Hmdb loader

Showing Protein Alpha-1-syntrophin (HMDBP08001)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP08001
Secondary Accession Numbers
  • 13712
Name Alpha-1-syntrophin
Synonyms
  1. 59 kDa dystrophin-associated protein A1 acidic component 1
  2. Pro-TGF-alpha cytoplasmic domain-interacting protein 1
  3. Syntrophin-1
  4. TACIP1
Gene Name SNTA1
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 extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5- biphosphate
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. Cell membrane
  2. Cytoplasm
  3. Peripheral membrane protein
  4. Cytoplasmic side
  5. cytoskeleton
  6. Cell junction
  7. sarcolemma
Gene Properties
Chromosome Location Chromosome:2
Locus 20q11.2
SNPs SNTA1
Gene Sequence 
>1518 bp
ATGGCGTCCGGCAGGCGCGCCCCGCGCACCGGGCTGCTGGAGCTGCGCGCCGGGGCGGGC
TCGGGGGCCGGCGGCGAGCGATGGCAGCGGGTGCTGCTGAGTCTGGCGGAGGACGTGCTG
ACCGTGAGCCCCGCCGACGGCGACCCTGGTCCCGAGCCCGGCGCTCCGCGGGAGCAGGAG
CCCGCGCAGCTCAACGGCGCCGCGGAGCCGGGCGCCGGGCCCCCGCAGCTGCCAGAGGCG
CTACTGCTCCAGCGGCGCCGCGTGACGGTGCGCAAGGCCGACGCCGGTGGGCTGGGCATC
AGCATCAAAGGCGGCCGGGAGAACAAGATGCCTATTCTCATTTCCAAGATCTTCAAGGGA
TTGGCAGCTGACCAGACAGAGGCCCTTTTTGTGGGGGATGCCATCCTGTCTGTGAATGGG
GAAGACTTGTCCTCTGCTACCCATGATGAGGCGGTGCAGGTCCTCAAGAAGACAGGCAAG
GAGGTGGTGCTGGAGGTCAAGTATATGAAGGACGTCTCACCGTATTTCAAGAACTCTACT
GGTGGGACCTCGGTCGGCTGGGACTCACCTCCTGCCTCACCCCTTCAGCGGCAGCCTTCC
TCCCCTGGCCCCACACCCCGGAACTTCAGCGAGGCCAAACACATGTCCTTGAAGATGGCA
TATGTCTCGAAGAGGTGCACCCCCAATGACCCGGAGCCCAGGTATCTGGAGATCTGCTCG
GCAGATGGTCAAGACACCCTCTTCCTGAGGGCCAAGGATGAGGCTAGTGCGAGGTCGTGG
GCGACTGCCATCCAAGCCCAGGTCAATACTCTGACGCCGCGGGTCAAGGATGAGCTGCAG
GCACTGTTGGCAGCCACCAGCACAGCTGGGAGCCAGGACATCAAGCAGATTGGCTGGCTA
ACTGAGCAGCTGCCCAGTGGGGGCACAGCCCCCACCCTGGCCCTGCTAACTGAAAAGGAA
CTGCTCCTCTACTTGTCTCTCCCCGAGACCCGCGAGGCCCTGAGCCGGCCAGCCCGTACT
GCCCCACTCATCGCCACCAGACTGGTGCACTCAGGCCCCTCCAAGGGCTCAGTGCCCTAC
GATGCAGAGCTCTCTTTTGCCCTGCGCACGGGCACGCGTCACGGTGTGGACACTCACCTG
TTCAGCGTGGAGTCACCGCAGGAGCTGGCTGCCTGGACCCGCCAGCTTGTGGATGGCTGT
CACCGGGCCGCCGAGGGTGTGCAGGAGGTGTCTACAGCCTGCACGTGGAATGGGCGTCCC
TGCAGCCTGTCTGTGCACATCGACAAGGGCTTCACACTGTGGGCGGCTGAGCCAGGTGCA
GCCCGAGCTGTGCTCCTGCGACAGCCCTTCGAGAAGCTGCAGATGTCTTCAGATGACGGT
GCCAGTCTCCTTTTCCTGGATTTTGGAGGTGCTGAAGGCGAGATCCAGCTGGACCTGCAC
TCGTGTCCCAAAACCATAGTCTTCATCATCCACTCCTTCCTGTCGGCCAAAGTCACCCGC
CTCGGGCTGTTGGCCTAG
Protein Properties
Number of Residues 505
Molecular Weight 53894.7
Theoretical pI 6.79
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Alpha-1-syntrophin
MASGRRAPRTGLLELRAGAGSGAGGERWQRVLLSLAEDVLTVSPADGDPGPEPGAPREQE
PAQLNGAAEPGAGPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKG
LAADQTEALFVGDAILSVNGEDLSSATHDEAVQVLKKTGKEVVLEVKYMKDVSPYFKNST
GGTSVGWDSPPASPLQRQPSSPGPTPRNFSEAKHMSLKMAYVSKRCTPNDPEPRYLEICS
ADGQDTLFLRAKDEASARSWATAIQAQVNTLTPRVKDELQALLAATSTAGSQDIKQIGWL
TEQLPSGGTAPTLALLTEKELLLYLSLPETREALSRPARTAPLIATRLVHSGPSKGSVPY
DAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRP
CSLSVHIDKGFTLWAAEPGAARAVLLRQPFEKLQMSSDDGASLLFLDFGGAEGEIQLDLH
SCPKTIVFIIHSFLSAKVTRLGLLA
GenBank ID Protein 158257420
UniProtKB/Swiss-Prot ID Q13424
UniProtKB/Swiss-Prot Entry Name SNTA1_HUMAN
PDB IDs
GenBank Gene ID AK291994
GeneCard ID SNTA1
GenAtlas ID SNTA1
HGNC ID HGNC:11167
References
General References
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  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
  6. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed:11780052 ]
  7. Olalla L, Aledo JC, Bannenberg G, Marquez J: The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins. FEBS Lett. 2001 Jan 19;488(3):116-22. [PubMed:11163757 ]
  8. Hasegawa M, Cuenda A, Spillantini MG, Thomas GM, Buee-Scherrer V, Cohen P, Goedert M: Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition. J Biol Chem. 1999 Apr 30;274(18):12626-31. [PubMed:10212242 ]
  9. Fernandez-Larrea J, Merlos-Suarez A, Urena JM, Baselga J, Arribas J: A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface. Mol Cell. 1999 Apr;3(4):423-33. [PubMed:10230395 ]
  10. 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 ]
  11. Castello A, Brocheriou V, Chafey P, Kahn A, Gilgenkrantz H: Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast. FEBS Lett. 1996 Mar 25;383(1-2):124-8. [PubMed:8612778 ]
  12. Wu G, Ai T, Kim JJ, Mohapatra B, Xi Y, Li Z, Abbasi S, Purevjav E, Samani K, Ackerman MJ, Qi M, Moss AJ, Shimizu W, Towbin JA, Cheng J, Vatta M: alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium channel disruption. Circ Arrhythm Electrophysiol. 2008 Aug;1(3):193-201. doi: 10.1161/CIRCEP.108.769224. [PubMed:19684871 ]
  13. Ueda K, Valdivia C, Medeiros-Domingo A, Tester DJ, Vatta M, Farrugia G, Ackerman MJ, Makielski JC: Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex. Proc Natl Acad Sci U S A. 2008 Jul 8;105(27):9355-60. doi: 10.1073/pnas.0801294105. Epub 2008 Jun 30. [PubMed:18591664 ]