O94941 · RNF37_HUMAN

  • Protein
    RING finger protein 37
  • Gene
    UBOX5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates.

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 Componentfocal adhesion
Cellular Componentnuclear body
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase binding
Molecular Functionubiquitin-ubiquitin ligase activity
Biological Processprotein polyubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RING finger protein 37
  • EC number
  • Alternative names
    • RING-type E3 ubiquitin transferase RNF37
    • U-box domain-containing protein 5
    • UbcM4-interacting protein 5
      (hUIP5
      )
    • Ubiquitin-conjugating enzyme 7-interacting protein 5

Gene names

    • Name
      UBOX5
    • Synonyms
      KIAA0860
      , RNF37
      , UBCE7IP5
      , UIP5

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O94941
  • Secondary accessions
    • Q6IAR5
    • Q86X87
    • Q9H4J2

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Note: Enriched in nuclear bodies.

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_04640296in dbSNP:rs999409
Natural variantVAR_046403479in dbSNP:rs34205880

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 570 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000560761-541RING finger protein 37
Modified residue451Asymmetric dimethylarginine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in liver, heart, brain, kidney and testis.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with UBE2L3. Interacts with VCP.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, zinc finger.

TypeIDPosition(s)Description
Domain258-338U-box
Zinc finger483-528RING-type

Domain

The U-box domain mediates interaction with E2 ubiquitin ligases and is required for the ubiquitin-protein ligase activity.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

O94941-1

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
    541
  • Mass (Da)
    58,966
  • Last updated
    1999-05-01 v1
  • Checksum
    4AF1A0C5115FAF7B
MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLPHPSLKARIDHFLLQHSIPGCHLLGRAQTALAVIPSSIVLPSQKRKIEQAEHVPDSNFGVNASCFSATSPLVLPTTSEHTAKKMKATNEPSLTHMDCSTGPLSHEQKLSQSLEIALASTLGSMPSFTARLTRGQLQHLGTRGSNTSWRPGTGSEQPGSILGPECASCKRVFSPYFKKEPVYQLPCGHLLCRPCLGEKQRSLPMTCTACQRPVASQDVLRVHF

O94941-2

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

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A2A2Q6A2A2Q6_HUMANUBOX588

Sequence caution

The sequence BAA74883.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_042899419-472in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB020667
EMBL· GenBank· DDBJ
BAA74883.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK022444
EMBL· GenBank· DDBJ
BAG51073.1
EMBL· GenBank· DDBJ
mRNA
CR457089
EMBL· GenBank· DDBJ
CAG33370.1
EMBL· GenBank· DDBJ
mRNA
AL121891
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471133
EMBL· GenBank· DDBJ
EAX10550.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471133
EMBL· GenBank· DDBJ
EAX10551.1
EMBL· GenBank· DDBJ
Genomic DNA
BC000515
EMBL· GenBank· DDBJ
AAH00515.1
EMBL· GenBank· DDBJ
mRNA
BC046122
EMBL· GenBank· DDBJ
AAH46122.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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