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Q13105

- ZBT17_HUMAN

UniProt

Q13105 - ZBT17_HUMAN

Protein

Zinc finger and BTB domain-containing protein 17

Gene

ZBTB17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri306 – 32823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri334 – 35623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri362 – 38423C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri390 – 41223C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri418 – 44023C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri446 – 46823C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri474 – 49623C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri502 – 52423C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri530 – 55223C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri558 – 58023C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri586 – 60823C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri614 – 63724C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri717 – 73923C2H2-type 13PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. ectoderm development Source: Ensembl
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. gastrulation with mouth forming second Source: Ensembl
    6. negative regulation of cell cycle Source: UniProtKB
    7. positive regulation of transcription, DNA-templated Source: Ensembl
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger and BTB domain-containing protein 17
    Alternative name(s):
    Myc-interacting zinc finger protein 1
    Short name:
    Miz-1
    Zinc finger protein 151
    Zinc finger protein 60
    Gene namesi
    Name:ZBTB17
    Synonyms:MIZ1, ZNF151, ZNF60
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12936. ZBTB17.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37522.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 803803Zinc finger and BTB domain-containing protein 17PRO_0000047730Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki397 – 397Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki481 – 481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Undergoes 'Lys-48'-linked polyubiquitination at Lys-397 and Lys-481 and subsequent proteasomal degradation in a TRAF2-dependent manner.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ13105.
    PaxDbiQ13105.
    PRIDEiQ13105.

    PTM databases

    PhosphoSiteiQ13105.

    Expressioni

    Tissue specificityi

    Expressed in germinal center B-cells.1 Publication

    Gene expression databases

    ArrayExpressiQ13105.
    BgeeiQ13105.
    CleanExiHS_ZBTB17.
    GenevestigatoriQ13105.

    Organism-specific databases

    HPAiHPA005789.

    Interactioni

    Subunit structurei

    Homooligomerizes (via the BTB/POZ domain), multimerization is required for DNA binding. Interacts (via the C-terminal zinc fingers) with GIF1; the interaction results in the recruitment of MYB to the CDKN1A/p21 and CDKN1B promoters and repression of transcription. Interacts with TRAF2, interfering with the binding of UBC13 to TRAF2, and inhibiting TRAF2 E3 ligase activity. Interacts with MYC (via the C-terminal helix-loop-helix motif); the interaction inhibits ZBTB17 transactivation and growth arrest activities and renders it insoluble in the nucleus. Also interacts with HCFC1, MAGEA4 and TMPRSS11A. Interacts with BCL6; the interaction inhibits ZBTB17 transactivation activity on target genes involved in cell cycle arrest.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HCFC1P516109EBI-372156,EBI-396176
    MAGEA4P433585EBI-372156,EBI-743122
    MYCP011064EBI-372156,EBI-447544
    TOPBP1Q925472EBI-372156,EBI-308302

    Protein-protein interaction databases

    BioGridi113503. 18 interactions.
    DIPiDIP-5968N.
    IntActiQ13105. 9 interactions.
    MINTiMINT-1527698.
    STRINGi9606.ENSP00000364895.

    Structurei

    Secondary structure

    1
    803
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2018
    Beta strandi26 – 305
    Beta strandi33 – 375
    Helixi39 – 457
    Helixi47 – 559
    Helixi56 – 583
    Helixi59 – 646
    Helixi67 – 7913
    Turni86 – 883
    Helixi89 – 9810
    Helixi102 – 11211
    Turni421 – 4233
    Beta strandi426 – 4283
    Helixi430 – 4389
    Turni457 – 4593
    Helixi460 – 46910
    Turni477 – 4793
    Beta strandi482 – 4843
    Helixi486 – 49712
    Turni505 – 5073
    Beta strandi510 – 5123
    Helixi514 – 52512
    Turni533 – 5353
    Beta strandi538 – 5414
    Helixi542 – 55312
    Turni561 – 5633
    Helixi570 – 5789

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LVRNMR-A500-528[»]
    2LVTNMR-A528-556[»]
    2LVUNMR-A556-581[»]
    2M0DNMR-A416-444[»]
    2M0ENMR-A444-472[»]
    2M0FNMR-A472-500[»]
    2Q81X-ray2.10A/B/C/D2-115[»]
    3M52X-ray2.59A/B1-115[»]
    ProteinModelPortaliQ13105.
    SMRiQ13105. Positions 1-115, 303-776.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13105.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 104104BTBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 30840Interaction with MYCAdd
    BLAST
    Regioni637 – 803167Interaction with HCFC1Add
    BLAST
    Regioni637 – 71882Interaction with MYCAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 13 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri306 – 32823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri334 – 35623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri362 – 38423C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri390 – 41223C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri418 – 44023C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri446 – 46823C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri474 – 49623C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri502 – 52423C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri530 – 55223C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri558 – 58023C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri586 – 60823C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri614 – 63724C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri717 – 73923C2H2-type 13PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000231298.
    HOVERGENiHBG054919.
    KOiK10500.
    OMAiCDSCGDK.
    OrthoDBiEOG7KSX7Q.
    PhylomeDBiQ13105.
    TreeFamiTF332047.

    Family and domain databases

    Gene3Di3.30.160.60. 13 hits.
    3.30.710.10. 1 hit.
    InterProiIPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00651. BTB. 1 hit.
    [Graphical view]
    SMARTiSM00225. BTB. 1 hit.
    SM00355. ZnF_C2H2. 13 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 13 hits.
    PS50157. ZINC_FINGER_C2H2_2. 13 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13105-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDFPQHSQHV LEQLNQQRQL GLLCDCTFVV DGVHFKAHKA VLAACSEYFK    50
    MLFVDQKDVV HLDISNAAGL GQVLEFMYTA KLSLSPENVD DVLAVATFLQ 100
    MQDIITACHA LKSLAEPATS PGGNAEALAT EGGDKRAKEE KVATSTLSRL 150
    EQAGRSTPIG PSRDLKEERG GQAQSAASGA EQTEKADAPR EPPPVELKPD 200
    PTSGMAAAEA EAALSESSEQ EMEVEPARKG EEEQKEQEEQ EEEGAGPAEV 250
    KEEGSQLENG EAPEENENEE SAGTDSGQEL GSEARGLRSG TYGDRTESKA 300
    YGSVIHKCED CGKEFTHTGN FKRHIRIHTG EKPFSCRECS KAFSDPAACK 350
    AHEKTHSPLK PYGCEECGKS YRLISLLNLH KKRHSGEARY RCEDCGKLFT 400
    TSGNLKRHQL VHSGEKPYQC DYCGRSFSDP TSKMRHLETH DTDKEHKCPH 450
    CDKKFNQVGN LKAHLKIHIA DGPLKCRECG KQFTTSGNLK RHLRIHSGEK 500
    PYVCIHCQRQ FADPGALQRH VRIHTGEKPC QCVMCGKAFT QASSLIAHVR 550
    QHTGEKPYVC ERCGKRFVQS SQLANHIRHH DNIRPHKCSV CSKAFVNVGD 600
    LSKHIIIHTG EKPYLCDKCG RGFNRVDNLR SHVKTVHQGK AGIKILEPEE 650
    GSEVSVVTVD DMVTLATEAL AATAVTQLTV VPVGAAVTAD ETEVLKAEIS 700
    KAVKQVQEED PNTHILYACD SCGDKFLDAN SLAQHVRIHT AQALVMFQTD 750
    ADFYQQYGPG GTWPAGQVLQ AGELVFRPRD GAEGQPALAE TSPTAPECPP 800
    PAE 803
    Length:803
    Mass (Da):87,928
    Last modified:April 26, 2005 - v3
    Checksum:iC159D177C8A2D4A3
    GO
    Isoform 2 (identifier: Q13105-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         679-679: T → TGPATLPA

    Note: No experimental confirmation available.

    Show »
    Length:810
    Mass (Da):88,535
    Checksum:iE59D5EBF4A77C210
    GO
    Isoform 3 (identifier: Q13105-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-131: MDFPQHSQHV...GGNAEALATE → MMCWPWPLSS...PQKVCPVPSP

    Note: No experimental confirmation available.

