Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc finger and BTB domain-containing protein 4

Gene

ZBTB4

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

Functioni

Transcriptional repressor with bimodal DNA-binding specificity. Represses transcription in a methyl-CpG-dependent manner. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Can also bind specifically to a single methyl-CpG pair and can bind hemimethylated DNA but with a lower affinity compared to methylated DNA (PubMed:16354688).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri234 – 25623C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri309 – 33123C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri337 – 35923C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri365 – 38824C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri726 – 74823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri765 – 78723C2H2-type 6PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • methyl-CpG binding Source: UniProtKB
  • methyl-CpNpG binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger and BTB domain-containing protein 4
Alternative name(s):
KAISO-like zinc finger protein 1
Short name:
KAISO-L1
Gene namesi
Name:ZBTB4
Synonyms:KIAA1538
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:23847. ZBTB4.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi795 – 7951T → A: Impaired HIPK2-mediated phosphorylation; when associated with A-797 and A-983. 1 Publication
Mutagenesisi797 – 7971T → A: Impaired HIPK2-mediated phosphorylation; when associated with A-795 and A-983. 1 Publication
Mutagenesisi983 – 9831T → A: Impaired HIPK2-mediated phosphorylation; when associated with A-795 and A-797. 1 Publication

Organism-specific databases

PharmGKBiPA134959224.

Polymorphism and mutation databases

BioMutaiZBTB4.
DMDMi46577564.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10131013Zinc finger and BTB domain-containing protein 4PRO_0000047712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki40 – 40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei391 – 3911PhosphoserineCombined sources
Cross-linki615 – 615Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei795 – 7951Phosphothreonine; by HIPK21 Publication
Modified residuei797 – 7971Phosphothreonine; by HIPK21 Publication
Modified residuei983 – 9831Phosphothreonine; by HIPK21 Publication

Post-translational modificationi

Phosphorylated by HIPK2. This phosphorylation reduces stability and triggers ZBTB4 protein degradation in response to DNA damage.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9P1Z0.
MaxQBiQ9P1Z0.
PaxDbiQ9P1Z0.
PRIDEiQ9P1Z0.

PTM databases

iPTMnetiQ9P1Z0.
PhosphoSiteiQ9P1Z0.

Expressioni

Gene expression databases

BgeeiQ9P1Z0.
CleanExiHS_ZBTB4.
GenevisibleiQ9P1Z0. HS.

Organism-specific databases

HPAiCAB008980.

Interactioni

Subunit structurei

Interacts with HIPK2. Interacts with CBFA2T3. Interacts with ZBTB38.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121693. 7 interactions.
IntActiQ9P1Z0. 1 interaction.
STRINGi9606.ENSP00000307858.

