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Q9Y2K1

- ZBTB1_HUMAN

UniProt

Q9Y2K1 - ZBTB1_HUMAN

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Protein

Zinc finger and BTB domain-containing protein 1

Gene

ZBTB1

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

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri216 – 23823C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri448 – 47023C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri534 – 55623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri578 – 60023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri606 – 62823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri634 – 65623C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri662 – 68423C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri686 – 70924C2H2-type 8PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. B cell differentiation Source: Ensembl
  2. innate immune response Source: UniProtKB-KW
  3. mRNA transcription from RNA polymerase II promoter Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. positive regulation of natural killer cell differentiation Source: UniProtKB
  6. positive regulation of pro-T cell differentiation Source: UniProtKB
  7. positive regulation of T cell differentiation Source: UniProtKB
  8. positive regulation of T cell mediated immunity Source: UniProtKB
  9. protein homooligomerization Source: UniProtKB
  10. T cell differentiation in thymus Source: Ensembl
  11. thymus development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Differentiation, Immunity, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger and BTB domain-containing protein 1
Gene namesi
Name:ZBTB1
Synonyms:KIAA0997
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20259. ZBTB1.

Subcellular locationi

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.

GO - Cellular componenti

  1. nuclear body Source: UniProtKB
  2. nucleoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi265 – 2651K → R: Reduces sumoylation. Inhibits transcriptional repressive activity. Inhibits sumoylation and reduces transcriptional repressive activity; when associated with R-328. 1 Publication
Mutagenesisi325 – 3251I → S: Reduces sumoylation of Lys-328.
Mutagenesisi326 – 3261I → N: Reduces sumoylation of Lys-328.
Mutagenesisi328 – 3281K → R: Reduces sumoylation. Does not reduce transcriptional repressive activity. Inhibits sumoylation but does not reduce transcriptional repressive activity; when associated with R-265. 1 Publication

Organism-specific databases

PharmGKBiPA128395769.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Zinc finger and BTB domain-containing protein 1PRO_0000047707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki265 – 265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-linki328 – 328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residuei355 – 3551Phosphoserine1 Publication
Modified residuei356 – 3561Phosphothreonine1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y2K1.
PaxDbiQ9Y2K1.
PRIDEiQ9Y2K1.

PTM databases

PhosphoSiteiQ9Y2K1.

Expressioni

Gene expression databases

BgeeiQ9Y2K1.
CleanExiHS_ZBTB1.
ExpressionAtlasiQ9Y2K1. baseline and differential.
GenevestigatoriQ9Y2K1.

Organism-specific databases

HPAiHPA050516.
HPA054552.

Interactioni

Subunit structurei

Homodimer. Homooligomer. Isoform 1 and isoform 2 can homodimerize. Heterodimer of isoform 1 and isoform 2.2 Publications

Protein-protein interaction databases

BioGridi116556. 89 interactions.
IntActiQ9Y2K1. 6 interactions.
MINTiMINT-7032151.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2K1.
SMRiQ9Y2K1. Positions 4-109, 412-479, 533-709.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Domaini

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 (PubMed:20797634).1 Publication

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 8 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri216 – 23823C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri448 – 47023C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri534 – 55623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri578 – 60023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri606 – 62823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri634 – 65623C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri662 – 68423C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri686 – 70924C2H2-type 8PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG277648.
GeneTreeiENSGT00690000102095.
HOGENOMiHOG000056456.
HOVERGENiHBG057764.
InParanoidiQ9Y2K1.
KOiK10488.
OMAiCTNRHSY.
OrthoDBiEOG7NPFSR.
PhylomeDBiQ9Y2K1.
TreeFamiTF332229.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
3.30.710.10. 1 hit.
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. 8 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y2K1-1) [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
MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR
60 70 80 90 100
MFFMNHQHST AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA
110 120 130 140 150
MNYLQLYNVP DCLEDIQDAD CSSSKCSSSA SSKQNSKMIF GVRMYEDTVA
160 170 180 190 200
RNGNEANRWC AEPSSTVNTP HNREADEESL QLGNFPEPLF DVCKKSSVSK
210 220 230 240 250
LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN RHLYQNTRSY
260 270 280 290 300
HRIVDIRDGK DSNIKAEFGE KDSSKTFSAQ TDKYRGDTSQ AADDSASTTG
310 320 330 340 350
SRKSSTVESE IASEEKSRAA ERKRIIIKME PEDIPTDELK DFNIIKVTDK
360 370 380 390 400
DCNESTDNDE LEDEPEEPFY RYYVEEDVSI KKSGRKTLKP RMSVSADERG
410 420 430 440 450
GLENMRPPNN SSPVQEDAEN ASCELCGLTI TEEDLSSHYL AKHIENICAC
460 470 480 490 500
GKCGQILVKG RQLQEHAQRC GEPQDLTMNG LGNTEEKMDL EENPDEQSEI
510 520 530 540 550
RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG QRFETENLVV
560 570 580 590 600
EHMSSCLDQD MFKSAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH
610 620 630 640 650
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV
660 670 680 690 700
RHMISHLSAG ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD
710
MRSHYNAKHL KRT
Length:713
Mass (Da):82,016
Last modified:April 26, 2004 - v3
Checksum:i4B120DD45FA14305
GO
Isoform 2 (identifier: Q9Y2K1-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:644
Mass (Da):73,682
Checksum:i122AD0D3D565098F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031T → N in BAA76841. (PubMed:10231032)Curated
Sequence conflicti334 – 3341I → T in AAH50719. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei633 – 71381RYVCS…HLKRT → SGEIGPSKPVEK in isoform 2. 1 PublicationVSP_040976Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32097.1. [Q9Y2K1-2]
CCDS45126.1. [Q9Y2K1-1]
RefSeqiNP_001116801.1. NM_001123329.1. [Q9Y2K1-1]
NP_055765.2. NM_014950.2. [Q9Y2K1-2]
XP_005267467.1. XM_005267410.1. [Q9Y2K1-1]
XP_005267468.1. XM_005267411.2. [Q9Y2K1-1]
UniGeneiHs.605143.

