Q62417 · SRBS1_MOUSE

  • Protein
    Sorbin and SH3 domain-containing protein 1
  • Gene
    Sorbs1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions.

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 Componentadherens junction
Cellular Componentcell-substrate junction
Cellular Componentcytoplasm
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentflotillin complex
Cellular Componentfocal adhesion
Cellular Componentmembrane
Cellular Componentmembrane raft
Cellular Componentnuclear matrix
Cellular Componentnucleus
Cellular Componentstress fiber
Cellular Componentsynapse
Molecular Functioninsulin receptor binding
Molecular Functionprotein kinase binding
Molecular Functionsignaling receptor complex adaptor activity
Molecular Functionubiquitin protein ligase binding
Biological Processacetylcholine receptor signaling pathway
Biological Processcell-substrate adhesion
Biological Processcellular response to insulin stimulus
Biological Processfocal adhesion assembly
Biological Processinsulin receptor signaling pathway
Biological Processpositive regulation of glucose import
Biological Processpositive regulation of glycogen biosynthetic process
Biological Processpositive regulation of insulin receptor signaling pathway
Biological Processpositive regulation of lipid biosynthetic process
Biological Processpositive regulation of protein localization to plasma membrane
Biological Processregulation of skeletal muscle acetylcholine-gated channel clustering
Biological Processstress fiber assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sorbin and SH3 domain-containing protein 1
  • Alternative names
    • Ponsin
    • SH3 domain protein 5
    • SH3P12
    • c-Cbl-associated protein (CAP)

Gene names

    • Name
      Sorbs1
    • Synonyms
      Kiaa1296
      , Sh3d5

Organism names

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

Accessions

  • Primary accession
    Q62417
  • Secondary accessions
    • Q80TF8
    • Q8BZI3
    • Q8K3Y2
    • Q921F8
    • Q9Z0Z8
    • Q9Z0Z9

Proteomes

Organism-specific databases

Subcellular Location

Note: Colocalized with PXN at focal adhesions during myogenic differentiation (By similarity).
Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions. Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000721861-1290Sorbin and SH3 domain-containing protein 1
Modified residue51Phosphothreonine
Modified residue55Phosphoserine
Modified residue58Phosphoserine
Modified residue62Phosphoserine
Modified residue164In isoform Q62417-2; Phosphoserine
Modified residue164In isoform Q62417-5; Phosphoserine
Modified residue175In isoform Q62417-6; Phosphoserine
Modified residue179Phosphothreonine
Modified residue185Phosphoserine
Modified residue194In isoform Q62417-4; Phosphoserine
Modified residue204Phosphoserine
Modified residue209Phosphoserine
Modified residue254Phosphoserine
Modified residue261Phosphoserine
Modified residue270Phosphoserine
Modified residue288In isoform Q62417-7; Phosphoserine
Modified residue325Phosphotyrosine; by ABL1
Modified residue345Phosphoserine
Modified residue346In isoform Q62417-2; Phosphoserine
Modified residue346In isoform Q62417-5; Phosphoserine
Modified residue357In isoform Q62417-6; Phosphoserine
Modified residue376Phosphoserine
Modified residue376In isoform Q62417-4; Phosphoserine
Modified residue407Phosphoserine
Modified residue421Phosphotyrosine; by ABL1
Modified residue432Phosphoserine
Modified residue470In isoform Q62417-7; Phosphoserine
Modified residue475Phosphothreonine
Modified residue969Phosphoserine
Modified residue1189Phosphothreonine
Modified residue1193Phosphotyrosine
Modified residue1198Phosphotyrosine
Modified residue1201Phosphoserine
Modified residue1209Phosphoserine
Modified residue1238Phosphotyrosine; by ABL1

Post-translational modification

O-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all tissues tested: heart, brain, spleen, lung, liver, muscle, kidney and testis. Expressed in 3T3-L1 adipocytes but not in 3T3-L1 fibroblasts.

