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Protein

Zinc finger CCCH-type antiviral protein 1

Gene

ZC3HAV1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri73 – 86C3H1-type 1PROSITE-ProRule annotationAdd BLAST14
Zinc fingeri88 – 110C3H1-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri150 – 172C3H1-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri169 – 193C3H1-type 4PROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • NAD+ ADP-ribosyltransferase activity Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to exogenous dsRNA Source: Ensembl
  • defense response to virus Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • negative regulation of viral genome replication Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of interferon-alpha production Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: UniProtKB
  • positive regulation of RIG-I signaling pathway Source: UniProtKB
  • positive regulation of type I interferon production Source: Ensembl
  • response to virus Source: UniProtKB
  • suppression by virus of host molecular function Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-6802952. Signaling by BRAF and RAF fusions.

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
Proteomesi
  • UP000005640 Componenti: 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

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • Golgi apparatus Source: HPA
  • late endosome Source: Ensembl
  • lysosome Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi56829.
OpenTargetsiENSG00000105939.
PharmGKBiPA134944289.

Polymorphism and mutation databases

BioMutaiZC3HAV1.
DMDMi223634727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002113432 – 902Zinc finger CCCH-type antiviral protein 1Add BLAST901

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei257Phosphoserine; by GSK3-betaCombined sources1
Modified residuei263Phosphoserine; by GSK3-betaBy similarity1
Modified residuei267Phosphoserine; by GSK3-betaBy similarity1
Modified residuei271Phosphoserine; by GSK3-betaCombined sources1
Modified residuei273PhosphothreonineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei302PhosphoserineCombined sources1
Modified residuei327PhosphoserineBy similarity1
Modified residuei335PhosphoserineCombined sources1
Modified residuei355PhosphoserineCombined sources1
Modified residuei378PhosphoserineCombined sources1
Modified residuei387PhosphoserineCombined sources1
Modified residuei393PhosphothreonineCombined sources1
Modified residuei407PhosphoserineCombined sources1
Modified residuei469PhosphoserineCombined sources1
Modified residuei492PhosphoserineCombined sources1
Modified residuei494PhosphoserineCombined sources1
Modified residuei554PhosphothreonineCombined sources1
Modified residuei590PhosphoserineCombined sources1
Isoform 3 (identifier: Q7Z2W4-3)
Modified residuei572PhosphoserineCombined sources1

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

EPDiQ7Z2W4.
MaxQBiQ7Z2W4.
PaxDbiQ7Z2W4.
PeptideAtlasiQ7Z2W4.
PRIDEiQ7Z2W4.

PTM databases

iPTMnetiQ7Z2W4.
PhosphoSitePlusiQ7Z2W4.
SwissPalmiQ7Z2W4.

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

BgeeiENSG00000105939.
CleanExiHS_ZC3HAV1.
ExpressionAtlasiQ7Z2W4. baseline and differential.
GenevisibleiQ7Z2W4. HS.

Organism-specific databases

HPAiHPA047818.
HPA059096.

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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi121203. 132 interactors.
DIPiDIP-37896N.
IntActiQ7Z2W4. 17 interactors.
MINTiMINT-5006396.
STRINGi9606.ENSP00000242351.

Structurei

Secondary structure

1902
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi729 – 732Combined sources4
Helixi738 – 748Combined sources11
Beta strandi754 – 763Combined sources10
Helixi765 – 778Combined sources14
Beta strandi783 – 790Combined sources8
Helixi791 – 793Combined sources3
Helixi794 – 800Combined sources7
Helixi804 – 807Combined sources4
Beta strandi812 – 814Combined sources3
Beta strandi816 – 823Combined sources8
Helixi824 – 830Combined sources7
Helixi835 – 837Combined sources3
Beta strandi838 – 845Combined sources8
Beta strandi849 – 852Combined sources4
Beta strandi866 – 869Combined sources4
Beta strandi871 – 873Combined sources3
Beta strandi876 – 879Combined sources4
Helixi882 – 884Combined sources3
Beta strandi885 – 895Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X5YX-ray1.05A724-896[»]
4X52X-ray2.08A/B/C/D726-896[»]
ProteinModelPortaliQ7Z2W4.
SMRiQ7Z2W4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z2W4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini594 – 681WWEPROSITE-ProRule annotationAdd BLAST88
Domaini716 – 902PARP catalyticPROSITE-ProRule annotationAdd BLAST187

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 254N-terminal domainAdd BLAST253
Regioni224 – 254Binding to EXOSC5By similarityAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi69 – 76Nuclear localization signalBy similarity8
Motifi285 – 292Nuclear export signalBy similarity8

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)DescriptionActionsGraphical viewLength
Zinc fingeri73 – 86C3H1-type 1PROSITE-ProRule annotationAdd BLAST14
Zinc fingeri88 – 110C3H1-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri150 – 172C3H1-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri169 – 193C3H1-type 4PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IEI4. Eukaryota.
ENOG410ZFB8. LUCA.
GeneTreeiENSGT00760000119084.
HOVERGENiHBG050384.
InParanoidiQ7Z2W4.
KOiK15259.
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.
PF02825. WWE. 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. AlignAdd to basket

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

        10         20         30         40         50
MADPEVCCFI TKILCAHGGR MALDALLQEI ALSEPQLCEV LQVAGPDRFV
60 70 80 90 100
VLETGGEAGI TRSVVATTRA RVCRRKYCQR PCDNLHLCKL NLLGRCNYSQ
110 120 130 140 150
SERNLCKYSH EVLSEENFKV LKNHELSGLN KEELAVLLLQ SDPFFMPEIC
160 170 180 190 200
KSYKGEGRQQ ICNQQPPCSR LHICDHFTRG NCRFPNCLRS HNLMDRKVLA
210 220 230 240 250
IMREHGLNPD VVQNIQDICN SKHMQKNPPG PRAPSSHRRN MAYRARSKSR
260 270 280 290 300
DRFFQGSQEF LASASASAER SCTPSPDQIS HRASLEDAPV DDLTRKFTYL
310 320 330 340 350
GSQDRARPPS GSSKATDLGG TSQAGTSQRF LENGSQEDLL HGNPGSTYLA
360 370 380 390 400
SNSTSAPNWK SLTSWTNDQG ARRKTVFSPT LPAARSSLGS LQTPEAVTTR
410 420 430 440 450
KGTGLLSSDY RIINGKSGTQ DIQPGPLFNN NADGVATDIT STRSLNYKST
460 470 480 490 500
SSGHREISSP RIQDAGPASR DVQATGRIAD DADPRVALVN DSLSDVTSTT
510 520 530 540 550
SSRVDDHDSE EICLDHLCKG CPLNGSCSKV HFHLPYRWQM LIGKTWTDFE
560 570 580 590 600
HMETIEKGYC NPGIHLCSVG SYTINFRVMS CDSFPIRRLS TPSSVTKPAN
610 620 630 640 650
SVFTTKWIWY WKNESGTWIQ YGEEKDKRKN SNVDSSYLES LYQSCPRGVV
660 670 680 690 700
PFQAGSRNYE LSFQGMIQTN IASKTQKDVI RRPTFVPQWY VQQMKRGPDH
710 720 730 740 750
QPAKTSSVSL TATFRPQEDF CFLSSKKYKL SEIHHLHPEY VRVSEHFKAS
760 770 780 790 800
MKNFKIEKIK KIENSELLDK FTWKKSQMKE EGKLLFYATS RAYVESICSN
810 820 830 840 850
NFDSFLHETH ENKYGKGIYF AKDAIYSHKN CPYDAKNVVM FVAQVLVGKF
860 870 880 890 900
TEGNITYTSP PPQFDSCVDT RSNPSVFVIF QKDQVYPQYV IEYTEDKACV

IS
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.Combined sources
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)DescriptionActionsGraphical viewLength
Sequence conflicti245A → T in CAE11868 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018454485R → K.1 PublicationCorresponds to variant rs2236426dbSNPEnsembl.1
Natural variantiVAR_018455565H → Q.2 PublicationsCorresponds to variant rs2297241dbSNPEnsembl.1
Natural variantiVAR_054319701Q → E.3 PublicationsCorresponds to variant rs2297236dbSNPEnsembl.1
Natural variantiVAR_018456851T → I.2 PublicationsCorresponds to variant rs3735007dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0102681 – 539Missing in isoform 4 and isoform 5. 2 PublicationsAdd BLAST539
Alternative sequenceiVSP_010270491 – 624DSLSD…QYGEE → GKYKGKTLWASTFVHDIPNG SSQVVDKTTDVEKTGATGFG LTMAVKAEKDMLCTGSQSLR NLVPTTPGESTAPAQVSTLP QSPAALSSSNRAAVWGAQGQ NCTQVPVSSASELTRKTTGS AQCKSLKDKGASVS in isoform 3. 1 PublicationAdd BLAST134
Alternative sequenceiVSP_010271625 – 902Missing in isoform 3. 1 PublicationAdd BLAST278
Alternative sequenceiVSP_010269699 – 902DHQPA…ACVIS → E in isoform 2 and isoform 5. 2 PublicationsAdd BLAST204

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q7Z2W4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X5YX-ray1.05A724-896[»]
4X52X-ray2.08A/B/C/D726-896[»]
ProteinModelPortaliQ7Z2W4.
SMRiQ7Z2W4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121203. 132 interactors.
DIPiDIP-37896N.
IntActiQ7Z2W4. 17 interactors.
MINTiMINT-5006396.
STRINGi9606.ENSP00000242351.

PTM databases

iPTMnetiQ7Z2W4.
PhosphoSitePlusiQ7Z2W4.
SwissPalmiQ7Z2W4.

Polymorphism and mutation databases

BioMutaiZC3HAV1.
DMDMi223634727.

Proteomic databases

EPDiQ7Z2W4.
MaxQBiQ7Z2W4.
PaxDbiQ7Z2W4.
PeptideAtlasiQ7Z2W4.
PRIDEiQ7Z2W4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242351; ENSP00000242351; ENSG00000105939. [Q7Z2W4-1]
ENST00000471652; ENSP00000419855; ENSG00000105939. [Q7Z2W4-2]
GeneIDi56829.
KEGGihsa:56829.
UCSCiuc003vun.4. human. [Q7Z2W4-1]

Organism-specific databases

CTDi56829.
DisGeNETi56829.
GeneCardsiZC3HAV1.
H-InvDBHIX0007129.
HGNCiHGNC:23721. ZC3HAV1.
HPAiHPA047818.
HPA059096.
MIMi607312. gene.
neXtProtiNX_Q7Z2W4.
OpenTargetsiENSG00000105939.
PharmGKBiPA134944289.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEI4. Eukaryota.
ENOG410ZFB8. LUCA.
GeneTreeiENSGT00760000119084.
HOVERGENiHBG050384.
InParanoidiQ7Z2W4.
KOiK15259.
PhylomeDBiQ7Z2W4.
TreeFamiTF338389.

Enzyme and pathway databases

ReactomeiR-HSA-6802952. Signaling by BRAF and RAF fusions.

Miscellaneous databases

ChiTaRSiZC3HAV1. human.
EvolutionaryTraceiQ7Z2W4.
GeneWikiiZC3HAV1.
GenomeRNAii56829.
PMAP-CutDBQ7Z2W4.
PROiQ7Z2W4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105939.
CleanExiHS_ZC3HAV1.
ExpressionAtlasiQ7Z2W4. baseline and differential.
GenevisibleiQ7Z2W4. HS.

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.
PF02825. WWE. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
PS50103. ZF_C3H1. 3 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.