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 27-MAR-2024, entry version 190. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 59. 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.ENSP00000466022; -. 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; 9606-ENSP00000284000; -. DR PeptideAtlas; P53567; -. DR ProteomicsDB; 56585; -. DR Pumba; P53567; -. DR Antibodypedia; 1652; 400 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 AGR; HGNC:1837; -. 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; 2966182at2759; -. 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; 14 hits in 1172 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 198 other cell types or tissues. 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:0006351; P:DNA-templated transcription; IEA:InterPro. 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; NAS: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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR CDD; cd14713; bZIP_CEBPG; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR031106; C/EBP. DR PANTHER; PTHR23334; CCAAT/ENHANCER BINDING PROTEIN; 1. DR PANTHER; PTHR23334:SF69; CCAAT_ENHANCER-BINDING PROTEIN GAMMA; 1. DR Pfam; PF07716; bZIP_2; 1. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR Genevisible; P53567; HS. 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 //