Q8TEC5 · SH3R2_HUMAN

  • Protein
    E3 ubiquitin-protein ligase SH3RF2
  • Gene
    SH3RF2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Has E3 ubiquitin-protein ligase activity (PubMed:24130170).
Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation (PubMed:22128169).
Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein stability via inhibition of its ubiquitin-mediated proteasomal degradation (PubMed:24130170).
Inhibits PPP1CA phosphatase activity (PubMed:19389623, PubMed:19945436).

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 Componentnucleoplasm
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionphosphatase binding
Molecular Functionprotein phosphatase 1 binding
Molecular Functionprotein phosphatase inhibitor activity
Molecular Functionubiquitin protein ligase activity
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of JNK cascade
Biological Processnegative regulation of protein ubiquitination
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of JNK cascade
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processprotein autoubiquitination
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase SH3RF2
  • EC number
  • Alternative names
    • Heart protein phosphatase 1-binding protein (HEPP1)
    • POSH-eliminating RING protein
    • Protein phosphatase 1 regulatory subunit 39
    • RING finger protein 158
    • RING-type E3 ubiquitin transferase SH3RF2
    • SH3 domain-containing RING finger protein 2

Gene names

    • Name
      SH3RF2
    • Synonyms
      POSH3
      , POSHER
      , PPP1R39, RNF158

Organism names

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

Accessions

  • Primary accession
    Q8TEC5
  • Secondary accessions
    • A8K961
    • Q08AM9
    • Q6GMR9
    • Q8N5S8
    • Q96LP8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_05211816in dbSNP:rs34739859
Natural variantVAR_052119174in dbSNP:rs34942619
Natural variantVAR_029788267in dbSNP:rs758037
Natural variantVAR_052120477in dbSNP:rs35165046
Natural variantVAR_029789592in dbSNP:rs2962525
Mutagenesis643Significant loss of interaction with PPP1CA. Significant loss of interaction with PPP1CA; when associated with G-645.
Mutagenesis645Significant loss of interaction with PPP1CA. Significant loss of interaction with PPP1CA; when associated with G-643.
Natural variantVAR_029790687in dbSNP:rs11435
Natural variantVAR_029791710in dbSNP:rs1056149

Variants

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

The viewer provides 969 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 (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002695121-729UniProtE3 ubiquitin-protein ligase SH3RF2
Modified residue (large scale data)112PRIDEPhosphoserine
Modified residue (large scale data)508PRIDEPhosphoserine
Modified residue649UniProtPhosphoserine
Modified residue (large scale data)649PRIDEPhosphoserine

Post-translational modification

Autoubiquitinated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Heart (at protein level). Up-regulated in colon cancer tissues as compared to normal colon tissues (at protein level). Testis. In the heart, present in the apex, left atrium, right atrium, left ventricle and right ventricle, but not in the aorta.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with FASLG and PPP1CA (PubMed:19389623, PubMed:19807924, PubMed:19945436).
Interacts with PAK4 and TNFRSF1A (PubMed:24130170).
Interacts with DLK1, MAP3K10/MLK2, MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3. Interacts with RAC1 (both active GTP- or inactive GDP-bound forms) (By similarity).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, region, domain, compositional bias.

TypeIDPosition(s)Description
Zinc finger12-53RING-type
Region78-105Disordered
Domain125-184SH3 1
Domain187-252SH3 2
Region258-297Disordered
Compositional bias266-288Polar residues
Region370-459Interaction with PAK4
Domain380-441SH3 3
Region497-526Disordered
Compositional bias499-526Polar residues
Region610-677Disordered
Compositional bias636-669Polar residues
Region641-646Interaction with PPP1CA

Domain

The RING finger domain is required for ubiquitin ligase activity and autoubiquitination.

Sequence similarities

Belongs to the SH3RF family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q8TEC5-1

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
    729
  • Mass (Da)
    79,320
  • Last updated
    2010-05-18 v3
  • Checksum
    F85CCC0188DA8477
MDDLTLLDLLECPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECRTPVFSNIEALPANLLLVRLLDGVRSGQSSGRGGSFRRPGTMTLQDGRKSRTNPRRLQASPFRLVPNVRIHMDGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQLPQPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLTARHLLEKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPGQFSITTALNTLNRMVHSPSGRHMVEISTPVLISSSNPSVITQPMEKADVPSSCVGQVSTYHPAPVSPGHSTAVVSLPGSQQHLSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFRKTSSFPDSRSPGLYTTWTLSTSSVSSQGSISEGDPRQSRPFKSVFVPTAIVNPVRSTAGPGTLGQGSLRKGRSSMRKNGSLQRPLQSGIPTLVVGSLRRSPTMVLRPQQFQFYQPQGIPSSPSAVVVEMGSKPALTGEPALTCISRGSEAWIHSAASSLIMEDKEIPIKSEPLPKPPASAPPSILVKPENSRNGIEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPATLKASQPEAASLGPEMTVLFAHRSGCHSGQQTDLRRKSALGKATTLVSTASGTQTVFPSK

Q8TEC5-2

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

Q8TEC5-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAH31650.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAB85025.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0220581-508in isoform 2
Alternative sequenceVSP_0406621-543in isoform 3
Sequence conflict148in Ref. 2; BAB85025
Sequence conflict168in Ref. 2; BAB85025
Compositional bias266-288Polar residues
Compositional bias499-526Polar residues
Alternative sequenceVSP_022059509-519in isoform 2
Compositional bias636-669Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK058046
EMBL· GenBank· DDBJ
BAB71639.1
EMBL· GenBank· DDBJ
mRNA
AK074234
EMBL· GenBank· DDBJ
BAB85025.1
EMBL· GenBank· DDBJ
mRNA Different termination.
AK292576
EMBL· GenBank· DDBJ
BAF85265.1
EMBL· GenBank· DDBJ
mRNA
AC005216
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC005351
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC011359
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC091887
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC031650
EMBL· GenBank· DDBJ
AAH31650.2
EMBL· GenBank· DDBJ
mRNA Different initiation
BC073914
EMBL· GenBank· DDBJ
AAH73914.1
EMBL· GenBank· DDBJ
mRNA
BC125106
EMBL· GenBank· DDBJ
AAI25107.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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