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Q9Y2K1

- ZBTB1_HUMAN

UniProt

Q9Y2K1 - ZBTB1_HUMAN

Protein

Zinc finger and BTB domain-containing protein 1

Gene

ZBTB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (26 Apr 2004)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional repressor. Represses cAMP-responsive element (CRE)-mediated transcriptional activation. Involved in lymphoid lineage commitment and differentiation. Plays a key role in the instruction of early lymphoid progenitors to develop into T-cell lineage.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri216 – 23823C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri448 – 47023C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri534 – 55623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri578 – 60023C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri606 – 62823C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri634 – 65623C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri662 – 68423C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri686 – 70924C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein heterodimerization activity Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: Ensembl
    2. innate immune response Source: UniProtKB-KW
    3. mRNA transcription from RNA polymerase II promoter Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. positive regulation of natural killer cell differentiation Source: UniProtKB
    6. positive regulation of pro-T cell differentiation Source: UniProtKB
    7. positive regulation of T cell differentiation Source: UniProtKB
    8. positive regulation of T cell mediated immunity Source: UniProtKB
    9. protein homooligomerization Source: UniProtKB
    10. T cell differentiation in thymus Source: Ensembl
    11. thymus development Source: UniProtKB

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Differentiation, Immunity, Innate immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger and BTB domain-containing protein 1
    Gene namesi
    Name:ZBTB1
    Synonyms:KIAA0997
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20259. ZBTB1.

    Subcellular locationi

    Nucleus. Nucleusnucleoplasm
    Note: Localized in dot-like structures in the nucleus. Colocalized with SMRT in nuclear bodies. The sumoylated form is preferentially located in the nucleoplasm outside the nuclear bodies.

    GO - Cellular componenti

    1. nuclear body Source: UniProtKB
    2. nucleoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi265 – 2651K → R: Reduces sumoylation. Inhibits transcriptional repressive activity. Inhibits sumoylation and reduces transcriptional repressive activity; when associated with R-328. 1 Publication
    Mutagenesisi325 – 3251I → S: Reduces sumoylation of Lys-328.
    Mutagenesisi326 – 3261I → N: Reduces sumoylation of Lys-328.
    Mutagenesisi328 – 3281K → R: Reduces sumoylation. Does not reduce transcriptional repressive activity. Inhibits sumoylation but does not reduce transcriptional repressive activity; when associated with R-265. 1 Publication

    Organism-specific databases

    PharmGKBiPA128395769.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 713713Zinc finger and BTB domain-containing protein 1PRO_0000047707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki265 – 265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
    Cross-linki328 – 328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
    Modified residuei355 – 3551Phosphoserine1 Publication
    Modified residuei356 – 3561Phosphothreonine1 Publication

    Post-translational modificationi

    Sumoylated with SUMO2 at Lys-328 and to a lesser extent at Lys-265. Sumoylation inhibits its transcriptional repression activity and regulates its subcellular localization.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y2K1.
    PaxDbiQ9Y2K1.
    PRIDEiQ9Y2K1.

    PTM databases

    PhosphoSiteiQ9Y2K1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2K1.
    BgeeiQ9Y2K1.
    CleanExiHS_ZBTB1.
    GenevestigatoriQ9Y2K1.

    Organism-specific databases

    HPAiHPA050516.
    HPA054552.

    Interactioni

    Subunit structurei

    Homodimer. Homooligomer. Isoform 1 and isoform 2 can homodimerize. Heterodimer of isoform 1 and isoform 2.2 Publications

    Protein-protein interaction databases

    BioGridi116556. 86 interactions.
    IntActiQ9Y2K1. 6 interactions.
    MINTiMINT-7032151.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2K1.
    SMRiQ9Y2K1. Positions 4-109, 410-479, 533-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Domaini

    Both the BTB domain and C2H2-type motifs are necessary for transriptional repression activity. The BTB domain is also necessary for oligomerization and efficient sumoylation. The hydrophobic cluster preceding Lys-328 enhanced sumoylation efficiency (PubMed:20797634).1 Publication

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 8 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri216 – 23823C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri448 – 47023C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri534 – 55623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri578 – 60023C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri606 – 62823C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri634 – 65623C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri662 – 68423C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri686 – 70924C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG277648.
    HOGENOMiHOG000056456.
    HOVERGENiHBG057764.
    InParanoidiQ9Y2K1.
    KOiK10488.
    OMAiCTNRHSY.
    OrthoDBiEOG7NPFSR.
    PhylomeDBiQ9Y2K1.
    TreeFamiTF332229.

    Family and domain databases

    Gene3Di3.30.160.60. 2 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. 8 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2K1-1) [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

    MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR    50
    MFFMNHQHST AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA 100
    MNYLQLYNVP DCLEDIQDAD CSSSKCSSSA SSKQNSKMIF GVRMYEDTVA 150
    RNGNEANRWC AEPSSTVNTP HNREADEESL QLGNFPEPLF DVCKKSSVSK 200
    LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN RHLYQNTRSY 250
    HRIVDIRDGK DSNIKAEFGE KDSSKTFSAQ TDKYRGDTSQ AADDSASTTG 300
    SRKSSTVESE IASEEKSRAA ERKRIIIKME PEDIPTDELK DFNIIKVTDK 350
    DCNESTDNDE LEDEPEEPFY RYYVEEDVSI KKSGRKTLKP RMSVSADERG 400
    GLENMRPPNN SSPVQEDAEN ASCELCGLTI TEEDLSSHYL AKHIENICAC 450
    GKCGQILVKG RQLQEHAQRC GEPQDLTMNG LGNTEEKMDL EENPDEQSEI 500
    RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG QRFETENLVV 550
    EHMSSCLDQD MFKSAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH 600
    TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV 650
    RHMISHLSAG ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD 700
    MRSHYNAKHL KRT 713
    Length:713
    Mass (Da):82,016
    Last modified:April 26, 2004 - v3
    Checksum:i4B120DD45FA14305
    GO
    Isoform 2 (identifier: Q9Y2K1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         633-713: RYVCSICDQG...HYNAKHLKRT → SGEIGPSKPVEK

    Show »
    Length:644
    Mass (Da):73,682
    Checksum:i122AD0D3D565098F
    GO

    Sequence cautioni

    The sequence BAA76841.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti203 – 2031T → N in BAA76841. (PubMed:10231032)Curated
    Sequence conflicti334 – 3341I → T in AAH50719. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei633 – 71381RYVCS…HLKRT → SGEIGPSKPVEK in isoform 2. 1 PublicationVSP_040976Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK291743 mRNA. Translation: BAF84432.1.
    AB023214 mRNA. Translation: BAA76841.2. Different initiation.
    AL049869 Genomic DNA. No translation available.
    BC050719 mRNA. Translation: AAH50719.1.
    BX248777 mRNA. Translation: CAD66584.1.
    CCDSiCCDS32097.1. [Q9Y2K1-2]
    CCDS45126.1. [Q9Y2K1-1]
    RefSeqiNP_001116801.1. NM_001123329.1. [Q9Y2K1-1]
    NP_055765.2. NM_014950.2. [Q9Y2K1-2]
    XP_005267467.1. XM_005267410.1. [Q9Y2K1-1]
    XP_005267468.1. XM_005267411.2. [Q9Y2K1-1]
    UniGeneiHs.605143.

    Genome annotation databases

    EnsembliENST00000358738; ENSP00000351587; ENSG00000126804. [Q9Y2K1-2]
    ENST00000554015; ENSP00000451000; ENSG00000126804. [Q9Y2K1-1]
    GeneIDi22890.
    KEGGihsa:22890.
    UCSCiuc001xhh.4. human. [Q9Y2K1-1]
    uc001xhi.2. human. [Q9Y2K1-2]

