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Q7Z2W4

- ZCCHV_HUMAN

UniProt

Q7Z2W4 - ZCCHV_HUMAN

Protein

Zinc finger CCCH-type antiviral protein 1

Gene

ZC3HAV1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs).4 Publications

    Temperature dependencei

    Thermostable.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri73 – 8614C3H1-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri88 – 11023C3H1-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri150 – 17223C3H1-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri169 – 19325C3H1-type 4PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. NAD+ ADP-ribosyltransferase activity Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to exogenous dsRNA Source: Ensembl
    2. defense response to virus Source: UniProtKB-KW
    3. innate immune response Source: UniProtKB-KW
    4. negative regulation of viral genome replication Source: UniProtKB
    5. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    6. positive regulation of interferon-alpha production Source: UniProtKB
    7. positive regulation of interferon-beta production Source: UniProtKB
    8. positive regulation of mRNA catabolic process Source: UniProtKB
    9. positive regulation of RIG-I signaling pathway Source: UniProtKB
    10. positive regulation of type I interferon production Source: Ensembl
    11. response to virus Source: UniProtKB

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger CCCH-type antiviral protein 1
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 13
    Short name:
    ARTD13
    Zinc finger CCCH domain-containing protein 2
    Zinc finger antiviral protein
    Short name:
    ZAP
    Gene namesi
    Name:ZC3HAV1
    Synonyms:ZC3HDC2
    ORF Names:PRO1677
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:23721. ZC3HAV1.

    Subcellular locationi

    Isoform 1 : Cytoplasm. Nucleus
    Note: Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. Golgi apparatus Source: HPA
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134944289.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 902901Zinc finger CCCH-type antiviral protein 1PRO_0000211343Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei257 – 2571Phosphoserine; by GSK3-beta1 Publication
    Modified residuei263 – 2631Phosphoserine; by GSK3-betaBy similarity
    Modified residuei267 – 2671Phosphoserine; by GSK3-betaBy similarity
    Modified residuei271 – 2711Phosphoserine; by GSK3-beta1 Publication
    Modified residuei273 – 2731Phosphothreonine1 Publication
    Modified residuei275 – 2751Phosphoserine1 Publication
    Modified residuei284 – 2841Phosphoserine7 Publications
    Modified residuei302 – 3021Phosphoserine2 Publications
    Modified residuei327 – 3271PhosphoserineBy similarity
    Modified residuei335 – 3351Phosphoserine2 Publications
    Modified residuei378 – 3781Phosphoserine2 Publications
    Modified residuei387 – 3871Phosphoserine2 Publications
    Modified residuei393 – 3931Phosphothreonine3 Publications
    Modified residuei492 – 4921Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-275 is essential for sequential phosphorylation of Ser-271, Ser-267, Ser-263 and Ser-257 by GSK3-beta. Phosphorylation by GSK3-beta enhances its antiviral activity By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z2W4.
    PaxDbiQ7Z2W4.
    PRIDEiQ7Z2W4.

    PTM databases

    PhosphoSiteiQ7Z2W4.

    Miscellaneous databases

    PMAP-CutDBQ7Z2W4.

    Expressioni

    Inductioni

    By type I interferon (IFN) and viruses. Isoform 2 is up-regulated by 3'-PPP-RNA.1 Publication

    Gene expression databases

    ArrayExpressiQ7Z2W4.
    BgeeiQ7Z2W4.
    CleanExiHS_ZC3HAV1.
    GenevestigatoriQ7Z2W4.

    Organism-specific databases

    HPAiHPA047818.

    Interactioni

    Subunit structurei

    Homodimer or homooligomer. Homooligomerization is essential for its antiviral activity. Interacts with EXOSC5 By similarity. Interacts (via N-terminal domain) with DDX17 in an RNA-independent manner By similarity. Interacts with EXOSC3, EXOSC7, DCP2 and DCP1A. Interacts with PARN in an RNA-independent manner. Interacts with XRN1 in an RNA-dependent manner. Isoform 2 interacts (via zinc-fingers) with DDX58/RIG-I in an RNA-dependent manner. Interacts (via N-terminal domain) with DHX30 (via N-terminus) in an RNA-independent manner.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX58O957864EBI-922559,EBI-995350

    Protein-protein interaction databases

    BioGridi121203. 26 interactions.
    DIPiDIP-37896N.
    IntActiQ7Z2W4. 9 interactions.
    MINTiMINT-5006396.
    STRINGi9606.ENSP00000242351.

    Structurei

    Secondary structure

    1
    902
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi729 – 7324
    Helixi738 – 74811
    Beta strandi754 – 76310
    Helixi765 – 77814
    Beta strandi783 – 7908
    Helixi791 – 7933
    Helixi794 – 8007
    Helixi804 – 8074
    Beta strandi812 – 8143
    Beta strandi816 – 8238
    Helixi824 – 8307
    Helixi835 – 8373
    Beta strandi838 – 8458
    Beta strandi849 – 8524
    Beta strandi866 – 8694
    Beta strandi871 – 8733
    Beta strandi876 – 8794
    Helixi882 – 8843
    Beta strandi885 – 89511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X5YX-ray1.05A724-896[»]
    ProteinModelPortaliQ7Z2W4.
    SMRiQ7Z2W4. Positions 3-225, 726-896.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z2W4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini594 – 68188WWEPROSITE-ProRule annotationAdd
    BLAST
    Domaini716 – 902187PARP catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 254253N-terminal domainAdd
    BLAST
    Regioni224 – 25431Binding to EXOSC5By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi69 – 768Nuclear localization signalBy similarity
    Motifi285 – 2928Nuclear export signalBy similarity

    Domaini

    The N-terminal domain is sufficient to bind to viral RNAs and promote their degradation. The second and fourth zinc fingers are involved in binding to specific viral RNAs.1 Publication

    Sequence similaritiesi

    Contains 4 C3H1-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
    Contains 1 WWE domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri73 – 8614C3H1-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri88 – 11023C3H1-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri150 – 17223C3H1-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri169 – 19325C3H1-type 4PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG83866.
    HOVERGENiHBG050384.
    InParanoidiQ7Z2W4.
    KOiK15259.
    OrthoDBiEOG7P5T0J.
    PhylomeDBiQ7Z2W4.
    TreeFamiTF338389.

    Family and domain databases

    Gene3Di3.90.228.10. 1 hit.
    InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004170. WWE-dom.
    IPR000571. Znf_CCCH.
    [Graphical view]
    PfamiPF00644. PARP. 1 hit.
    [Graphical view]
    PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
    PS50918. WWE. 1 hit.
    PS50103. ZF_C3H1. 3 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z2W4-1) [UniParc]FASTAAdd to Basket

