ID CEBPZ_HUMAN Reviewed; 1054 AA.
AC Q03701; Q8NE75;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=CCAAT/enhancer-binding protein zeta;
DE AltName: Full=CCAAT-box-binding transcription factor;
DE Short=CBF;
DE Short=CCAAT-binding factor;
GN Name=CEBPZ; Synonyms=CBF2;
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 VARIANT ILE-102.
RX PubMed=2247079; DOI=10.1128/mcb.10.12.6709-6717.1990;
RA Lum L., Sultzman L., Kaufman R., Linzer D.I.H., Wu B.;
RT "A cloned human CCAAT-box-binding factor stimulates transcription from the
RT human hsp70 promoter.";
RL Mol. Cell. Biol. 10:6709-6717(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-835, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-978, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-973, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-695, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-629 AND SER-959,
RP VARIANT [LARGE SCALE ANALYSIS] ILE-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Stimulates transcription from the HSP70 promoter.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the CBF/MAK21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51924.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M37197; AAA51924.1; ALT_FRAME; mRNA.
DR EMBL; AC007390; AAY14815.1; -; Genomic_DNA.
DR EMBL; BC034475; AAH34475.1; -; mRNA.
DR CCDS; CCDS1787.1; -.
DR PIR; A36368; A36368.
DR RefSeq; NP_005751.2; NM_005760.2.
DR AlphaFoldDB; Q03701; -.
DR SMR; Q03701; -.
DR BioGRID; 115455; 256.
DR IntAct; Q03701; 71.
DR MINT; Q03701; -.
DR STRING; 9606.ENSP00000234170; -.
DR GlyGen; Q03701; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03701; -.
DR MetOSite; Q03701; -.
DR PhosphoSitePlus; Q03701; -.
DR SwissPalm; Q03701; -.
DR BioMuta; CEBPZ; -.
DR DMDM; 308153621; -.
DR SWISS-2DPAGE; Q03701; -.
DR EPD; Q03701; -.
DR jPOST; Q03701; -.
DR MassIVE; Q03701; -.
DR MaxQB; Q03701; -.
DR PaxDb; 9606-ENSP00000234170; -.
DR PeptideAtlas; Q03701; -.
DR ProteomicsDB; 58219; -.
DR Pumba; Q03701; -.
DR Antibodypedia; 14550; 226 antibodies from 34 providers.
DR DNASU; 10153; -.
DR Ensembl; ENST00000234170.10; ENSP00000234170.5; ENSG00000115816.15.
DR GeneID; 10153; -.
DR KEGG; hsa:10153; -.
DR MANE-Select; ENST00000234170.10; ENSP00000234170.5; NM_005760.3; NP_005751.2.
DR UCSC; uc002rpz.5; human.
DR AGR; HGNC:24218; -.
DR CTD; 10153; -.
DR DisGeNET; 10153; -.
DR GeneCards; CEBPZ; -.
DR HGNC; HGNC:24218; CEBPZ.
DR HPA; ENSG00000115816; Low tissue specificity.
DR MIM; 612828; gene.
DR neXtProt; NX_Q03701; -.
DR OpenTargets; ENSG00000115816; -.
DR PharmGKB; PA134977051; -.
DR VEuPathDB; HostDB:ENSG00000115816; -.
DR eggNOG; KOG2038; Eukaryota.
DR GeneTree; ENSGT00390000006395; -.
DR InParanoid; Q03701; -.
DR OMA; EIWCNDE; -.
DR OrthoDB; 1214522at2759; -.
DR PhylomeDB; Q03701; -.
DR TreeFam; TF105010; -.
DR PathwayCommons; Q03701; -.
DR SignaLink; Q03701; -.
DR BioGRID-ORCS; 10153; 722 hits in 1198 CRISPR screens.
DR ChiTaRS; CEBPZ; human.
DR GeneWiki; CCAAT/enhancer_binding_protein_zeta; -.
DR GenomeRNAi; 10153; -.
DR Pharos; Q03701; Tbio.
DR PRO; PR:Q03701; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q03701; Protein.
DR Bgee; ENSG00000115816; Expressed in calcaneal tendon and 211 other cell types or tissues.
DR ExpressionAtlas; Q03701; baseline and differential.
DR Genevisible; Q03701; HS.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IGI:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005612; CCAAT-binding_factor.
DR InterPro; IPR040155; CEBPZ/Mak21-like.
DR PANTHER; PTHR12048; CCAAT-BINDING FACTOR-RELATED; 1.
DR PANTHER; PTHR12048:SF0; CCAAT_ENHANCER-BINDING PROTEIN ZETA; 1.
DR Pfam; PF03914; CBF; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1054
FT /note="CCAAT/enhancer-binding protein zeta"
FT /id="PRO_0000173470"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..902
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..930
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 695
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 15
FT /note="P -> S (in dbSNP:rs3213746)"
FT /id="VAR_031399"
FT VARIANT 102
FT /note="V -> I (in dbSNP:rs2098386)"
FT /evidence="ECO:0000269|PubMed:2247079,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_026043"
FT VARIANT 303
FT /note="K -> R (in dbSNP:rs17020328)"
FT /id="VAR_031400"
FT VARIANT 639
FT /note="N -> S (in dbSNP:rs3180252)"
FT /id="VAR_055622"
FT CONFLICT 589
FT /note="R -> G (in Ref. 1; AAA51924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1054 AA; 120974 MW; 20E33175688BA985 CRC64;
MAAVKEPLEF HAKRPWRPEE AVEDPDEEDE DNTSEAENGF SLEEVLRLGG TKQDYLMLAT
LDENEEVIDG GKKGAIDDLQ QGELEAFIQN LNLAKYTKAS LVEEDEPAEK ENSSKKEVKI
PKINNKNTAE SQRTSVNKVK NKNRPEPHSD ENGSTTPKVK KDKQNIFEFF ERQTLLLRPG
GKWYDLEYSN EYSLKPQPQD VVSKYKTLAQ KLYQHEINLF KSKTNSQKGA SSTWMKAIVS
SGTLGDRMAA MILLIQDDAV HTLQFVETLV NLVKKKGSKQ QCLMALDTFK ELLITDLLPD
NRKLRIFSQR PFDKLEQLSS GNKDSRDRRL ILWYFEHQLK HLVAEFVQVL ETLSHDTLVT
TKTRALTVAH ELLCNKPEEE KALLVQVVNK LGDPQNRIAT KASHLLETLL CKHPNMKGVV
SGEVERLLFR SNISSKAQYY AICFLNQMAL SHEESELANK LITVYFCFFR TCVKKKDVES
KMLSALLTGV NRAYPYSQTG DDKVREQIDT LFKVLHIVNF NTSVQALMLL FQVMNSQQTI
SDRYYTALYR KMLDPGLMTC SKQAMFLNLV YKSLKADIVL RRVKAFVKRL LQVTCQQMPP
FICGALYLVS EILKAKPGLR SQLDDHPESD DEENFIDAND DEDMEKFTDA DKETEIVKKL
ETEETVPETD VETKKPEVAS WVHFDNLKGG KQLNKYDPFS RNPLFCGAEN TSLWELKKLS
VHFHPSVALF AKTILQGNYI QYSGDPLQDF TLMRFLDRFV YRNPKPHKGK ENTDSVVMQP
KRKHFIKDIR HLPVNSKEFL AKEESQIPVD EVFFHRYYKK VAVKEKQKRD ADEESIEDVD
DEEFEELIDT FEDDNCFSSG KDDMDFAGNV KKRTKGAKDN TLDEDSEGSD DELGNLDDDE
VSLGSMDDEE FAEVDEDGGT FMDVLDDESE SVPELEVHSK VSTKKSKRKG TDDFDFAGSF
QGPRKKKRNL NDSSLFVSAE EFGHLLDENM GSKFDNIGMN AMANKDNASL KQLRWEAERD
DWLHNRDAKS IIKKKKHFKK KRIKTTQKTK KQRK
//
