Q99592 (ZBT18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. 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.
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cerebellum development Inferred from electronic annotation. Source: Compara cerebral cortex development Inferred from electronic annotation. Source: Compara hippocampus development Inferred from electronic annotation. Source: Compara homeostasis of number of cells Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB neuron development Inferred from electronic annotation. Source: Compara regulation of cell division Inferred from electronic annotation. Source: Compara skeletal muscle tissue development Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear chromosome Traceable author statement Ref.2. Source: ProtInc
Molecular_function	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 zinc ion binding Inferred from electronic annotation. Source: InterPro
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 522	522	Zinc finger and BTB domain-containing protein 18		PRO_0000047477
Regions
	Domain	24 – 91	68	BTB
	Zinc finger	370 – 392	23	C2H2-type 1
	Zinc finger	410 – 432	23	C2H2-type 2
	Zinc finger	438 – 460	23	C2H2-type 3
	Zinc finger	466 – 489	24	C2H2-type 4
	Region	310 – 427	118	Interaction with DNMT3A
Amino acid modifications
	Modified residue	516	1	Phosphoserine Ref.9
	Modified residue	517	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	1	1	M → MCPKGYEDSM in isoform 2.		VSP_035381
	Natural variant	132	1	E → G. Ref.1 Corresponds to variant rs1048824 [ dbSNP | Ensembl ].		VAR_012768
Experimental info
	Sequence conflict	51	1	L → I in AAH36677. Ref.6
	Sequence conflict	166 – 262	97	KLNIL…YFSSQ → IEHPAQQKGLGGRAWEHVDA IALRLSRHPPGWRRGRATRH SSWKNSSQPLQLNRVFVPE in AAA81368. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: DE024B66E02DCE75	FASTA	522	58,354
	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
	Isoform 2 [UniParc]. Checksum: EA03FF68F0FD4668	FASTA	531	59,366
	10 20 30 40 50 60 MCPKGYEDSM EFPDHSRHLL QCLSEQRHQG FLCDCTVLVG DAQFRAHRAV LASCSMYFHL 70 80 90 100 110 120 FYKDQLDKRD IVHLNSDIVT APAFALLLEF MYEGKLQFKD LPIEDVLAAA SYLHMYDIVK 130 140 150 160 170 180 VCKKKLKEKA TTEADSTKKE EDASSCSDKV ESLSDGSSHI AGDLPSDEDE GEDEKLNILP 190 200 210 220 230 240 SKRDLAAEPG NMWMRLPSDS AGIPQAGGEA EPHATAAGKT VASPCSSTES LSQRSVTSVR 250 260 270 280 290 300 DSADVDCVLD LSVKSSLSGV ENLNSSYFSS QDVLRSNLVQ VKVEKEASCD ESDVGTNDYD 310 320 330 340 350 360 MEHSTVKESV STNNRVQYEP AHLAPLREDS VLRELDREDK ASDDEMMTPE SERVQVEGGM 370 380 390 400 410 420 ESSLLPYVSN ILSPAGQIFM CPLCNKVFPS PHILQIHLST HFREQDGIRS KPAADVNVPT 430 440 450 460 470 480 CSLCGKTFSC MYTLKRHERT HSGEKPYTCT QCGKSFQYSH NLSRHAVVHT REKPHACKWC 490 500 510 520 530 ERRFTQSGDL YRHIRKFHCE LVNSLSVKSE ALSLPTVRDW TLEDSSQELW K

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	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.
IPI	IPI00007360. IPI00409637.
PIR	I39200.
RefSeq	NP_006343.2. NM_006352.3. NP_991331.1. NM_205768.2.
UniGene	Hs.69997.
3D structure databases
ProteinModelPortal	Q99592.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99592. 3 interactions.
STRING	9606.ENSP00000351539.
PTM databases
PhosphoSite	Q99592.
Polymorphism databases
DMDM	20141020.
Proteomic databases
PaxDb	Q99592.
PRIDE	Q99592.
Protocols and materials databases
DNASU	10472.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358704; ENSP00000351539; ENSG00000179456.
GeneID	10472.
KEGG	hsa:10472.
UCSC	uc001iad.4. human. uc001iae.3. human.
Organism-specific databases
CTD	10472.
GeneCards	GC01P244215.
HGNC	HGNC:13030. ZBTB18.
MIM	608433. gene.
neXtProt	NX_Q99592.
PharmGKB	PA37608.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5048.
HOGENOM	HOG000234147.
HOVERGEN	HBG059113.
InParanoid	Q99592.
OMA	PYEPAHL.
OrthoDB	EOG47SSDG.
Enzyme and pathway databases
SignaLink	Q99592.
Gene expression databases
Bgee	Q99592.
CleanEx	HS_ZNF238.
Genevestigator	Q99592.
GermOnline	ENSG00000179456. Homo sapiens.
Family and domain databases
Gene3D	3.30.160.60. 3 hits. 3.30.710.10. 1 hit.
InterPro	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]
Pfam	PF00651. BTB. 1 hit. PF00096. zf-C2H2. 1 hit. [Graphical view]
SMART	SM00225. BTB. 1 hit. SM00355. ZnF_C2H2. 4 hits. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. PS00028. ZINC_FINGER_C2H2_1. 4 hits. PS50157. ZINC_FINGER_C2H2_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZNF238. human.
GenomeRNAi	10472.
NextBio	39714.
SOURCE	Search...

Entry information

Entry name

ZBT18_HUMAN

Accession

Primary (citable) accession number: Q99592
Secondary accession number(s): A8K5U3 , Q13397, Q5VU40, Q8N463, Q9UD99

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	May 1, 1997
Last modified:	May 29, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.