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Q03701

- CEBPZ_HUMAN

UniProt

Q03701 - CEBPZ_HUMAN

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Protein
CCAAT/enhancer-binding protein zeta
Gene
CEBPZ, CBF2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Stimulates transcription from the HSP70 promoter.

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. 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: Chromosome 2

Organism-specific databases

HGNCiHGNC:24218. CEBPZ.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134977051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10541054CCAAT/enhancer-binding protein zeta
PRO_0000173470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei629 – 6291Phosphoserine5 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.
GenevestigatoriQ03701.

Organism-specific databases

HPAiHPA052065.

Interactioni

Protein-protein interaction databases

BioGridi115455. 22 interactions.
IntActiQ03701. 9 interactions.
MINTiMINT-255293.
STRINGi9606.ENSP00000234170.

Structurei

3D structure databases

ProteinModelPortaliQ03701.

Family & Domainsi

Sequence similaritiesi

Belongs to the CBF/MAK21 family.

Phylogenomic databases

eggNOGiCOG5593.
HOGENOMiHOG000168357.
HOVERGENiHBG050881.
InParanoidiQ03701.
KOiK14832.
OMAiNQMVLSH.
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

MAAVKEPLEF HAKRPWRPEE AVEDPDEEDE DNTSEAENGF SLEEVLRLGG     50
TKQDYLMLAT LDENEEVIDG GKKGAIDDLQ QGELEAFIQN LNLAKYTKAS 100
LVEEDEPAEK ENSSKKEVKI PKINNKNTAE SQRTSVNKVK NKNRPEPHSD 150
ENGSTTPKVK KDKQNIFEFF ERQTLLLRPG GKWYDLEYSN EYSLKPQPQD 200
VVSKYKTLAQ KLYQHEINLF KSKTNSQKGA SSTWMKAIVS SGTLGDRMAA 250
MILLIQDDAV HTLQFVETLV NLVKKKGSKQ QCLMALDTFK ELLITDLLPD 300
NRKLRIFSQR PFDKLEQLSS GNKDSRDRRL ILWYFEHQLK HLVAEFVQVL 350
ETLSHDTLVT TKTRALTVAH ELLCNKPEEE KALLVQVVNK LGDPQNRIAT 400
KASHLLETLL CKHPNMKGVV SGEVERLLFR SNISSKAQYY AICFLNQMAL 450
SHEESELANK LITVYFCFFR TCVKKKDVES KMLSALLTGV NRAYPYSQTG 500
DDKVREQIDT LFKVLHIVNF NTSVQALMLL FQVMNSQQTI SDRYYTALYR 550
KMLDPGLMTC SKQAMFLNLV YKSLKADIVL RRVKAFVKRL LQVTCQQMPP 600
FICGALYLVS EILKAKPGLR SQLDDHPESD DEENFIDAND DEDMEKFTDA 650
DKETEIVKKL ETEETVPETD VETKKPEVAS WVHFDNLKGG KQLNKYDPFS 700
RNPLFCGAEN TSLWELKKLS VHFHPSVALF AKTILQGNYI QYSGDPLQDF 750
TLMRFLDRFV YRNPKPHKGK ENTDSVVMQP KRKHFIKDIR HLPVNSKEFL 800
AKEESQIPVD EVFFHRYYKK VAVKEKQKRD ADEESIEDVD DEEFEELIDT 850
FEDDNCFSSG KDDMDFAGNV KKRTKGAKDN TLDEDSEGSD DELGNLDDDE 900
VSLGSMDDEE FAEVDEDGGT FMDVLDDESE SVPELEVHSK VSTKKSKRKG 950
TDDFDFAGSF QGPRKKKRNL NDSSLFVSAE EFGHLLDENM GSKFDNIGMN 1000
AMANKDNASL KQLRWEAERD DWLHNRDAKS IIKKKKHFKK KRIKTTQKTK 1050
KQRK 1054
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti589 – 5891R → G in AAA51924. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi308153621.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37197 mRNA. Translation: AAA51924.1 . Frameshift.
AC007390 Genomic DNA. Translation: AAY14815.1 .
BC034475 mRNA. Translation: AAH34475.1 .
CCDSi CCDS1787.1.
PIRi A36368.
RefSeqi NP_005751.2. NM_005760.2.
UniGenei Hs.135406.

3D structure databases

ProteinModelPortali Q03701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115455. 22 interactions.
IntActi Q03701. 9 interactions.
MINTi MINT-255293.
STRINGi 9606.ENSP00000234170.

PTM databases

PhosphoSitei Q03701.

Polymorphism databases

DMDMi 308153621.

2D gel databases

SWISS-2DPAGE Q03701.

Proteomic databases

MaxQBi Q03701.
PaxDbi Q03701.
PRIDEi Q03701.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234170 ; ENSP00000234170 ; ENSG00000115816 .
GeneIDi 10153.
KEGGi hsa:10153.
UCSCi uc002rpz.3. human.

Organism-specific databases

CTDi 10153.
GeneCardsi GC02M037428.
H-InvDB HIX0001972.
HIX0161881.
HGNCi HGNC:24218. CEBPZ.
HPAi HPA052065.
MIMi 612828. gene.
neXtProti NX_Q03701.
PharmGKBi PA134977051.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5593.
HOGENOMi HOG000168357.
HOVERGENi HBG050881.
InParanoidi Q03701.
KOi K14832.
OMAi NQMVLSH.
OrthoDBi EOG7NW68M.
PhylomeDBi Q03701.
TreeFami TF105010.

Miscellaneous databases

GeneWikii CCAAT/enhancer_binding_protein_zeta.
GenomeRNAii 10153.
NextBioi 38432.
PROi Q03701.
SOURCEi Search...

Gene expression databases

Bgeei Q03701.
CleanExi HS_CEBPZ.
Genevestigatori Q03701.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR005612. CCAAT-binding_factor.
[Graphical view ]
Pfami PF03914. CBF. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
ProtoNeti Search...

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].

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: September 3, 2014
This is version 116 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

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