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Protein

Zinc finger and BTB domain-containing protein 43

Gene

ZBTB43

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri373 – 39422C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri400 – 42223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri428 – 45023C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger and BTB domain-containing protein 43
Alternative name(s):
Zinc finger and BTB domain-containing protein 22B
Zinc finger protein 297B
ZnF-x
Gene namesi
Name:ZBTB43
Synonyms:KIAA0414, ZBTB22B, ZNF297B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17908. ZBTB43.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Zinc finger and BTB domain-containing protein 43PRO_0000047519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43298.
PaxDbiO43298.
PRIDEiO43298.

PTM databases

PhosphoSiteiO43298.

Expressioni

Gene expression databases

BgeeiO43298.
CleanExiHS_ZBTB43.
ExpressionAtlasiO43298. baseline and differential.
GenevestigatoriO43298.

Organism-specific databases

HPAiHPA016825.

Interactioni

Subunit structurei

Interacts with BDP1.1 Publication

Protein-protein interaction databases

BioGridi116727. 26 interactions.
IntActiO43298. 7 interactions.
MINTiMINT-2796003.
STRINGi9606.ENSP00000362556.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi380 – 3834Combined sources
Helixi384 – 39411Combined sources
Beta strandi399 – 4013Combined sources
Turni403 – 4053Combined sources
Beta strandi408 – 4125Combined sources
Helixi413 – 4197Combined sources
Turni420 – 4223Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi436 – 4383Combined sources
Helixi440 – 45819Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSHNMR-A370-466[»]
ProteinModelPortaliO43298.
SMRiO43298. Positions 7-121, 367-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43298.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 9765BTBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri373 – 39422C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri400 – 42223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri428 – 45023C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000231975.
HOVERGENiHBG056510.
InParanoidiO43298.
KOiK10514.
OMAiTESINTM.
OrthoDBiEOG7Q8CN4.
PhylomeDBiO43298.
TreeFamiTF333162.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O43298-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEPGTNSFRV EFPDFSSTIL QKLNQQRQQG QLCDVSIVVQ GHIFRAHKAV
60 70 80 90 100
LAASSPYFCD QVLLKNSRRI VLPDVMNPRV FENILLSSYT GRLVMPAPEI
110 120 130 140 150
VSYLTAASFL QMWHVVDKCT EVLEGNPTVL CQKLNHGSDH QSPSSSSYNG
160 170 180 190 200
LVESFELGSG GHTDFPKAQE LRDGENEEES TKDELSSQLT EHEYLPSNSS
210 220 230 240 250
TEHDRLSTEM ASQDGEEGAS DSAEFHYTRP MYSKPSIMAH KRWIHVKPER
260 270 280 290 300
LEQACEGMDV HATYDEHQVT ESINTVQTEH TVQPSGVEED FHIGEKKVEA
310 320 330 340 350
EFDEQADESN YDEQVDFYGS SMEEFSGERS DGNLIGHRQE AALAAGYSEN
360 370 380 390 400
IEMVTGIKEE ASHLGFSATD KLYPCQCGKS FTHKSQRDRH MSMHLGLRPY
410 420 430 440 450
GCGVCGKKFK MKHHLVGHMK IHTGIKPYEC NICAKRFMWR DSFHRHVTSC
460
TKSYEAAKAE QNTTEAN
Length:467
Mass (Da):52,630
Last modified:June 1, 1998 - v1
Checksum:i9DFB6CEEB8562425
GO

Sequence cautioni

The sequence BAA24844.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007874 mRNA. Translation: BAA24844.2. Different initiation.
AF049907 mRNA. Translation: AAC05500.1.
BT007194 mRNA. Translation: AAP35858.1.
AL161731 Genomic DNA. Translation: CAI40920.1.
CH471090 Genomic DNA. Translation: EAW87643.1.
BC008828 mRNA. Translation: AAH08828.1.
CCDSiCCDS6867.1.
RefSeqiNP_001129248.1. NM_001135776.1.
NP_054726.1. NM_014007.3.
XP_005251892.1. XM_005251835.1.
XP_005251893.1. XM_005251836.1.
UniGeneiHs.355581.

Genome annotation databases

EnsembliENST00000373457; ENSP00000362556; ENSG00000169155.
ENST00000373464; ENSP00000362563; ENSG00000169155.
ENST00000449886; ENSP00000390344; ENSG00000169155.
GeneIDi23099.
KEGGihsa:23099.
UCSCiuc004bql.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007874 mRNA. Translation: BAA24844.2. Different initiation.
AF049907 mRNA. Translation: AAC05500.1.
BT007194 mRNA. Translation: AAP35858.1.
AL161731 Genomic DNA. Translation: CAI40920.1.
CH471090 Genomic DNA. Translation: EAW87643.1.
BC008828 mRNA. Translation: AAH08828.1.
CCDSiCCDS6867.1.
RefSeqiNP_001129248.1. NM_001135776.1.
NP_054726.1. NM_014007.3.
XP_005251892.1. XM_005251835.1.
XP_005251893.1. XM_005251836.1.
UniGeneiHs.355581.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSHNMR-A370-466[»]
ProteinModelPortaliO43298.
SMRiO43298. Positions 7-121, 367-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116727. 26 interactions.
IntActiO43298. 7 interactions.
MINTiMINT-2796003.
STRINGi9606.ENSP00000362556.

PTM databases

PhosphoSiteiO43298.

Proteomic databases

MaxQBiO43298.
PaxDbiO43298.
PRIDEiO43298.

Protocols and materials databases

DNASUi23099.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373457; ENSP00000362556; ENSG00000169155.
ENST00000373464; ENSP00000362563; ENSG00000169155.
ENST00000449886; ENSP00000390344; ENSG00000169155.
GeneIDi23099.
KEGGihsa:23099.
UCSCiuc004bql.3. human.

Organism-specific databases

CTDi23099.
GeneCardsiGC09P129567.
HGNCiHGNC:17908. ZBTB43.
HPAiHPA016825.
neXtProtiNX_O43298.
PharmGKBiPA38257.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000231975.
HOVERGENiHBG056510.
InParanoidiO43298.
KOiK10514.
OMAiTESINTM.
OrthoDBiEOG7Q8CN4.
PhylomeDBiO43298.
TreeFamiTF333162.

Miscellaneous databases

ChiTaRSiZBTB43. human.
EvolutionaryTraceiO43298.
GenomeRNAii23099.
NextBioi44277.
PROiO43298.

Gene expression databases

BgeeiO43298.
CleanExiHS_ZBTB43.
ExpressionAtlasiO43298. baseline and differential.
GenevestigatoriO43298.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. Zhang X., Liu C.-X., Lisitsina M.N., Musco S., Lisitsyn N.A.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Muscle.
  7. "The zinc finger protein ZNF297B interacts with BDP1, a subunit of TFIIIB."
    Schoenen F., Wirth B.
    Biol. Chem. 387:277-284(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BDP1.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Solution structure of tandem repeat of the ZF-C2H2 domains of human zinc finger protein 297B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 370-466.

Entry informationi

Entry nameiZBT43_HUMAN
AccessioniPrimary (citable) accession number: O43298
Secondary accession number(s): Q5JU96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 1998
Last modified: February 4, 2015
This is version 135 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.