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Showing Protein Beta-2-syntrophin (HMDBP08002)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP08002
Secondary Accession Numbers
  • 13713
Name Beta-2-syntrophin
Synonyms
  1. 59 kDa dystrophin-associated protein A1 basic component 2
  2. SNT3
  3. SNTL
  4. Syntrophin-3
  5. Syntrophin-like
Gene Name SNTB2
Protein Type Unknown
Biological Properties
General Function Involved in protein binding
Specific 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
Pathways
  • Acebutolol Action Pathway
  • Alprenolol Action Pathway
  • Amiodarone Action Pathway
  • Amlodipine Action Pathway
  • Arbutamine Action Pathway
  • Atenolol Action Pathway
  • Betaxolol Action Pathway
  • Bevantolol Action Pathway
  • Bisoprolol Action Pathway
  • Bopindolol Action Pathway
  • Bupranolol Action Pathway
  • Carteolol Action Pathway
  • Carvedilol Action Pathway
  • Diltiazem Action Pathway
  • Disopyramide Action Pathway
  • Dobutamine Action Pathway
  • Epinephrine Action Pathway
  • Esmolol Action Pathway
  • Felodipine Action Pathway
  • Flecainide Action Pathway
  • Fosphenytoin (Antiarrhythmic) Action Pathway
  • Fosphenytoin (Antiarrhythmic) Metabolism Pathway
  • Ibutilide Action Pathway
  • Isoprenaline Action Pathway
  • Isradipine Action Pathway
  • Labetalol Action Pathway
  • Levobunolol Action Pathway
  • Lidocaine (Antiarrhythmic) Action Pathway
  • Metipranolol Action Pathway
  • Metoprolol Action Pathway
  • Mexiletine Action Pathway
  • Muscle/Heart Contraction
  • Nadolol Action Pathway
  • Nebivolol Action Pathway
  • Nifedipine Action Pathway
  • Nimodipine Action Pathway
  • Nisoldipine Action Pathway
  • Nitrendipine Action Pathway
  • Oxprenolol Action Pathway
  • Penbutolol Action Pathway
  • Phenytoin (Antiarrhythmic) Action Pathway
  • Pindolol Action Pathway
  • Practolol Action Pathway
  • Procainamide (Antiarrhythmic) Action Pathway
  • Propranolol Action Pathway
  • Quinidine Action Pathway
  • Sotalol Action Pathway
  • Timolol Action Pathway
  • Tocainide Action Pathway
  • Verapamil Action Pathway
Reactions Not Available
GO Classification
Function
binding
protein binding
Cellular Location
  1. Cytoplasm
  2. Peripheral membrane protein
  3. Cytoplasmic vesicle
  4. Membrane
  5. cytoskeleton
  6. secretory vesicle membrane
  7. Cell junction
Gene Properties
Chromosome Location Chromosome:1
Locus 16q22.1
SNPs SNTB2
Gene Sequence 
>1623 bp
ATGAGGGTAGCTGCGGCGACTGCGGCGGCTGGAGCGGGGCCGGCCATGGCGGTGTGGACG
CGGGCCACCAAAGCGGGGCTGGTGGAGCTGCTCCTGAGGGAGCGCTGGGTCCGAGTGGTG
GCCGAGCTGAGCGGGGAGAGCCTGAGCCTGACGGGCGACGCCGCCGCGGCCGAGCTGGAG
CCCGCTCTGGGACCCGCGGCCGCCGCCTTCAACGGCCTCCCAAACGGCGGCGGCGCGGGC
GACTCGCTGCCCGGGAGCCCAAGCCGCGGCCTGGGGCCCCCGAGCCCGCCGGCGCCGCCT
CGGGGCCCCGCGGGTGAGGCGGGCGCGTCGCCGCCCGTGCGCCGGGTGCGGGTGGTGAAG
CAAGAGGCGGGCGGCCTGGGCATCAGCATCAAGGGCGGCCGCGAGAACCGGATGCCGATC
CTCATCTCCAAGATCTTCCCCGGGCTGGCTGCCGACCAGAGCCGGGCGCTGCGGCTGGGC
GACGCCATCCTGTCGGTGAACGGCACCGACCTGCGCCAGGCCACCCACGACCAGGCCGTG
CAGGCGCTGAAGCGCGCGGGCAAGGAGGTGCTGCTGGAGGTCAAGTTCATCCGAGAAGTA
ACACCATATATCAAGAAGCCATCATTAGTATCAGATCTGCCGTGGGAAGGTGCAGCCCCC
