Q7Z2W4 (ZCCHV_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Zinc finger CCCH-type antiviral protein 1 Alternative name(s): Zinc finger CCCH domain-containing protein 2 Zinc finger antiviral protein Short name=ZAP | ||||||
| Gene names |
| ||||||
| Organism | Homo sapiens (Human) | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 902 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Induces an innate immunity to viral infections by preventing the accumulation of viral RNAs in the cytoplasm. Seems to recruit the RNA processing exosome to degrade the target RNAs. Inhibits alphavirus and filovirus replication By similarity. |
| Subunit structure | Interacts with EXOSC5 By similarity. |
| Subcellular location | Cytoplasm. Nucleus. Note: Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner By similarity. |
| Domain | The second and fourth zinc fingers are involved in binding to specific viral RNAs By similarity. |
| Sequence similarities | Contains 4 C3H1-type zinc fingers. Contains 1 PARP catalytic domain. Contains 1 WWE domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antiviral defense |
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Repeat Zinc-finger |
| Ligand | Metal-binding RNA-binding Zinc |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | response to virus Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: InterPro RNA bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DDX58 | O95786 | 3 | EBI-922540,EBI-995350 |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q7Z2W4-1) 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) 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. | ||||||
| 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 | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||||||||||
| Chain | 2 – 902 | 901 | 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 | 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 | 2 | 1 | N-acetylalanine Ref.14 | |||||||||||||||||||||||||||||||||||
| Modified residue | 257 | 1 | Phosphoserine Ref.14 Ref.15 | |||||||||||||||||||||||||||||||||||
| Modified residue | 271 | 1 | Phosphoserine Ref.7 Ref.13 | |||||||||||||||||||||||||||||||||||
| Modified residue | 273 | 1 | Phosphothreonine Ref.7 Ref.13 Ref.14 | |||||||||||||||||||||||||||||||||||
| Modified residue | 275 | 1 | Phosphoserine Ref.7 Ref.11 Ref.13 Ref.14 | |||||||||||||||||||||||||||||||||||
| Modified residue | 284 | 1 | Phosphoserine Ref.7 Ref.8 Ref.11 Ref.13 Ref.15 | |||||||||||||||||||||||||||||||||||
| Modified residue | 302 | 1 | Phosphoserine Ref.13 | |||||||||||||||||||||||||||||||||||
| Modified residue | 327 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||
| Modified residue | 335 | 1 | Phosphoserine Ref.15 | |||||||||||||||||||||||||||||||||||
| Modified residue | 378 | 1 | Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 | |||||||||||||||||||||||||||||||||||
| Modified residue | 387 | 1 | Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 | |||||||||||||||||||||||||||||||||||
| Modified residue | 390 | 1 | Phosphoserine Ref.14 | |||||||||||||||||||||||||||||||||||
| Modified residue | 393 | 1 | Phosphothreonine Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 | |||||||||||||||||||||||||||||||||||
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 | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 729 – 732 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 738 – 748 | 11 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 754 – 763 | 10 | ||||||||||||||||||||||||||||||||||||
| Helix | 765 – 778 | 14 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 784 – 790 | 7 | ||||||||||||||||||||||||||||||||||||
| Helix | 791 – 793 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 794 – 800 | 7 | ||||||||||||||||||||||||||||||||||||
| Helix | 804 – 807 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 819 – 823 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 824 – 830 | 7 | ||||||||||||||||||||||||||||||||||||
| Helix | 835 – 837 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 838 – 845 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 866 – 869 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 871 – 873 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 876 – 878 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 882 – 884 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 885 – 895 | 11 | ||||||||||||||||||||||||||||||||||||
Sequences
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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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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: 17974005] [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. Tsui L.-C.Science 300:767-772(2003) [PubMed: 12690205] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS GLU-701 AND ILE-851. Tissue: Brain and Uterus. |
| [6] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [7] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-273; SER-275 AND SER-284, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [8] | "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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-378 AND THR-393, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-387 AND THR-393, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, MASS SPECTROMETRY. Tissue: Platelet. |
| [11] | "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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-284; SER-378; SER-387 AND THR-393, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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: 18669648] [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. |
| [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-273; SER-275; SER-378; SER-387; SER-390 AND THR-393, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-284; SER-335; SER-378; SER-387 AND THR-393, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [16] | "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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | 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 |
| ||||||||||||
| ProteinModelPortal | Q7Z2W4. | ||||||||||||
| SMR | Q7Z2W4. Positions 67-111, 148-205, 726-896. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q7Z2W4. 7 interactions. | ||||||||||||
| STRING | Q7Z2W4. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q7Z2W4. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 223634727. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q7Z2W4. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000242351; ENSP00000242351; ENSG00000105939. | ||||||||||||
| GeneID | 56829. | ||||||||||||
| KEGG | hsa:56829. | ||||||||||||
| UCSC | uc003vuo.1. human. uc003vup.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 56829. | ||||||||||||
| GeneCards | GC07M138728. | ||||||||||||
| HGNC | HGNC:23721. ZC3HAV1. | ||||||||||||
| HPA | HPA047818. | ||||||||||||
| MIM | 607312. gene. | ||||||||||||
| neXtProt | NX_Q7Z2W4. | ||||||||||||
| PharmGKB | PA134944289. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG11312. | ||||||||||||
| GeneTree | ENSGT00600000084343. | ||||||||||||
| HOVERGEN | HBG050384. | ||||||||||||
| InParanoid | Q7Z2W4. | ||||||||||||
| OMA | GMIQTNI. | ||||||||||||
| 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] | ||||||||||||
| KO | K15259. | ||||||||||||
| 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 | |||||||||||||
| NextBio | 62226. | ||||||||||||
| PMAP-CutDB | Q7Z2W4. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | ZCCHV_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q7Z2W4 Secondary accession number(s): A4D1R2 Q9P0Y7 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with