    Also known as: ZAPL

    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

    MADPEVCCFI TKILCAHGGR MALDALLQEI ALSEPQLCEV LQVAGPDRFV    50
    VLETGGEAGI TRSVVATTRA RVCRRKYCQR PCDNLHLCKL NLLGRCNYSQ 100
    SERNLCKYSH EVLSEENFKV LKNHELSGLN KEELAVLLLQ SDPFFMPEIC 150
    KSYKGEGRQQ ICNQQPPCSR LHICDHFTRG NCRFPNCLRS HNLMDRKVLA 200
    IMREHGLNPD VVQNIQDICN SKHMQKNPPG PRAPSSHRRN MAYRARSKSR 250
    DRFFQGSQEF LASASASAER SCTPSPDQIS HRASLEDAPV DDLTRKFTYL 300
    GSQDRARPPS GSSKATDLGG TSQAGTSQRF LENGSQEDLL HGNPGSTYLA 350
    SNSTSAPNWK SLTSWTNDQG ARRKTVFSPT LPAARSSLGS LQTPEAVTTR 400
    KGTGLLSSDY RIINGKSGTQ DIQPGPLFNN NADGVATDIT STRSLNYKST 450
    SSGHREISSP RIQDAGPASR DVQATGRIAD DADPRVALVN DSLSDVTSTT 500
    SSRVDDHDSE EICLDHLCKG CPLNGSCSKV HFHLPYRWQM LIGKTWTDFE 550
    HMETIEKGYC NPGIHLCSVG SYTINFRVMS CDSFPIRRLS TPSSVTKPAN 600
    SVFTTKWIWY WKNESGTWIQ YGEEKDKRKN SNVDSSYLES LYQSCPRGVV 650
    PFQAGSRNYE LSFQGMIQTN IASKTQKDVI RRPTFVPQWY VQQMKRGPDH 700
    QPAKTSSVSL TATFRPQEDF CFLSSKKYKL SEIHHLHPEY VRVSEHFKAS 750
    MKNFKIEKIK KIENSELLDK FTWKKSQMKE EGKLLFYATS RAYVESICSN 800
    NFDSFLHETH ENKYGKGIYF AKDAIYSHKN CPYDAKNVVM FVAQVLVGKF 850
    TEGNITYTSP PPQFDSCVDT RSNPSVFVIF QKDQVYPQYV IEYTEDKACV 900
    IS 902
    Length:902
    Mass (Da):101,431
    Last modified:February 10, 2009 - v3
    Checksum:i72AB311D23658E24
    GO
    Isoform 2 (identifier: Q7Z2W4-2) [UniParc]FASTAAdd to Basket

    Also known as: ZAPS

    The sequence of this isoform differs from the canonical sequence as follows:
         699-902: DHQPAKTSSV...YTEDKACVIS → E

    Note: No experimental confirmation available.

    Show »
    Length:699
    Mass (Da):77,903
    Checksum:i372C52B7678BD888
    GO
    Isoform 3 (identifier: Q7Z2W4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         491-624: DSLSDVTSTT...SGTWIQYGEE → GKYKGKTLWA...SLKDKGASVS
         625-902: Missing.

    Note: No experimental confirmation available. Contains a phosphoserine at position 572.

    Show »
    Length:624
    Mass (Da):67,590
    Checksum:i1900A164D585DEFE
    GO
    Isoform 4 (identifier: Q7Z2W4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-539: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:363
    Mass (Da):42,115
    Checksum:iF47044E719F91DFA
    GO
    Isoform 5 (identifier: Q7Z2W4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-539: Missing.
         699-902: DHQPAKTSSV...YTEDKACVIS → E

    Note: No experimental confirmation available.

    Show »
    Length:160
    Mass (Da):18,586
    Checksum:iEC59CEFD5B5CB421
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti245 – 2451A → T in CAE11868. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti485 – 4851R → K.1 Publication
    Corresponds to variant rs2236426 [ dbSNP | Ensembl ].
    VAR_018454
    Natural varianti565 – 5651H → Q.2 Publications
    Corresponds to variant rs2297241 [ dbSNP | Ensembl ].
    VAR_018455
    Natural varianti701 – 7011Q → E.3 Publications
    Corresponds to variant rs2297236 [ dbSNP | Ensembl ].
    VAR_054319
    Natural varianti851 – 8511T → I.2 Publications
    Corresponds to variant rs3735007 [ dbSNP | Ensembl ].
    VAR_018456

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 539539Missing in isoform 4 and isoform 5. 2 PublicationsVSP_010268Add
    BLAST
    Alternative sequencei491 – 624134DSLSD…QYGEE → GKYKGKTLWASTFVHDIPNG SSQVVDKTTDVEKTGATGFG LTMAVKAEKDMLCTGSQSLR NLVPTTPGESTAPAQVSTLP QSPAALSSSNRAAVWGAQGQ NCTQVPVSSASELTRKTTGS AQCKSLKDKGASVS in isoform 3. 1 PublicationVSP_010270Add
    BLAST
    Alternative sequencei625 – 902278Missing in isoform 3. 1 PublicationVSP_010271Add
    BLAST
    Alternative sequencei699 – 902204DHQPA…ACVIS → E in isoform 2 and isoform 5. 2 PublicationsVSP_010269Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF138863 mRNA. Translation: AAF61195.1.
    AK055851 mRNA. Translation: BAB71028.1.
    AK023350 mRNA. Translation: BAB14537.1.
    BX571742 mRNA. Translation: CAE11868.1.
    CH236950 Genomic DNA. Translation: EAL24040.1.
    CH236950 Genomic DNA. Translation: EAL24041.1.
    BC025308 mRNA. Translation: AAH25308.1.
    BC027462 mRNA. Translation: AAH27462.1.
    BC033105 mRNA. Translation: AAH33105.1.
    BC040956 mRNA. Translation: AAH40956.1.
    CCDSiCCDS55171.1. [Q7Z2W4-2]
    CCDS5851.1. [Q7Z2W4-1]
    RefSeqiNP_064504.2. NM_020119.3. [Q7Z2W4-1]
    NP_078901.3. NM_024625.3. [Q7Z2W4-2]
    UniGeneiHs.133512.

    Genome annotation databases

    EnsembliENST00000242351; ENSP00000242351; ENSG00000105939. [Q7Z2W4-1]
    ENST00000471652; ENSP00000419855; ENSG00000105939. [Q7Z2W4-2]
    GeneIDi56829.
    KEGGihsa:56829.
    UCSCiuc003vun.3. human. [Q7Z2W4-1]
    uc003vuo.3. human. [Q7Z2W4-5]
    uc003vup.3. human. [Q7Z2W4-2]

    Polymorphism databases

    DMDMi223634727.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF138863 mRNA. Translation: AAF61195.1 .
    AK055851 mRNA. Translation: BAB71028.1 .
    AK023350 mRNA. Translation: BAB14537.1 .
    BX571742 mRNA. Translation: CAE11868.1 .
    CH236950 Genomic DNA. Translation: EAL24040.1 .
    CH236950 Genomic DNA. Translation: EAL24041.1 .
    BC025308 mRNA. Translation: AAH25308.1 .
    BC027462 mRNA. Translation: AAH27462.1 .
    BC033105 mRNA. Translation: AAH33105.1 .
    BC040956 mRNA. Translation: AAH40956.1 .
    CCDSi CCDS55171.1. [Q7Z2W4-2 ]
    CCDS5851.1. [Q7Z2W4-1 ]
    RefSeqi NP_064504.2. NM_020119.3. [Q7Z2W4-1 ]
    NP_078901.3. NM_024625.3. [Q7Z2W4-2 ]
    UniGenei Hs.133512.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X5Y X-ray 1.05 A 724-896 [» ]
    ProteinModelPortali Q7Z2W4.
    SMRi Q7Z2W4. Positions 3-225, 726-896.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121203. 26 interactions.
    DIPi DIP-37896N.
    IntActi Q7Z2W4. 9 interactions.
    MINTi MINT-5006396.
    STRINGi 9606.ENSP00000242351.

    PTM databases

    PhosphoSitei Q7Z2W4.

    Polymorphism databases

    DMDMi 223634727.

