Q8BFU3 · RN214_MOUSE

  • Protein
    RING finger protein 214
  • Gene
    Rnf214
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionmetal ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    RING finger protein 214

Gene names

    • Name
      Rnf214

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
    • FVB/N-3
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8BFU3
  • Secondary accessions
    • Q3UWM9
    • Q6P3A7
    • Q80VI8
    • Q8BNZ6
    • Q8CC56

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00002805472-668RING finger protein 214
Modified residue15Phosphoserine
Modified residue40Phosphoserine
Modified residue48Phosphoserine
Modified residue54Phosphoserine
Modified residue196Phosphoserine
Modified residue497Phosphoserine
Modified residue511Phosphoserine
Modified residue516Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, coiled coil, zinc finger.

Type
IDPosition(s)Description
Region1-87Disordered
Compositional bias37-61Polar residues
Region103-125Disordered
Coiled coil220-379
Region486-552Disordered
Compositional bias488-504Polar residues
Zinc finger623-665RING-type; atypical

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

This entry describes 5 isoforms produced by Alternative splicing.

Q8BFU3-1

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.

  • Length
    668
  • Mass (Da)
    73,625
  • Last updated
    2003-03-01 v1
  • Checksum
    ECF534164BCCDE7E
MAASEVAGLGAGTPSPSESSALCASKSDESLPDGLSPKDSAQKQKNLSPPSVSSQMITKESNRNAHLEHPEQNPGSSVGDTSAAHEEVVGENLVATALCLSGNGSQSDLKDLTNPAGEEGDTSLRESLHPVTRSLKAGCHSKQLASGNCSEEKCPAASVLKEGSRDAGLDLLPVVPPANGVEGVRVDQDDDQDSSSLKLSQNIAVQTDFKTADSEVNTDQDIEKNLDKMMTERTLLKERYQEVLDKQRQVESQLQVQLKQLQQRREEEMKNHQEILKAIQDVTIKREETKKKIEKEKKEFLQKEQDLKAEIEKLCEKGRREVWEMELDRLKNQDGEINRNIMEETERAWKAEILSLESRKELLVLKLEEAEKEAELHLTYLKSTPPTLETVRSKQEWETRLNGVRIMKKNVRDQFNSHIQLVRNGAKLSSLPQIPTPTLPPPPSEADFMLQVFQPSPSLTPRMPFSIGQVTMPMVMPSADPRSLSFPILNPALSQSSQPSPPLPGSHGRNSPGLGSLVSPHGPHMPPAASIPPPPGLGGIKASSETPRPQPVDKLEKILEKLLTRFPQCNKAQMTNILQQIKTARTTMAGLTMEELIQLVAARLAEHERVASSTQAPPTCKLCLMCQKLVQPSELHPMACTHALHKECIKFWAQTNTNDTCPFCPTLK

Q8BFU3-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 52-206: Missing
    • 615-615: Q → QPLGRIRALHPAPLAQISPPMFLPSAQVSYPGRSSH

Q8BFU3-3

  • Name
    3
  • Note
    May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8BFU3-4

  • Name
    4
  • Note
    May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 616-668: APPTCKLCLMCQKLVQPSELHPMACTHALHKECIKFWAQTNTNDTCPFCPTLK → VRGASGRELRPAERLRKKPTRRSGHEEIRARNICSAFLIIRSEFLLPSFLPSFLPSFLPSFLPFFLSFLLVKFICVYVCVCVLCGSRKTTCGSPFSSTM

Q8BFU3-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1L1SQE1A0A1L1SQE1_MOUSERnf21445
E0CZF4E0CZF4_MOUSERnf21436

Sequence caution

The sequence AAH49909.1 differs from that shown. Reason: Erroneous initiation
The sequence BAC28499.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.
The sequence BAC37365.1 differs from that shown. Reason: Erroneous initiation
The sequence BAE22885.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0237731-55in isoform 3
Compositional bias37-61Polar residues
Alternative sequenceVSP_02377452-206in isoform 2 and isoform 5
Sequence conflict361in Ref. 1; BAE22885
Compositional bias488-504Polar residues
Sequence conflict512in Ref. 1; BAC37365
Sequence conflict579in Ref. 1; BAC37365
Alternative sequenceVSP_023775615in isoform 2
Alternative sequenceVSP_023776616-668in isoform 4

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK028768
EMBL· GenBank· DDBJ
BAC26109.1
EMBL· GenBank· DDBJ
mRNA
AK030208
EMBL· GenBank· DDBJ
BAC26843.1
EMBL· GenBank· DDBJ
mRNA
AK032376
EMBL· GenBank· DDBJ
BAC27844.1
EMBL· GenBank· DDBJ
mRNA
AK033867
EMBL· GenBank· DDBJ
BAC28499.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AK051527
EMBL· GenBank· DDBJ
BAC34663.1
EMBL· GenBank· DDBJ
mRNA
AK078706
EMBL· GenBank· DDBJ
BAC37365.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK136229
EMBL· GenBank· DDBJ
BAE22885.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC023073
EMBL· GenBank· DDBJ
AAH23073.1
EMBL· GenBank· DDBJ
mRNA
BC049909
EMBL· GenBank· DDBJ
AAH49909.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC064100
EMBL· GenBank· DDBJ
AAH64100.1
EMBL· GenBank· DDBJ
mRNA
BC094247
EMBL· GenBank· DDBJ
AAH94247.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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