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Q61235 (SNTB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-2-syntrophin
Alternative name(s):
59 kDa dystrophin-associated protein A1 basic component 2
Syntrophin-3
Short name=SNT3
Syntrophin-like
Short name=SNTL
Gene names
Name:Sntb2
Synonyms:Snt2b2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN By similarity.

Subunit structure

Monomer and homodimer Probable. Interacts with the dystrophin protein DMD and related protein DTNA; and with the other members of the syntrophin family: SNTA1 and SNTB1. Interacts with the neuroregulin receptor ERBB4. Interacts with PTPRN when phosphorylated, protecting PTPRN from protein cleavage by CAPN1. Dephosphorylation upon insulin stimulation disrupts the interaction with PTPRN and results in the cleavage of PTPRN By similarity. Interacts with the sodium channel proteins SCN4A and SCN5A. Interacts with SAST, MAST205, microtubules and microtubule-associated proteins. Interacts with the dystrophin related protein UTRN. Ref.3 Ref.4 Ref.5

Subcellular location

Membrane. Cytoplasmic vesiclesecretory vesicle membrane; Peripheral membrane protein. Cell junction By similarity. Cytoplasmcytoskeleton. Note: Membrane-associated. In insulinoma cell line, it is enriched in secretory granules By similarity. In muscle, it is exclusively localized at the neuromuscular junction. Ref.3

Tissue specificity

Ubiquitous. Expressed at high levels in the testis. Ref.3

Domain

The PH 1 domain mediates the oligomerization in a calcium dependent manner By similarity.

The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane By similarity.

The SU domain binds calmodulin in a calcium-dependent manner By similarity.

Post-translational modification

Phosphorylated. Partially dephosphorylated upon insulin stimulation By similarity.

Sequence similarities

Belongs to the syntrophin family.

Contains 1 PDZ (DHR) domain.

Contains 2 PH domains.

Contains 1 SU (syntrophin unique) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Beta-2-syntrophin
PRO_0000184012

Regions

Domain95 – 17884PDZ
Domain143 – 280138PH 1
Domain305 – 417113PH 2
Domain464 – 52057SU
Region498 – 52023Calmodulin-binding By similarity
Compositional bias57 – 604Poly-Gly

Amino acid modifications

Modified residue751Phosphoserine Ref.8
Modified residue901Phosphoserine Ref.8 Ref.9
Modified residue2021Phosphoserine By similarity
Modified residue2131Phosphoserine By similarity
Modified residue3731Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q61235 [UniParc].

Last modified May 1, 1997. Version 2.
Checksum: 9F6886837C1CDB20

FASTA52056,382
        10         20         30         40         50         60 
MAVWTRATKA GLVELLLRER WVRVVAELSG ESLSLTGDAA AVEPEPPAAA FNGLPNGGGG 

        70         80         90        100        110        120 
ESLPGSPNRG LGPPSPPAPP RGPAGEASAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI 

       130        140        150        160        170        180 
LISKIFPGLA ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV 

       190        200        210        220        230        240 
TPYIKKPSLV SDLPWEGASP QSPSFSGSED SGSPKHQNTT KDRKVIPLKM CFAARNLSMP 

       250        260        270        280        290        300 
DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM ALLPQVLAEL NAMLGATSTA 

       310        320        330        340        350        360 
GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV 

       370        380        390        400        410        420 
ATRLVHSGSG CRSPSLGSDL TFATRTGSRQ GIEMHLFRVE THRDLSTWTR ILVQGCHAAA 

       430        440        450        460        470        480 
ELIKEVSLGC TLSGQEVRFT VHYEHGFTIT RDNGGASSIL YRYPFERLKM SADDGIRNLY 

       490        500        510        520 
LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV 

« Hide

References

« Hide 'large scale' references
[1]"Mouse alpha 1- and beta 2-syntrophin gene structure, chromosome localization, and homology with a discs large domain."
Adams M.E., Dwyer T.M., Dowler L.L., White R.A., Froehner S.C.
J. Biol. Chem. 270:25859-25865(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Diaphragm.
[2]"Two forms of mouse syntrophin, a 58 kDa dystrophin-associated protein, differ in primary structure and tissue distribution."
Adams M.E., Butler M.H., Dwyer T.M., Peters M.F., Murnane A.A., Froehner S.C.
Neuron 11:531-540(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-520.
Tissue: Diaphragm.
[3]"Differential association of syntrophin pairs with the dystrophin complex."
Peters M.F., Adams M.E., Froehner S.C.
J. Cell Biol. 138:81-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH UTRN.
[4]"Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins."
Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R., Froehner S.C.
J. Neurosci. 18:128-137(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCN4A AND SCN5A.
[5]"Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases."
Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K., Chamberlain J.S.
Nat. Neurosci. 2:611-617(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAST; MAST205; MICROTUBULES AND MICROTUBULE-ASSOCIATED PROTEINS.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00678 mRNA. Translation: AAC53060.1.
RefSeqNP_033255.1. NM_009229.4.
UniGeneMm.30228.

3D structure databases

ProteinModelPortalQ61235.
SMRQ61235. Positions 6-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203384. 1 interaction.
IntActQ61235. 4 interactions.
MINTMINT-99343.

PTM databases

PhosphoSiteQ61235.

Proteomic databases

PaxDbQ61235.
PRIDEQ61235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047425; ENSMUSP00000037324; ENSMUSG00000041308.
GeneID20650.
KEGGmmu:20650.
UCSCuc009ngt.1. mouse.

Organism-specific databases

CTD6645.
MGIMGI:101771. Sntb2.

Phylogenomic databases

eggNOGNOG318350.
GeneTreeENSGT00550000074581.
HOGENOMHOG000231596.
HOVERGENHBG054204.
InParanoidQ61235.
OMAAIHTNIA.
OrthoDBEOG7R56VZ.
PhylomeDBQ61235.
TreeFamTF317932.

Gene expression databases

ArrayExpressQ61235.
BgeeQ61235.
CleanExMM_SNTB2.
GenevestigatorQ61235.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR001849. Pleckstrin_homology.
IPR028550. SNTB2.
IPR015482. Syntrophin.
[Graphical view]
PANTHERPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF8. PTHR10554:SF8. 1 hit.
PfamPF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNTB2. mouse.
NextBio299071.
PROQ61235.
SOURCESearch...

Entry information

Entry nameSNTB2_MOUSE
AccessionPrimary (citable) accession number: Q61235
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot