SNTA1_HUMAN - dbPTM
SNTA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNTA1_HUMAN
UniProt AC Q13424
Protein Name Alpha-1-syntrophin
Gene Name SNTA1
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Cell membrane, sarcolemma
Peripheral membrane protein
Cytoplasmic side. Cell junction. Cytoplasm, cytoskeleton. In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions..
Protein Description 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-bisphosphate (By similarity)..
Protein Sequence MASGRRAPRTGLLELRAGAGSGAGGERWQRVLLSLAEDVLTVSPADGDPGPEPGAPREQEPAQLNGAAEPGAGPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQVLKKTGKEVVLEVKYMKDVSPYFKNSTGGTSVGWDSPPASPLQRQPSSPGPTPRNFSEAKHMSLKMAYVSKRCTPNDPEPRYLEICSADGQDTLFLRAKDEASARSWATAIQAQVNTLTPRVKDELQALLAATSTAGSQDIKQIGWLTEQLPSGGTAPTLALLTEKELLLYLSLPETREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRPCSLSVHIDKGFTLWAAEPGAARAVLLRQPFEKLQMSSDDGASLLFLDFGGAEGEIQLDLHSCPKTIVFIIHSFLSAKVTRLGLLA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationSGRRAPRTGLLELRA
CCCCCCCCCCEEEEC		30.9921964256
21PhosphorylationELRAGAGSGAGGERW
EEECCCCCCCCHHHH		25.57-
89PhosphorylationLLQRRRVTVRKADAG
HHHCCCEEEEECHHC		16.87-
101PhosphorylationDAGGLGISIKGGREN
HHCCCCEEEECCCCC		19.2230266825
109MethylationIKGGRENKMPILISK
EECCCCCCCCCHHHH		41.10-
109UbiquitinationIKGGRENKMPILISK
EECCCCCCCCCHHHH		41.10-
109TrimethylationIKGGRENKMPILISK
EECCCCCCCCCHHHH		41.10-
157AcetylationEAVQVLKKTGKEVVL
HHHHHHHHHCCEEEE		59.3511793337
160AcetylationQVLKKTGKEVVLEVK
HHHHHHCCEEEEEEE		53.2011793349
167AcetylationKEVVLEVKYMKDVSP
CEEEEEEEECCCCCC		30.1911793361
173PhosphorylationVKYMKDVSPYFKNST
EEECCCCCCCCCCCC		24.8226462736
175PhosphorylationYMKDVSPYFKNSTGG
ECCCCCCCCCCCCCC		21.4928152594
179PhosphorylationVSPYFKNSTGGTSVG
CCCCCCCCCCCCCCC		29.0830266825
180PhosphorylationSPYFKNSTGGTSVGW
CCCCCCCCCCCCCCC		49.3723663014
183PhosphorylationFKNSTGGTSVGWDSP
CCCCCCCCCCCCCCC		22.9123663014
184PhosphorylationKNSTGGTSVGWDSPP
CCCCCCCCCCCCCCC		23.1630266825
189PhosphorylationGTSVGWDSPPASPLQ
CCCCCCCCCCCCCCC		26.6930266825
193PhosphorylationGWDSPPASPLQRQPS
CCCCCCCCCCCCCCC		31.7330266825
200PhosphorylationSPLQRQPSSPGPTPR
CCCCCCCCCCCCCCC		40.6130266825
201PhosphorylationPLQRQPSSPGPTPRN
CCCCCCCCCCCCCCC		40.3330266825
205PhosphorylationQPSSPGPTPRNFSEA
CCCCCCCCCCCHHHH		40.5722199227
210PhosphorylationGPTPRNFSEAKHMSL
CCCCCCHHHHHHHEH		39.9530631047
216PhosphorylationFSEAKHMSLKMAYVS
HHHHHHHEHHHHHHC		25.2628450419
272PhosphorylationQAQVNTLTPRVKDEL
HHHHHHCCHHHHHHH		13.6524719451
276UbiquitinationNTLTPRVKDELQALL
HHCCHHHHHHHHHHH		46.9229967540
291PhosphorylationAATSTAGSQDIKQIG
HHHCCCCCHHHHHHH		23.40-
312PhosphorylationPSGGTAPTLALLTEK
CCCCCCCCHHHHCHH		23.38-
326PhosphorylationKELLLYLSLPETREA
HHHHHHHCCHHHHHH		28.4622210691
330PhosphorylationLYLSLPETREALSRP
HHHCCHHHHHHHCCH		31.6922210691
340PhosphorylationALSRPARTAPLIATR
HHCCHHHHHCEEEEE		34.4320068231
346PhosphorylationRTAPLIATRLVHSGP
HHHCEEEEECCCCCC		19.9720068231
365PhosphorylationVPYDAELSFALRTGT
CCCCEEEEEEECCCC		10.4424076635
411PhosphorylationAEGVQEVSTACTWNG
HHHHHEEECEEEECC		14.99-
412PhosphorylationEGVQEVSTACTWNGR
HHHHEEECEEEECCE		30.81-
415PhosphorylationQEVSTACTWNGRPCS
HEEECEEEECCEECE		21.36-
422PhosphorylationTWNGRPCSLSVHIDK
EECCEECEEEEEECC		26.7624076635
424PhosphorylationNGRPCSLSVHIDKGF
CCEECEEEEEECCCC		8.7124076635
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
193SPhosphorylationKinaseMK12P53778
PhosphoELM
193SPhosphorylationKinaseMAPK12Q63538
GPS
193SPhosphorylationKinaseMAPK-FAMILY-GPS
193SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
201SPhosphorylationKinaseMK12P53778
PhosphoELM
201SPhosphorylationKinaseMAPK12Q63538
GPS
201SPhosphorylationKinaseMAPK-FAMILY-GPS
201SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNTA1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SNTA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
16169070
GLSK_HUMANGLSphysical
11163757
DMD_HUMANDMDphysical
8576247
UTRO_HUMANUTRNphysical
8576247
DMD_HUMANDMDphysical
9412493
SCN1A_HUMANSCN1Aphysical
9412493
SCN5A_HUMANSCN5Aphysical
9412493
NOS1_HUMANNOS1physical
9412493
MK12_HUMANMAPK12physical
10212242
MAGE1_HUMANMAGEE1physical
14623885
5HT2B_HUMANHTR2Bphysical
15123239
5HT2C_HUMANHTR2Cphysical
15123239
ADA1D_HUMANADRA1Dphysical
15123239
ADA2A_HUMANADRA2Aphysical
15123239
ADHX_HUMANADH5physical
15123239
AGTR2_HUMANAGTR2physical
15123239
ARY1_HUMANNAT1physical
15123239
AT2B2_HUMANATP2B2physical
15123239
ATS6_HUMANADAMTS6physical
15123239
ADRB1_HUMANADRB1physical
15123239
AGRB2_HUMANBAI2physical
15123239
AGRB3_HUMANBAI3physical
15123239
C3AR_HUMANC3AR1physical
15123239
CD3E_HUMANCD3Ephysical
15123239
KCNA4_HUMANKCNA4physical
15123239
KCNA5_HUMANKCNA5physical
15123239
SCN4A_HUMANSCN4Aphysical
15123239
COPB_HUMANCOPB1physical
15123239
F189B_HUMANFAM189Bphysical
15123239
GCYA2_HUMANGUCY1A2physical
15123239
EAA5_HUMANSLC1A7physical
15123239
F8I2_HUMANF8A1physical
15123239
FABPL_HUMANFABP1physical
15123239
GOGA2_HUMANGOLGA2physical
15123239
GLSL_HUMANGLS2physical
15123239
PRLHR_HUMANPRLHRphysical
15123239
GTR3_HUMANSLC2A3physical
15123239
GUAD_HUMANGDAphysical
15123239
TLX3_HUMANTLX3physical
15123239
IL2RA_HUMANIL2RAphysical
15123239
IL9_HUMANIL9physical
15123239
KCNJ4_HUMANKCNJ4physical
15123239
KCJ10_HUMANKCNJ10physical
15123239
KCJ15_HUMANKCNJ15physical
15123239
ITB5_HUMANITGB5physical
15123239
KPSH1_HUMANPSKH1physical
15123239
MAP4_HUMANMAP4physical
15123239
MAS_HUMANMAS1physical
15123239
MCM7_HUMANMCM7physical
15123239
MOT2_HUMANSLC16A7physical
15123239
MTMR2_HUMANMTMR2physical
15123239
NMU_HUMANNMUphysical
15123239
SC6A3_HUMANSLC6A3physical
15123239
PROF2_HUMANPFN2physical
15123239
RBTN1_HUMANLMO1physical
15123239
SCTR_HUMANSCTRphysical
15123239
SSR1_HUMANSSTR1physical
15123239
TGFA_HUMANTGFAphysical
15123239
VATO_HUMANATP6V0Bphysical
15123239
MRP4_HUMANABCC4physical
18045536
DTNA_HUMANDTNAphysical
18468998
DMD_HUMANDMDphysical
18468998
GNAT3_HUMANGNAT3physical
18468998
NPT2C_HUMANSLC34A3physical
18468998
NEBU_HUMANNEBphysical
18468998
PLCB3_HUMANPLCB3physical
18468998
RGS11_HUMANRGS11physical
18468998
RYR2_HUMANRYR2physical
18468998
STAM1_HUMANSTAMphysical
18468998
UTRO_HUMANUTRNphysical
18468998
Drug and Disease Associations
Kegg Disease
H00720 Long QT syndrome, including: Romano-Ward syndrome; Jervell and Lange-Nielsen syndrome (JLNS)
OMIM Disease
612955Long QT syndrome 12 (LQT12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNTA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, ANDMASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, ANDMASS SPECTROMETRY.

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