Q7Z2W4 (ZCCHV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ZC3HAV1
Synonyms:	ZC3HDC2
ORF Names:	PRO1677

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	902 AA.
Sequence status	Complete.
Protein existence	Evidence 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.22 Ref.23 Ref.25
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.16 Ref.17 Ref.22 Ref.23
Subcellular location	Isoform 1: Cytoplasm Ref.22. Nucleus. Note: Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner By similarity. Ref.22 Isoform 2: Cytoplasm Ref.22.
Induction	By type I interferon (IFN) and viruses. Isoform 2 is up-regulated by 3'-PPP-RNA. Ref.22
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.15
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.15

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to exogenous dsRNA Inferred from electronic annotation. Source: Compara 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.23Ref.22. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.22. Source: UniProtKB positive regulation of RIG-I signaling pathway Inferred from mutant phenotype Ref.22. Source: UniProtKB positive regulation of interferon-alpha production Inferred from direct assay Ref.22. Source: UniProtKB positive regulation of interferon-beta production Inferred from direct assay Ref.22. Source: UniProtKB positive regulation of mRNA catabolic process Inferred from direct assay Ref.23. Source: UniProtKB positive regulation of type I interferon production Inferred from electronic annotation. Source: Compara response to virus Inferred from direct assay Ref.23. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytoplasm Inferred from direct assay Ref.22. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX58	O95786	4	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 902

902

Zinc finger CCCH-type antiviral protein 1

PRO_0000211343

Regions

Domain

594 – 681

88

WWE

Domain

716 – 902

187

PARP catalytic

Zinc finger

73 – 86

14

C3H1-type 1

Zinc finger

88 – 110

23

C3H1-type 2

Zinc finger

150 – 172

23

C3H1-type 3

Zinc finger

169 – 193

25

C3H1-type 4

Region

1 – 254

254

N-terminal domain

Region

224 – 254

31

Binding to EXOSC5 By similarity

Motif

69 – 76

8

Nuclear localization signal By similarity

Motif

285 – 292

8

Nuclear export signal By similarity

Amino acid modifications

Modified residue

257

1

Phosphoserine; by GSK3-beta Ref.14

Modified residue

263

1

Phosphoserine; by GSK3-beta By similarity

Modified residue

267

1

Phosphoserine; by GSK3-beta By similarity

Modified residue

271

1

Phosphoserine; by GSK3-beta Ref.12

Modified residue

273

1

Phosphothreonine Ref.12

Modified residue

275

1

Phosphoserine Ref.12

Modified residue

284

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.12 Ref.14 Ref.18 Ref.24

Modified residue

302

1

Phosphoserine Ref.12 Ref.18

Modified residue

327

1

Phosphoserine By similarity

Modified residue

335

1

Phosphoserine Ref.14 Ref.18

Modified residue

355

1

Phosphoserine By similarity

Modified residue

378

1

Phosphoserine Ref.12 Ref.18

Modified residue

387

1

Phosphoserine Ref.12 Ref.14

Modified residue

393

1

Phosphothreonine Ref.12 Ref.14 Ref.18

Modified residue

492

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

1 – 539

539

Missing in isoform 4 and isoform 5.

VSP_010268

Alternative sequence

491 – 624

134

DSLSD…QYGEE → GKYKGKTLWASTFVHDIPNG SSQVVDKTTDVEKTGATGFG LTMAVKAEKDMLCTGSQSLR NLVPTTPGESTAPAQVSTLP QSPAALSSSNRAAVWGAQGQ NCTQVPVSSASELTRKTTGS AQCKSLKDKGASVS in isoform 3.

VSP_010270

Alternative sequence

625 – 902

278

Missing in isoform 3.

VSP_010271

Alternative sequence

699 – 902

204

DHQPA…ACVIS → E in isoform 2 and isoform 5.

VSP_010269

Natural variant

485

1

R → K. Ref.2
Corresponds to variant rs2236426 [ dbSNP | Ensembl ].

VAR_018454

Natural variant

565

1

H → Q. Ref.1 Ref.2
Corresponds to variant rs2297241 [ dbSNP | Ensembl ].

VAR_018455

Natural variant

701

1

Q → E. Ref.2 Ref.3 Ref.5
Corresponds to variant rs2297236 [ dbSNP | Ensembl ].

VAR_054319

Natural variant

851

1

T → I. Ref.3 Ref.5
Corresponds to variant rs3735007 [ dbSNP | Ensembl ].

VAR_018456

Experimental info

Sequence conflict

245

1

A → T in CAE11868. Ref.3

Secondary structure

1

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902

Helix Strand Turn

Details...

