Q8WTR7 · ZN473_HUMAN
- ProteinZinc finger protein 473
- GeneZNF473
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids871 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | Cajal body | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA-binding transcription activator activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | mRNA 3'-end processing by stem-loop binding and cleavage | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
The subsequence AEEFVTLKDVGMDFTLGDWEQLGLEQGDTFWDTALDNCQDLFLLDPPRPNLTSHPDGSEDLEPLAGGSPEATSPDVTETK, which contains the KRAB domain, shows transcriptional activator activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameZinc finger protein 473
- Alternative names
Gene names
- Community suggested namesZNF473
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WTR7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Stable component of Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052839 | 59 | in dbSNP:rs10419876 | |||
Sequence: S → G | ||||||
Natural variant | VAR_052840 | 74 | in dbSNP:rs10419911 | |||
Sequence: S → G | ||||||
Natural variant | VAR_052841 | 164 | in dbSNP:rs16981705 | |||
Sequence: T → M | ||||||
Natural variant | VAR_052842 | 309 | in dbSNP:rs16981706 | |||
Sequence: E → G | ||||||
Natural variant | VAR_052843 | 654 | in dbSNP:rs10424809 | |||
Sequence: T → I | ||||||
Natural variant | VAR_052844 | 662 | in dbSNP:rs10426374 | |||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 978 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000047604 | 1-871 | UniProt | Zinc finger protein 473 | |||
Sequence: MAEEFVTLKDVGMDFTLGDWEQLGLEQGDTFWDTALDNCQDLFLLDPPRPNLTSHPDGSEDLEPLAGGSPEATSPDVTETKNSPLMEDFFEEGFSQEIIEMLSKDGFWNSNFGEACIEDTWLDSLLGDPESLLRSDIATNGESPTECKSHELKRGLSPVSTVSTGEDSMVHNVSEKTLTPAKSKEYRGEFFSYSDHSQQDSVQEGEKPYQCSECGKSFSGSYRLTQHWITHTREKPTVHQECEQGFDRNASLSVYPKTHTGYKFYVCNEYGTTFSQSTYLWHQKTHTGEKPCKSQDSDHPPSHDTQPGEHQKTHTDSKSYNCNECGKAFTRIFHLTRHQKIHTRKRYECSKCQATFNLRKHLIQHQKTHAAKTTSECQECGKIFRHSSLLIEHQALHAGEEPYKCNERGKSFRHNSTLKIHQRVHSGEKPYKCSECGKAFHRHTHLNEHRRIHTGYRPHKCQECVRSFSRPSHLMRHQAIHTAEKPYSCAECKETFSDNNRLVQHQKMHTVKTPYECQECGERFICGSTLKCHESVHAREKQGFFVSGKILDQNPEQKEKCFKCNKCEKTFSCSKYLTQHERIHTRGVKPFECDQCGKAFGQSTRLIHHQRIHSRVRLYKWGEQGKAISSASLIKLQSFHTKEHPFKCNECGKTFSHSAHLSKHQLIHAGENPFKCSKCDRVFTQRNYLVQHERTHARKKPLVCNECGKTFRQSSCLSKHQRIHSGEKPYVCDYCGKAFGLSAELVRHQRIHTGEKPYVCQECGKAFTQSSCLSIHRRVHTGEKPYRCGECGKAFAQKANLTQHQRIHTGEKPYSCNVCGKAFVLSAHLNQHLRVHTQETLYQCQRCQKAFRCHSSLSRHQRVHNKQQYCL | |||||||
Cross-link | 148 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 157 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 419 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 549 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 558 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 635 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with the SLBP/pre-mRNA complex but not with SLBP alone. Interacts with LSM11 in a U7 snRNP-dependent manner.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-75 | KRAB | ||||
Sequence: VTLKDVGMDFTLGDWEQLGLEQGDTFWDTALDNCQDLFLLDPPRPNLTSHPDGSEDLEPLAGGSPEATSP | ||||||
Region | 47-81 | Disordered | ||||
Sequence: PPRPNLTSHPDGSEDLEPLAGGSPEATSPDVTETK | ||||||
Region | 140-164 | Disordered | ||||
Sequence: NGESPTECKSHELKRGLSPVSTVST | ||||||
Zinc finger | 209-231 | C2H2-type 1 | ||||
Sequence: YQCSECGKSFSGSYRLTQHWITH | ||||||
Zinc finger | 265-286 | C2H2-type 2; degenerate | ||||
Sequence: YVCNEYGTTFSQSTYLWHQKTH | ||||||
Compositional bias | 290-317 | Basic and acidic residues | ||||
Sequence: KPCKSQDSDHPPSHDTQPGEHQKTHTDS | ||||||
Region | 290-318 | Disordered | ||||
Sequence: KPCKSQDSDHPPSHDTQPGEHQKTHTDSK | ||||||
Region | 312-552 | Interaction with SLBP/pre-mRNA complex | ||||
Sequence: KTHTDSKSYNCNECGKAFTRIFHLTRHQKIHTRKRYECSKCQATFNLRKHLIQHQKTHAAKTTSECQECGKIFRHSSLLIEHQALHAGEEPYKCNERGKSFRHNSTLKIHQRVHSGEKPYKCSECGKAFHRHTHLNEHRRIHTGYRPHKCQECVRSFSRPSHLMRHQAIHTAEKPYSCAECKETFSDNNRLVQHQKMHTVKTPYECQECGERFICGSTLKCHESVHAREKQGFFVSGKILD | ||||||
Zinc finger | 320-342 | C2H2-type 3 | ||||
Sequence: YNCNECGKAFTRIFHLTRHQKIH | ||||||
Zinc finger | 347-369 | C2H2-type 4 | ||||
Sequence: YECSKCQATFNLRKHLIQHQKTH | ||||||
Zinc finger | 375-397 | C2H2-type 5 | ||||
Sequence: SECQECGKIFRHSSLLIEHQALH | ||||||
Zinc finger | 403-425 | C2H2-type 6; degenerate | ||||
Sequence: YKCNERGKSFRHNSTLKIHQRVH | ||||||
Zinc finger | 431-453 | C2H2-type 7 | ||||
Sequence: YKCSECGKAFHRHTHLNEHRRIH | ||||||
Zinc finger | 459-481 | C2H2-type 8 | ||||
Sequence: HKCQECVRSFSRPSHLMRHQAIH | ||||||
Zinc finger | 487-509 | C2H2-type 9 | ||||
Sequence: YSCAECKETFSDNNRLVQHQKMH | ||||||
Zinc finger | 515-537 | C2H2-type 10 | ||||
Sequence: YECQECGERFICGSTLKCHESVH | ||||||
Zinc finger | 562-584 | C2H2-type 11 | ||||
Sequence: FKCNKCEKTFSCSKYLTQHERIH | ||||||
Zinc finger | 591-613 | C2H2-type 12 | ||||
Sequence: FECDQCGKAFGQSTRLIHHQRIH | ||||||
Zinc finger | 646-668 | C2H2-type 13 | ||||
Sequence: FKCNECGKTFSHSAHLSKHQLIH | ||||||
Zinc finger | 674-696 | C2H2-type 14 | ||||
Sequence: FKCSKCDRVFTQRNYLVQHERTH | ||||||
Zinc finger | 702-724 | C2H2-type 15 | ||||
Sequence: LVCNECGKTFRQSSCLSKHQRIH | ||||||
Zinc finger | 730-752 | C2H2-type 16 | ||||
Sequence: YVCDYCGKAFGLSAELVRHQRIH | ||||||
Zinc finger | 758-780 | C2H2-type 17 | ||||
Sequence: YVCQECGKAFTQSSCLSIHRRVH | ||||||
Zinc finger | 786-808 | C2H2-type 18 | ||||
Sequence: YRCGECGKAFAQKANLTQHQRIH | ||||||
Zinc finger | 814-836 | C2H2-type 19 | ||||
Sequence: YSCNVCGKAFVLSAHLNQHLRVH | ||||||
Zinc finger | 842-864 | C2H2-type 20 | ||||
Sequence: YQCQRCQKAFRCHSSLSRHQRVH |
Domain
The C2H2-type zinc finger 2 to 6 are necessary and sufficient for discrete Cajal bodies localization. The C2H2-type zinc finger 5 to 10 are necessary and sufficient for interaction with LSM11. The C2H2-type zinc finger 2 to 8 are necessary for interaction with the SLBP/RNA complex in the histone pre-mRNAs. The C2H2-type zinc finger 2 to 10 confer activity in histone pre-mRNA processing.
Sequence similarities
Belongs to the krueppel C2H2-type zinc-finger protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length871
- Mass (Da)100,182
- Last updated2002-03-01 v1
- Checksum959AFB7C3C2D5456
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 290-317 | Basic and acidic residues | ||||
Sequence: KPCKSQDSDHPPSHDTQPGEHQKTHTDS | ||||||
Sequence conflict | 486 | in Ref. 6 | ||||
Sequence: P → A | ||||||
Sequence conflict | 588 | in Ref. 2; BAA86455 | ||||
Sequence: V → M |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF454744 EMBL· GenBank· DDBJ | AAL51029.1 EMBL· GenBank· DDBJ | mRNA | ||
AB032967 EMBL· GenBank· DDBJ | BAA86455.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292452 EMBL· GenBank· DDBJ | BAF85141.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471177 EMBL· GenBank· DDBJ | EAW52593.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC018612 EMBL· GenBank· DDBJ | AAH18612.1 EMBL· GenBank· DDBJ | mRNA | ||
AL080143 EMBL· GenBank· DDBJ | CAB45736.1 EMBL· GenBank· DDBJ | mRNA |