Genome annotation databases

EnsembliENST00000358738; ENSP00000351587; ENSG00000126804. [Q9Y2K1-2]
ENST00000554015; ENSP00000451000; ENSG00000126804. [Q9Y2K1-1]
GeneIDi22890.
KEGGihsa:22890.
UCSCiuc001xhh.4. human. [Q9Y2K1-1]
uc001xhi.2. human. [Q9Y2K1-2]

Polymorphism databases

DMDMi46577710.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32097.1. [Q9Y2K1-2 ]
CCDS45126.1. [Q9Y2K1-1 ]
RefSeqi NP_001116801.1. NM_001123329.1. [Q9Y2K1-1 ]
NP_055765.2. NM_014950.2. [Q9Y2K1-2 ]
XP_005267467.1. XM_005267410.1. [Q9Y2K1-1 ]
XP_005267468.1. XM_005267411.2. [Q9Y2K1-1 ]
UniGenei Hs.605143.

3D structure databases

ProteinModelPortali Q9Y2K1.
SMRi Q9Y2K1. Positions 4-109, 412-479, 533-709.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116556. 89 interactions.
IntActi Q9Y2K1. 6 interactions.
MINTi MINT-7032151.

PTM databases

PhosphoSitei Q9Y2K1.

Polymorphism databases

DMDMi 46577710.

Proteomic databases

MaxQBi Q9Y2K1.
PaxDbi Q9Y2K1.
PRIDEi Q9Y2K1.

Protocols and materials databases

DNASUi 22890.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358738 ; ENSP00000351587 ; ENSG00000126804 . [Q9Y2K1-2 ]
ENST00000554015 ; ENSP00000451000 ; ENSG00000126804 . [Q9Y2K1-1 ]
GeneIDi 22890.
KEGGi hsa:22890.
UCSCi uc001xhh.4. human. [Q9Y2K1-1 ]
uc001xhi.2. human. [Q9Y2K1-2 ]

Organism-specific databases

CTDi 22890.
GeneCardsi GC14P064971.
H-InvDB HIX0011734.
HGNCi HGNC:20259. ZBTB1.
HPAi HPA050516.
HPA054552.
neXtProti NX_Q9Y2K1.
PharmGKBi PA128395769.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG277648.
GeneTreei ENSGT00690000102095.
HOGENOMi HOG000056456.
HOVERGENi HBG057764.
InParanoidi Q9Y2K1.
KOi K10488.
OMAi CTNRHSY.
OrthoDBi EOG7NPFSR.
PhylomeDBi Q9Y2K1.
TreeFami TF332229.

Miscellaneous databases

ChiTaRSi ZBTB1. human.
GenomeRNAii 22890.
NextBioi 43493.
PROi Q9Y2K1.

Gene expression databases

Bgeei Q9Y2K1.
CleanExi HS_ZBTB1.
ExpressionAtlasi Q9Y2K1. baseline and differential.
Genevestigatori Q9Y2K1.

Family and domain databases

Gene3Di 3.30.160.60. 2 hits.
3.30.710.10. 1 hit.
InterProi 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 ]
Pfami PF00651. BTB. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view ]
SMARTi SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
PROSITEi PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiZBTB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2K1
Secondary accession number(s): A8K6S8, Q86SW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 26, 2004
Last modified: October 29, 2014
This is version 130 of the entry and version 3 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3