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Protein

Zinc finger and BTB domain-containing protein 1

Gene

Zbtb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional repressor (By similarity). Represses cAMP-responsive element (CRE)-mediated transcriptional activation (By similarity). In addition, has a role in translesion DNA synthesis. Requires for UV-inducible RAD18 loading, PCNA monoubiquitination, POLH recruitment to replication factories and efficient translesion DNA synthesis (By similarity). Plays a key role in the transcriptional regulation of T lymphocyte development (PubMed:22201126, PubMed:22753936).By similarity2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri216 – 24227C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri448 – 47023C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri533 – 55826UBZ-typeBy similarityAdd
BLAST
Zinc fingeri578 – 60023C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri606 – 62823C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri634 – 65623C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri662 – 68423C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri686 – 70924C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • B cell differentiation Source: MGI
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to UV Source: MGI
  • chromatin remodeling Source: UniProtKB
  • DNA repair Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • mRNA transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of natural killer cell differentiation Source: UniProtKB
  • positive regulation of pro-T cell differentiation Source: UniProtKB
  • positive regulation of T cell differentiation Source: UniProtKB
  • positive regulation of T cell mediated immunity Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • T cell differentiation in thymus Source: MGI
  • thymus development Source: UniProtKB
  • translesion synthesis Source: UniProtKB
Complete GO annotation...

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2442326. Zbtb1.

Subcellular locationi

  • Nucleus By similarity
  • Nucleusnucleoplasm By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Thymus of embryos show a small number of T-cell progenitors that are unable to progress through thymic differentiation. Adult mice show vestigial thymus and lymph nodes and a reduced spleen size. In the periphery and in the spleen, display an absence of mature T-cells, a reduced number of NK cells, but a normal number of mature B-cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Zinc finger and BTB domain-containing protein 1PRO_0000047708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki266 – 266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki276 – 276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki328 – 328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei356 – 3561PhosphothreonineCombined sources

Post-translational modificationi

Sumoylated with SUMO2 at Lys-328 and to a lesser extent at Lys-266. Sumoylation inhibits its transcriptional repression activity and regulates its subcellular localization (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91VL9.
MaxQBiQ91VL9.
PaxDbiQ91VL9.
PRIDEiQ91VL9.

PTM databases

PhosphoSiteiQ91VL9.

Expressioni

Tissue specificityi

Expressed strongly in thymus and spleen, less in lymph nodes and peripheral blood mononuclear cells (PBMCs) and weakly in bone marrow. Strongly expressed in immature, but weakly in mature bone marrow-lymphocyte B.1 Publication

Gene expression databases

BgeeiQ91VL9.
CleanExiMM_ZBTB1.
ExpressionAtlasiQ91VL9. baseline and differential.
GenevisibleiQ91VL9. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Homodimer (PubMed:22753936). Interacts (via BTB domain) with TRIM28 (unphosphorylated or phosphorylated form) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041955.

Structurei

3D structure databases

ProteinModelPortaliQ91VL9.
SMRiQ91VL9. Positions 4-146, 416-478, 533-709.
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 transcriptional repression activity. The BTB domain is also necessary for oligomerization and efficient sumoylation. The hydrophobic cluster preceding Lys-328 enhanced sumoylation efficiency (By similarity).By similarity
The UBZ-type zinc finger domain is required for targeting ZBTB1 to UV damage sites and for PCNA monoubiquitination. UBZ-type zinc finger domain mediates binding to 'Lys-63'-linked polyubiquitin chains (in vitro).By similarity

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 UBZ-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri216 – 24227C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri448 – 47023C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri533 – 55826UBZ-typeBy similarityAdd
BLAST
Zinc fingeri578 – 60023C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri606 – 62823C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri634 – 65623C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri662 – 68423C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri686 – 70924C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129682.
HOGENOMiHOG000056456.
HOVERGENiHBG057764.
InParanoidiQ91VL9.
KOiK10488.
OMAiSHYLSKH.
OrthoDBiEOG7NPFSR.
PhylomeDBiQ91VL9.
TreeFamiTF332229.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/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. 8 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]

Sequencei

Sequence statusi: Complete.

