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Q13425 (SNTB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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:D16S2531E, SNT2B2, SNTL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length540 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.

Subunit structure

Monomer and homodimer Probable. Interacts with the other members of the syntrophin family: SNTA1 and SNTB1; and with the sodium channel proteins SCN4A and SCN5A. Interacts with SAST, MAST205, microtubules and microtubule-associated proteins By similarity. Interacts with the dystrophin protein DMD and related proteins DTNA and UTRN, and 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. Ref.1 Ref.2 Ref.4 Ref.5

Subcellular location

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

Tissue specificity

Ubiquitous. Isoform 1 is the predominant isoform. Weak level of isoform 2 is present in all tested tissues, except in liver and heart where it is highly expressed.

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.

Sequence similarities

Belongs to the syntrophin family.

Contains 1 PDZ (DHR) domain.

Contains 2 PH domains.

Contains 1 SU (syntrophin unique) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13425-1)

Also known as: Beta2-syntrophin58;

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.
Isoform 2 (identifier: Q13425-2)

Also known as: Beta2-syntrophin28;

The sequence of this isoform differs from the canonical sequence as follows:
     266-267: LI → QN
     268-540: Missing.
Note: Lacks domains required for interaction with dystrophin related proteins. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Beta-2-syntrophin
PRO_0000184011

Regions

Domain115 – 19884PDZ
Domain163 – 300138PH 1
Domain325 – 437113PH 2
Domain484 – 54057SU
Region518 – 54023Calmodulin-binding By similarity
Compositional bias54 – 574Poly-Ala
Compositional bias66 – 694Poly-Ala

Amino acid modifications

Modified residue951Phosphoserine Ref.9 Ref.13
Modified residue1101Phosphoserine Ref.7 Ref.8 Ref.13
Modified residue2221Phosphoserine Ref.10 Ref.13
Modified residue2331Phosphoserine Ref.10
Modified residue3931Phosphoserine Ref.10 Ref.13

Natural variations

Alternative sequence266 – 2672LI → QN in isoform 2.
VSP_006358
Alternative sequence268 – 540273Missing in isoform 2.
VSP_006359
Natural variant4241D → E.
Corresponds to variant rs1058482 [ dbSNP | Ensembl ].
VAR_014076

Secondary structure

................ 540
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta2-syntrophin58) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 53A9F3340DC024ED

FASTA54057,950
        10         20         30         40         50         60 
MRVAAATAAA GAGPAMAVWT RATKAGLVEL LLRERWVRVV AELSGESLSL TGDAAAAELE 

        70         80         90        100        110        120 
PALGPAAAAF NGLPNGGGAG DSLPGSPSRG LGPPSPPAPP RGPAGEAGAS PPVRRVRVVK 

       130        140        150        160        170        180 
QEAGGLGISI KGGRENRMPI LISKIFPGLA ADQSRALRLG DAILSVNGTD LRQATHDQAV 

       190        200        210        220        230        240 
QALKRAGKEV LLEVKFIREV TPYIKKPSLV SDLPWEGAAP QSPSFSGSED SGSPKHQNST 

       250        260        270        280        290        300 
KDRKIIPLKM CFAARNLSMP DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM 

       310        320        330        340        350        360 
ALLPQVLAEL NAMLGATSTA GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM AVTEKDLLLY 

       370        380        390        400        410        420 
DCMPWTRDAW ASPCHSYPLV ATRLVHSGSG CRSPSLGSDL TFATRTGSRQ GIEMHLFRVE 

       430        440        450        460        470        480 
THRDLSSWTR ILVQGCHAAA ELIKEVSLGC MLNGQEVRLT IHYENGFTIS RENGGSSSIL 

       490        500        510        520        530        540 
YRYPFERLKM SADDGIRNLY LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV 

« Hide

Isoform 2 (Beta2-syntrophin28) [UniParc].

Checksum: 45DF36C82C013228
Show »

FASTA26727,677

References

« Hide 'large scale' references
[1]"The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives."
Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.
J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DMD; DTNA AND UTRN.
Tissue: Muscle.
[2]"The receptor tyrosine phosphatase-like protein ICA512 binds the PDZ domains of beta2-syntrophin and nNOS in pancreatic beta-cells."
Ort T., Maksimova E., Dirkx R., Kachinsky A.M., Berghs S., Froehner S.C., Solimena M.
Eur. J. Cell Biol. 79:621-630(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PTPRN.
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Mammary gland.
[4]"The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses."
Garcia R.A., Vasudevan K., Buonanno A.
Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4.
[5]"Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated cleavage of ICA512 upon stimulation of insulin secretion."
Ort T., Voronov S., Guo J., Zawalich K., Froehner S.C., Zawalich W., Solimena M.
EMBO J. 20:4013-4023(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRN.
[6]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-233 AND SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-222 AND SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40572 mRNA. Translation: AAC50449.1.
AF243385 mRNA. Translation: AAK15149.1.
BC048215 mRNA. Translation: AAH48215.1.
RefSeqNP_006741.1. NM_006750.3.
UniGeneHs.461117.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VRFX-ray2.00A/B/C/D112-200[»]
ProteinModelPortalQ13425.
SMRQ13425. Positions 17-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112528. 17 interactions.
IntActQ13425. 11 interactions.
MINTMINT-239533.
STRING9606.ENSP00000338191.

PTM databases

PhosphoSiteQ13425.

Polymorphism databases

DMDM23822158.

Proteomic databases

PaxDbQ13425.
PeptideAtlasQ13425.
PRIDEQ13425.

Protocols and materials databases

DNASU6645.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336278; ENSP00000338191; ENSG00000168807. [Q13425-1]
ENST00000467311; ENSP00000436443; ENSG00000168807. [Q13425-2]
ENST00000562438; ENSP00000458999; ENSG00000260873. [Q13425-1]
GeneID6645.
KEGGhsa:6645.
UCSCuc002ewu.3. human. [Q13425-1]

Organism-specific databases

CTD6645.
GeneCardsGC16P069221.
HGNCHGNC:11169. SNTB2.
HPAHPA001394.
MIM600027. gene.
neXtProtNX_Q13425.
PharmGKBPA36009.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318350.
HOGENOMHOG000231596.
HOVERGENHBG054204.
InParanoidQ13425.
OMAAIHTNIA.
PhylomeDBQ13425.
TreeFamTF317932.

Gene expression databases

ArrayExpressQ13425.
BgeeQ13425.
CleanExHS_SNTB2.
GenevestigatorQ13425.

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. human.
EvolutionaryTraceQ13425.
GeneWikiSNTB2.
GenomeRNAi6645.
NextBio25895.
PROQ13425.
SOURCESearch...

Entry information

Entry nameSNTB2_HUMAN
AccessionPrimary (citable) accession number: Q13425
Secondary accession number(s): Q9BY09
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM