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Q9Y2K1 (ZBTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1
Gene names
Name:ZBTB1
Synonyms:KIAA0997
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional repressor. Represses cAMP-responsive element (CRE)-mediated transcriptional activation. Involved in lymphoid lineage commitment and differentiation. Plays a key role in the instruction of early lymphoid progenitors to develop into T-cell lineage. Ref.7 Ref.8

Subunit structure

Homodimer. Homooligomer. Isoform 1 and isoform 2 can homodimerize. Heterodimer of isoform 1 and isoform 2. Ref.7 Ref.9

Subcellular location

Nucleus. Nucleusnucleoplasm. Note: Localized in dot-like structures in the nucleus. Colocalized with SMRT in nuclear bodies. The sumoylated form is preferentially located in the nucleoplasm outside the nuclear bodies. Ref.7 Ref.8 Ref.9

Domain

Both the BTB domain and C2H2-type motifs are necessary for transriptional repression activity. The BTB domain is also necessary for oligomerization and efficient sumoylation. The hydrophobic cluster preceding Lys-328 enhanced sumoylation efficiency (Ref.7).

Post-translational modification

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. Ref.7

Sequence similarities

Contains 1 BTB (POZ) domain.

Contains 8 C2H2-type zinc fingers.

Sequence caution

The sequence BAA76841.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
Immunity
Innate immunity
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

positive regulation of T cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T cell mediated immunity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of natural killer cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of pro-T cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.7. Source: UniProtKB

thymus development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnuclear body

Inferred from direct assay Ref.7. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from direct assay Ref.9. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2K1-1)

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: Q9Y2K1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     633-713: RYVCSICDQG...HYNAKHLKRT → SGEIGPSKPVEK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 713713Zinc finger and BTB domain-containing protein 1
PRO_0000047707

Regions

Domain24 – 9168BTB
Zinc finger216 – 23823C2H2-type 1; atypical
Zinc finger448 – 47023C2H2-type 2; atypical
Zinc finger534 – 55623C2H2-type 3; atypical
Zinc finger578 – 60023C2H2-type 4
Zinc finger606 – 62823C2H2-type 5
Zinc finger634 – 65623C2H2-type 6
Zinc finger662 – 68423C2H2-type 7
Zinc finger686 – 70924C2H2-type 8

Amino acid modifications

Modified residue3551Phosphoserine Ref.6
Modified residue3561Phosphothreonine Ref.6
Cross-link265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) Ref.7
Cross-link328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) Ref.7

Natural variations

Alternative sequence633 – 71381RYVCS…HLKRT → SGEIGPSKPVEK in isoform 2.
VSP_040976

Experimental info

Mutagenesis2651K → R: Reduces sumoylation. Inhibits transcriptional repressive activity. Inhibits sumoylation and reduces transcriptional repressive activity; when associated with R-328. Ref.7
Mutagenesis3251I → S: Reduces sumoylation of Lys-328.
Mutagenesis3261I → N: Reduces sumoylation of Lys-328.
Mutagenesis3281K → R: Reduces sumoylation. Does not reduce transcriptional repressive activity. Inhibits sumoylation but does not reduce transcriptional repressive activity; when associated with R-265. Ref.7
Sequence conflict2031T → N in BAA76841. Ref.2
Sequence conflict3341I → T in AAH50719. Ref.4

Sequences

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

Last modified April 26, 2004. Version 3.
Checksum: 4B120DD45FA14305

FASTA71382,016
        10         20         30         40         50         60 
MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR MFFMNHQHST 

        70         80         90        100        110        120 
AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA MNYLQLYNVP DCLEDIQDAD 

       130        140        150        160        170        180 
CSSSKCSSSA SSKQNSKMIF GVRMYEDTVA RNGNEANRWC AEPSSTVNTP HNREADEESL 

       190        200        210        220        230        240 
QLGNFPEPLF DVCKKSSVSK LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN 

       250        260        270        280        290        300 
RHLYQNTRSY HRIVDIRDGK DSNIKAEFGE KDSSKTFSAQ TDKYRGDTSQ AADDSASTTG 

       310        320        330        340        350        360 
SRKSSTVESE IASEEKSRAA ERKRIIIKME PEDIPTDELK DFNIIKVTDK DCNESTDNDE 

