SYAP1_HUMAN - dbPTM
SYAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYAP1_HUMAN
UniProt AC Q96A49
Protein Name Synapse-associated protein 1 {ECO:0000305}
Gene Name SYAP1 {ECO:0000312|HGNC:HGNC:16273}
Organism Homo sapiens (Human).
Sequence Length 352
Subcellular Localization Cytoplasm, perinuclear region . Golgi apparatus . Perikaryon . Cell projection, axon . Cell projection, dendrite . Cell projection, growth cone . Cell junction, synapse, presynaptic cell membrane . Cell junction, synapse, postsynaptic cell membrane . Memb
Protein Description Plays a role in adipocyte differentiation by promoting mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth factor stimulation. [PubMed: 23300339]
Protein Sequence MFRGLSSWLGLQQPVAGGGQPNGDAPPEQPSETVAESAEEELQQAGDQELLHQAKDFGNYLFNFASAATKKITESVAETAQTIKKSVEEGKIDGIIDKTIIGDFQKEQKKFVEEQHTKKSEAAVPPWVDTNDEETIQQQILALSADKRNFLRDPPAGVQFNFDFDQMYPVALVMLQEDELLSKMRFALVPKLVKEEVFWRNYFYRVSLIKQSAQLTALAAQQQAAGKEEKSNGREQDLPLAEAVRPKTPPVVIKSQLKTQEDEEEISTSPGVSEFVSDAFDACNLNQEDLRKEMEQLVLDKKQEETAVLEEDSADWEKELQQELQEYEVVTESEKRDENWDKEIEKMLQEEN
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
6Phosphorylation--MFRGLSSWLGLQQ
--CCCCHHHHCCCCC		23.4527251275
7Phosphorylation-MFRGLSSWLGLQQP
-CCCCHHHHCCCCCC		31.2227251275
60PhosphorylationQAKDFGNYLFNFASA
HHHHHHHHHHHHHHH		17.0425394399
66PhosphorylationNYLFNFASAATKKIT
HHHHHHHHHHHHHHH		17.8221712546
70AcetylationNFASAATKKITESVA
HHHHHHHHHHHHHHH		37.1323954790
70UbiquitinationNFASAATKKITESVA
HHHHHHHHHHHHHHH		37.1321890473
70UbiquitinationNFASAATKKITESVA
HHHHHHHHHHHHHHH		37.1321890473
702-HydroxyisobutyrylationNFASAATKKITESVA
HHHHHHHHHHHHHHH		37.13-
71AcetylationFASAATKKITESVAE
HHHHHHHHHHHHHHH		50.9724471243
71UbiquitinationFASAATKKITESVAE
HHHHHHHHHHHHHHH		50.9729967540
73PhosphorylationSAATKKITESVAETA
HHHHHHHHHHHHHHH		30.9622210691
73O-linked_GlycosylationSAATKKITESVAETA
HHHHHHHHHHHHHHH		30.9646299723
75PhosphorylationATKKITESVAETAQT
HHHHHHHHHHHHHHH		20.2724732914
79O-linked_GlycosylationITESVAETAQTIKKS
HHHHHHHHHHHHHHH		17.8355833959
79PhosphorylationITESVAETAQTIKKS
HHHHHHHHHHHHHHH		17.8324732914
82O-linked_GlycosylationSVAETAQTIKKSVEE
HHHHHHHHHHHHHHC		32.0935107131
82PhosphorylationSVAETAQTIKKSVEE
HHHHHHHHHHHHHHC		32.0924732914
84UbiquitinationAETAQTIKKSVEEGK
HHHHHHHHHHHHCCC		42.2421890473
84UbiquitinationAETAQTIKKSVEEGK
HHHHHHHHHHHHCCC		42.2421890473
842-HydroxyisobutyrylationAETAQTIKKSVEEGK
HHHHHHHHHHHHCCC		42.24-
86PhosphorylationTAQTIKKSVEEGKID
HHHHHHHHHHCCCCC		29.7425849741
91UbiquitinationKKSVEEGKIDGIIDK
HHHHHCCCCCEEEEC		40.6929967540
98UbiquitinationKIDGIIDKTIIGDFQ
CCCEEEECHHHHHHH		31.0832015554
982-HydroxyisobutyrylationKIDGIIDKTIIGDFQ
CCCEEEECHHHHHHH		31.08-
99PhosphorylationIDGIIDKTIIGDFQK
CCEEEECHHHHHHHH		17.6828555341
106UbiquitinationTIIGDFQKEQKKFVE
HHHHHHHHHHHHHHH		63.2032015554
110UbiquitinationDFQKEQKKFVEEQHT
HHHHHHHHHHHHHHC		55.1029967540
117PhosphorylationKFVEEQHTKKSEAAV
HHHHHHHCCHHHCCC		39.6020068231
119UbiquitinationVEEQHTKKSEAAVPP
HHHHHCCHHHCCCCC		55.4729967540
147UbiquitinationILALSADKRNFLRDP
HHHHCCCCCCCCCCC		49.2921890473
147AcetylationILALSADKRNFLRDP
HHHHCCCCCCCCCCC		49.2926051181
191MalonylationMRFALVPKLVKEEVF
CCHHHHHHHHHHHHH		59.4426320211
191AcetylationMRFALVPKLVKEEVF
CCHHHHHHHHHHHHH		59.4419608861
191UbiquitinationMRFALVPKLVKEEVF
CCHHHHHHHHHHHHH		59.4422817900
194UbiquitinationALVPKLVKEEVFWRN
HHHHHHHHHHHHHHH		59.6022053931
194UbiquitinationALVPKLVKEEVFWRN
HHHHHHHHHHHHHHH		59.6021890473
194AcetylationALVPKLVKEEVFWRN
HHHHHHHHHHHHHHH		59.6027452117
207PhosphorylationRNYFYRVSLIKQSAQ
HHHHHHHHHHHHHHH		18.5124719451
210UbiquitinationFYRVSLIKQSAQLTA
HHHHHHHHHHHHHHH		43.4223000965
210UbiquitinationFYRVSLIKQSAQLTA
HHHHHHHHHHHHHHH		43.4221890473
227UbiquitinationAQQQAAGKEEKSNGR
HHHHHCCCHHHCCCC		58.9532015554
231PhosphorylationAAGKEEKSNGREQDL
HCCCHHHCCCCCCCC		48.0423403867
248PhosphorylationAEAVRPKTPPVVIKS
HHHCCCCCCCEEEEC		35.1929255136
255PhosphorylationTPPVVIKSQLKTQED
CCCEEEECCCCCCCC		29.6226074081
259PhosphorylationVIKSQLKTQEDEEEI
EEECCCCCCCCHHHH		45.8728122231
267PhosphorylationQEDEEEISTSPGVSE
CCCHHHHCCCCCHHH		26.5530278072
268PhosphorylationEDEEEISTSPGVSEF
CCHHHHCCCCCHHHH		44.6026503892
269PhosphorylationDEEEISTSPGVSEFV
CHHHHCCCCCHHHHH		16.9325159151
273PhosphorylationISTSPGVSEFVSDAF
HCCCCCHHHHHHHHH		31.0930278072
277PhosphorylationPGVSEFVSDAFDACN
CCHHHHHHHHHHHCC		28.6630278072
292UbiquitinationLNQEDLRKEMEQLVL
CCHHHHHHHHHHHHH		69.5729967540
294SulfoxidationQEDLRKEMEQLVLDK
HHHHHHHHHHHHHCH		4.4521406390
3012-HydroxyisobutyrylationMEQLVLDKKQEETAV
HHHHHHCHHHHHHHH		52.79-
301UbiquitinationMEQLVLDKKQEETAV
HHHHHHCHHHHHHHH		52.7929967540
302UbiquitinationEQLVLDKKQEETAVL
HHHHHCHHHHHHHHH		63.7129967540
313PhosphorylationTAVLEEDSADWEKEL
HHHHHCCCCHHHHHH		31.2625159151
327PhosphorylationLQQELQEYEVVTESE
HHHHHHHHHCCCCHH		10.8928674151
331PhosphorylationLQEYEVVTESEKRDE
HHHHHCCCCHHHCCC		38.6828796482
333PhosphorylationEYEVVTESEKRDENW
HHHCCCCHHHCCCHH		38.7728796482
335UbiquitinationEVVTESEKRDENWDK
HCCCCHHHCCCHHHH		74.5532015554
342AcetylationKRDENWDKEIEKMLQ
HCCCHHHHHHHHHHH		52.8126051181
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

Oops, there are no upstream regulatory protein records of SYAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYAP1_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 SYAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN1_HUMANPIN1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYAP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-248 AND SER-269, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248 AND TYR-327, 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 THR-248, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, AND MASSSPECTROMETRY.

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