    Show »
    Length:721
    Mass (Da):79,228
    Checksum:i7C8788248C093F0D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731V → M in CAA70889. (PubMed:9312026)Curated
    Sequence conflicti334 – 3341F → S in BAG63326. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 131131MDFPQ…ALATE → MMCWPWPLSSKCRTSSRPAM PSSHLLSRLPALGEMRRPWP QKVCPVPSP in isoform 3. 1 PublicationVSP_044564Add
    BLAST
    Alternative sequencei679 – 6791T → TGPATLPA in isoform 2. 1 PublicationVSP_013424

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09723 mRNA. Translation: CAA70889.1.
    AK301896 mRNA. Translation: BAG63326.1.
    AL034555 Genomic DNA. Translation: CAB85445.1.
    AL034555 Genomic DNA. Translation: CAI19524.1.
    AL355994 Genomic DNA. No translation available.
    BC126163 mRNA. Translation: AAI26164.1.
    BC143965 mRNA. Translation: AAI43966.1.
    M88369 Genomic DNA. Translation: AAA61327.1.
    U20647 mRNA. Translation: AAC50256.1.
    CCDSiCCDS165.1. [Q13105-1]
    CCDS55576.1. [Q13105-3]
    PIRiD45193.
    I38940.
    RefSeqiNP_001229813.1. NM_001242884.1. [Q13105-3]
    NP_001274532.1. NM_001287603.1. [Q13105-2]
    NP_003434.2. NM_003443.2. [Q13105-1]
    UniGeneiHs.433764.

    Genome annotation databases

    EnsembliENST00000375733; ENSP00000364885; ENSG00000116809. [Q13105-2]
    ENST00000375743; ENSP00000364895; ENSG00000116809. [Q13105-1]
    ENST00000537142; ENSP00000438529; ENSG00000116809. [Q13105-3]
    GeneIDi7709.
    KEGGihsa:7709.
    UCSCiuc001axl.4. human. [Q13105-1]
    uc010obr.2. human. [Q13105-2]

    Polymorphism databases

    DMDMi62906906.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09723 mRNA. Translation: CAA70889.1 .
    AK301896 mRNA. Translation: BAG63326.1 .
    AL034555 Genomic DNA. Translation: CAB85445.1 .
    AL034555 Genomic DNA. Translation: CAI19524.1 .
    AL355994 Genomic DNA. No translation available.
    BC126163 mRNA. Translation: AAI26164.1 .
    BC143965 mRNA. Translation: AAI43966.1 .
    M88369 Genomic DNA. Translation: AAA61327.1 .
    U20647 mRNA. Translation: AAC50256.1 .
    CCDSi CCDS165.1. [Q13105-1 ]
    CCDS55576.1. [Q13105-3 ]
    PIRi D45193.
    I38940.
    RefSeqi NP_001229813.1. NM_001242884.1. [Q13105-3 ]
    NP_001274532.1. NM_001287603.1. [Q13105-2 ]
    NP_003434.2. NM_003443.2. [Q13105-1 ]
    UniGenei Hs.433764.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LVR NMR - A 500-528 [» ]
    2LVT NMR - A 528-556 [» ]
    2LVU NMR - A 556-581 [» ]
    2M0D NMR - A 416-444 [» ]
    2M0E NMR - A 444-472 [» ]
    2M0F NMR - A 472-500 [» ]
    2Q81 X-ray 2.10 A/B/C/D 2-115 [» ]
    3M52 X-ray 2.59 A/B 1-115 [» ]
    ProteinModelPortali Q13105.
    SMRi Q13105. Positions 1-115, 303-776.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113503. 18 interactions.
    DIPi DIP-5968N.
    IntActi Q13105. 9 interactions.
    MINTi MINT-1527698.
    STRINGi 9606.ENSP00000364895.

    PTM databases

    PhosphoSitei Q13105.

    Polymorphism databases

    DMDMi 62906906.

    Proteomic databases

    MaxQBi Q13105.
    PaxDbi Q13105.
    PRIDEi Q13105.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375733 ; ENSP00000364885 ; ENSG00000116809 . [Q13105-2 ]
    ENST00000375743 ; ENSP00000364895 ; ENSG00000116809 . [Q13105-1 ]
    ENST00000537142 ; ENSP00000438529 ; ENSG00000116809 . [Q13105-3 ]
    GeneIDi 7709.
    KEGGi hsa:7709.
    UCSCi uc001axl.4. human. [Q13105-1 ]
    uc010obr.2. human. [Q13105-2 ]

    Organism-specific databases

    CTDi 7709.
    GeneCardsi GC01M016268.
    HGNCi HGNC:12936. ZBTB17.
    HPAi HPA005789.
    MIMi 604084. gene.
    neXtProti NX_Q13105.
    PharmGKBi PA37522.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000231298.
    HOVERGENi HBG054919.
    KOi K10500.
    OMAi CDSCGDK.
    OrthoDBi EOG7KSX7Q.
    PhylomeDBi Q13105.
    TreeFami TF332047.

