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Protein

Zinc finger and BTB domain-containing protein 18

Gene

ZBTB18

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

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri370 – 39223C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri410 – 43223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri438 – 46023C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri466 – 48924C2H2-type 4PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. sequence-specific DNA binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. cerebellum development Source: Ensembl
  2. cerebral cortex development Source: Ensembl
  3. hippocampus development Source: Ensembl
  4. homeostasis of number of cells Source: Ensembl
  5. in utero embryonic development Source: Ensembl
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. neuron development Source: Ensembl
  9. regulation of cell division Source: Ensembl
  10. skeletal muscle tissue development Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ99592.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ZBTB18
Synonyms:RP58, TAZ1, ZNF238
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13030. ZBTB18.

Subcellular locationi

Nucleus
Note: Associates with condensed chromatin.

GO - Cellular componenti

  1. intercellular bridge Source: HPA
  2. microtubule cytoskeleton Source: HPA
  3. nuclear chromosome Source: ProtInc
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 221 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:612337

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi612337. phenotype.
Orphaneti36367. Distal monosomy 1q.
PharmGKBiPA37608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Zinc finger and BTB domain-containing protein 18PRO_0000047477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei516 – 5161Phosphoserine1 Publication
Modified residuei517 – 5171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99592.
PRIDEiQ99592.

PTM databases

PhosphoSiteiQ99592.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ99592.
CleanExiHS_ZNF238.
GenevestigatoriQ99592.

Organism-specific databases

HPAiHPA044652.

Interactioni

Subunit structurei

Interacts with DNMT3A.1 Publication

Protein-protein interaction databases

BioGridi115735. 9 interactions.
IntActiQ99592. 3 interactions.
STRINGi9606.ENSP00000351539.

Structurei

3D structure databases

ProteinModelPortaliQ99592.
SMRiQ99592. Positions 2-113, 370-489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 9168BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni310 – 427118Interaction with DNMT3AAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri370 – 39223C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri410 – 43223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri438 – 46023C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri466 – 48924C2H2-type 4PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118922.
HOGENOMiHOG000234147.
HOVERGENiHBG059113.
InParanoidiQ99592.
OMAiGGEAETH.
OrthoDBiEOG73FQM8.
PhylomeDBiQ99592.
TreeFamiTF337437.

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.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 4 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99592-1) [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
MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH
60 70 80 90 100
LFYKDQLDKR DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA
110 120 130 140 150
ASYLHMYDIV KVCKKKLKEK ATTEADSTKK EEDASSCSDK VESLSDGSSH
160 170 180 190 200
IAGDLPSDED EGEDEKLNIL PSKRDLAAEP GNMWMRLPSD SAGIPQAGGE
210 220 230 240 250
AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL DLSVKSSLSG
260 270 280 290 300
VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES
310 320 330 340 350
VSTNNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG
360 370 380 390 400
MESSLLPYVS NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR
410 420 430 440 450
SKPAADVNVP TCSLCGKTFS CMYTLKRHER THSGEKPYTC TQCGKSFQYS
460 470 480 490 500
HNLSRHAVVH TREKPHACKW CERRFTQSGD LYRHIRKFHC ELVNSLSVKS
510 520
EALSLPTVRD WTLEDSSQEL WK
Length:522
Mass (Da):58,354
Last modified:May 1, 1997 - v1
Checksum:iDE024B66E02DCE75
GO
Isoform 2 (identifier: Q99592-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:531
Mass (Da):59,366
Checksum:iEA03FF68F0FD4668
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511L → I in AAH36677. (PubMed:15489334)Curated
Sequence conflicti166 – 26297KLNIL…YFSSQ → IEHPAQQKGLGGRAWEHVDA IALRLSRHPPGWRRGRATRH SSWKNSSQPLQLNRVFVPE in AAA81368. (PubMed:7633419)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321E → G.1 Publication
Corresponds to variant rs1048824 [ dbSNP | Ensembl ].
VAR_012768

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MCPKGYEDSM in isoform 2. 2 PublicationsVSP_035381

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1622.1. [Q99592-2]
PIRiI39200.
RefSeqiNP_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]
UniGeneiHs.69997.

Genome annotation databases

EnsembliENST00000358704; ENSP00000351539; ENSG00000179456. [Q99592-2]
ENST00000622512; ENSP00000481278; ENSG00000179456. [Q99592-1]
GeneIDi10472.
KEGGihsa:10472.
UCSCiuc001iad.5. human. [Q99592-2]
uc001iae.4. human. [Q99592-1]

Polymorphism databases

DMDMi20141020.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1622.1. [Q99592-2]
PIRiI39200.
RefSeqiNP_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]
UniGeneiHs.69997.

3D structure databases

ProteinModelPortaliQ99592.
SMRiQ99592. Positions 2-113, 370-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115735. 9 interactions.
IntActiQ99592. 3 interactions.
STRINGi9606.ENSP00000351539.

PTM databases

PhosphoSiteiQ99592.

Polymorphism databases

DMDMi20141020.

Proteomic databases

PaxDbiQ99592.
PRIDEiQ99592.

Protocols and materials databases

DNASUi10472.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358704; ENSP00000351539; ENSG00000179456. [Q99592-2]
ENST00000622512; ENSP00000481278; ENSG00000179456. [Q99592-1]
GeneIDi10472.
KEGGihsa:10472.
UCSCiuc001iad.5. human. [Q99592-2]
uc001iae.4. human. [Q99592-1]

Organism-specific databases

CTDi10472.
GeneCardsiGC01P244216.
HGNCiHGNC:13030. ZBTB18.
HPAiHPA044652.
MIMi608433. gene.
612337. phenotype.
neXtProtiNX_Q99592.
Orphaneti36367. Distal monosomy 1q.
PharmGKBiPA37608.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118922.
HOGENOMiHOG000234147.
HOVERGENiHBG059113.
InParanoidiQ99592.
OMAiGGEAETH.
OrthoDBiEOG73FQM8.
PhylomeDBiQ99592.
TreeFamiTF337437.

Enzyme and pathway databases

SignaLinkiQ99592.

Miscellaneous databases

GeneWikiiZNF238.
GenomeRNAii10472.
NextBioi39714.
PROiQ99592.
SOURCEiSearch...

Gene expression databases

BgeeiQ99592.
CleanExiHS_ZNF238.
GenevestigatoriQ99592.

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.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 4 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. "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. 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.

Entry informationi

Entry nameiZBT18_HUMAN
AccessioniPrimary (citable) accession number: Q99592
Secondary accession number(s): A8K5U3
, Q13397, Q5VU40, Q8N463, Q9UD99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: May 1, 1997
Last modified: February 4, 2015
This is version 143 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.