    Proteomic databases

    MaxQBi Q7Z2W4.
    PaxDbi Q7Z2W4.
    PRIDEi Q7Z2W4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242351 ; ENSP00000242351 ; ENSG00000105939 . [Q7Z2W4-1 ]
    ENST00000471652 ; ENSP00000419855 ; ENSG00000105939 . [Q7Z2W4-2 ]
    GeneIDi 56829.
    KEGGi hsa:56829.
    UCSCi uc003vun.3. human. [Q7Z2W4-1 ]
    uc003vuo.3. human. [Q7Z2W4-5 ]
    uc003vup.3. human. [Q7Z2W4-2 ]

    Organism-specific databases

    CTDi 56829.
    GeneCardsi GC07M138728.
    H-InvDB HIX0007129.
    HGNCi HGNC:23721. ZC3HAV1.
    HPAi HPA047818.
    MIMi 607312. gene.
    neXtProti NX_Q7Z2W4.
    PharmGKBi PA134944289.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83866.
    HOVERGENi HBG050384.
    InParanoidi Q7Z2W4.
    KOi K15259.
    OrthoDBi EOG7P5T0J.
    PhylomeDBi Q7Z2W4.
    TreeFami TF338389.

    Miscellaneous databases

    ChiTaRSi ZC3HAV1. human.
    EvolutionaryTracei Q7Z2W4.
    GeneWikii ZC3HAV1.
    GenomeRNAii 56829.
    NextBioi 62226.
    PMAP-CutDB Q7Z2W4.
    PROi Q7Z2W4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z2W4.
    Bgeei Q7Z2W4.
    CleanExi HS_ZC3HAV1.
    Genevestigatori Q7Z2W4.

    Family and domain databases

    Gene3Di 3.90.228.10. 1 hit.
    InterProi IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004170. WWE-dom.
    IPR000571. Znf_CCCH.
    [Graphical view ]
    Pfami PF00644. PARP. 1 hit.
    [Graphical view ]
    PROSITEi PS51059. PARP_CATALYTIC. 1 hit.
    PS50918. WWE. 1 hit.
    PS50103. ZF_C3H1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional prediction of the coding sequences of 5 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Zhou G., Wei H., Bi J., Xu W., Zai Y., Feng F., Liu M., He F.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT GLN-565.
      Tissue: Fetal liver.
    2. "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] (ISOFORMS 3 AND 4), VARIANTS LYS-485; GLN-565 AND GLU-701.
      Tissue: Kidney and Ovarian carcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-701 AND ILE-851.
      Tissue: Endometrium.
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2), VARIANTS GLU-701 AND ILE-851.
      Tissue: Brain and Uterus.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein."
      Kerns J.A., Emerman M., Malik H.S.
      PLoS Genet. 4:E21-E21(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-273; SER-275; SER-284; SER-302; SER-378; SER-387 AND THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "ZAP-mediated mRNA degradation."
      Zhu Y., Gao G.
      RNA Biol. 5:65-67(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-284; SER-335; SER-387 AND THR-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Expression and RNA-binding of human zinc-finger antiviral protein."
      Jeong M.S., Kim E.J., Jang S.B.
      Biochem. Biophys. Res. Commun. 396:696-702(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, RNA-BINDING, DOMAIN N-TERMINAL.
    17. "Identification of a dominant negative inhibitor of human zinc finger antiviral protein reveals a functional endogenous pool and critical homotypic interactions."
      Law L.M., Albin O.R., Carroll J.W., Jones C.T., Rice C.M., Macdonald M.R.
      J. Virol. 84:4504-4512(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    18. "DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein."
      Ye P., Liu S., Zhu Y., Chen G., Gao G.
      Protein Cell 1:956-964(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DHX30.
    19. "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-284; SER-302; SER-335; SER-378; THR-393 AND SER-492, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
      Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
      Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: REVIEW.
    23. Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH DDX58/RIG-I.
    24. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
      Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EXOSC3; EXOSC7; PARN; DCP2; DCP1A AND XRN1.
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Zinc-finger antiviral protein inhibits XMRV infection."
      Wang X., Tu F., Zhu Y., Gao G.
      PLoS ONE 7:E39159-E39159(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiZCCHV_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z2W4
    Secondary accession number(s): A4D1R2
    , A4D1S4, Q8IW57, Q8TAJ3, Q96N79, Q9H8R9, Q9P0Y7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 113 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3