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Protein

Zinc finger and BTB domain-containing protein 1

Gene

ZBTB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional repressor (PubMed:20797634). Represses cAMP-responsive element (CRE)-mediated transcriptional activation (PubMed:21706167). 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 (PubMed:24657165). Plays a key role in the transcriptional regulation of T lymphocyte development (By similarity).By similarity3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri216 – 242C2H2-type 1; atypicalPROSITE-ProRule annotationAdd BLAST27
Zinc fingeri448 – 470C2H2-type 2; atypicalPROSITE-ProRule annotationAdd BLAST23
Zinc fingeri533 – 558UBZ-type1 PublicationAdd BLAST26
Zinc fingeri578 – 600C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri606 – 628C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri634 – 656C2H2-type 6PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri662 – 684C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri686 – 709C2H2-type 8PROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • B cell differentiation Source: Ensembl
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to UV Source: UniProtKB
  • 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: Ensembl
  • thymus development Source: UniProtKB
  • translesion synthesis Source: UniProtKB

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processDifferentiation, DNA damage, DNA repair, Immunity, Innate immunity, Transcription, Transcription regulation
LigandMetal-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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000126804.13.
HGNCiHGNC:20259. ZBTB1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi265K → R: Reduces sumoylation. Inhibits transcriptional repressive activity. Inhibits sumoylation and reduces transcriptional repressive activity; when associated with R-328. 1 Publication1
Mutagenesisi325I → S: Reduces sumoylation of Lys-328. 1
Mutagenesisi326I → N: Reduces sumoylation of Lys-328. 1
Mutagenesisi328K → R: Reduces sumoylation. Does not reduce transcriptional repressive activity. Inhibits sumoylation but does not reduce transcriptional repressive activity; when associated with R-265. 1 Publication1
Mutagenesisi536C → A: Abolishes binding to ubiquitin; Abolishes recruitment to DNA lesion sites. 1 Publication1
Mutagenesisi539C → A: Abolishes binding to ubiquitin; Abolishes recruitment to DNA lesion sites. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000126804.
PharmGKBiPA128395769.

Polymorphism and mutation databases

BioMutaiZBTB1.
DMDMi46577710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000477071 – 713Zinc finger and BTB domain-containing protein 1Add BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki3Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki303Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki316Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki340Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki346Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei355PhosphoserineCombined sources1
Modified residuei356PhosphothreonineCombined sources1
Cross-linki381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

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

EPDiQ9Y2K1.
PaxDbiQ9Y2K1.
PeptideAtlasiQ9Y2K1.
PRIDEiQ9Y2K1.

PTM databases

iPTMnetiQ9Y2K1.
PhosphoSitePlusiQ9Y2K1.

Expressioni

Gene expression databases

BgeeiENSG00000126804.
CleanExiHS_ZBTB1.
ExpressionAtlasiQ9Y2K1. baseline and differential.
GenevisibleiQ9Y2K1. HS.

Organism-specific databases

HPAiHPA050516.

Interactioni

Subunit structurei

Homodimer. Homooligomer. Isoform 1 and isoform 2 can homodimerize. Heterodimer of isoform 1 and isoform 2. Interacts (via BTB domain) with TRIM28 (unphosphorylated or phosphorylated form) (PubMed:24657165).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi116556. 105 interactors.
IntActiQ9Y2K1. 22 interactors.
MINTiMINT-7032151.
STRINGi9606.ENSP00000378201.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2K1.
SMRiQ9Y2K1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 91BTBPROSITE-ProRule annotationAdd BLAST68

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 (PubMed:20797634).1 Publication
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).1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri216 – 242C2H2-type 1; atypicalPROSITE-ProRule annotationAdd BLAST27
Zinc fingeri448 – 470C2H2-type 2; atypicalPROSITE-ProRule annotationAdd BLAST23
Zinc fingeri533 – 558UBZ-type1 PublicationAdd BLAST26
Zinc fingeri578 – 600C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri606 – 628C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri634 – 656C2H2-type 6PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri662 – 684C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri686 – 709C2H2-type 8PROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00850000132316.
HOGENOMiHOG000056456.
HOVERGENiHBG057764.
InParanoidiQ9Y2K1.
KOiK10488.
OMAiSHYLSKH.
OrthoDBiEOG091G032Z.
PhylomeDBiQ9Y2K1.
TreeFamiTF332229.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR013087. Znf_C2H2_type.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF00651. BTB. 1 hit.
SMARTiView protein in SMART
SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
SUPFAMiSSF54695. SSF54695. 1 hit.
SSF57667. SSF57667. 2 hits.
PROSITEiView protein in PROSITE
PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        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 SSKQNSKMIF GVRMYEDTVA
160 170 180 190 200
RNGNEANRWC AEPSSTVNTP HNREADEESL QLGNFPEPLF DVCKKSSVSK
210 220 230 240 250
LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN RHLYQNTRSY
260 270 280 290 300
HRIVDIRDGK DSNIKAEFGE KDSSKTFSAQ TDKYRGDTSQ AADDSASTTG
310 320 330 340 350
SRKSSTVESE IASEEKSRAA ERKRIIIKME PEDIPTDELK DFNIIKVTDK
360 370 380 390 400
DCNESTDNDE LEDEPEEPFY RYYVEEDVSI KKSGRKTLKP RMSVSADERG
410 420 430 440 450
GLENMRPPNN SSPVQEDAEN ASCELCGLTI TEEDLSSHYL AKHIENICAC
460 470 480 490 500
GKCGQILVKG RQLQEHAQRC GEPQDLTMNG LGNTEEKMDL EENPDEQSEI
510 520 530 540 550
RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG QRFETENLVV
560 570 580 590 600
EHMSSCLDQD MFKSAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH
610 620 630 640 650
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV
660 670 680 690 700
RHMISHLSAG ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD
710
MRSHYNAKHL KRT
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti203T → N in BAA76841 (PubMed:10231032).Curated1
Sequence conflicti334I → T in AAH50719 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_040976633 – 713RYVCS…HLKRT → SGEIGPSKPVEK in isoform 2. 1 PublicationAdd BLAST81

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011534868.1. XM_011536566.2. [Q9Y2K1-1]
XP_011534870.1. XM_011536568.2. [Q9Y2K1-2]
XP_016876583.1. XM_017021094.1. [Q9Y2K1-1]
XP_016876584.1. XM_017021095.1. [Q9Y2K1-1]
UniGeneiHs.605143.

Genome annotation databases

EnsembliENST00000358738; ENSP00000351587; ENSG00000126804. [Q9Y2K1-2]
ENST00000554015; ENSP00000451000; ENSG00000126804. [Q9Y2K1-1]
GeneIDi22890.
KEGGihsa:22890.
UCSCiuc001xhh.5. human. [Q9Y2K1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiZBTB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2K1
Secondary accession number(s): A8K6S8, Q86SW8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 26, 2004
Last modified: September 27, 2017
This is version 158 of the entry and version 3 of the sequence. See 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot