Q9Z131 · 3BP5_MOUSE

  • Protein
    SH3 domain-binding protein 5
  • Gene
    Sh3bp5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Functions as a guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25 (By similarity).
Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death

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
Cellular Componentcytoplasmic vesicle membrane
Cellular Componentmitochondrion
Cellular Componentnuclear body
Molecular Functionguanyl-nucleotide exchange factor activity
Molecular Functionprotein kinase inhibitor activity
Molecular FunctionSH3 domain binding
Biological Processintracellular signal transduction
Biological Processnegative regulation of protein kinase activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    SH3 domain-binding protein 5
  • Short names
    SH3BP-5
  • Alternative names
    • SH3 domain-binding protein that preferentially associates with BTK

Gene names

    • Name
      Sh3bp5
    • Synonyms
      Sab

Organism names

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

Accessions

  • Primary accession
    Q9Z131
  • Secondary accessions
    • Q3TTD6
    • Q8C903
    • Q8VCZ0

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasmic vesicle membrane
; Peripheral membrane protein
Mitochondrion
Note: Colocalizes with RAB11A on cytoplasmic vesicle membranes.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000643691-463SH3 domain-binding protein 5
Modified residue354Phosphoserine; by MAPK12 and MAPK9
Modified residue378Phosphoserine
Modified residue379Phosphoserine
Modified residue421Phosphoserine
Modified residue424Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with BTK (By similarity).
Interacts with all isoforms of MAPK8, MAPK9, MAPK10 and MAPK12 (By similarity).
Interacts with GDP-bound and nucleotide-free forms of RAB11A (PubMed:26506309).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, coiled coil.

TypeIDPosition(s)Description
Compositional bias1-26Basic and acidic residues
Region1-69Disordered
Compositional bias27-46Acidic residues
Region33-268Sufficient for interaction with RAB11A and for guanine nucleotide exchange activity
Coiled coil47-93
Coiled coil100-148
Coiled coil157-203
Coiled coil214-258
Compositional bias309-336Polar residues
Region309-348Disordered
Region372-429Disordered
Compositional bias382-398Basic and acidic residues
Compositional bias399-429Polar residues

Domain

The N-terminal half of the protein mediates interaction with RAB11A and functions as a guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemble into coiled coils, giving rise to a 'V' shape.

Sequence similarities

Belongs to the SH3BP5 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.

Q9Z131-1

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
    463
  • Mass (Da)
    51,807
  • Last updated
    2007-01-23 v3
  • Checksum
    A4274A91DDD91670
MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPRGCGVGAEGSIASVENLPVSKPEPDAISVASEAFEDDNCSNLVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVARPGSLDLPSPVSLSEFGMMFPILGPRSECSGASSPECEVERGDRAEGAENKMSDKANNNRVLGSTNGGSGRSRSQSSTSLESQALETRMKQLSLQCSKGRDGIIADIKMIFIFYTFLQ

Q9Z131-2

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

Q9Z131-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-70: MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEEEEVDPRIQGELEKLNQSTDDINRRETELE → MDWARTVMASTGLAPASAAPHTGSRAQPCLFLAPVPPHFAWFIFLDPALPCSTLAQSVSFKPCCGVVK
    • 455-463: IFIFYTFLQ → VQIG

Sequence caution

The sequence BAC31530.1 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Compositional bias1-26Basic and acidic residues
Alternative sequenceVSP_0225721-70in isoform 3
Compositional bias27-46Acidic residues
Sequence conflict299in Ref. 1; BAC31530
Compositional bias309-336Polar residues
Compositional bias382-398Basic and acidic residues
Compositional bias399-429Polar residues
Alternative sequenceVSP_010882455-463in isoform 2 and isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK043375
EMBL· GenBank· DDBJ
BAC31530.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK161427
EMBL· GenBank· DDBJ
BAE36389.1
EMBL· GenBank· DDBJ
mRNA
BC018237
EMBL· GenBank· DDBJ
AAH18237.2
EMBL· GenBank· DDBJ
mRNA
BC053741
EMBL· GenBank· DDBJ
AAH53741.2
EMBL· GenBank· DDBJ
mRNA
AB016835
EMBL· GenBank· DDBJ
BAA75641.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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