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Protein

Z-DNA-binding protein 1

Gene

Zbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the detection by the host's innate immune system of DNA from viral, bacterial or even host origin. Plays a role in host defense against tumors and pathogens. Acts as a cytoplasmic DNA sensor which, when activated, induces the recruitment of TBK1 and IRF3 to its C-terminal region and activates the downstream interferon regulatory factor (IRF) and NF-kappa B transcription factors, leading to type-I interferon production. ZBP1-induced NF-kappaB activation probably involves the recruitment of the RHIM containing kinases RIPK1 and RIPK3.2 Publications

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. double-stranded RNA adenosine deaminase activity Source: InterPro
  3. left-handed Z-DNA binding Source: MGI
  4. RNA binding Source: InterPro

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
  3. positive regulation of type I interferon-mediated signaling pathway Source: MGI
  4. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.
REACT_196519. Regulation of innate immune responses to cytosolic DNA.
REACT_198980. IRF3 mediated activation of type 1 IFN.
REACT_222971. RIP-mediated NFkB activation via ZBP1.

Names & Taxonomyi

Protein namesi
Recommended name:
Z-DNA-binding protein 1
Alternative name(s):
DNA-dependent activator of IFN-regulatory factors
Short name:
DAI
Tumor stroma and activated macrophage protein DLM-1
Gene namesi
Name:Zbp1
Synonyms:Dlm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1927449. Zbp1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Z-DNA-binding protein 1PRO_0000066565Add
BLAST

Proteomic databases

MaxQBiQ9QY24.
PaxDbiQ9QY24.
PRIDEiQ9QY24.

PTM databases

PhosphoSiteiQ9QY24.

Expressioni

Tissue specificityi

Expressed in lung, spleen and liver. Lower levels were seen in heart, kidney and testis. Expression is greatly up-regulated in tumor stromal cells and activated macrophages.

Inductioni

By interferon gamma and lipopolysaccharides (LPS).

Gene expression databases

BgeeiQ9QY24.
CleanExiMM_ZBP1.
ExpressionAtlasiQ9QY24. baseline and differential.
GenevestigatoriQ9QY24.

Interactioni

Subunit structurei

Interacts (via RIP homotypic interaction motif) with murid herpesvirus 1 viral inhibitor of RIP activation (via RIP homotypic interaction motif); this interaction inhibits recruitment of RIPK1 and RIPK3 to ZBP1 and prevents ZBP1-induced NFkappa-B activation.1 Publication

Protein-protein interaction databases

DIPiDIP-29879N.
STRINGi10090.ENSMUSP00000029018.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2513Combined sources
Helixi31 – 388Combined sources
Helixi42 – 5413Combined sources
Beta strandi57 – 626Combined sources
Beta strandi65 – 684Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J75X-ray1.85A8-70[»]
2HEOX-ray1.70A/D8-70[»]
ProteinModelPortaliQ9QY24.
SMRiQ9QY24. Positions 13-69, 92-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QY24.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati6 – 7267DRADA 1Add
BLAST
Repeati82 – 14766DRADA 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi188 – 20518RIP homotypic interaction motif (RHIM) 1Add
BLAST
Motifi237 – 26125RIP homotypic interaction motif (RHIM) 2Add
BLAST

Sequence similaritiesi

Contains 2 DRADA repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG38978.
GeneTreeiENSGT00390000002234.
HOGENOMiHOG000230878.
HOVERGENiHBG036279.
InParanoidiQ9QY24.
KOiK12965.
PhylomeDBiQ9QY24.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR000607. dsRNA_A_deaminase.
IPR025735. RHIM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF12721. RHIM. 2 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00550. Zalpha. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QY24-1) [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
MAEAPVDLST GDNLEQKILQ VLSDDGGPVK IGQLVKKCQV PKKTLNQVLY
60 70 80 90 100
RLKKEDRVSS PEPATWSIGG AASGDGAPAI PENSSAQPSL DERILRFLEA
110 120 130 140 150
NGPHRALHIA KALGMTTAKE VNPLLYSMRN KHLLSYDGQT WKIYHSRQEG
160 170 180 190 200
QDIAHSGVTQ ESPAIICQHN PVNMICQQGA NSHISIANSN AIQIGHGNVI
210 220 230 240 250
VREKACGEPG PRTSHPLPLA WDASAQDMPP VAHGAQYIYM DKSLLQQVQL
260 270 280 290 300
GHHNEMSLVG DAGKHPSYSF SDSPPEVSTT TADPGASFNM QTFEPGPHPE
310 320 330 340 350
GDTVQTVHIK SCFLEDATIG NGNKMTIHLR SKGEVMESGD SEEPKKEDTG
360 370 380 390 400
TSSEATPPRS CQHTPSDSML PTSELRAMAL GDSSPQTTEP VLREHEVQDI
410
ESSQDTGLSK Q
Length:411
Mass (Da):44,331
Last modified:May 1, 2000 - v1
Checksum:i6D5F7B526A7DAA40
GO
Isoform 2 (identifier: Q9QY24-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-187: AHSGVTQESPAIICQHNPVNMICQQGANSHISIA → VLPCSPGCPRTHHVDQAGLEPTEIFLLLPIKFWD
     188-411: Missing.

Show »
Length:187
Mass (Da):20,569
Checksum:i216A1996CDD858DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671S → R in AAH20033 (PubMed:15489334).Curated
Sequence conflicti83 – 831N → D in AAH20033 (PubMed:15489334).Curated
Sequence conflicti197 – 1971G → R in AAH20033 (PubMed:15489334).Curated
Sequence conflicti293 – 2931F → S in AAH20033 (PubMed:15489334).Curated
Sequence conflicti403 – 4031S → T in AAH20033 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei154 – 18734AHSGV…HISIA → VLPCSPGCPRTHHVDQAGLE PTEIFLLLPIKFWD in isoform 2. 1 PublicationVSP_004083Add
BLAST
Alternative sequencei188 – 411224Missing in isoform 2. 1 PublicationVSP_004084Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136520 mRNA. Translation: AAF17234.1.
AK008179 mRNA. Translation: BAB25513.1.
BC020033 mRNA. Translation: AAH20033.1.
CCDSiCCDS17142.1. [Q9QY24-1]
CCDS50813.1. [Q9QY24-2]
RefSeqiNP_001132991.1. NM_001139519.1. [Q9QY24-2]
UniGeneiMm.116687.

Genome annotation databases

EnsembliENSMUST00000109116; ENSMUSP00000104744; ENSMUSG00000027514. [Q9QY24-2]
GeneIDi58203.
KEGGimmu:58203.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136520 mRNA. Translation: AAF17234.1.
AK008179 mRNA. Translation: BAB25513.1.
BC020033 mRNA. Translation: AAH20033.1.
CCDSiCCDS17142.1. [Q9QY24-1]
CCDS50813.1. [Q9QY24-2]
RefSeqiNP_001132991.1. NM_001139519.1. [Q9QY24-2]
UniGeneiMm.116687.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J75X-ray1.85A8-70[»]
2HEOX-ray1.70A/D8-70[»]
ProteinModelPortaliQ9QY24.
SMRiQ9QY24. Positions 13-69, 92-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29879N.
STRINGi10090.ENSMUSP00000029018.

PTM databases

PhosphoSiteiQ9QY24.

Proteomic databases

MaxQBiQ9QY24.
PaxDbiQ9QY24.
PRIDEiQ9QY24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109116; ENSMUSP00000104744; ENSMUSG00000027514. [Q9QY24-2]
GeneIDi58203.
KEGGimmu:58203.

Organism-specific databases

CTDi81030.
MGIiMGI:1927449. Zbp1.

Phylogenomic databases

eggNOGiNOG38978.
GeneTreeiENSGT00390000002234.
HOGENOMiHOG000230878.
HOVERGENiHBG036279.
InParanoidiQ9QY24.
KOiK12965.
PhylomeDBiQ9QY24.

Enzyme and pathway databases

ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.
REACT_196519. Regulation of innate immune responses to cytosolic DNA.
REACT_198980. IRF3 mediated activation of type 1 IFN.
REACT_222971. RIP-mediated NFkB activation via ZBP1.

Miscellaneous databases

EvolutionaryTraceiQ9QY24.
NextBioi314185.
PROiQ9QY24.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QY24.
CleanExiMM_ZBP1.
ExpressionAtlasiQ9QY24. baseline and differential.
GenevestigatoriQ9QY24.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR000607. dsRNA_A_deaminase.
IPR025735. RHIM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF12721. RHIM. 2 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00550. Zalpha. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of DLM-1, a novel gene that is up-regulated in activated macrophages, using RNA differential display."
    Fu Y., Comella N., Tognazzi K., Brown L.F., Dvorak H.F., Kocher O.
    Gene 240:157-163(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C3Heb/FeJ.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Small intestine.
  3. "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: Mammary tumor.
  4. "DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response."
    Takaoka A., Wang Z., Choi M.K., Yanai H., Negishi H., Ban T., Lu Y., Miyagishi M., Kodama T., Honda K., Ohba Y., Taniguchi T.
    Nature 448:501-505(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB."
    Rebsamen M., Heinz L.X., Meylan E., Michallet M.C., Schroder K., Hofmann K., Vazquez J., Benedict C.A., Tschopp J.
    EMBO Rep. 10:916-922(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RIPK1; RIPK3 AND MURID HERPESVIRUS 1 VIRAL INHIBITOR OF RIP ACTIVATION.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins."
    Schwartz T., Behlke J., Lowenhaupt K., Heinemann U., Rich A.
    Nat. Struct. Biol. 8:761-765(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 8-70, DNA-BINDING.

Entry informationi

Entry nameiZBP1_MOUSE
AccessioniPrimary (citable) accession number: Q9QY24
Secondary accession number(s): Q8VE02, Q9D8B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.