CAGTCACCAAGCTTTAGTGGCAGTGAGGACTCTGGTTCGCCAAAACACCAGAACAGCACC
AAGGACAGGAAGATCATCCCTCTCAAAATGTGCTTTGCTGCTAGAAACCTAAGCATGCCG
GATCTGGAAAACAGATTGATAGAGCTACATTCTCCTGATAGCAGGAACACGTTGATCCTA
CGCTGCAAAGATACAGCCACAGCACACTCCTGGTTCGTAGCTATCCACACCAACATAATG
GCTCTCCTCCCACAGGTGTTGGCTGAACTCAACGCCATGCTTGGGGCAACCAGTACAGCA
GGAGGCAGTAAAGAGGTGAAGCATATTGCCTGGCTGGCAGAACAGGCAAAACTAGATGGT
GGAAGACAGCAATGGAGACCTGTCCTCATGGCTGTGACTGAGAAGGATTTGCTGCTCTAT
GACTGTATGCCGTGGACAAGAGATGCCTGGGCGTCACCATGCCACAGCTACCCACTTGTT
GCCACCAGGTTGGTTCATTCTGGCTCCGGATGTCGATCCCCCTCCCTTGGATCTGACCTT
ACATTTGCTACCAGGACAGGCTCTCGACAGGGCATTGAGATGCATCTCTTCAGGGTGGAG
ACACATCGGGATCTGTCATCCTGGACCAGGATACTTGTTCAGGGTTGCCATGCTGCTGCT
GAGCTGATCAAGGAAGTCTCTCTAGGCTGCATGTTAAATGGCCAAGAGGTGAGGCTTACT
ATTCACTATGAAAATGGGTTCACCATCTCAAGGGAAAATGGAGGCTCCAGCAGCATATTG
TACCGCTACCCCTTTGAAAGGCTGAAGATGTCTGCTGATGATGGCATCCGAAATCTATAC
TTGGATTTTGGTGGTCCCGAGGGAGAACTGACCATGGACCTGCACTCTTGTCCGAAGCCG
ATTGTATTTGTGTTGCACACGTTTTTATCGGCCAAAGTCACTCGTATGGGACTGCTTGTA
TGA
Protein Properties
Number of Residues 540
Molecular Weight 57949.0
Theoretical pI 9.07
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Beta-2-syntrophin
MRVAAATAAAGAGPAMAVWTRATKAGLVELLLRERWVRVVAELSGESLSLTGDAAAAELE
PALGPAAAAFNGLPNGGGAGDSLPGSPSRGLGPPSPPAPPRGPAGEAGASPPVRRVRVVK
QEAGGLGISIKGGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAV
QALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGAAPQSPSFSGSEDSGSPKHQNST
KDRKIIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIM
ALLPQVLAELNAMLGATSTAGGSKEVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLY
DCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVE
THRDLSSWTRILVQGCHAAAELIKEVSLGCMLNGQEVRLTIHYENGFTISRENGGSSSIL
YRYPFERLKMSADDGIRNLYLDFGGPEGELTMDLHSCPKPIVFVLHTFLSAKVTRMGLLV
GenBank ID Protein 5803177
UniProtKB/Swiss-Prot ID Q13425
UniProtKB/Swiss-Prot Entry Name SNTB2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_006750.3
GeneCard ID SNTB2
GenAtlas ID SNTB2
HGNC ID HGNC:11169
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  6. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  8. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  9. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [PubMed:18220336 ]
  10. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed:14759258 ]
  11. Garcia RA, Vasudevan K, Buonanno A: The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3596-601. [PubMed:10725395 ]
  12. Ahn AH, Freener CA, Gussoni E, Yoshida M, Ozawa E, Kunkel LM: The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives. J Biol Chem. 1996 Feb 2;271(5):2724-30. [PubMed:8576247 ]
  13. Ort T, Maksimova E, Dirkx R, Kachinsky AM, Berghs S, Froehner SC, Solimena M: The receptor tyrosine phosphatase-like protein ICA512 binds the PDZ domains of beta2-syntrophin and nNOS in pancreatic beta-cells. Eur J Cell Biol. 2000 Sep;79(9):621-30. [PubMed:11043403 ]
  14. Ort T, Voronov S, Guo J, Zawalich K, Froehner SC, Zawalich W, Solimena M: Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated cleavage of ICA512 upon stimulation of insulin secretion. EMBO J. 2001 Aug 1;20(15):4013-23. [PubMed:11483505 ]