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Q7Z2W4

- ZCCHV_HUMAN

UniProt

Q7Z2W4 - ZCCHV_HUMAN

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Protein

Zinc finger CCCH-type antiviral protein 1

Gene
ZC3HAV1, ZC3HDC2, PRO1677
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1Add
BLAST
Zinc fingeri88 – 11023C3H1-type 2Add
BLAST
Zinc fingeri150 – 17223C3H1-type 3Add
BLAST
Zinc fingeri169 – 19325C3H1-type 4Add
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
Complete GO annotation...

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.1 Publication
Isoform 2 : Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134944289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
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-beta By similarity
Modified residuei267 – 2671Phosphoserine; by GSK3-beta By 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 – 3271Phosphoserine By 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.

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.4 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.

Miscellaneous databases

EvolutionaryTraceiQ7Z2W4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini594 – 68188WWEAdd
BLAST
Domaini716 – 902187PARP catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 254253N-terminal domainAdd
BLAST
Regioni224 – 25431Binding to EXOSC5 By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi69 – 768Nuclear localization signal By similarity
Motifi285 – 2928Nuclear export signal By 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 1 WWE domain.

Zinc finger

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

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. VSP_010268Add
BLAST
Alternative sequencei491 – 624134DSLSD…QYGEE → GKYKGKTLWASTFVHDIPNG SSQVVDKTTDVEKTGATGFG LTMAVKAEKDMLCTGSQSLR NLVPTTPGESTAPAQVSTLP QSPAALSSSNRAAVWGAQGQ NCTQVPVSSASELTRKTTGS AQCKSLKDKGASVS in isoform 3. VSP_010270Add
BLAST
Alternative sequencei625 – 902278Missing in isoform 3. VSP_010271Add
BLAST
Alternative sequencei699 – 902204DHQPA…ACVIS → E in isoform 2 and isoform 5. VSP_010269Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451A → T in CAE11868. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 112 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

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