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Q99592

- ZBT18_HUMAN

UniProt

Q99592 - ZBT18_HUMAN

Protein

Zinc finger and BTB domain-containing protein 18

Gene

ZBTB18

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 139 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Transcriptional repressor that plays a role in various developmental processes such as myogenesis and brain development. Plays a key role in myogenesis by directly repressing the expression of ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in controlling cell division of progenitor cells and regulating the survival of postmitotic cortical neurons. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. May also play a role in the organization of chromosomes in the nucleus.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri370 – 39223C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri410 – 43223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri438 – 46023C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri466 – 48924C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cerebellum development Source: Ensembl
    2. cerebral cortex development Source: Ensembl
    3. hippocampus development Source: Ensembl
    4. homeostasis of number of cells Source: Ensembl
    5. in utero embryonic development Source: Ensembl
    6. negative regulation of transcription, DNA-templated Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. neuron development Source: Ensembl
    9. regulation of cell division Source: Ensembl
    10. skeletal muscle tissue development Source: UniProtKB
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ99592.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger and BTB domain-containing protein 18
    Alternative name(s):
    58 kDa repressor protein
    Transcriptional repressor RP58
    Translin-associated zinc finger protein 1
    Short name:
    TAZ-1
    Zinc finger protein 238
    Zinc finger protein C2H2-171
    Gene namesi
    Name:ZBTB18
    Synonyms:RP58, TAZ1, ZNF238
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:13030. ZBTB18.

    Subcellular locationi

    Nucleus
    Note: Associates with condensed chromatin.

    GO - Cellular componenti

    1. intercellular bridge Source: HPA
    2. microtubule cytoskeleton Source: HPA
    3. nuclear chromosome Source: ProtInc
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal dominant 22 (MRD22) [MIM:612337]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Additional MRD22 patients have limited or no speech, and variable but characteristic facial features, including round face, prominent forehead, flat nasal bridge, hypertelorism, epicanthal folds, and low-set ears. Other features may include hypotonia, poor growth, microcephaly, agenesis of the corpus callosum, and seizures.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi612337. phenotype.
    Orphaneti36367. Distal monosomy 1q.
    PharmGKBiPA37608.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522Zinc finger and BTB domain-containing protein 18PRO_0000047477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei516 – 5161Phosphoserine1 Publication
    Modified residuei517 – 5171Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ99592.
    PRIDEiQ99592.

    PTM databases

    PhosphoSiteiQ99592.

    Expressioni

    Tissue specificityi

    Lymphoid tissues, testis, heart, brain, skeletal muscle, and pancreas and, at much lower level, other tissues.

    Gene expression databases

    BgeeiQ99592.
    CleanExiHS_ZNF238.
    GenevestigatoriQ99592.

    Organism-specific databases

    HPAiHPA044652.

    Interactioni

    Subunit structurei

    Interacts with DNMT3A.1 Publication

    Protein-protein interaction databases

    BioGridi115735. 7 interactions.
    IntActiQ99592. 3 interactions.
    STRINGi9606.ENSP00000351539.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99592.
    SMRiQ99592. Positions 2-113, 370-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 9168BTBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni310 – 427118Interaction with DNMT3AAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri370 – 39223C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri410 – 43223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri438 – 46023C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri466 – 48924C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000234147.
    HOVERGENiHBG059113.
    InParanoidiQ99592.
    OMAiGGEAETH.
    OrthoDBiEOG73FQM8.
    PhylomeDBiQ99592.
    TreeFamiTF337437.

    Family and domain databases

    Gene3Di3.30.160.60. 3 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.
    PF00096. zf-C2H2. 1 hit.
    [Graphical view]
    SMARTiSM00225. BTB. 1 hit.
    SM00355. ZnF_C2H2. 4 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99592-1) [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

    MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH    50
    LFYKDQLDKR DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA 100
    ASYLHMYDIV KVCKKKLKEK ATTEADSTKK EEDASSCSDK VESLSDGSSH 150
    IAGDLPSDED EGEDEKLNIL PSKRDLAAEP GNMWMRLPSD SAGIPQAGGE 200
    AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL DLSVKSSLSG 250
    VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES 300
    VSTNNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG 350
    MESSLLPYVS NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR 400
    SKPAADVNVP TCSLCGKTFS CMYTLKRHER THSGEKPYTC TQCGKSFQYS 450
    HNLSRHAVVH TREKPHACKW CERRFTQSGD LYRHIRKFHC ELVNSLSVKS 500
    EALSLPTVRD WTLEDSSQEL WK 522
    Length:522
    Mass (Da):58,354
    Last modified:May 1, 1997 - v1
    Checksum:iDE024B66E02DCE75
    GO
    Isoform 2 (identifier: Q99592-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MCPKGYEDSM

    Show »
    Length:531
    Mass (Da):59,366
    Checksum:iEA03FF68F0FD4668
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511L → I in AAH36677. (PubMed:15489334)Curated
    Sequence conflicti166 – 26297KLNIL…YFSSQ → IEHPAQQKGLGGRAWEHVDA IALRLSRHPPGWRRGRATRH SSWKNSSQPLQLNRVFVPE in AAA81368. (PubMed:7633419)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321E → G.1 Publication
    Corresponds to variant rs1048824 [ dbSNP | Ensembl ].
    VAR_012768

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MCPKGYEDSM in isoform 2. 2 PublicationsVSP_035381

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38896 mRNA. Translation: AAA81368.1.
    X95072 mRNA. Translation: CAA64468.1.
    AJ001388 mRNA. Translation: CAA04718.1.
    AJ223321 Genomic DNA. Translation: CAA11262.1.
    AK291408 mRNA. Translation: BAF84097.1.
    AL590483 Genomic DNA. Translation: CAH71954.2.
    BC036677 mRNA. Translation: AAH36677.2.
    CCDSiCCDS1622.1. [Q99592-2]
    PIRiI39200.
    RefSeqiNP_001265125.1. NM_001278196.1. [Q99592-1]
    NP_006343.2. NM_006352.4. [Q99592-1]
    NP_991331.1. NM_205768.2. [Q99592-2]
    XP_005273063.1. XM_005273006.1. [Q99592-1]
    UniGeneiHs.69997.

    Genome annotation databases

    EnsembliENST00000358704; ENSP00000351539; ENSG00000179456. [Q99592-2]
    GeneIDi10472.
    KEGGihsa:10472.
    UCSCiuc001iad.5. human. [Q99592-2]
    uc001iae.4. human. [Q99592-1]

    Polymorphism databases

    DMDMi20141020.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38896 mRNA. Translation: AAA81368.1 .
    X95072 mRNA. Translation: CAA64468.1 .
    AJ001388 mRNA. Translation: CAA04718.1 .
    AJ223321 Genomic DNA. Translation: CAA11262.1 .
    AK291408 mRNA. Translation: BAF84097.1 .
    AL590483 Genomic DNA. Translation: CAH71954.2 .
    BC036677 mRNA. Translation: AAH36677.2 .
    CCDSi CCDS1622.1. [Q99592-2 ]
    PIRi I39200.
    RefSeqi NP_001265125.1. NM_001278196.1. [Q99592-1 ]
    NP_006343.2. NM_006352.4. [Q99592-1 ]
    NP_991331.1. NM_205768.2. [Q99592-2 ]
    XP_005273063.1. XM_005273006.1. [Q99592-1 ]
    UniGenei Hs.69997.

    3D structure databases

    ProteinModelPortali Q99592.
    SMRi Q99592. Positions 2-113, 370-486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115735. 7 interactions.
    IntActi Q99592. 3 interactions.
    STRINGi 9606.ENSP00000351539.

    PTM databases

    PhosphoSitei Q99592.

    Polymorphism databases

    DMDMi 20141020.

    Proteomic databases

    PaxDbi Q99592.
    PRIDEi Q99592.

    Protocols and materials databases

    DNASUi 10472.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358704 ; ENSP00000351539 ; ENSG00000179456 . [Q99592-2 ]
    GeneIDi 10472.
    KEGGi hsa:10472.
    UCSCi uc001iad.5. human. [Q99592-2 ]
    uc001iae.4. human. [Q99592-1 ]

    Organism-specific databases

    CTDi 10472.
    GeneCardsi GC01P244216.
    HGNCi HGNC:13030. ZBTB18.
    HPAi HPA044652.
    MIMi 608433. gene.
    612337. phenotype.
    neXtProti NX_Q99592.
    Orphaneti 36367. Distal monosomy 1q.
    PharmGKBi PA37608.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000234147.
    HOVERGENi HBG059113.
    InParanoidi Q99592.
    OMAi GGEAETH.
    OrthoDBi EOG73FQM8.
    PhylomeDBi Q99592.
    TreeFami TF337437.

    Enzyme and pathway databases

    SignaLinki Q99592.

    Miscellaneous databases

    ChiTaRSi ZNF238. human.
    GeneWikii ZNF238.
    GenomeRNAii 10472.
    NextBioi 39714.
    PROi Q99592.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99592.
    CleanExi HS_ZNF238.
    Genevestigatori Q99592.

    Family and domain databases

    Gene3Di 3.30.160.60. 3 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.
    PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    SMARTi SM00225. BTB. 1 hit.
    SM00355. ZnF_C2H2. 4 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rapid isolation and characterization of 118 novel C2H2-type zinc finger cDNAs expressed in human brain."
      Becker K.G., Nagle J.W., Canning R.D., Biddison W.E., Ozato K., Drew P.D.
      Hum. Mol. Genet. 4:685-691(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-132.
      Tissue: Hippocampus.
    2. "RP58 associates with condensed chromatin and mediates a sequence-specific transcriptional repression."
      Aoki K., Meng G., Suzuki K., Takashi T., Kameoka Y., Nakahara K., Ishida R., Kasai M.
      J. Biol. Chem. 273:26698-26704(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DNA-BINDING.
      Tissue: Spleen.
    3. "Structural analysis of the gene encoding RP58, a sequence-specific transrepressor associated with heterochromatin."
      Meng G., Inazawa J., Ishida R., Tokura K., Nakahara K., Aoki K., Kasai M.
      Gene 242:59-64(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "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 2).
      Tissue: Brain.
    5. "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].
    6. "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] (ISOFORM 2).
      Tissue: Brain.
    7. "3,400 new expressed sequence tags identify diversity of transcripts in human brain."
      Adams M.D., Kerlavage A.R., Fields C., Venter J.C.
      Nat. Genet. 4:256-267(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM 1).
      Tissue: Brain.
    8. "Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription."
      Fuks F., Burgers W.A., Godin N., Kasai M., Kouzarides T.
      EMBO J. 20:2536-2544(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMT3A.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516 AND SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "A de novo non-sense mutation in ZBTB18 in a patient with features of the 1q43q44 microdeletion syndrome."
      de Munnik S.A., Garcia-Minaur S., Hoischen A., van Bon B.W., Boycott K.M., Schoots J., Hoefsloot L.H., Knoers N.V., Bongers E.M., Brunner H.G.
      Eur. J. Hum. Genet. 22:844-846(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRD22.

    Entry informationi

    Entry nameiZBT18_HUMAN
    AccessioniPrimary (citable) accession number: Q99592
    Secondary accession number(s): A8K5U3
    , Q13397, Q5VU40, Q8N463, Q9UD99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2002
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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 1
      Human chromosome 1: 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

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