylation on cell cycle inhibition. 1 Publication	1
Mutagenesisⁱ	285	Y → A: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with R-293. 1 Publication	1
Mutagenesisⁱ	285	Y → A: Increases interaction with TFDP1 and TFDP2, reduces DNA-binding, transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction. 2 Publications	1
Mutagenesisⁱ	287	V → A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-290. 1 Publication	1
Mutagenesisⁱ	289	R → A: Loss of DNA-binding and transcription factor activity. 1 Publication	1
Mutagenesisⁱ	290	E → A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-287. 1 Publication	1
Mutagenesisⁱ	293	N → R: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with A-285. 1 Publication	1
Mutagenesisⁱ	294	I → A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-297. 2 Publications	1
Mutagenesisⁱ	296	V → A: No effect on DNA-binding and transcription factor activity, but modified sequence specificity. 1 Publication	1
Mutagenesisⁱ	297	R → A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-294. 2 Publications	1
Mutagenesisⁱ	299	S → D: Isoform-4: Stimulates nucleolar retention of isoform-4. No effect on interaction with NPM1, TAF1A and UBTF. 1 Publication	1
Mutagenesisⁱ	301	D → A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-304. 2 Publications	1
Mutagenesisⁱ	304	K → A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-301. 2 Publications	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076615	1 – 358	CCAAT/enhancer-binding protein alphaAdd BLAST		358

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	159	N6-acetyllysine; alternateBy similarity	1
Cross-linkⁱ	159	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linkⁱ	159	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	193	PhosphoserineBy similarity	1
Modified residueⁱ	222	Phosphothreonine; by GSK3By similarity	1
Modified residueⁱ	226	Phosphothreonine; by GSK3By similarity	1
Modified residueⁱ	230	Phosphoserine; by GSK3By similarity	1

Post-translational modificationⁱ

Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2.1 Publication

Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation. Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 are phosphorylated only during feeding but not during fasting. Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters.By similarity

Ubiquitinated by COP1 upon interaction with TRIB1.By similarity

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P05554
PRIDEⁱ	P05554

PTM databases

iPTMnetⁱ	P05554
PhosphoSitePlusⁱ	P05554

Expressionⁱ

Tissue specificityⁱ

Isoform 2 and isoform 3 are expressed in liver (at protein level).1 Publication

Developmental stageⁱ

Isoform 2 and isoform 3 are not expressed at 1 day before birth, relative concentration of both isoforms increases with the age of the animal, reaching maximal levels in the adulthood.1 Publication

Gene expression databases

Genevisibleⁱ	P05554 RN

Genevisibleⁱ

P05554 RN

Interactionⁱ

Subunit structureⁱ

Binds DNA as a homodimer and as a heterodimer (PubMed:1884998, PubMed:8367486, PubMed:12578822). Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (PubMed:1884998, PubMed:1377818). Can form stable homodimers (also isoform 2 and isoform 3 dimers) and heterodimers with CEBPB (with isoform 2 and isoform 3) and CEBPG (PubMed:1377818, PubMed:8367486). Interacts with PRDM16 (By similarity). Interacts with UBN1 (By similarity). Interacts with ZNF638; this interaction increases transcriptional activation (By similarity). Interacts with the complex TFDP2:E2F1; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity). Interacts with RB1 (By similarity). Interacts (when phosphorylated at SER-193) with CDK2, CDK4, E2F4 and SMARCA2 (By similarity). Interacts with SREBPF1 (By similarity). Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (By similarity). Isoform 1 and Isoform 4 interact with TAF1A and UBTF (PubMed:20075868). Isoform 4 interacts with NPM1 (PubMed:20075868). Interacts (via recognition sequence) with TRIB1 (By similarity).By similarity5 Publications

GO - Molecular functionⁱ

histone deacetylase binding
Source: RGD
Inferred from physical interactionⁱ
- 23639777
HMG box domain binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16582099
protein domain specific binding
Source: RGD
Inferred from physical interactionⁱ
- 11356826
protein heterodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 1377818
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 2171780
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20176812