Beta strand

729 – 732

4

Helix

738 – 748

11

Beta strand

754 – 763

10

Helix

765 – 778

14

Beta strand

783 – 790

8

Helix

791 – 793

3

Helix

794 – 800

7

Helix

804 – 807

4

Beta strand

812 – 814

3

Beta strand

816 – 823

8

Helix

824 – 830

7

Helix

835 – 837

3

Beta strand

838 – 845

8

Beta strand

849 – 852

4

Beta strand

866 – 869

4

Beta strand

871 – 873

3

Beta strand

876 – 879

4

Helix

882 – 884

3

Beta strand

885 – 895

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ZAPL) [UniParc]. Last modified February 10, 2009. Version 3. Checksum: 72AB311D23658E24	FASTA	902	101,431
	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
	Isoform 2 (ZAPS) [UniParc]. Checksum: 372C52B7678BD888	FASTA	699	77,903
	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 LSFQGMIQTN IASKTQKDVI RRPTFVPQWY VQQMKRGPE
	Isoform 3 [UniParc]. Checksum: 1900A164D585DEFE	FASTA	624	67,590
	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 GKYKGKTLWA STFVHDIPNG SSQVVDKTTD VEKTGATGFG LTMAVKAEKD 550 560 570 580 590 600 MLCTGSQSLR NLVPTTPGES TAPAQVSTLP QSPAALSSSN RAAVWGAQGQ NCTQVPVSSA 610 620 SELTRKTTGS AQCKSLKDKG ASVS
	Isoform 4 [UniParc]. Checksum: F47044E719F91DFA	FASTA	363	42,115
	10 20 30 40 50 60 MLIGKTWTDF EHMETIEKGY CNPGIHLCSV GSYTINFRVM SCDSFPIRRL STPSSVTKPA 70 80 90 100 110 120 NSVFTTKWIW YWKNESGTWI QYGEEKDKRK NSNVDSSYLE SLYQSCPRGV VPFQAGSRNY 130 140 150 160 170 180 ELSFQGMIQT NIASKTQKDV IRRPTFVPQW YVQQMKRGPD HQPAKTSSVS LTATFRPQED 190 200 210 220 230 240 FCFLSSKKYK LSEIHHLHPE YVRVSEHFKA SMKNFKIEKI KKIENSELLD KFTWKKSQMK 250 260 270 280 290 300 EEGKLLFYAT SRAYVESICS NNFDSFLHET HENKYGKGIY FAKDAIYSHK NCPYDAKNVV 310 320 330 340 350 360 MFVAQVLVGK FTEGNITYTS PPPQFDSCVD TRSNPSVFVI FQKDQVYPQY VIEYTEDKAC VIS
	Isoform 5 [UniParc]. Checksum: EC59CEFD5B5CB421	FASTA	160	18,586
	10 20 30 40 50 60 MLIGKTWTDF EHMETIEKGY CNPGIHLCSV GSYTINFRVM SCDSFPIRRL STPSSVTKPA 70 80 90 100 110 120 NSVFTTKWIW YWKNESGTWI QYGEEKDKRK NSNVDSSYLE SLYQSCPRGV VPFQAGSRNY 130 140 150 160 ELSFQGMIQT NIASKTQKDV IRRPTFVPQW YVQQMKRGPE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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.
[20]	"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].
[21]	"ZAPS electrifies RIG-I signaling." Liu H.M., Gale M. Jr. Nat. Immunol. 12:11-12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[22]	"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.
[23]	"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.
[24]	"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, MASS SPECTROMETRY.
[25]	"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.

IPI

IPI00332936.
IPI00410067.
IPI00410069.
IPI00410070.
IPI00410071.

RefSeq

NP_064504.2. NM_020119.3.
NP_078901.3. NM_024625.3.

UniGene

Hs.133512.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2X5Y	X-ray	1.05	A	724-896	[»]

ProteinModelPortal

Q7Z2W4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7Z2W4. 6 interactions.

STRING

9606.ENSP00000242351.

PTM databases

PhosphoSite

Q7Z2W4.

Polymorphism databases

DMDM

223634727.

Proteomic databases

PaxDb

Q7Z2W4.

PRIDE

Q7Z2W4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000242351; ENSP00000242351; ENSG00000105939.
ENST00000471652; ENSP00000419855; ENSG00000105939.

GeneID

56829.

KEGG

hsa:56829.

UCSC

uc003vun.3. human.
uc003vuo.3. human.
uc003vup.3. human.

Organism-specific databases

CTD

56829.

GeneCards

GC07M138728.

H-InvDB

HIX0007129.

HGNC

HGNC:23721. ZC3HAV1.

HPA

HPA047818.

MIM

607312. gene.

neXtProt

NX_Q7Z2W4.

PharmGKB

PA134944289.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG83866.

HOVERGEN

HBG050384.

InParanoid

Q7Z2W4.

KO

K15259.

OrthoDB

EOG4HHP1P.

Gene expression databases

ArrayExpress

Q7Z2W4.

Bgee

Q7Z2W4.

CleanEx

HS_ZC3HAV1.

Genevestigator

Q7Z2W4.

GermOnline

ENSG00000105939. Homo sapiens.

Family and domain databases

InterPro

IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004170. WWE-dom.
IPR000571. Znf_CCCH.
[Graphical view]

Pfam

PF00644. PARP. 1 hit.
[Graphical view]

PROSITE

PS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
PS50103. ZF_C3H1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ZC3HAV1. human.

EvolutionaryTrace

Q7Z2W4.

GenomeRNAi

56829.

NextBio

62226.

PMAP-CutDB

Q7Z2W4.

SOURCE

Search...

Entry information

Entry name

ZCCHV_HUMAN

Accession

Primary (citable) accession number: Q7Z2W4
Secondary accession number(s): A4D1R2 , A4D1S4, Q8IW57, Q8TAJ3, Q96N79, Q9H8R9, Q9P0Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.