       370        380        390        400        410        420 
LEDEPEEPFY RYYVEEDVSI KKSGRKTLKP RMSVSADERG GLENMRPPNN SSPVQEDAEN 

       430        440        450        460        470        480 
ASCELCGLTI TEEDLSSHYL AKHIENICAC GKCGQILVKG RQLQEHAQRC GEPQDLTMNG 

       490        500        510        520        530        540 
LGNTEEKMDL EENPDEQSEI RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG 

       550        560        570        580        590        600 
QRFETENLVV EHMSSCLDQD MFKSAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH 

       610        620        630        640        650        660 
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV RHMISHLSAG 

       670        680        690        700        710 
ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD MRSHYNAKHL KRT 

« Hide

Isoform 2 [UniParc].

Checksum: 122AD0D3D565098F
Show »

FASTA64473,682

References

« Hide 'large scale' references
[1]"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 1).
Tissue: Placenta.
[2]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 1).
Tissue: Eye.
[5]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-417.
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND THR-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif."
Matic I., Schimmel J., Hendriks I.A., van Santen M.A., van de Rijke F., van Dam H., Gnad F., Mann M., Vertegaal A.C.
Mol. Cell 39:641-652(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUMOYLATION AT LYS-265 AND LYS-328, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-265 AND LYS-328, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Novel human BTB/POZ domain-containing zinc finger protein ZBTB1 inhibits transcriptional activities of CRE."
Liu Q., Yao F., Wang M., Zhou B., Cheng H., Wang W., Jin L., Lin Q., Wang J.C.
Mol. Cell. Biochem. 357:405-414(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Transcription factor zinc finger and BTB domain 1 is essential for lymphocyte development."
Punwani D., Simon K., Choi Y., Dutra A., Gonzalez-Espinosa D., Pak E., Naradikian M., Song C.H., Zhang J., Bodine D.M., Puck J.M.
J. Immunol. 189:1253-1264(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001116801.1. NM_001123329.1.
NP_055765.2. NM_014950.2.
XP_005267467.1. XM_005267410.1.
XP_005267468.1. XM_005267411.2.
UniGeneHs.605143.

3D structure databases

ProteinModelPortalQ9Y2K1.
SMRQ9Y2K1. Positions 4-109, 533-709.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116556. 7 interactions.
IntActQ9Y2K1. 6 interactions.
MINTMINT-7032151.

PTM databases

PhosphoSiteQ9Y2K1.

Polymorphism databases

DMDM46577710.

Proteomic databases

PaxDbQ9Y2K1.
PRIDEQ9Y2K1.

Protocols and materials databases

DNASU22890.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358738; ENSP00000351587; ENSG00000126804. [Q9Y2K1-2]
ENST00000394712; ENSP00000378201; ENSG00000126804. [Q9Y2K1-1]
ENST00000554015; ENSP00000451000; ENSG00000126804. [Q9Y2K1-1]
GeneID22890.
KEGGhsa:22890.
UCSCuc001xhh.4. human. [Q9Y2K1-1]
uc001xhi.2. human. [Q9Y2K1-2]

Organism-specific databases

CTD22890.
GeneCardsGC14P064971.
H-InvDBHIX0011734.
HGNCHGNC:20259. ZBTB1.
HPAHPA050516.
HPA054552.
neXtProtNX_Q9Y2K1.
PharmGKBPA128395769.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277648.
HOGENOMHOG000056456.
HOVERGENHBG057764.
InParanoidQ9Y2K1.
KOK10488.
OMACTNRHSY.
OrthoDBEOG7NPFSR.
PhylomeDBQ9Y2K1.
TreeFamTF332229.

Gene expression databases

ArrayExpressQ9Y2K1.
BgeeQ9Y2K1.
CleanExHS_ZBTB1.
GenevestigatorQ9Y2K1.

Family and domain databases

Gene3D3.30.160.60. 2 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. 8 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZBTB1. human.
GenomeRNAi22890.
NextBio43493.
PROQ9Y2K1.

Entry information

Entry nameZBTB1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2K1
Secondary accession number(s): A8K6S8, Q86SW8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 125 of the entry and version 3 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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM