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Protein

CCAAT/enhancer-binding protein zeta

Gene

CEBPZ

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

Functioni

Stimulates transcription from the HSP70 promoter.

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB

GO - Biological processi

  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein zeta
Alternative name(s):
CCAAT-box-binding transcription factor
Short name:
CBF
Short name:
CCAAT-binding factor
Gene namesi
Name:CEBPZ
Synonyms:CBF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24218. CEBPZ.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134977051.

Polymorphism and mutation databases

BioMutaiCEBPZ.
DMDMi308153621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10541054CCAAT/enhancer-binding protein zetaPRO_0000173470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei629 – 6291Phosphoserine6 Publications
Modified residuei695 – 6951N6-acetyllysine1 Publication
Modified residuei835 – 8351Phosphoserine1 Publication
Modified residuei973 – 9731Phosphoserine1 Publication
Modified residuei978 – 9781Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ03701.
PaxDbiQ03701.
PRIDEiQ03701.

2D gel databases

SWISS-2DPAGEQ03701.

PTM databases

PhosphoSiteiQ03701.

Expressioni

Gene expression databases

BgeeiQ03701.
CleanExiHS_CEBPZ.
ExpressionAtlasiQ03701. baseline and differential.
GenevisibleiQ03701. HS.

Organism-specific databases

HPAiHPA052065.

Interactioni

Protein-protein interaction databases

BioGridi115455. 37 interactions.
IntActiQ03701. 11 interactions.
MINTiMINT-255293.
STRINGi9606.ENSP00000234170.

Structurei

3D structure databases

ProteinModelPortaliQ03701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CBF/MAK21 family.Curated

Phylogenomic databases

eggNOGiCOG5593.
GeneTreeiENSGT00390000006395.
HOGENOMiHOG000168357.
HOVERGENiHBG050881.
InParanoidiQ03701.
KOiK14832.
OMAiDNCFSSG.
OrthoDBiEOG7NW68M.
PhylomeDBiQ03701.
TreeFamiTF105010.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR005612. CCAAT-binding_factor.
[Graphical view]
PfamiPF03914. CBF. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Q03701-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVKEPLEF HAKRPWRPEE AVEDPDEEDE DNTSEAENGF SLEEVLRLGG
60 70 80 90 100
TKQDYLMLAT LDENEEVIDG GKKGAIDDLQ QGELEAFIQN LNLAKYTKAS
110 120 130 140 150
LVEEDEPAEK ENSSKKEVKI PKINNKNTAE SQRTSVNKVK NKNRPEPHSD
160 170 180 190 200
ENGSTTPKVK KDKQNIFEFF ERQTLLLRPG GKWYDLEYSN EYSLKPQPQD
210 220 230 240 250
VVSKYKTLAQ KLYQHEINLF KSKTNSQKGA SSTWMKAIVS SGTLGDRMAA
260 270 280 290 300
MILLIQDDAV HTLQFVETLV NLVKKKGSKQ QCLMALDTFK ELLITDLLPD
310 320 330 340 350
NRKLRIFSQR PFDKLEQLSS GNKDSRDRRL ILWYFEHQLK HLVAEFVQVL
360 370 380 390 400
ETLSHDTLVT TKTRALTVAH ELLCNKPEEE KALLVQVVNK LGDPQNRIAT
410 420 430 440 450
KASHLLETLL CKHPNMKGVV SGEVERLLFR SNISSKAQYY AICFLNQMAL
460 470 480 490 500
SHEESELANK LITVYFCFFR TCVKKKDVES KMLSALLTGV NRAYPYSQTG
510 520 530 540 550
DDKVREQIDT LFKVLHIVNF NTSVQALMLL FQVMNSQQTI SDRYYTALYR
560 570 580 590 600
KMLDPGLMTC SKQAMFLNLV YKSLKADIVL RRVKAFVKRL LQVTCQQMPP
610 620 630 640 650
FICGALYLVS EILKAKPGLR SQLDDHPESD DEENFIDAND DEDMEKFTDA
660 670 680 690 700
DKETEIVKKL ETEETVPETD VETKKPEVAS WVHFDNLKGG KQLNKYDPFS
710 720 730 740 750
RNPLFCGAEN TSLWELKKLS VHFHPSVALF AKTILQGNYI QYSGDPLQDF
760 770 780 790 800
TLMRFLDRFV YRNPKPHKGK ENTDSVVMQP KRKHFIKDIR HLPVNSKEFL
810 820 830 840 850
AKEESQIPVD EVFFHRYYKK VAVKEKQKRD ADEESIEDVD DEEFEELIDT
860 870 880 890 900
FEDDNCFSSG KDDMDFAGNV KKRTKGAKDN TLDEDSEGSD DELGNLDDDE
910 920 930 940 950
VSLGSMDDEE FAEVDEDGGT FMDVLDDESE SVPELEVHSK VSTKKSKRKG
960 970 980 990 1000
TDDFDFAGSF QGPRKKKRNL NDSSLFVSAE EFGHLLDENM GSKFDNIGMN
1010 1020 1030 1040 1050
AMANKDNASL KQLRWEAERD DWLHNRDAKS IIKKKKHFKK KRIKTTQKTK

KQRK
Length:1,054
Mass (Da):120,974
Last modified:October 5, 2010 - v3
Checksum:i20E33175688BA985
GO

Sequence cautioni

The sequence AAA51924.1 differs from that shown. Reason: Frameshift at position 998. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti589 – 5891R → G in AAA51924 (PubMed:2247079).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151P → S.
Corresponds to variant rs3213746 [ dbSNP | Ensembl ].
VAR_031399
Natural varianti102 – 1021V → I.1 Publication
Corresponds to variant rs2098386 [ dbSNP | Ensembl ].
VAR_026043
Natural varianti303 – 3031K → R.
Corresponds to variant rs17020328 [ dbSNP | Ensembl ].
VAR_031400
Natural varianti639 – 6391N → S.
Corresponds to variant rs3180252 [ dbSNP | Ensembl ].
VAR_055622

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37197 mRNA. Translation: AAA51924.1. Frameshift.
AC007390 Genomic DNA. Translation: AAY14815.1.
BC034475 mRNA. Translation: AAH34475.1.
CCDSiCCDS1787.1.
PIRiA36368.
RefSeqiNP_005751.2. NM_005760.2.
UniGeneiHs.135406.

Genome annotation databases

EnsembliENST00000234170; ENSP00000234170; ENSG00000115816.
GeneIDi10153.
KEGGihsa:10153.
UCSCiuc002rpz.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37197 mRNA. Translation: AAA51924.1. Frameshift.
AC007390 Genomic DNA. Translation: AAY14815.1.
BC034475 mRNA. Translation: AAH34475.1.
CCDSiCCDS1787.1.
PIRiA36368.
RefSeqiNP_005751.2. NM_005760.2.
UniGeneiHs.135406.

3D structure databases

ProteinModelPortaliQ03701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115455. 37 interactions.
IntActiQ03701. 11 interactions.
MINTiMINT-255293.
STRINGi9606.ENSP00000234170.

PTM databases

PhosphoSiteiQ03701.

Polymorphism and mutation databases

BioMutaiCEBPZ.
DMDMi308153621.

2D gel databases

SWISS-2DPAGEQ03701.

Proteomic databases

MaxQBiQ03701.
PaxDbiQ03701.
PRIDEiQ03701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234170; ENSP00000234170; ENSG00000115816.
GeneIDi10153.
KEGGihsa:10153.
UCSCiuc002rpz.3. human.

Organism-specific databases

CTDi10153.
GeneCardsiGC02M037428.
H-InvDBHIX0001972.
HIX0161881.
HGNCiHGNC:24218. CEBPZ.
HPAiHPA052065.
MIMi612828. gene.
neXtProtiNX_Q03701.
PharmGKBiPA134977051.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5593.
GeneTreeiENSGT00390000006395.
HOGENOMiHOG000168357.
HOVERGENiHBG050881.
InParanoidiQ03701.
KOiK14832.
OMAiDNCFSSG.
OrthoDBiEOG7NW68M.
PhylomeDBiQ03701.
TreeFamiTF105010.

Miscellaneous databases

ChiTaRSiCEBPZ. human.
GeneWikiiCCAAT/enhancer_binding_protein_zeta.
GenomeRNAii10153.
NextBioi38432.
PROiQ03701.
SOURCEiSearch...

Gene expression databases

BgeeiQ03701.
CleanExiHS_CEBPZ.
ExpressionAtlasiQ03701. baseline and differential.
GenevisibleiQ03701. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR005612. CCAAT-binding_factor.
[Graphical view]
PfamiPF03914. CBF. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cloned human CCAAT-box-binding factor stimulates transcription from the human hsp70 promoter."
    Lum L., Sultzman L., Kaufman R., Linzer D.I.H., Wu B.
    Mol. Cell. Biol. 10:6709-6717(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-102.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Testis.
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-835, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-978, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCEBPZ_HUMAN
AccessioniPrimary (citable) accession number: Q03701
Secondary accession number(s): Q8NE75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 5, 2010
Last modified: July 22, 2015
This is version 125 of the entry and version 3 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.