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Q03701

- CEBPZ_HUMAN

UniProt

Q03701 - CEBPZ_HUMAN

Protein

CCAAT/enhancer-binding protein zeta

Gene

CEBPZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Stimulates transcription from the HSP70 promoter.

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    4. 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

    1. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    2. transcription from RNA polymerase II promoter Source: ProtInc

    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

    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 zetaPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CBF/MAK21 family.Curated

    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.

    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:
    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

    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: October 1, 2014
    This is version 117 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