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	246437, 3 interactors
ComplexPortalⁱ	CPX-60 CHOP-C/EBPalpha complex CPX-64 C/EBPalpha complex
Database of interacting proteins More...DIPⁱ	DIP-28138N
IntActⁱ	P05554, 5 interactors
STRINGⁱ	10116.ENSRNOP00000063123

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Helixⁱ	282 – 338	Combined sources		57

Show more details

3D structure databases

ProteinModelPortalⁱ	P05554
SMRⁱ	P05554
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P05554

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	282 – 345	bZIPPROSITE-ProRule annotationAdd BLAST		64

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 70	Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiation1 PublicationAdd BLAST	70
Regionⁱ	54 – 72	Required for interaction with TRIB1By similarityAdd BLAST	19
Regionⁱ	126 – 200	Required to induce adipocyte differentiation1 PublicationAdd BLAST	75
Regionⁱ	180 – 194	Required to functionally cooperate with SREBF1 in promoter activationBy similarityAdd BLAST	15
Regionⁱ	240 – 358	Interaction with FOXO1By similarityAdd BLAST	119
Regionⁱ	286 – 313	Basic motifPROSITE-ProRule annotationAdd BLAST	28
Regionⁱ	317 – 345	Leucine-zipperPROSITE-ProRule annotationAdd BLAST	29

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	181 – 190	Poly-Pro		10
Compositional biasⁱ	262 – 272	Poly-GlyAdd BLAST		11

Domainⁱ

The recognition sequence (54-72) is required for interaction with TRIB1.By similarity

Sequence similaritiesⁱ

Belongs to the bZIP family. C/EBP subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG3119 Eukaryota ENOG410YJ8G LUCA
HOGENOMⁱ	HOG000013112
HOVERGENⁱ	HBG050879
InParanoidⁱ	P05554
KEGG Orthology (KO) More...KOⁱ	K09055
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G11FC
PhylomeDBⁱ	P05554
TreeFamⁱ	TF105008

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR016468 C/EBP_chordates
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07716 bZIP_2, 1 hit
PIRSFⁱ	PIRSF005879 CCAAT/enhancer-binding, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative initiation. Align Add to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: P05554-1) [UniParc]FASTA Add to basket

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

        10         20         30         40         50
MESADFYEAE PRPPMSSHLQ SPPHAPSNAA FGFPRGAGPA PPPAPPAAPE 
        60         70         80         90        100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAAGPAGG 
       110        120        130        140        150
GGDFDYPGAP AGPGGAVMSA GAHGPPPGYG CAAAGYLDGR LEPLYERVGA 
       160        170        180        190        200
PALRPLVIKQ EPREEDEAKQ LALAGLFPYQ PPPPPPPPHP HASPAHLAAP 
       210        220        230        240        250
HLQFQIAHCG QTTMHLQPGH PTPPPTPVPS PHPAPAMGAA GLPGPGGSLK 
       260        270        280        290        300
GLAGPHPDLR TGGGGGGGAG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR 
       310        320        330        340        350
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL 

VKAMGNCA

Length:358

Mass (Da):37,371

Last modified:February 1, 1996 - v3

Checksum:ⁱ4DA8F112F6EA95D0

GO

Isoform 2 (identifier: P05554-2) [UniParc]FASTA Add to basket

Also known as: CEBPalpha-p421 Publication

The sequence of this isoform differs from the canonical sequence as follows:
1-14: Missing.

« Hide

        10         20         30         40         50
MSSHLQSPPH APSNAAFGFP RGAGPAPPPA PPAAPEPLGG ICEHETSIDI 
        60         70         80         90        100
SAYIDPAAFN DEFLADLFQH SRQQEKAKAA AGPAGGGGDF DYPGAPAGPG 
       110        120        130        140        150
GAVMSAGAHG PPPGYGCAAA GYLDGRLEPL YERVGAPALR PLVIKQEPRE 
       160        170        180        190        200
EDEAKQLALA GLFPYQPPPP PPPPHPHASP AHLAAPHLQF QIAHCGQTTM 
       210        220        230        240        250
HLQPGHPTPP PTPVPSPHPA PAMGAAGLPG PGGSLKGLAG PHPDLRTGGG 
       260        270        280        290        300
GGGGAGAGKA KKSVDKNSNE YRVRRERNNI AVRKSRDKAK QRNVETQQKV 
       310        320        330        340 
LELTSDNDRL RKRVEQLSRE LDTLRGIFRQ LPESSLVKAM GNCA

Show »

Length:344

Mass (Da):35,750

Checksum:ⁱ530FA6D51C5E7BDA

GO

Isoform 3 (identifier: P05554-3) [UniParc]FASTA Add to basket

Also known as: C/EBPalpha-p301 Publication

The sequence of this isoform differs from the canonical sequence as follows:
1-117: Missing.

« Hide

        10         20         30         40         50
MSAGAHGPPP GYGCAAAGYL DGRLEPLYER VGAPALRPLV IKQEPREEDE 
        60         70         80         90        100
AKQLALAGLF PYQPPPPPPP PHPHASPAHL AAPHLQFQIA HCGQTTMHLQ 
       110        120        130        140        150
PGHPTPPPTP VPSPHPAPAM GAAGLPGPGG SLKGLAGPHP DLRTGGGGGG 
       160        170        180        190        200
GAGAGKAKKS VDKNSNEYRV RRERNNIAVR KSRDKAKQRN VETQQKVLEL 
       210        220        230        240 
TSDNDRLRKR VEQLSRELDT LRGIFRQLPE SSLVKAMGNC A

Show »

Length:241

Mass (Da):25,526

Checksum:ⁱ16713D706888AA35

GO

Isoform 4 (identifier: P05554-4) [UniParc]FASTA Add to basket

Also known as: extended-C/EBPalpha1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MRGRGRVGVLGGRRRQRRHAQAGGRRGSPCRENSNSPM

« Hide

        10         20         30         40         50
MRGRGRVGVL GGRRRQRRHA QAGGRRGSPC RENSNSPMES ADFYEAEPRP 
        60         70         80         90        100
PMSSHLQSPP HAPSNAAFGF PRGAGPAPPP APPAAPEPLG GICEHETSID 
       110        120        130        140        150
ISAYIDPAAF NDEFLADLFQ HSRQQEKAKA AAGPAGGGGD FDYPGAPAGP 
       160        170        180        190        200
GGAVMSAGAH GPPPGYGCAA AGYLDGRLEP LYERVGAPAL RPLVIKQEPR 
       210        220        230        240        250
EEDEAKQLAL AGLFPYQPPP PPPPPHPHAS PAHLAAPHLQ FQIAHCGQTT 
       260        270        280        290        300
MHLQPGHPTP PPTPVPSPHP APAMGAAGLP GPGGSLKGLA GPHPDLRTGG 
       310        320        330        340        350
GGGGGAGAGK AKKSVDKNSN EYRVRRERNN IAVRKSRDKA KQRNVETQQK 
       360        370        380        390 
VLELTSDNDR LRKRVEQLSR ELDTLRGIFR QLPESSLVKA MGNCA

Note: Mutagenesis in position: 14: RRQR -> AAAA abolishes nucleolar localization and prevents induction of 45S pre-RNA.1 Publication

Show »

Length:395

Mass (Da):41,440

Checksum:ⁱ01D1DA74BD4A48C8

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0H2UI22	A0A0H2UI22_RAT		CCAAT/enhancer-binding protein alph... CCAAT/enhancer-binding protein alpha	Cebpa	395	Annotation score:

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_057551	1 – 117	Missing in isoform 3. 1 PublicationAdd BLAST	117
Alternative sequenceⁱVSP_057552	1 – 14	Missing in isoform 2. 1 PublicationAdd BLAST	14
Alternative sequenceⁱVSP_057609	1	M → MRGRGRVGVLGGRRRQRRHA QAGGRRGSPCRENSNSPM in isoform 4.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X12752 Genomic DNA Translation: CAA31242.1 AC109741 Genomic DNA No translation available.
PIRⁱ	S06890 A54265
NCBI Reference Sequences More...RefSeqⁱ	NP_001274506.1, NM_001287577.1 [P05554-4] NP_001274507.1, NM_001287578.1 [P05554-2] NP_001274508.1, NM_001287579.1 [P05554-3] NP_036656.1, NM_012524.3 [P05554-1]

Genome annotation databases

GeneIDⁱ	24252
KEGGⁱ	rno:24252
UCSC genome browser More...UCSCⁱ	RGD:2326 rat [P05554-1]

Keywords - Coding sequence diversityⁱ

Alternative initiation

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P05554	CCAAT/enhancer-binding protein alpha		RAT		395	UniRef100_P05554
Isoform 3 of CCAAT/enhancer-binding protein alpha		RAT		241
C/EBP alpha (Fragment)		RAT		35
Isoform 2 of CCAAT/enhancer-binding protein alpha		RAT		344

Protein	Similar proteins		Species	Score	Length	Source
P05554	CCAAT/enhancer-binding protein alpha		MOUSE		359	UniRef90_P53566
CCAAT/enhancer-binding protein alpha		BOVIN		353
Isoform 4 of CCAAT/enhancer-binding protein alpha		RAT		395
CCAAT/enhancer-binding protein alpha		MESAU		369
CEBPA isoform 1		PANTR		362
+72

Protein	Similar proteins		Species	Score	Length	Source
P05554	CCAAT/enhancer-binding protein alpha		MOUSE		359	UniRef50_P53566
CCAAT/enhancer-binding protein alpha		BOVIN		353
Isoform 4 of CCAAT/enhancer-binding protein alpha		RAT		395
CCAAT/enhancer-binding protein alpha		MESAU		369
CEBPA isoform 1		PANTR		362
+89

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X12752 Genomic DNA Translation: CAA31242.1 AC109741 Genomic DNA No translation available.
PIRⁱ	S06890 A54265
RefSeqⁱ	NP_001274506.1, NM_001287577.1 [P05554-4] NP_001274507.1, NM_001287578.1 [P05554-2] NP_001274508.1, NM_001287579.1 [P05554-3] NP_036656.1, NM_012524.3 [P05554-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1NWQ	X-ray	2.80	A/C	281-340	[»]
ProteinModelPortalⁱ	P05554
SMRⁱ	P05554
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	246437, 3 interactors
ComplexPortalⁱ	CPX-60 CHOP-C/EBPalpha complex CPX-64 C/EBPalpha complex
DIPⁱ	DIP-28138N
IntActⁱ	P05554, 5 interactors
STRINGⁱ	10116.ENSRNOP00000063123

PTM databases

iPTMnetⁱ	P05554
PhosphoSitePlusⁱ	P05554

Proteomic databases

PaxDbⁱ	P05554
PRIDEⁱ	P05554

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	24252
KEGGⁱ	rno:24252
UCSCⁱ	RGD:2326 rat [P05554-1]

Organism-specific databases

CTDⁱ	1050
RGDⁱ	2326 Cebpa

Phylogenomic databases

eggNOGⁱ	KOG3119 Eukaryota ENOG410YJ8G LUCA
HOGENOMⁱ	HOG000013112
HOVERGENⁱ	HBG050879
InParanoidⁱ	P05554
KOⁱ	K09055
OrthoDBⁱ	EOG091G11FC
PhylomeDBⁱ	P05554
TreeFamⁱ	TF105008

Miscellaneous databases

EvolutionaryTraceⁱ	P05554
Protein Ontology More...PROⁱ	PR:P05554

Gene expression databases

Genevisibleⁱ	P05554 RN

Genevisibleⁱ

P05554 RN

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR016468 C/EBP_chordates
Pfamⁱ	View protein in Pfam PF07716 bZIP_2, 1 hit
PIRSFⁱ	PIRSF005879 CCAAT/enhancer-binding, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CEBPA_RAT
Accessionⁱ	P05554Primary (citable) accession number: P05554
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
	Last sequence update:	February 1, 1996
	Last modified:	November 7, 2018
	This is version 156 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P05554 (CEBPA_RAT)

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CCAAT/enhancer-binding protein alpha

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