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Q9QY24

- ZBP1_MOUSE

UniProt

Q9QY24 - ZBP1_MOUSE

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Protein

Z-DNA-binding protein 1

Gene
Zbp1, Dlm1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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: Reactome
  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

ArrayExpressiQ9QY24.
BgeeiQ9QY24.
CleanExiMM_ZBP1.
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 – 2513
Helixi31 – 388
Helixi42 – 5413
Beta strandi57 – 626
Beta strandi65 – 684

3D structure databases

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

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG38978.
GeneTreeiENSGT00390000002234.
HOGENOMiHOG000230878.
HOVERGENiHBG036279.
InParanoidiQ9QY24.
KOiK12965.
OMAiPGCPRTH.
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. Align

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

MAEAPVDLST GDNLEQKILQ VLSDDGGPVK IGQLVKKCQV PKKTLNQVLY    50
RLKKEDRVSS PEPATWSIGG AASGDGAPAI PENSSAQPSL DERILRFLEA 100
NGPHRALHIA KALGMTTAKE VNPLLYSMRN KHLLSYDGQT WKIYHSRQEG 150
QDIAHSGVTQ ESPAIICQHN PVNMICQQGA NSHISIANSN AIQIGHGNVI 200
VREKACGEPG PRTSHPLPLA WDASAQDMPP VAHGAQYIYM DKSLLQQVQL 250
GHHNEMSLVG DAGKHPSYSF SDSPPEVSTT TADPGASFNM QTFEPGPHPE 300
GDTVQTVHIK SCFLEDATIG NGNKMTIHLR SKGEVMESGD SEEPKKEDTG 350
TSSEATPPRS CQHTPSDSML PTSELRAMAL GDSSPQTTEP VLREHEVQDI 400
ESSQDTGLSK Q 411
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei154 – 18734AHSGV…HISIA → VLPCSPGCPRTHHVDQAGLE PTEIFLLLPIKFWD in isoform 2. VSP_004083Add
BLAST
Alternative sequencei188 – 411224Missing in isoform 2. VSP_004084Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671S → R in AAH20033. 1 Publication
Sequence conflicti83 – 831N → D in AAH20033. 1 Publication
Sequence conflicti197 – 1971G → R in AAH20033. 1 Publication
Sequence conflicti293 – 2931F → S in AAH20033. 1 Publication
Sequence conflicti403 – 4031S → T in AAH20033. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF136520 mRNA. Translation: AAF17234.1 .
AK008179 mRNA. Translation: BAB25513.1 .
BC020033 mRNA. Translation: AAH20033.1 .
CCDSi CCDS17142.1. [Q9QY24-1 ]
CCDS50813.1. [Q9QY24-2 ]
RefSeqi NP_001132991.1. NM_001139519.1. [Q9QY24-2 ]
UniGenei Mm.116687.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J75 X-ray 1.85 A 8-70 [» ]
2HEO X-ray 1.70 A/D 8-70 [» ]
ProteinModelPortali Q9QY24.
SMRi Q9QY24. Positions 13-69, 92-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29879N.
STRINGi 10090.ENSMUSP00000029018.

PTM databases

PhosphoSitei Q9QY24.

Proteomic databases

MaxQBi Q9QY24.
PaxDbi Q9QY24.
PRIDEi Q9QY24.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109116 ; ENSMUSP00000104744 ; ENSMUSG00000027514 . [Q9QY24-2 ]
GeneIDi 58203.
KEGGi mmu:58203.

Organism-specific databases

CTDi 81030.
MGIi MGI:1927449. Zbp1.

Phylogenomic databases

eggNOGi NOG38978.
GeneTreei ENSGT00390000002234.
HOGENOMi HOG000230878.
HOVERGENi HBG036279.
InParanoidi Q9QY24.
KOi K12965.
OMAi PGCPRTH.
PhylomeDBi Q9QY24.

Enzyme and pathway databases

Reactomei REACT_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

EvolutionaryTracei Q9QY24.
NextBioi 314185.
PROi Q9QY24.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9QY24.
Bgeei Q9QY24.
CleanExi MM_ZBP1.
Genevestigatori Q9QY24.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR000607. dsRNA_A_deaminase.
IPR025735. RHIM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF12721. RHIM. 2 hits.
PF02295. z-alpha. 2 hits.
[Graphical view ]
SMARTi SM00550. Zalpha. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 109 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

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