Q91VL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR
60 70 80 90 100
MFFMNHQHST AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA
110 120 130 140 150
MNYLQLYNVP DCLEDIQDAD CSSSKCSSSA SSRQSSKMIF GVRMYEDTVA
160 170 180 190 200
RNGNEANRWC AEPSSTVNTP HHREPEEESL QLANFPEPLF DVCKKSSVSK
210 220 230 240 250
LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN RHSYQNTTRA
260 270 280 290 300
YHRIVDIRDG KDSNIKAELA EKDSSKTFSA QPDKYREDAN QAPDDSASTT
310 320 330 340 350
GSRKSTVEAG IAGEEKSRAT ETKRIIIKME PEDIPADDMK DFNIIKVTEK
360 370 380 390 400
DCNESTDNDE LEDEPEEPFY RYYVEEDVGI KKSGRKTLKP RMSISVDERG
410 420 430 440 450
GLENMRPPNN TSPIQEDAEN ASCELCGLTI TEEDLSSHYL AKHIENICAC
460 470 480 490 500
GKCGQILVKG RQLQEHAQRC GEPQDLTMNG LGNADEKMDM EENPDEQSEI
510 520 530 540 550
RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG QRFETENLVV
560 570 580 590 600
EHMSSCLDQD MFKGAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH
610 620 630 640 650
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV
660 670 680 690 700
RHMISHLSGG ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD
710
MRSHYNAKHL KRT
Length:713
Mass (Da):81,952
Last modified:December 1, 2001 - v1
Checksum:i7ECD7EA1E9C88500
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti472 – 4721E → K in AAH03372 (PubMed:15489334).Curated
Sequence conflicti643 – 6431N → K in BAC26603 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029762 mRNA. Translation: BAC26603.1.
AK035036 mRNA. Translation: BAC28921.1.
AK049397 mRNA. Translation: BAC33733.1.
BC003372 mRNA. Translation: AAH03372.1.
BC012239 mRNA. Translation: AAH12239.1.
CCDSiCCDS25992.1.
RefSeqiNP_848859.1. NM_178744.2.
XP_006515958.1. XM_006515895.2.
XP_006515959.1. XM_006515896.2.
UniGeneiMm.77065.

Genome annotation databases

EnsembliENSMUST00000042779; ENSMUSP00000041955; ENSMUSG00000033454.
GeneIDi268564.
KEGGimmu:268564.
UCSCiuc007nyd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029762 mRNA. Translation: BAC26603.1.
AK035036 mRNA. Translation: BAC28921.1.
AK049397 mRNA. Translation: BAC33733.1.
BC003372 mRNA. Translation: AAH03372.1.
BC012239 mRNA. Translation: AAH12239.1.
CCDSiCCDS25992.1.
RefSeqiNP_848859.1. NM_178744.2.
XP_006515958.1. XM_006515895.2.
XP_006515959.1. XM_006515896.2.
UniGeneiMm.77065.

3D structure databases

ProteinModelPortaliQ91VL9.
SMRiQ91VL9. Positions 4-146, 416-478, 533-709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041955.

PTM databases

PhosphoSiteiQ91VL9.

Proteomic databases

EPDiQ91VL9.
MaxQBiQ91VL9.
PaxDbiQ91VL9.
PRIDEiQ91VL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042779; ENSMUSP00000041955; ENSMUSG00000033454.
GeneIDi268564.
KEGGimmu:268564.
UCSCiuc007nyd.2. mouse.

Organism-specific databases

CTDi22890.
MGIiMGI:2442326. Zbtb1.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129682.
HOGENOMiHOG000056456.
HOVERGENiHBG057764.
InParanoidiQ91VL9.
KOiK10488.
OMAiSHYLSKH.
OrthoDBiEOG7NPFSR.
PhylomeDBiQ91VL9.
TreeFamiTF332229.

Miscellaneous databases

ChiTaRSiZbtb1. mouse.
NextBioi392385.
PROiQ91VL9.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VL9.
CleanExiMM_ZBTB1.
ExpressionAtlasiQ91VL9. baseline and differential.
GenevisibleiQ91VL9. MM.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/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. 8 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. "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: Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND THR-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Spleen and Testis.
  4. "ZBTB1 is a determinant of lymphoid development."
    Siggs O.M., Li X., Xia Y., Beutler B.
    J. Exp. Med. 209:19-27(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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: FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiZBTB1_MOUSE
AccessioniPrimary (citable) accession number: Q91VL9
Secondary accession number(s): Q8CDP7, Q99LD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.