Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-2-syntrophin

Gene

SNTB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SNTB2
Synonyms:D16S2531E, SNT2B2, SNTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:11169. SNTB2.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. dystrophin-associated glycoprotein complex Source: ProtInc
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: ProtInc
  6. microtubule Source: UniProtKB-KW
  7. protein complex Source: MGI
  8. synapse Source: Ensembl
  9. transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36009.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Beta-2-syntrophinPRO_0000184011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951Phosphoserine2 Publications
Modified residuei110 – 1101Phosphoserine3 Publications
Modified residuei222 – 2221Phosphoserine2 Publications
Modified residuei233 – 2331Phosphoserine1 Publication
Modified residuei393 – 3931Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated. Partially dephosphorylated upon insulin stimulation.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13425.
PaxDbiQ13425.
PeptideAtlasiQ13425.
PRIDEiQ13425.

PTM databases

PhosphoSiteiQ13425.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ13425.
CleanExiHS_SNTB2.
ExpressionAtlasiQ13425. baseline and differential.
GenevestigatoriQ13425.

Organism-specific databases

HPAiHPA001394.

Interactioni

Subunit structurei

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.By similarity4 PublicationsCurated

Protein-protein interaction databases

BioGridi112528. 21 interactions.
IntActiQ13425. 11 interactions.
MINTiMINT-239533.
STRINGi9606.ENSP00000338191.

Structurei

Secondary structure

1
540
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1197Combined sources
Beta strandi127 – 1337Combined sources
Helixi134 – 1363Combined sources
Beta strandi138 – 1458Combined sources
Helixi150 – 1545Combined sources
Beta strandi161 – 1666Combined sources
Helixi176 – 1849Combined sources
Beta strandi188 – 1969Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VRFX-ray2.00A/B/C/D112-200[»]
ProteinModelPortaliQ13425.
SMRiQ13425. Positions 79-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13425.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 19884PDZPROSITE-ProRule annotationAdd
BLAST
Domaini163 – 300138PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini325 – 437113PH 2PROSITE-ProRule annotationAdd
BLAST
Domaini484 – 54057SUAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni518 – 54023Calmodulin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 574Poly-Ala
Compositional biasi66 – 694Poly-Ala

Domaini

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

Sequence similaritiesi

Belongs to the syntrophin family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG318350.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ13425.
OMAiLYQGRQC.
PhylomeDBiQ13425.
TreeFamiTF317932.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001849. PH_domain.
IPR028550. SNTB2.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF8. PTHR10554:SF8. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13425-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRVAAATAAA GAGPAMAVWT RATKAGLVEL LLRERWVRVV AELSGESLSL
60 70 80 90 100
TGDAAAAELE PALGPAAAAF NGLPNGGGAG DSLPGSPSRG LGPPSPPAPP
110 120 130 140 150
RGPAGEAGAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI LISKIFPGLA
160 170 180 190 200
ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV
210 220 230 240 250
TPYIKKPSLV SDLPWEGAAP QSPSFSGSED SGSPKHQNST KDRKIIPLKM
260 270 280 290 300
CFAARNLSMP DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM
310 320 330 340 350
ALLPQVLAEL NAMLGATSTA GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM
360 370 380 390 400
AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV ATRLVHSGSG CRSPSLGSDL
410 420 430 440 450
TFATRTGSRQ GIEMHLFRVE THRDLSSWTR ILVQGCHAAA ELIKEVSLGC
460 470 480 490 500
MLNGQEVRLT IHYENGFTIS RENGGSSSIL YRYPFERLKM SADDGIRNLY
510 520 530 540
LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV
Length:540
Mass (Da):57,950
Last modified:November 1, 1996 - v1
Checksum:i53A9F3340DC024ED
GO
Isoform 2 (identifier: Q13425-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:267
Mass (Da):27,677
Checksum:i45DF36C82C013228
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti424 – 4241D → E.
Corresponds to variant rs1058482 [ dbSNP | Ensembl ].
VAR_014076

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei266 – 2672LI → QN in isoform 2. 1 PublicationVSP_006358
Alternative sequencei268 – 540273Missing in isoform 2. 1 PublicationVSP_006359Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40572 mRNA. Translation: AAC50449.1.
AF243385 mRNA. Translation: AAK15149.1.
BC048215 mRNA. Translation: AAH48215.1.
CCDSiCCDS10873.1. [Q13425-1]
RefSeqiNP_006741.1. NM_006750.3. [Q13425-1]
UniGeneiHs.461117.

Genome annotation databases

EnsembliENST00000336278; ENSP00000338191; ENSG00000168807. [Q13425-1]
ENST00000467311; ENSP00000436443; ENSG00000168807. [Q13425-2]
ENST00000562438; ENSP00000458999; ENSG00000260873.
GeneIDi6645.
KEGGihsa:6645.
UCSCiuc002ewu.3. human. [Q13425-1]

Polymorphism databases

DMDMi23822158.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40572 mRNA. Translation: AAC50449.1.
AF243385 mRNA. Translation: AAK15149.1.
BC048215 mRNA. Translation: AAH48215.1.
CCDSiCCDS10873.1. [Q13425-1]
RefSeqiNP_006741.1. NM_006750.3. [Q13425-1]
UniGeneiHs.461117.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VRFX-ray2.00A/B/C/D112-200[»]
ProteinModelPortaliQ13425.
SMRiQ13425. Positions 79-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112528. 21 interactions.
IntActiQ13425. 11 interactions.
MINTiMINT-239533.
STRINGi9606.ENSP00000338191.

PTM databases

PhosphoSiteiQ13425.

Polymorphism databases

DMDMi23822158.

Proteomic databases

MaxQBiQ13425.
PaxDbiQ13425.
PeptideAtlasiQ13425.
PRIDEiQ13425.

Protocols and materials databases

DNASUi6645.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336278; ENSP00000338191; ENSG00000168807. [Q13425-1]
ENST00000467311; ENSP00000436443; ENSG00000168807. [Q13425-2]
ENST00000562438; ENSP00000458999; ENSG00000260873.
GeneIDi6645.
KEGGihsa:6645.
UCSCiuc002ewu.3. human. [Q13425-1]

Organism-specific databases

CTDi6645.
GeneCardsiGC16P069221.
HGNCiHGNC:11169. SNTB2.
HPAiHPA001394.
MIMi600027. gene.
neXtProtiNX_Q13425.
PharmGKBiPA36009.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG318350.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ13425.
OMAiLYQGRQC.
PhylomeDBiQ13425.
TreeFamiTF317932.

Miscellaneous databases

ChiTaRSiSNTB2. human.
EvolutionaryTraceiQ13425.
GeneWikiiSNTB2.
GenomeRNAii6645.
NextBioi25895.
PROiQ13425.
SOURCEiSearch...

Gene expression databases

BgeeiQ13425.
CleanExiHS_SNTB2.
ExpressionAtlasiQ13425. baseline and differential.
GenevestigatoriQ13425.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001849. PH_domain.
IPR028550. SNTB2.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF8. PTHR10554:SF8. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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].

Entry informationi

Entry nameiSNTB2_HUMAN
AccessioniPrimary (citable) accession number: Q13425
Secondary accession number(s): Q9BY09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.