    Polymorphism databases

    DMDMi46577710.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK291743 mRNA. Translation: BAF84432.1 .
    AB023214 mRNA. Translation: BAA76841.2 . Different initiation.
    AL049869 Genomic DNA. No translation available.
    BC050719 mRNA. Translation: AAH50719.1 .
    BX248777 mRNA. Translation: CAD66584.1 .
    CCDSi CCDS32097.1. [Q9Y2K1-2 ]
    CCDS45126.1. [Q9Y2K1-1 ]
    RefSeqi NP_001116801.1. NM_001123329.1. [Q9Y2K1-1 ]
    NP_055765.2. NM_014950.2. [Q9Y2K1-2 ]
    XP_005267467.1. XM_005267410.1. [Q9Y2K1-1 ]
    XP_005267468.1. XM_005267411.2. [Q9Y2K1-1 ]
    UniGenei Hs.605143.

    3D structure databases

    ProteinModelPortali Q9Y2K1.
    SMRi Q9Y2K1. Positions 4-109, 410-479, 533-712.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116556. 86 interactions.
    IntActi Q9Y2K1. 6 interactions.
    MINTi MINT-7032151.

    PTM databases

    PhosphoSitei Q9Y2K1.

    Polymorphism databases

    DMDMi 46577710.

    Proteomic databases

    MaxQBi Q9Y2K1.
    PaxDbi Q9Y2K1.
    PRIDEi Q9Y2K1.

    Protocols and materials databases

    DNASUi 22890.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358738 ; ENSP00000351587 ; ENSG00000126804 . [Q9Y2K1-2 ]
    ENST00000554015 ; ENSP00000451000 ; ENSG00000126804 . [Q9Y2K1-1 ]
    GeneIDi 22890.
    KEGGi hsa:22890.
    UCSCi uc001xhh.4. human. [Q9Y2K1-1 ]
    uc001xhi.2. human. [Q9Y2K1-2 ]

    Organism-specific databases

    CTDi 22890.
    GeneCardsi GC14P064971.
    H-InvDB HIX0011734.
    HGNCi HGNC:20259. ZBTB1.
    HPAi HPA050516.
    HPA054552.
    neXtProti NX_Q9Y2K1.
    PharmGKBi PA128395769.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277648.
    HOGENOMi HOG000056456.
    HOVERGENi HBG057764.
    InParanoidi Q9Y2K1.
    KOi K10488.
    OMAi CTNRHSY.
    OrthoDBi EOG7NPFSR.
    PhylomeDBi Q9Y2K1.
    TreeFami TF332229.

    Miscellaneous databases

    ChiTaRSi ZBTB1. human.
    GenomeRNAii 22890.
    NextBioi 43493.
    PROi Q9Y2K1.

    Gene expression databases

    ArrayExpressi Q9Y2K1.
    Bgeei Q9Y2K1.
    CleanExi HS_ZBTB1.
    Genevestigatori Q9Y2K1.

    Family and domain databases

    Gene3Di 3.30.160.60. 2 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. 8 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. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 1).
      Tissue: Placenta.
    2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [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] (ISOFORM 1).
      Tissue: Eye.
    5. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-417.
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND THR-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif."
      Matic I., Schimmel J., Hendriks I.A., van Santen M.A., van de Rijke F., van Dam H., Gnad F., Mann M., Vertegaal A.C.
      Mol. Cell 39:641-652(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUMOYLATION AT LYS-265 AND LYS-328, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-265 AND LYS-328, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Novel human BTB/POZ domain-containing zinc finger protein ZBTB1 inhibits transcriptional activities of CRE."
      Liu Q., Yao F., Wang M., Zhou B., Cheng H., Wang W., Jin L., Lin Q., Wang J.C.
      Mol. Cell. Biochem. 357:405-414(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Transcription factor zinc finger and BTB domain 1 is essential for lymphocyte development."
      Punwani D., Simon K., Choi Y., Dutra A., Gonzalez-Espinosa D., Pak E., Naradikian M., Song C.H., Zhang J., Bodine D.M., Puck J.M.
      J. Immunol. 189:1253-1264(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiZBTB1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2K1
    Secondary accession number(s): A8K6S8, Q86SW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 129 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3