Q7TPV2 · DZIP3_MOUSE

  • Protein
    E3 ubiquitin-protein ligase DZIP3
  • Gene
    Dzip3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

E3 Ubiquitin ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Able to specifically bind RNA.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

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
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Molecular Functionphosphatase binding
Molecular Functionpolyubiquitin modification-dependent protein binding
Molecular FunctionRNA binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Biological Processprotein polyubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase DZIP3
  • EC number
  • Alternative names
    • DAZ-interacting protein 3 homolog
    • RING-type E3 ubiquitin transferase DZIP3

Gene names

    • Name
      Dzip3
    • Synonyms
      Kiaa0675

Organism names

  • Taxonomic identifier
  • Strains
    • C3H/He
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q7TPV2
  • Secondary accessions
    • Q148V3
    • Q80TU4
    • Q8BYK7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000558991-1204E3 ubiquitin-protein ligase DZIP3

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Probably interacts with DAZL.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-22Disordered
Region640-681Disordered
Coiled coil746-861
Coiled coil906-941
Region1088-1141Disordered
Compositional bias1098-1124Polar residues
Zinc finger1144-1184RING-type; atypical

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q7TPV2-1

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
    1,204
  • Mass (Da)
    138,021
  • Last updated
    2004-07-19 v2
  • Checksum
    9522730708DB570C
MDSLAEEFFVSGNPDVEEQTKEETEIIAEKPVTQLDKQKMDISADPEPVNALLEIKKVLNPISALPKGVFPNIEKFIQEDFSFQTMQREVTTHSQTGEEIVPALTLHFLITQLEMALRNIQASNYTAQQINVGYYLTLLFLYGVALTERAKKEDCIEAENKFLVMKMVIQESEICENFMCLVYFGRGLLRCAQKRYNGALLEFYKSLQEIGDTDDNWFEVDPTDDEDLPTTFKDSLNNFIKTTESNIMKETICSYLDCERSCEADILKNTNYKGFFQLMCSKSCCIYFHKICWKKFKNLKYPGESDQSFSGQKCLKEGCPGDMVRMLQCDVPGIVKILFEVVRKDEYITIENLGASYKNLMSLELTDTDIRPKFNLKPNTKDEVPIFKLDYNYFYHLLHIIIISGTDMVRQIFDEAMPPTLLKKELLIHKNVLEPYYNHLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPRKGWDMEPPSSDLSKSADILRLCKYRDILLSEILMNGLTELQFNSIWKKVSDILLRLGMKQDDLDKVKENPIENISLDYHQLSIYLGIPVPEIIQRMLSCYQQGITLQSITGSQRLDVEEFQNDEEDLSPPVMEYNIDVKSNTEIQLAEINKDVASIPSESSTESVKDLQEVKSKTKKKKRTKSNKKDKDSEDEQVSYMVEKDDQLETEQVDVNTLSTYMKTDTSDAQEDSAAEDKFCSLDELHILDMVEQGSSGKESTDFKETEKERLAHQHQLYKLQYECEDYKRQLKTVTFRWQENQMLIKKKEKIIVSLNQQVAFGINKMSKLQRQIHAKDDEIKNLKDQLSLKRSQWEMEKHNLESTVKTYLNKLNAETSRALTAEVYFLQCRRDFGLLHLEQTEKECLNQLARVTHMAASNLESLQLKAAVDSWNAIVADVRNKIAFLRTQYNEQINKVKQGFALSTLPPVQLPPPPPSPEILIQQFLGRPLVKESFFRPILTVPQMPAVCPGVISAAVQPRPPLMPGITWAMPTPIGDTVSPSASLCSEPLMINWERITDRLKTAFPQQTRKELTDFLQQLKDSHGKSVSRLTFDEIVYKISQMIEPKKSESEEKSAQDGNNASPSHTASQPNAPQDPKSAQGSATWEGDKDMDNEEEEEEPCVICHENLSPENLSVLPCAHKFHSQCIRPWLMQQGTCPTCRLHVLQPEEFPGHPNGQLPKI

Q7TPV2-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q7TPV2-3

  • Name
    3
  • 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
F6Z1P8F6Z1P8_MOUSEDzip3167
E9QNZ2E9QNZ2_MOUSEDzip31204

Sequence caution

The sequence BAC65626.1 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0109731-889in isoform 3
Sequence conflict306in Ref. 2; AAH52893
Alternative sequenceVSP_010977382-587in isoform 2
Sequence conflict650in Ref. 2; AAH52893
Alternative sequenceVSP_010974890-899in isoform 3
Compositional bias1098-1124Polar residues
Alternative sequenceVSP_0109751135-1153in isoform 3
Alternative sequenceVSP_0109761154-1204in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK122344
EMBL· GenBank· DDBJ
BAC65626.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC052893
EMBL· GenBank· DDBJ
AAH52893.1
EMBL· GenBank· DDBJ
mRNA
BC117953
EMBL· GenBank· DDBJ
AAI17954.1
EMBL· GenBank· DDBJ
mRNA
BC117954
EMBL· GenBank· DDBJ
AAI17955.1
EMBL· GenBank· DDBJ
mRNA
AK039172
EMBL· GenBank· DDBJ
BAC30265.1
EMBL· GenBank· DDBJ
mRNA
BI736207
EMBL· GenBank· DDBJ
-mRNA No translation available.
CN535823
EMBL· GenBank· DDBJ
-mRNA No translation available.
BG070132
EMBL· GenBank· DDBJ
-mRNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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