Structurei

3D structure databases

ProteinModelPortaliQ9P1Z0.
SMRiQ9P1Z0. Positions 8-57, 227-422, 665-698, 716-750, 762-795.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 152123BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 348163Interaction with CBFA2T31 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili627 – 66337Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi435 – 536102Pro-richAdd
BLAST
Compositional biasi610 – 65445Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 6 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri234 – 25623C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri309 – 33123C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri337 – 35923C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri365 – 38824C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri726 – 74823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri765 – 78723C2H2-type 6PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00810000125416.
HOGENOMiHOG000065759.
HOVERGENiHBG055508.
InParanoidiQ9P1Z0.
KOiK10491.
OMAiNMVLPDE.
OrthoDBiEOG74J978.
PhylomeDBiQ9P1Z0.
TreeFamiTF333100.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 2 hits.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P1Z0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPPAEVTDP SHAPAVLRQL NEQRLRGLFC DVTLIAGDTK FPAHRSVLAA
60 70 80 90 100
SSPFFREALL TSAPLPLPPA TGGAAPNPAT TTAASSSSSS SSSSSSSSSS
110 120 130 140 150
ASSSSSSSSS SPPPASPPAS SPPRVLELPG VPAAAFSDVL NFIYSARLAL
160 170 180 190 200
PGGGGDGAAV AEIGALGRRL GISRLQGLGE GGDAWVPPTP APMATSQPEE
210 220 230 240 250
DSFGPGPRPA GEWEGDRAEA QAPDLQCSLP RRPLPCPQCG KSFIHPKRLQ
260 270 280 290 300
THEAQCRRGA STRGSTGLGA GGAGPGGPAG VDASALPPPV GFRGGPEHVV
310 320 330 340 350
KVVGGHVLYV CAACERSYVT LSSLKRHSNV HSWRRKYPCR YCEKVFALAE
360 370 380 390 400
YRTKHEVWHT GERRYQCIFC WETFVTYYNL KTHQRAFHGI SPGLLASEKT
410 420 430 440 450
PNGGYKPKLN TLKLYRLLPM RAAKRPYKTY SQGAPEAPLS PTLNTPAPVA
460 470 480 490 500
MPASPPPGPP PAPEPGPPPS VITFAHPAPS VIVHGGSSSG GGGSGTASTG
510 520 530 540 550
GSQAASVITY TAPPRPPKKR EYPPPPPEPA ATPTSPATAV SPATAAGPAM
560 570 580 590 600
ATTTEEAKGR NPRAGRTLTY TAKPVGGIGG GGGPPTGAGR GPSQLQAPPP
610 620 630 640 650
LCQITVRIGE EAIVKRRISE TDLRPGELSG EEMEESEEDE EEEDEEEEEE
660 670 680 690 700
DEEESKAGGE DQLWRPYYSY KPKRKAGAAG GASVGGSGLP RGRRPPRWRQ
710 720 730 740 750
KLERRSWEET PAAESPAGRA RTERRHRCGD CAQTFTTLRK LRKHQEAHGG
760 770 780 790 800
GSHSSRAGRR PSTRFTCPHC AKVCKTAAAL SRHGQRHAAE RPGGTPTPVI
810 820 830 840 850
AYSKGSAGTR PGDVKEEAPQ EMQVSSSSGE AGGGSTAAEE ASETASLQDP
860 870 880 890 900
IISGGEEPPV VASGGSYVYP PVQEFPLALI GGGREPGGGR GKSGSEGPVG
910 920 930 940 950
AGEGDRMEGI GAAKVTFYPE PYPLVYGPQL LAAYPYNFSN LAALPVALNM
960 970 980 990 1000
VLPDEKGAGA LPFLPGVFGY AVNPQAAPPA PPTPPPPTLP PPIPPKGEGE
1010
RAGVERTQKG DVG
Length:1,013
Mass (Da):105,114
Last modified:April 26, 2004 - v3
Checksum:iCA4AB6A5230C2F52
GO

Sequence cautioni

The sequence BAA96062.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881P → S in AAH43352 (PubMed:15489334).Curated
Sequence conflicti674 – 6741R → C in AAH43352 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti539 – 5391A → V.
Corresponds to variant rs35231078 [ dbSNP | Ensembl ].
VAR_052913
Natural varianti550 – 5501M → I.
Corresponds to variant rs871990 [ dbSNP | Ensembl ].
VAR_018383
Natural varianti561 – 5611N → S.
Corresponds to variant rs34914463 [ dbSNP | Ensembl ].
VAR_052914

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY302699 mRNA. Translation: AAP59447.1.
AB040971 mRNA. Translation: BAA96062.2. Different initiation.
AK122971 mRNA. Translation: BAG53828.1.
CH471108 Genomic DNA. Translation: EAW90185.1.
BC033259 mRNA. Translation: AAH33259.1.
BC043352 mRNA. Translation: AAH43352.1.
CCDSiCCDS11107.1.
RefSeqiNP_001122305.1. NM_001128833.1.
NP_065950.2. NM_020899.3.
XP_006721626.1. XM_006721563.2.
XP_006721627.1. XM_006721564.1.
XP_011522274.1. XM_011523972.1.
UniGeneiHs.35096.

Genome annotation databases

EnsembliENST00000311403; ENSP00000307858; ENSG00000174282.
ENST00000380599; ENSP00000369973; ENSG00000174282.
GeneIDi57659.
KEGGihsa:57659.
UCSCiuc002ghc.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY302699 mRNA. Translation: AAP59447.1.
AB040971 mRNA. Translation: BAA96062.2. Different initiation.
AK122971 mRNA. Translation: BAG53828.1.
CH471108 Genomic DNA. Translation: EAW90185.1.
BC033259 mRNA. Translation: AAH33259.1.
BC043352 mRNA. Translation: AAH43352.1.
CCDSiCCDS11107.1.
RefSeqiNP_001122305.1. NM_001128833.1.
NP_065950.2. NM_020899.3.
XP_006721626.1. XM_006721563.2.
XP_006721627.1. XM_006721564.1.
XP_011522274.1. XM_011523972.1.
UniGeneiHs.35096.

3D structure databases

ProteinModelPortaliQ9P1Z0.
SMRiQ9P1Z0. Positions 8-57, 227-422, 665-698, 716-750, 762-795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121693. 7 interactions.
IntActiQ9P1Z0. 1 interaction.
STRINGi9606.ENSP00000307858.

PTM databases

iPTMnetiQ9P1Z0.
PhosphoSiteiQ9P1Z0.

Polymorphism and mutation databases

BioMutaiZBTB4.
DMDMi46577564.

Proteomic databases

EPDiQ9P1Z0.
MaxQBiQ9P1Z0.
PaxDbiQ9P1Z0.
PRIDEiQ9P1Z0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311403; ENSP00000307858; ENSG00000174282.
ENST00000380599; ENSP00000369973; ENSG00000174282.
GeneIDi57659.
KEGGihsa:57659.
UCSCiuc002ghc.5. human.

Organism-specific databases

CTDi57659.
GeneCardsiZBTB4.
HGNCiHGNC:23847. ZBTB4.
HPAiCAB008980.
MIMi612308. gene.
neXtProtiNX_Q9P1Z0.
PharmGKBiPA134959224.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00810000125416.
HOGENOMiHOG000065759.
HOVERGENiHBG055508.
InParanoidiQ9P1Z0.
KOiK10491.
OMAiNMVLPDE.
OrthoDBiEOG74J978.
PhylomeDBiQ9P1Z0.
TreeFamiTF333100.

Miscellaneous databases

ChiTaRSiZBTB4. human.
GenomeRNAii57659.
NextBioi64421.
PROiQ9P1Z0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P1Z0.
CleanExiHS_ZBTB4.
GenevisibleiQ9P1Z0. HS.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 2 hits.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel zinc-finger-protein encoding gene on 17p13.1."
    Weber A., Klinkhammer B., Glaum A., Bergmann E., Berwanger B., Eilers M., Christiansen H.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  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].
    Tissue: Uterus.
  5. 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].
    Tissue: Brain and Uterus.
  7. "A family of human zinc finger proteins that bind methylated DNA and repress transcription."
    Filion G.J., Zhenilo S., Salozhin S., Yamada D., Prokhortchouk E., Defossez P.A.
    Mol. Cell. Biol. 26:169-181(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH ZBTB38.
  8. "The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4."
    Yamada D., Perez-Torrado R., Filion G., Caly M., Jammart B., Devignot V., Sasai N., Ravassard P., Mallet J., Sastre-Garau X., Schmitz M.L., Defossez P.A.
    Oncogene 28:2535-2544(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-795; THR-797 AND THR-983 BY HIPK2, MUTAGENESIS OF THR-795; THR-797 AND THR-983, INTERACTION WITH HIPK2.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: INTERACTION WITH CBFA2T3.
  11. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZBTB4_HUMAN
AccessioniPrimary (citable) accession number: Q9P1Z0
Secondary accession number(s): B3KVL6
, Q7Z697, Q86XJ4, Q8N4V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: March 16, 2016
This is version 131 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 17
    Human chromosome 17: 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

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 one 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.