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Q13425

- SNTB2_HUMAN

UniProt

Q13425 - SNTB2_HUMAN

Protein

Beta-2-syntrophin

Gene

SNTB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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
    2. protein binding Source: UniProtKB

    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

    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. cell junction Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. dystrophin-associated glycoprotein complex Source: ProtInc
    4. extracellular vesicular exosome Source: UniProt
    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

    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

    ArrayExpressiQ13425.
    BgeeiQ13425.
    CleanExiHS_SNTB2.
    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. 17 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 – 1197
    Beta strandi127 – 1337
    Helixi134 – 1363
    Beta strandi138 – 1458
    Helixi150 – 1545
    Beta strandi161 – 1666
    Helixi176 – 1849
    Beta strandi188 – 1969

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VRFX-ray2.00A/B/C/D112-200[»]
    ProteinModelPortaliQ13425.
    SMRiQ13425. Positions 17-301.
    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.
    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

    MRVAAATAAA GAGPAMAVWT RATKAGLVEL LLRERWVRVV AELSGESLSL    50
    TGDAAAAELE PALGPAAAAF NGLPNGGGAG DSLPGSPSRG LGPPSPPAPP 100
    RGPAGEAGAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI LISKIFPGLA 150
    ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV 200
    TPYIKKPSLV SDLPWEGAAP QSPSFSGSED SGSPKHQNST KDRKIIPLKM 250
    CFAARNLSMP DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM 300
    ALLPQVLAEL NAMLGATSTA GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM 350
    AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV ATRLVHSGSG CRSPSLGSDL 400
    TFATRTGSRQ GIEMHLFRVE THRDLSSWTR ILVQGCHAAA ELIKEVSLGC 450
    MLNGQEVRLT IHYENGFTIS RENGGSSSIL YRYPFERLKM SADDGIRNLY 500
    LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV 540
    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:
    EMBL
    GenBank
    DDBJ
    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. [Q13425-1]
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40572 mRNA. Translation: AAC50449.1 .
    AF243385 mRNA. Translation: AAK15149.1 .
    BC048215 mRNA. Translation: AAH48215.1 .
    CCDSi CCDS10873.1. [Q13425-1 ]
    RefSeqi NP_006741.1. NM_006750.3. [Q13425-1 ]
    UniGenei Hs.461117.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VRF X-ray 2.00 A/B/C/D 112-200 [» ]
    ProteinModelPortali Q13425.
    SMRi Q13425. Positions 17-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112528. 17 interactions.
    IntActi Q13425. 11 interactions.
    MINTi MINT-239533.
    STRINGi 9606.ENSP00000338191.

    PTM databases

    PhosphoSitei Q13425.

    Polymorphism databases

    DMDMi 23822158.

    Proteomic databases

    MaxQBi Q13425.
    PaxDbi Q13425.
    PeptideAtlasi Q13425.
    PRIDEi Q13425.

    Protocols and materials databases

    DNASUi 6645.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336278 ; ENSP00000338191 ; ENSG00000168807 . [Q13425-1 ]
    ENST00000467311 ; ENSP00000436443 ; ENSG00000168807 . [Q13425-2 ]
    ENST00000562438 ; ENSP00000458999 ; ENSG00000260873 . [Q13425-1 ]
    GeneIDi 6645.
    KEGGi hsa:6645.
    UCSCi uc002ewu.3. human. [Q13425-1 ]

    Organism-specific databases

    CTDi 6645.
    GeneCardsi GC16P069221.
    HGNCi HGNC:11169. SNTB2.
    HPAi HPA001394.
    MIMi 600027. gene.
    neXtProti NX_Q13425.
    PharmGKBi PA36009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG318350.
    HOGENOMi HOG000231596.
    HOVERGENi HBG054204.
    InParanoidi Q13425.
    OMAi LYQGRQC.
    PhylomeDBi Q13425.
    TreeFami TF317932.

    Miscellaneous databases

    ChiTaRSi SNTB2. human.
    EvolutionaryTracei Q13425.
    GeneWikii SNTB2.
    GenomeRNAii 6645.
    NextBioi 25895.
    PROi Q13425.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13425.
    Bgeei Q13425.
    CleanExi HS_SNTB2.
    Genevestigatori Q13425.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    IPR001849. PH_domain.
    IPR028550. SNTB2.
    IPR015482. Syntrophin.
    [Graphical view ]
    PANTHERi PTHR10554. PTHR10554. 1 hit.
    PTHR10554:SF8. PTHR10554:SF8. 1 hit.
    Pfami PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50106. PDZ. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 146 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