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Q7Z2W4 (ZCCHV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ZC3HAV1
Synonyms:ZC3HDC2
ORF Names:PRO1677
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.11 Ref.23 Ref.24 Ref.27

Subunit structure

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. Ref.17 Ref.18 Ref.23 Ref.24

Subcellular location

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. Ref.23

Isoform 2: Cytoplasm Ref.23.

Induction

By type I interferon (IFN) and viruses. Isoform 2 is up-regulated by 3'-PPP-RNA. Ref.23

Domain

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. Ref.16

Post-translational modification

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.

Sequence similarities

Contains 4 C3H1-type zinc fingers.

Contains 1 PARP catalytic domain.

Contains 1 WWE domain.

Biophysicochemical properties

Temperature dependence:

Thermostable. Ref.16

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to exogenous dsRNA

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of viral genome replication

Inferred from direct assay Ref.24Ref.23. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.23. Source: UniProtKB

positive regulation of RIG-I signaling pathway

Inferred from mutant phenotype Ref.23. Source: UniProtKB

positive regulation of interferon-alpha production

Inferred from direct assay Ref.23. Source: UniProtKB

positive regulation of interferon-beta production

Inferred from direct assay Ref.23. Source: UniProtKB

positive regulation of mRNA catabolic process

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of type I interferon production

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from direct assay Ref.24. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionNAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.23. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX58O957864EBI-922559,EBI-995350

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z2W4-1)

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.
Isoform 2 (identifier: Q7Z2W4-2)

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.
Isoform 3 (identifier: Q7Z2W4-3)

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.
Isoform 4 (identifier: Q7Z2W4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-539: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q7Z2W4-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 902901Zinc finger CCCH-type antiviral protein 1
PRO_0000211343

Regions

Domain594 – 68188WWE
Domain716 – 902187PARP catalytic
Zinc finger73 – 8614C3H1-type 1
Zinc finger88 – 11023C3H1-type 2
Zinc finger150 – 17223C3H1-type 3
Zinc finger169 – 19325C3H1-type 4
Region2 – 254253N-terminal domain
Region224 – 25431Binding to EXOSC5 By similarity
Motif69 – 768Nuclear localization signal By similarity
Motif285 – 2928Nuclear export signal By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.14 Ref.26
Modified residue2571Phosphoserine; by GSK3-beta Ref.15
Modified residue2631Phosphoserine; by GSK3-beta By similarity
Modified residue2671Phosphoserine; by GSK3-beta By similarity
Modified residue2711Phosphoserine; by GSK3-beta Ref.12
Modified residue2731Phosphothreonine Ref.12
Modified residue2751Phosphoserine Ref.12
Modified residue2841Phosphoserine Ref.6 Ref.7 Ref.8 Ref.12 Ref.15 Ref.19 Ref.25
Modified residue3021Phosphoserine Ref.12 Ref.19
Modified residue3271Phosphoserine By similarity
Modified residue3351Phosphoserine Ref.15 Ref.19
Modified residue3781Phosphoserine Ref.12 Ref.19
Modified residue3871Phosphoserine Ref.12 Ref.15
Modified residue3931Phosphothreonine Ref.12 Ref.15 Ref.19
Modified residue4921Phosphoserine Ref.19

Natural variations

Alternative sequence1 – 539539Missing in isoform 4 and isoform 5.
VSP_010268
Alternative sequence491 – 624134DSLSD…QYGEE → GKYKGKTLWASTFVHDIPNG SSQVVDKTTDVEKTGATGFG LTMAVKAEKDMLCTGSQSLR NLVPTTPGESTAPAQVSTLP QSPAALSSSNRAAVWGAQGQ NCTQVPVSSASELTRKTTGS AQCKSLKDKGASVS in isoform 3.
VSP_010270
Alternative sequence625 – 902278Missing in isoform 3.
VSP_010271
Alternative sequence699 – 902204DHQPA…ACVIS → E in isoform 2 and isoform 5.
VSP_010269
Natural variant4851R → K. Ref.2
Corresponds to variant rs2236426 [ dbSNP | Ensembl ].
VAR_018454
Natural variant5651H → Q. Ref.1 Ref.2
Corresponds to variant rs2297241 [ dbSNP | Ensembl ].
VAR_018455
Natural variant7011Q → E. Ref.2 Ref.3 Ref.5
Corresponds to variant rs2297236 [ dbSNP | Ensembl ].
VAR_054319
Natural variant8511T → I. Ref.3 Ref.5
Corresponds to variant rs3735007 [ dbSNP | Ensembl ].
VAR_018456

Experimental info

Sequence conflict2451A → T in CAE11868. Ref.3

Secondary structure

.................................. 902
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ZAPL) [UniParc].

Last modified February 10, 2009. Version 3.
Checksum: 72AB311D23658E24

FASTA902101,431
        10         20         30         40         50         60 
MADPEVCCFI TKILCAHGGR MALDALLQEI ALSEPQLCEV LQVAGPDRFV VLETGGEAGI 

        70         80         90        100        110        120 
TRSVVATTRA RVCRRKYCQR PCDNLHLCKL NLLGRCNYSQ SERNLCKYSH EVLSEENFKV 

       130        140        150        160        170        180 
LKNHELSGLN KEELAVLLLQ SDPFFMPEIC KSYKGEGRQQ ICNQQPPCSR LHICDHFTRG 

       190        200        210        220        230        240 
NCRFPNCLRS HNLMDRKVLA IMREHGLNPD VVQNIQDICN SKHMQKNPPG PRAPSSHRRN 

       250        260        270        280        290        300 
MAYRARSKSR DRFFQGSQEF LASASASAER SCTPSPDQIS HRASLEDAPV DDLTRKFTYL 