Interaction

Subunit

Interacts (via SH3 domain 2) with PXN (By similarity).
Interacts with the long isoform of AFDN and with VCL. AFDN and VCL bind to SORBS1 in a competitive manner and do not form a ternary complex. Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3 domain. Interaction with ABL1 occurs only after insulin stimulation while this has no effect on the interaction with INPPL1. Interacts with the insulin receptor but dissociates from it following insulin stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin. Interacts (via third SH3 domain) with the Ten-1 ICD form of TENM1; the interaction induces the translocation of SORBS1 to the nucleus. Interacts with INSM1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q62417-2PXN P490238EBI-7072893, EBI-702209
XENO Q62417-2VCL P182063EBI-7072893, EBI-716775

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-211Disordered
Compositional bias38-64Polar residues
Compositional bias65-81Basic and acidic residues
Compositional bias82-96Polar residues
Compositional bias111-157Polar residues
Compositional bias188-203Basic and acidic residues
Domain202-247SoHo
Compositional bias238-254Basic and acidic residues
Region238-271Disordered
Region286-313Disordered
Region389-416Disordered
Compositional bias392-416Polar residues
Region463-482Disordered
Compositional bias465-482Polar residues
Region588-607Disordered
Compositional bias591-606Polar residues
Compositional bias697-726Polar residues
Region697-739Disordered
Region783-803Disordered
Region822-841Disordered
Compositional bias823-841Basic and acidic residues
Region862-972Disordered
Compositional bias898-916Polar residues
Compositional bias948-962Polar residues
Domain1049-1108SH3 1
Domain1123-1184SH3 2
Region1198-1227Disordered
Domain1229-1290SH3 3

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (7)
  • Sequence status
    Complete

This entry describes 7 isoforms produced by Alternative splicing.

Q62417-1

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
    1,290
  • Mass (Da)
    143,070
  • Last updated
    2004-08-16 v2
  • Checksum
    07C9A74BD794E390
MSSECDVGSSKAVVNGLASGNHGPDKDMDPTKICTGKGTVTLRASSSYRGTPSSSPVSPQESPKHESKSGLEPEDPSADEWKLSSSADTNGNAQPSPLAAKGYRSVHPSLSADKPQGSPLLNEVSSSHIETDSQDFPPTSRPSSAYPSTTIVNPTIVLLQHNRDPASERRAGEQDPVPTPAELTSPGRASERRAKDASRRVVRSAQDLSDVSTDEVGIPLRNTERSKDWYKTMFKQIHKLNRDDDSDVHSPRYSFSDDTKSPLSVPRSKSEMNYIEGEKVVKRSATLPLPARSSSLKSSPERNDWEPLDKKVDTRKYRAEPKSIYEYQPGKSSVLTNEKMSRDISPEEIDLKNEPWYKFFSELEFGRPTNLEKDLSFCQAELEADLEKVETVNKSPSANSPQSSAVSPTPDITSEPPGYIYSSNFHAVKRESDGTPGGLASLENERQIYKSVLEGGDIPLQGLSGLKRPSSSASTKVDRKGGNAHMISSSSVHSRTFHTSNALGPGCKHKKPLSAAKACISEILPSKFKPRLSAPSALLQEQKSVLLPSEKAQSCENLCVSLNDSKRGLPLRVGGSIENLLMRSRRDYDSKSSSTMSLQEYGTSSRRPCPLSRKAGLHFSMFYRDMHQINRAGLSLGSISSSSVRDLASHFERSSLTLARGELGASQEGSEHIPKHTVSSRITAFEQLIQRSRSMPSLDFSGRLSKSPTPVLSRSGLTSARSAESLLESTKLRPREMDGMDSGGVYASPTCSNMADHALSFRSLVPSEPLSICSDELDHCSNVSNDSREGSGGSVHGDFPKHRLNKCKGTCPASYTRFTTIRKHEQQSSRQSDWRSDSRGDKNSLLRNIHLMSPLPFRLKKPLQQHPRQPPPSDSSESPAGQKADLPCHDPQDQPHSAGKPQVPTRLSSRHTMARLSHNSEPPLDRPAGLEDCTRAINNGNPVPYSDHGLDRNNNPQSELAAAHGDSESPRHFIPADYLESTEEFIRRRHDDKEKLLADQRRLKREQEEADIAARRHTGVIPTHHQFITNERFGDLLNIDDTAKRKSGLEMRPARAKFDFKAQTLKELPLQKGDVVYIYRQIDQNWYEGEHHGRVGIFPRTYIELLPPAEKAQPRKLAPVQVLEYGEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVLKRPLVKTPVDYIDLPYSSSPSRSATVSPQQPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL

Q62417-2

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

Q62417-3

  • Name
    3
  • Synonyms
    Ponsin-2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q62417-4

  • Name
    4
  • Synonyms
    Ponsin-1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q62417-5

Q62417-6

Q62417-7

  • Name
    7
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 70-78: Missing
    • 117-117: G → GATSSSSAPSEVIVVPLYLVNTDRGQGQEGTARTPASLGPLGCVHTVPATTPAASPLTFPTLDDFIPPHLQRRPHHSQPASACGSLSPASQTSPPSPPPPLVPPVPEDLHRGLEPDLPGAVSSTG
    • 163-163: R → REQQKRLSSLS
    • 341-402: Missing
    • 477-965: Missing
    • 1212-1290: QPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL → VSKLSNSACSFHPQLCQRHTALLGLLFHALIKSYLEQAGWEFFSYMSVAFS

Computationally mapped potential isoform sequences

There are 13 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9PYX6E9PYX6_MOUSESorbs1724
A0A668KLG2A0A668KLG2_MOUSESorbs1352
E9Q6A3E9Q6A3_MOUSESorbs1714
A0A5F8MPJ2A0A5F8MPJ2_MOUSESorbs11189
D3Z5J3D3Z5J3_MOUSESorbs1938
A0A286YD34A0A286YD34_MOUSESorbs1126
A0A286YCQ0A0A286YCQ0_MOUSESorbs1684
A0A286YCN8A0A286YCN8_MOUSESorbs1170
A0A286YCI8A0A286YCI8_MOUSESorbs11290
A0A286YDN0A0A286YDN0_MOUSESorbs1695
A0A286YDJ3A0A286YDJ3_MOUSESorbs128
A0A668KL65A0A668KL65_MOUSESorbs11005
E9QNA7E9QNA7_MOUSESorbs1740

Sequence caution

The sequence BAC65769.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_05088526in isoform 4
Compositional bias38-64Polar residues
Compositional bias65-81Basic and acidic residues
Alternative sequenceVSP_05088670-78in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7
Compositional bias82-96Polar residues
Compositional bias111-157Polar residues
Alternative sequenceVSP_050887117in isoform 6
Alternative sequenceVSP_050888117in isoform 7
Alternative sequenceVSP_050889163in isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7
Compositional bias188-203Basic and acidic residues
Sequence conflict205in Ref. 7; BAC28980
Compositional bias238-254Basic and acidic residues
Sequence conflict308in Ref. 7; BAC28980
Alternative sequenceVSP_050890341-402in isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7
Alternative sequenceVSP_050891369-402in isoform 3
Compositional bias392-416Polar residues
Compositional bias465-482Polar residues
Alternative sequenceVSP_050892477-965in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7
Compositional bias591-606Polar residues
Compositional bias697-726Polar residues
Compositional bias823-841Basic and acidic residues
Compositional bias898-916Polar residues
Compositional bias948-962Polar residues
Alternative sequenceVSP_050893994-1049in isoform 3, isoform 4, isoform 5 and isoform 6
Sequence conflict1004in Ref. 4; AAM77354
Alternative sequenceVSP_0508941212-1290in isoform 7

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U58883
EMBL· GenBank· DDBJ
AAC71776.1
EMBL· GenBank· DDBJ
mRNA
AF078666
EMBL· GenBank· DDBJ
AAD16007.1
EMBL· GenBank· DDBJ
mRNA
AF078667
EMBL· GenBank· DDBJ
AAD16008.1
EMBL· GenBank· DDBJ
mRNA
AF521593
EMBL· GenBank· DDBJ
AAM77354.1
EMBL· GenBank· DDBJ
mRNA
AK122487
EMBL· GenBank· DDBJ
BAC65769.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK035212
EMBL· GenBank· DDBJ
BAC28980.1
EMBL· GenBank· DDBJ
mRNA
BC012703
EMBL· GenBank· DDBJ
AAH12703.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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