    Enzyme and pathway databases

    Reactomei REACT_18273. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi ZBTB17. human.
    EvolutionaryTracei Q13105.
    GeneWikii ZBTB17.
    GenomeRNAii 7709.
    NextBioi 29884.
    PROi Q13105.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13105.
    Bgeei Q13105.
    CleanExi HS_ZBTB17.
    Genevestigatori Q13105.

    Family and domain databases

    Gene3Di 3.30.160.60. 13 hits.
    3.30.710.10. 1 hit.
    InterProi IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00651. BTB. 1 hit.
    [Graphical view ]
    SMARTi SM00225. BTB. 1 hit.
    SM00355. ZnF_C2H2. 13 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 13 hits.
    PS50157. ZINC_FINGER_C2H2_2. 13 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYC.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    5. "Clustering of C2-H2 zinc finger motif sequences within telomeric and fragile site regions of human chromosomes."
      Lichter P., Bray P., Ried T., Dawid I.B., Ward D.C.
      Genomics 13:999-1007(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-342.
      Tissue: Placenta.
    6. "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs identify putative candidate genes for developmental and malignant disorders."
      Tommerup N., Vissing H.
      Genomics 27:259-264(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 580-803 (ISOFORM 1).
      Tissue: Insulinoma.
    7. "Association of Myc with the zinc-finger protein Miz-1 defines a novel pathway for gene regulation by Myc."
      Schneider A., Peukert K., Eilers M., Haenel F.
      Curr. Top. Microbiol. Immunol. 224:137-146(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Tissue: Cervix carcinoma.
    8. "Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1."
      Piluso D., Bilan P., Capone J.P.
      J. Biol. Chem. 277:46799-46808(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCFC1.
    9. "Myc represses differentiation-induced p21CIP1 expression via Miz-1-dependent interaction with the p21 core promoter."
      Wu S., Cetinkaya C., Munoz-Alonso M.J., von der Lehr N., Bahram F., Beuger V., Eilers M., Leon J., Larsson L.-G.
      Oncogene 22:351-360(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYC.
    10. "A cleaved form of MAGE-A4 binds to Miz-1 and induces apoptosis in human cells."
      Sakurai T., Itoh K., Higashitsuji H., Nagao T., Nonoguchi K., Chiba T., Fujita J.
      J. Biol. Chem. 279:15505-15514(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAGEA4, SUBCELLULAR LOCATION.
    11. "Induction of G1 cell cycle arrest and P15INK4b expression by ECRG1 through interaction with Miz-1."
      Zhao N., Wang J., Cui Y., Guo L., Lu S.-H.
      J. Cell. Biochem. 92:65-76(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMPRSS11A.
    12. "BCL6 interacts with the transcription factor Miz-1 to suppress the cyclin-dependent kinase inhibitor p21 and cell cycle arrest in germinal center B cells."
      Phan R.T., Saito M., Basso K., Niu H., Dalla-Favera R.
      Nat. Immunol. 6:1054-1060(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL CYCLE ARREST, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
    13. "Gfi-1 represses CDKN2B encoding p15INK4B through interaction with Miz-1."
      Basu S., Liu Q., Qiu Y., Dong F.
      Proc. Natl. Acad. Sci. U.S.A. 106:1433-1438(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "A beta-sheet interaction interface directs the tetramerisation of the Miz-1 POZ domain."
      Stead M.A., Trinh C.H., Garnett J.A., Carr S.B., Baron A.J., Edwards T.A., Wright S.C.
      J. Mol. Biol. 373:820-826(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-115, SUBUNIT.

    Entry informationi

    Entry nameiZBT17_HUMAN
    AccessioniPrimary (citable) accession number: Q13105
    Secondary accession number(s): A0AV07
    , B4DXB4, B7ZLQ9, F5H411, Q15932, Q5JYB2, Q9NUC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 153 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3