       310        320        330        340        350        360 
GSQDRARPPS GSSKATDLGG TSQAGTSQRF LENGSQEDLL HGNPGSTYLA SNSTSAPNWK 

       370        380        390        400        410        420 
SLTSWTNDQG ARRKTVFSPT LPAARSSLGS LQTPEAVTTR KGTGLLSSDY RIINGKSGTQ 

       430        440        450        460        470        480 
DIQPGPLFNN NADGVATDIT STRSLNYKST SSGHREISSP RIQDAGPASR DVQATGRIAD 

       490        500        510        520        530        540 
DADPRVALVN DSLSDVTSTT SSRVDDHDSE EICLDHLCKG CPLNGSCSKV HFHLPYRWQM 

       550        560        570        580        590        600 
LIGKTWTDFE HMETIEKGYC NPGIHLCSVG SYTINFRVMS CDSFPIRRLS TPSSVTKPAN 

       610        620        630        640        650        660 
SVFTTKWIWY WKNESGTWIQ YGEEKDKRKN SNVDSSYLES LYQSCPRGVV PFQAGSRNYE 

       670        680        690        700        710        720 
LSFQGMIQTN IASKTQKDVI RRPTFVPQWY VQQMKRGPDH QPAKTSSVSL TATFRPQEDF 

       730        740        750        760        770        780 
CFLSSKKYKL SEIHHLHPEY VRVSEHFKAS MKNFKIEKIK KIENSELLDK FTWKKSQMKE 

       790        800        810        820        830        840 
EGKLLFYATS RAYVESICSN NFDSFLHETH ENKYGKGIYF AKDAIYSHKN CPYDAKNVVM 

       850        860        870        880        890        900 
FVAQVLVGKF TEGNITYTSP PPQFDSCVDT RSNPSVFVIF QKDQVYPQYV IEYTEDKACV 


IS 

« Hide

Isoform 2 (ZAPS) [UniParc].

Checksum: 372C52B7678BD888
Show »

FASTA69977,903
Isoform 3 [UniParc].

Checksum: 1900A164D585DEFE
Show »

FASTA62467,590
Isoform 4 [UniParc].

Checksum: F47044E719F91DFA
Show »

FASTA36342,115
Isoform 5 [UniParc].

Checksum: EC59CEFD5B5CB421
Show »

FASTA16018,586

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"ZAPS electrifies RIG-I signaling."
Liu H.M., Gale M. Jr.
Nat. Immunol. 12:11-12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[23]"ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses."
Hayakawa S., Shiratori S., Yamato H., Kameyama T., Kitatsuji C., Kashigi F., Goto S., Kameoka S., Fujikura D., Yamada T., Mizutani T., Kazumata M., Sato M., Tanaka J., Asaka M., Ohba Y., Miyazaki T., Imamura M., Takaoka A.
Nat. Immunol. 12:37-44(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS55171.1. [Q7Z2W4-2]
CCDS5851.1. [Q7Z2W4-1]
RefSeqNP_064504.2. NM_020119.3. [Q7Z2W4-1]
NP_078901.3. NM_024625.3. [Q7Z2W4-2]
UniGeneHs.133512.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X5YX-ray1.05A724-896[»]
ProteinModelPortalQ7Z2W4.
SMRQ7Z2W4. Positions 3-225, 726-896.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121203. 24 interactions.
DIPDIP-37896N.
IntActQ7Z2W4. 9 interactions.
MINTMINT-5006396.
STRING9606.ENSP00000242351.

PTM databases

PhosphoSiteQ7Z2W4.

Polymorphism databases

DMDM223634727.

Proteomic databases

MaxQBQ7Z2W4.
PaxDbQ7Z2W4.
PRIDEQ7Z2W4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242351; ENSP00000242351; ENSG00000105939. [Q7Z2W4-1]
ENST00000471652; ENSP00000419855; ENSG00000105939. [Q7Z2W4-2]
GeneID56829.
KEGGhsa:56829.
UCSCuc003vun.3. human. [Q7Z2W4-1]
uc003vuo.3. human. [Q7Z2W4-5]
uc003vup.3. human. [Q7Z2W4-2]

Organism-specific databases

CTD56829.
GeneCardsGC07M138728.
H-InvDBHIX0007129.
HGNCHGNC:23721. ZC3HAV1.
HPAHPA047818.
MIM607312. gene.
neXtProtNX_Q7Z2W4.
PharmGKBPA134944289.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83866.
HOVERGENHBG050384.
InParanoidQ7Z2W4.
KOK15259.
OrthoDBEOG7P5T0J.
PhylomeDBQ7Z2W4.
TreeFamTF338389.

Gene expression databases

ArrayExpressQ7Z2W4.
BgeeQ7Z2W4.
CleanExHS_ZC3HAV1.
GenevestigatorQ7Z2W4.

Family and domain databases

Gene3D3.90.228.10. 1 hit.
InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004170. WWE-dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamPF00644. PARP. 1 hit.
[Graphical view]
PROSITEPS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
PS50103. ZF_C3H1. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZC3HAV1. human.
EvolutionaryTraceQ7Z2W4.
GeneWikiZC3HAV1.
GenomeRNAi56829.
NextBio62226.
PMAP-CutDBQ7Z2W4.
PROQ7Z2W4.
SOURCESearch...

Entry information

Entry nameZCCHV_HUMAN
AccessionPrimary (citable) accession number: Q7Z2W4
Secondary accession number(s): A4D1R2 expand/collapse secondary AC list , A4D1S4, Q8IW57, Q8TAJ3, Q96N79, Q9H8R9, Q9P0Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM