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Protein

CCAAT/enhancer-binding protein gamma

Gene

CEBPG

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

Functioni

Transcription factor that binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene. Might change the DNA-binding specificity of other transcription factors and recruit them to unusual DNA sites.

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: Ensembl
  • protein heterodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein gamma
Short name:
C/EBP gamma
Gene namesi
Name:CEBPG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1837. CEBPG.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26380.

Polymorphism and mutation databases

BioMutaiCEBPG.
DMDMi1705750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 150150CCAAT/enhancer-binding protein gammaPRO_0000076628Add
BLAST

Proteomic databases

MaxQBiP53567.
PaxDbiP53567.
PRIDEiP53567.

PTM databases

PhosphoSiteiP53567.

Expressioni

Gene expression databases

BgeeiP53567.
CleanExiHS_CEBPG.
GenevisibleiP53567. HS.

Organism-specific databases

HPAiHPA012024.

Interactioni

Subunit structurei

Binds DNA as a dimer and can form stable heterodimers with C/EBP alpha and beta and with Fos protein. Interacts with ZNF638; this interaction increases transcriptional activation (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ATF4P188483EBI-740209,EBI-492498
ATF4Q96AQ33EBI-740209,EBI-740263
DDIT3P35638-23EBI-740209,EBI-10173632

Protein-protein interaction databases

BioGridi107483. 22 interactions.
IntActiP53567. 6 interactions.
MINTiMINT-1445645.
STRINGi9606.ENSP00000284000.

Structurei

3D structure databases

ProteinModelPortaliP53567.
SMRiP53567. Positions 62-122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 12564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 9328Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni97 – 11822Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. C/EBP subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG281019.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000057291.
HOVERGENiHBG050880.
InParanoidiP53567.
KOiK10049.
OMAiADNVQPS.
OrthoDBiEOG7R56TQ.
PhylomeDBiP53567.
TreeFamiTF105009.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKISQQNST PGVNGISVIH TQAHASGLQQ VPQLVPAGPG GGGKAVAPSK
60 70 80 90 100
QSKKSSPMDR NSDEYRQRRE RNNMAVKKSR LKSKQKAQDT LQRVNQLKEE
110 120 130 140 150
NERLEAKIKL LTKELSVLKD LFLEHAHNLA DNVQSISTEN TTADGDNAGQ
Length:150
Mass (Da):16,408
Last modified:October 1, 1996 - v1
Checksum:i630D1C1F92A00186
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20240 mRNA. Translation: AAC50201.1.
AK313634 mRNA. Translation: BAG36393.1.
BT019819 mRNA. Translation: AAV38622.1.
BT019820 mRNA. Translation: AAV38623.1.
BC007582 mRNA. Translation: AAH07582.1.
BC013128 mRNA. Translation: AAH13128.1.
CCDSiCCDS12432.1.
PIRiJC4243.
RefSeqiNP_001239225.1. NM_001252296.1.
NP_001797.1. NM_001806.3.
UniGeneiHs.429666.

Genome annotation databases

EnsembliENST00000284000; ENSP00000284000; ENSG00000153879.
ENST00000585933; ENSP00000466022; ENSG00000153879.
GeneIDi1054.
KEGGihsa:1054.
UCSCiuc002nup.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20240 mRNA. Translation: AAC50201.1.
AK313634 mRNA. Translation: BAG36393.1.
BT019819 mRNA. Translation: AAV38622.1.
BT019820 mRNA. Translation: AAV38623.1.
BC007582 mRNA. Translation: AAH07582.1.
BC013128 mRNA. Translation: AAH13128.1.
CCDSiCCDS12432.1.
PIRiJC4243.
RefSeqiNP_001239225.1. NM_001252296.1.
NP_001797.1. NM_001806.3.
UniGeneiHs.429666.

3D structure databases

ProteinModelPortaliP53567.
SMRiP53567. Positions 62-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107483. 22 interactions.
IntActiP53567. 6 interactions.
MINTiMINT-1445645.
STRINGi9606.ENSP00000284000.

PTM databases

PhosphoSiteiP53567.

Polymorphism and mutation databases

BioMutaiCEBPG.
DMDMi1705750.

Proteomic databases

MaxQBiP53567.
PaxDbiP53567.
PRIDEiP53567.

Protocols and materials databases

DNASUi1054.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284000; ENSP00000284000; ENSG00000153879.
ENST00000585933; ENSP00000466022; ENSG00000153879.
GeneIDi1054.
KEGGihsa:1054.
UCSCiuc002nup.3. human.

Organism-specific databases

CTDi1054.
GeneCardsiGC19P033864.
HGNCiHGNC:1837. CEBPG.
HPAiHPA012024.
MIMi138972. gene.
neXtProtiNX_P53567.
PharmGKBiPA26380.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG281019.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000057291.
HOVERGENiHBG050880.
InParanoidiP53567.
KOiK10049.
OMAiADNVQPS.
OrthoDBiEOG7R56TQ.
PhylomeDBiP53567.
TreeFamiTF105009.

Miscellaneous databases

GeneWikiiCEBPG.
GenomeRNAii1054.
NextBioi4413.
PROiP53567.
SOURCEiSearch...

Gene expression databases

BgeeiP53567.
CleanExiHS_CEBPG.
GenevisibleiP53567. HS.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA encoding human C/EBP gamma, a protein binding to the PRE-I enhancer element of the human interleukin-4 promoter."
    Davydov I.V., Bohmann D., Krammer P.H., Li-Weber M.
    Gene 161:271-275(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: T-cell.
  2. "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].
    Tissue: Trachea.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Placenta.
  5. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiCEBPG_HUMAN
AccessioniPrimary (citable) accession number: P53567
Secondary accession number(s): B2R946, Q5U052
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 132 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.