CEBPG_HUMAN
ID CEBPG_HUMAN Reviewed; 150 AA.
AC P53567; B2R946; Q5U052;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=CCAAT/enhancer-binding protein gamma;
DE Short=C/EBP gamma;
GN Name=CEBPG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=T-cell;
RX PubMed=7665092; DOI=10.1016/0378-1119(95)00271-7;
RA Davydov I.V., Bohmann D., Krammer P.H., Li-Weber M.;
RT "Cloning of the cDNA encoding human C/EBP gamma, a protein binding to the
RT PRE-I enhancer element of the human interleukin-4 promoter.";
RL Gene 161:271-275(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription factor that binds to the promoter and the
CC enhancer regions of target genes. Binds to the enhancer element PRE-I
CC (positive regulatory element-I) of the IL-4 gene (PubMed:7665092).
CC Binds to the promoter and the enhancer of the immunoglobulin heavy
CC chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter.
CC {ECO:0000250|UniProtKB:P26801, ECO:0000250|UniProtKB:P53568,
CC ECO:0000269|PubMed:7665092}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers with
CC CEBPA and CEBPB. Interacts with ZNF638; this interaction increases
CC transcriptional activation. {ECO:0000250|UniProtKB:P26801,
CC ECO:0000250|UniProtKB:P53568}.
CC -!- INTERACTION:
CC P53567; P15336: ATF2; NbExp=2; IntAct=EBI-740209, EBI-1170906;
CC P53567; P18847: ATF3; NbExp=5; IntAct=EBI-740209, EBI-712767;
CC P53567; P18848: ATF4; NbExp=16; IntAct=EBI-740209, EBI-492498;
CC P53567; Q9Y2D1: ATF5; NbExp=8; IntAct=EBI-740209, EBI-492509;
CC P53567; Q16520: BATF; NbExp=4; IntAct=EBI-740209, EBI-749503;
CC P53567; Q8N1L9: BATF2; NbExp=2; IntAct=EBI-740209, EBI-742695;
CC P53567; Q9NR55: BATF3; NbExp=3; IntAct=EBI-740209, EBI-10312707;
CC P53567; P49715: CEBPA; NbExp=4; IntAct=EBI-740209, EBI-1172054;
CC P53567; P17676: CEBPB; NbExp=2; IntAct=EBI-740209, EBI-969696;
CC P53567; P49716: CEBPD; NbExp=2; IntAct=EBI-740209, EBI-7962058;
CC P53567; Q15744: CEBPE; NbExp=2; IntAct=EBI-740209, EBI-3907048;
CC P53567; P35638: DDIT3; NbExp=6; IntAct=EBI-740209, EBI-742651;
CC P53567; P35638-2: DDIT3; NbExp=3; IntAct=EBI-740209, EBI-10173632;
CC P53567; P01100: FOS; NbExp=2; IntAct=EBI-740209, EBI-852851;
CC P53567; Q16236: NFE2L2; NbExp=5; IntAct=EBI-740209, EBI-2007911;
CC P53567; O15212: PFDN6; NbExp=3; IntAct=EBI-740209, EBI-356973;
CC P53567; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-740209, EBI-10890294;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53568}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; U20240; AAC50201.1; -; mRNA.
DR EMBL; AK313634; BAG36393.1; -; mRNA.
DR EMBL; BT019819; AAV38622.1; -; mRNA.
DR EMBL; BT019820; AAV38623.1; -; mRNA.
DR EMBL; BC007582; AAH07582.1; -; mRNA.
DR EMBL; BC013128; AAH13128.1; -; mRNA.
DR CCDS; CCDS12432.1; -.
DR PIR; JC4243; JC4243.
DR RefSeq; NP_001239225.1; NM_001252296.1.
DR RefSeq; NP_001797.1; NM_001806.3.
DR AlphaFoldDB; P53567; -.
DR SMR; P53567; -.
DR BioGRID; 107483; 45.
DR ComplexPortal; CPX-516; bZIP transcription factor complex, CEBPG-CEBPG.
DR ComplexPortal; CPX-6527; bZIP transcription factor complex, ATF4-CEBPG.
DR ComplexPortal; CPX-6588; bZIP transcription factor complex, ATF5-CEBPG.
DR ComplexPortal; CPX-6782; bZIP transcription factor complex, ATF7-CEBPG.
DR ComplexPortal; CPX-7008; bZIP transcription factor complex, BATF-CEBPG.
DR ComplexPortal; CPX-7066; bZIP transcription factor complex, BATF2-CEBPG.
DR ComplexPortal; CPX-7097; bZIP transcription factor complex, BATF3-CEBPG.
DR IntAct; P53567; 25.
DR MINT; P53567; -.
DR STRING; 9606.ENSP00000284000; -.
DR iPTMnet; P53567; -.
DR PhosphoSitePlus; P53567; -.
DR BioMuta; CEBPG; -.
DR DMDM; 1705750; -.
DR EPD; P53567; -.
DR jPOST; P53567; -.
DR MassIVE; P53567; -.
DR MaxQB; P53567; -.
DR PaxDb; P53567; -.
DR PeptideAtlas; P53567; -.
DR PRIDE; P53567; -.
DR ProteomicsDB; 56585; -.
DR Antibodypedia; 1652; 379 antibodies from 35 providers.
DR DNASU; 1054; -.
DR Ensembl; ENST00000284000.9; ENSP00000284000.2; ENSG00000153879.9.
DR Ensembl; ENST00000585933.2; ENSP00000466022.2; ENSG00000153879.9.
DR Ensembl; ENST00000652630.1; ENSP00000499062.1; ENSG00000153879.9.
DR GeneID; 1054; -.
DR KEGG; hsa:1054; -.
DR MANE-Select; ENST00000284000.9; ENSP00000284000.2; NM_001806.4; NP_001797.1.
DR UCSC; uc002nup.4; human.
DR CTD; 1054; -.
DR DisGeNET; 1054; -.
DR GeneCards; CEBPG; -.
DR HGNC; HGNC:1837; CEBPG.
DR HPA; ENSG00000153879; Low tissue specificity.
DR MIM; 138972; gene.
DR neXtProt; NX_P53567; -.
DR OpenTargets; ENSG00000153879; -.
DR PharmGKB; PA26380; -.
DR VEuPathDB; HostDB:ENSG00000153879; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000160676; -.
DR HOGENOM; CLU_146813_0_0_1; -.
DR InParanoid; P53567; -.
DR OMA; HAHNFAD; -.
DR OrthoDB; 1532157at2759; -.
DR PhylomeDB; P53567; -.
DR TreeFam; TF105009; -.
DR PathwayCommons; P53567; -.
DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9648895; Response of EIF2AK1 (HRI) to heme deficiency.
DR SignaLink; P53567; -.
DR SIGNOR; P53567; -.
DR BioGRID-ORCS; 1054; 13 hits in 1096 CRISPR screens.
DR ChiTaRS; CEBPG; human.
DR GeneWiki; CEBPG; -.
DR GenomeRNAi; 1054; -.
DR Pharos; P53567; Tbio.
DR PRO; PR:P53567; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P53567; protein.
DR Bgee; ENSG00000153879; Expressed in secondary oocyte and 197 other tissues.
DR Genevisible; P53567; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0001889; P:liver development; ISS:UniProtKB.
DR GO; GO:0016071; P:mRNA metabolic process; IEA:Ensembl.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; TAS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; TAS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..150
FT /note="CCAAT/enhancer-binding protein gamma"
FT /id="PRO_0000076628"
FT DOMAIN 62..125
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 27..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..93
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 97..118
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 56..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 150 AA; 16408 MW; 630D1C1F92A00186 CRC64;
MSKISQQNST PGVNGISVIH TQAHASGLQQ VPQLVPAGPG GGGKAVAPSK QSKKSSPMDR
NSDEYRQRRE RNNMAVKKSR LKSKQKAQDT LQRVNQLKEE NERLEAKIKL LTKELSVLKD
LFLEHAHNLA DNVQSISTEN TTADGDNAGQ
