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Q99592 (ZBT18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ZBTB18
Synonyms:RP58, TAZ1, ZNF238
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Subunit structure

Interacts with DNMT3A. Ref.8

Subcellular location

Nucleus. Note: Associates with condensed chromatin.

Tissue specificity

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily.

Contains 1 BTB (POZ) domain.

Contains 4 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcerebellum development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

neuron development

Inferred from electronic annotation. Source: Ensembl

regulation of cell division

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintercellular bridge

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nuclear chromosome

Traceable author statement Ref.2. Source: ProtInc

nucleus

Traceable author statement PubMed 9013868. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 9013868. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from direct assay Ref.2. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.2PubMed 9770450. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99592-1)

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.
Isoform 2 (identifier: Q99592-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Zinc finger and BTB domain-containing protein 18
PRO_0000047477

Regions

Domain24 – 9168BTB
Zinc finger370 – 39223C2H2-type 1
Zinc finger410 – 43223C2H2-type 2
Zinc finger438 – 46023C2H2-type 3
Zinc finger466 – 48924C2H2-type 4
Region310 – 427118Interaction with DNMT3A

Amino acid modifications

Modified residue5161Phosphoserine Ref.9
Modified residue5171Phosphoserine Ref.9

Natural variations

Alternative sequence11M → MCPKGYEDSM in isoform 2.
VSP_035381
Natural variant1321E → G. Ref.1
Corresponds to variant rs1048824 [ dbSNP | Ensembl ].
VAR_012768

Experimental info

Sequence conflict511L → I in AAH36677. Ref.6
Sequence conflict166 – 26297KLNIL…YFSSQ → IEHPAQQKGLGGRAWEHVDA IALRLSRHPPGWRRGRATRH SSWKNSSQPLQLNRVFVPE in AAA81368. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: DE024B66E02DCE75

FASTA52258,354
        10         20         30         40         50         60 
MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR 

        70         80         90        100        110        120 
DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK 

       130        140        150        160        170        180 
ATTEADSTKK EEDASSCSDK VESLSDGSSH IAGDLPSDED EGEDEKLNIL PSKRDLAAEP 

       190        200        210        220        230        240 
GNMWMRLPSD SAGIPQAGGE AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL 

       250        260        270        280        290        300 
DLSVKSSLSG VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES 

       310        320        330        340        350        360 
VSTNNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG MESSLLPYVS 

       370        380        390        400        410        420 
NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR SKPAADVNVP TCSLCGKTFS 

       430        440        450        460        470        480 
CMYTLKRHER THSGEKPYTC TQCGKSFQYS HNLSRHAVVH TREKPHACKW CERRFTQSGD 

       490        500        510        520 
LYRHIRKFHC ELVNSLSVKS EALSLPTVRD WTLEDSSQEL WK 

« Hide

Isoform 2 [UniParc].

Checksum: EA03FF68F0FD4668
Show »

FASTA53159,366

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1622.1. [Q99592-2]
PIRI39200.
RefSeqNP_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]
UniGeneHs.69997.

3D structure databases

ProteinModelPortalQ99592.
SMRQ99592. Positions 2-113, 370-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115735. 7 interactions.
IntActQ99592. 3 interactions.
STRING9606.ENSP00000351539.

PTM databases

PhosphoSiteQ99592.

Polymorphism databases

DMDM20141020.

Proteomic databases

PaxDbQ99592.
PRIDEQ99592.

Protocols and materials databases

DNASU10472.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358704; ENSP00000351539; ENSG00000179456. [Q99592-2]
GeneID10472.
KEGGhsa:10472.
UCSCuc001iad.5. human. [Q99592-2]
uc001iae.4. human. [Q99592-1]

Organism-specific databases

CTD10472.
GeneCardsGC01P244216.
HGNCHGNC:13030. ZBTB18.
HPAHPA044652.
MIM608433. gene.
612337. phenotype.
neXtProtNX_Q99592.
Orphanet36367. Distal monosomy 1q.
PharmGKBPA37608.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000234147.
HOVERGENHBG059113.
InParanoidQ99592.
OMAGGEAETH.
OrthoDBEOG73FQM8.
PhylomeDBQ99592.
TreeFamTF337437.

Enzyme and pathway databases

SignaLinkQ99592.

Gene expression databases

BgeeQ99592.
CleanExHS_ZNF238.
GenevestigatorQ99592.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
3.30.710.10. 1 hit.
InterProIPR000210. 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]
PfamPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 4 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZNF238. human.
GeneWikiZNF238.
GenomeRNAi10472.
NextBio39714.
PROQ99592.
SOURCESearch...

Entry information

Entry nameZBT18_HUMAN
AccessionPrimary (citable) accession number: Q99592
Secondary accession number(s): A8K5U3 expand/collapse secondary AC list , Q13397, Q5VU40, Q8N463, Q9UD99
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM