LS14A_HUMAN - dbPTM
LS14A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LS14A_HUMAN
UniProt AC Q8ND56
Protein Name Protein LSM14 homolog A
Gene Name LSM14A
Organism Homo sapiens (Human).
Sequence Length 463
Subcellular Localization Cytoplasm, P-body . Cytoplasm, Stress granule .
Protein Description Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs..
Protein Sequence MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEVFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSTSSFQSMGSYGPFGRMPTYSQFSPSSLVGQQFGAVGVAGSSLTSFGTETSNSGTLPQSSAVGSAFTQDTRSLKTQLSQGRSSPQLDPLRKSPTMEQAVQTASAHLPAPAAVGRRSPVSTRPLPSASQKAGENQEHRRAEVHKVSRPENEQLRNDNKRQVAPGAPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKLKEDKLEKQEKPVNGEDKGDSGVDTQNSEGNADEEDPLGPNCYYDKTKSFFDNISCDDNRERRPTWAEERRLNAETFGIPLRPNRGRGGYRGRGGLGFRGGRGRGGGRGGTFTAPRGFRGGFRGGRGGREFADFEYRKTTAFGP
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
2Acetylation------MSGGTPYIG
------CCCCCCCCC		46.0220068231
2Phosphorylation------MSGGTPYIG
------CCCCCCCCC		46.0222199227
2 (in isoform 2)Acetylation-46.02-
2 (in isoform 2)Phosphorylation-46.02-
5Phosphorylation---MSGGTPYIGSKI
---CCCCCCCCCCEE		19.2222199227
5 (in isoform 2)Phosphorylation-19.2224719451
7Phosphorylation-MSGGTPYIGSKISL
-CCCCCCCCCCEEEE		20.1122199227
7 (in isoform 2)Phosphorylation-20.11-
10PhosphorylationGGTPYIGSKISLISK
CCCCCCCCEEEEEEE		19.7722199227
11UbiquitinationGTPYIGSKISLISKA
CCCCCCCEEEEEEEC		30.97-
11UbiquitinationGTPYIGSKISLISKA
CCCCCCCEEEEEEEC		30.97-
13PhosphorylationPYIGSKISLISKAEI
CCCCCEEEEEEECEE		24.3224719451
16PhosphorylationGSKISLISKAEIRYE
CCEEEEEEECEEEEC		30.9821601212
17AcetylationSKISLISKAEIRYEG
CEEEEEEECEEEECE		42.9425953088
22PhosphorylationISKAEIRYEGILYTI
EEECEEEECEEEEEE		24.9425884760
27PhosphorylationIRYEGILYTIDTENS
EEECEEEEEEECCCC		10.3425884760
40UbiquitinationNSTVALAKVRSFGTE
CCEEEEEEHHHCCCC		38.7422053931
40 (in isoform 2)Ubiquitination-38.7422053931
40UbiquitinationNSTVALAKVRSFGTE
CCEEEEEEHHHCCCC		38.74-
64PhosphorylationPRDEVFEYIIFRGSD
CHHHHEEEEEEECCC		6.4530835281
67UbiquitinationEVFEYIIFRGSDIKD
HHEEEEEEECCCCCC		5.4032015554
76PhosphorylationGSDIKDLTVCEPPKP
CCCCCCCEEECCCCC		32.9932142685
80UbiquitinationKDLTVCEPPKPQCSL
CCCEEECCCCCCCCC		36.7732015554
85PhosphorylationCEPPKPQCSLPQDPA
ECCCCCCCCCCCCCH		6.4732142685
86O-linked_GlycosylationEPPKPQCSLPQDPAI
CCCCCCCCCCCCCHH		37.5323301498
87PhosphorylationPPKPQCSLPQDPAIV
CCCCCCCCCCCCHHH		6.0933259812
89PhosphorylationKPQCSLPQDPAIVQS
CCCCCCCCCCHHHCC		74.7032142685
96PhosphorylationQDPAIVQSSLGSSTS
CCCHHHCCCCCCCCH		19.3528348404
97PhosphorylationDPAIVQSSLGSSTSS
CCHHHCCCCCCCCHH		21.4728348404
98PhosphorylationPAIVQSSLGSSTSSF
CHHHCCCCCCCCHHC		10.5132142685
100PhosphorylationIVQSSLGSSTSSFQS
HHCCCCCCCCHHCHH		35.4233259812
101PhosphorylationVQSSLGSSTSSFQSM
HCCCCCCCCHHCHHC		30.4328348404
102PhosphorylationQSSLGSSTSSFQSMG
CCCCCCCCHHCHHCC		30.0428348404
103PhosphorylationSSLGSSTSSFQSMGS
CCCCCCCHHCHHCCC		30.9727251275
109PhosphorylationTSSFQSMGSYGPFGR
CHHCHHCCCCCCCCC		23.9832645325
111PhosphorylationSFQSMGSYGPFGRMP
HCHHCCCCCCCCCCC		24.0846162747
119PhosphorylationGPFGRMPTYSQFSPS
CCCCCCCCCCCCCHH		26.85117993
122PhosphorylationGRMPTYSQFSPSSLV
CCCCCCCCCCHHHHH		32.2132645325
124PhosphorylationMPTYSQFSPSSLVGQ
CCCCCCCCHHHHHCC		19.0826074081
126PhosphorylationTYSQFSPSSLVGQQF
CCCCCCHHHHHCCCC		34.8026074081
127PhosphorylationYSQFSPSSLVGQQFG
CCCCCHHHHHCCCCC		30.3826074081
141O-linked_GlycosylationGAVGVAGSSLTSFGT
CCEEECCCCCEECCC		16.6723301498
141 (in isoform 3)Phosphorylation-16.6730153514
142 (in isoform 3)Phosphorylation-34.4530153514
148O-linked_GlycosylationSSLTSFGTETSNSGT
CCCEECCCCCCCCCC		33.7923301498
151PhosphorylationTSFGTETSNSGTLPQ
EECCCCCCCCCCCCC		23.8332142685
151 (in isoform 3)Phosphorylation-23.8330153514
163UbiquitinationLPQSSAVGSAFTQDT
CCCCHHCCCCCCCCH		16.9932015554
172PhosphorylationAFTQDTRSLKTQLSQ
CCCCCHHHHHHHHHC		35.9926074081
174MethylationTQDTRSLKTQLSQGR
CCCHHHHHHHHHCCC		35.16-
174UbiquitinationTQDTRSLKTQLSQGR
CCCHHHHHHHHHCCC		35.1632015554
1742-HydroxyisobutyrylationTQDTRSLKTQLSQGR
CCCHHHHHHHHHCCC		35.16-
174AcetylationTQDTRSLKTQLSQGR
CCCHHHHHHHHHCCC		35.1625953088
175PhosphorylationQDTRSLKTQLSQGRS
CCHHHHHHHHHCCCC		39.7825463755
175 (in isoform 2)Phosphorylation-39.78-
178PhosphorylationRSLKTQLSQGRSSPQ
HHHHHHHHCCCCCCC		22.2920201521
178 (in isoform 2)Phosphorylation-22.2924719451
181PhosphorylationKTQLSQGRSSPQLDP
HHHHHCCCCCCCCCH		26.7332142685
182PhosphorylationTQLSQGRSSPQLDPL
HHHHCCCCCCCCCHH		53.8720201521
182 (in isoform 2)Phosphorylation-53.8724719451
183PhosphorylationQLSQGRSSPQLDPLR
HHHCCCCCCCCCHHH		18.4622167270
183 (in isoform 2)Phosphorylation-18.4624719451
184UbiquitinationLSQGRSSPQLDPLRK
HHCCCCCCCCCHHHC		39.7524816145
187UbiquitinationGRSSPQLDPLRKSPT
CCCCCCCCHHHCCCH		34.6333845483
192PhosphorylationQLDPLRKSPTMEQAV
CCCHHHCCCHHHHHH		21.1129255136
192 (in isoform 2)Phosphorylation-21.1124719451
194PhosphorylationDPLRKSPTMEQAVQT
CHHHCCCHHHHHHHH		40.1929255136
194 (in isoform 2)Phosphorylation-40.1921406692
200UbiquitinationPTMEQAVQTASAHLP
CHHHHHHHHHHHCCC		34.0733845483
201PhosphorylationTMEQAVQTASAHLPA
HHHHHHHHHHHCCCC		18.9123927012
201 (in isoform 2)Phosphorylation-18.9124719451
203PhosphorylationEQAVQTASAHLPAPA
HHHHHHHHHCCCCCC		21.4323927012
203 (in isoform 2)Phosphorylation-21.4324719451
205PhosphorylationAVQTASAHLPAPAAV
HHHHHHHCCCCCCCC		29.8332645325
213UbiquitinationLPAPAAVGRRSPVST
CCCCCCCCCCCCCCC		17.9833845483
216PhosphorylationPAAVGRRSPVSTRPL
CCCCCCCCCCCCCCC		28.4325159151
216 (in isoform 2)Phosphorylation-28.4324719451
219PhosphorylationVGRRSPVSTRPLPSA
CCCCCCCCCCCCCCH		23.2920201521
219 (in isoform 2)Phosphorylation-23.2921406692
220PhosphorylationGRRSPVSTRPLPSAS
CCCCCCCCCCCCCHH		36.2223927012
220 (in isoform 2)Phosphorylation-36.2221406692
225PhosphorylationVSTRPLPSASQKAGE
CCCCCCCCHHHHCCC		48.5123927012
225 (in isoform 2)Phosphorylation-48.5121406692
226UbiquitinationSTRPLPSASQKAGEN
CCCCCCCHHHHCCCC		17.6532015554
227PhosphorylationTRPLPSASQKAGENQ
CCCCCCHHHHCCCCH		36.2317525332
227 (in isoform 2)Phosphorylation-36.23-
232UbiquitinationSASQKAGENQEHRRA
CHHHHCCCCHHHHHH		61.6823000965
235UbiquitinationQKAGENQEHRRAEVH
HHCCCCHHHHHHHHH		51.4423000965
243UbiquitinationHRRAEVHKVSRPENE
HHHHHHHHCCCCHHH		47.2724816145
245PhosphorylationRAEVHKVSRPENEQL
HHHHHHCCCCHHHHH		47.0969010177
245O-linked_GlycosylationRAEVHKVSRPENEQL
HHHHHHCCCCHHHHH		47.0923301498
248UbiquitinationVHKVSRPENEQLRND
HHHCCCCHHHHHCCC		72.7532015554
253UbiquitinationRPENEQLRNDNKRQV
CCHHHHHCCCCCCCC		48.4233845483
266PhosphorylationQVAPGAPSAPRRGRG
CCCCCCCCCCCCCCC		50.8223403867
266UbiquitinationQVAPGAPSAPRRGRG
CCCCCCCCCCCCCCC		50.8232015554
269MethylationPGAPSAPRRGRGGHR
CCCCCCCCCCCCCCC		54.09-
283UbiquitinationRGGRGRFGIRRDGPM
CCCCCCCCCCCCCCC		15.9033845483
291AcetylationIRRDGPMKFEKDFDF
CCCCCCCCEEECCCC		54.2125953088
291SumoylationIRRDGPMKFEKDFDF
CCCCCCCCEEECCCC		54.21-
291 (in isoform 2)Acetylation-54.21-
291SumoylationIRRDGPMKFEKDFDF
CCCCCCCCEEECCCC		54.2119608861
291UbiquitinationIRRDGPMKFEKDFDF
CCCCCCCCEEECCCC		54.2123000965
292UbiquitinationRRDGPMKFEKDFDFE
CCCCCCCEEECCCCH		13.1933845483
294AcetylationDGPMKFEKDFDFESA
CCCCCEEECCCCHHH		67.8218526157
294UbiquitinationDGPMKFEKDFDFESA
CCCCCEEECCCCHHH		67.8223000965
296UbiquitinationPMKFEKDFDFESANA
CCCEEECCCCHHHHH		20.1032015554
300PhosphorylationEKDFDFESANAQFNK
EECCCCHHHHHCCCH		27.1524173317
305UbiquitinationFESANAQFNKEEIDR
CHHHHHCCCHHHHHH		15.2132015554
307AcetylationSANAQFNKEEIDREF
HHHHCCCHHHHHHHH		59.0018526167
307UbiquitinationSANAQFNKEEIDREF
HHHHCCCHHHHHHHH		59.0032015554
317UbiquitinationIDREFHNKLKLKEDK
HHHHHHHHHHCCHHH		38.1329967540
340PhosphorylationNGEDKGDSGVDTQNS
CCCCCCCCCCCCCCC		49.7623401153
344PhosphorylationKGDSGVDTQNSEGNA
CCCCCCCCCCCCCCC		27.5223663014
347PhosphorylationSGVDTQNSEGNADEE
CCCCCCCCCCCCCCC		36.7422617229
362PhosphorylationDPLGPNCYYDKTKSF
CCCCCCCCCCCCHHH		22.727279253
363PhosphorylationPLGPNCYYDKTKSFF
CCCCCCCCCCCHHHH		17.1128796482
365UbiquitinationGPNCYYDKTKSFFDN
CCCCCCCCCHHHHHC		41.5529967540
366PhosphorylationPNCYYDKTKSFFDNI
CCCCCCCCHHHHHCC		29.0846162741
368PhosphorylationCYYDKTKSFFDNISC
CCCCCCHHHHHCCCC		36.0628450419
374PhosphorylationKSFFDNISCDDNRER
HHHHHCCCCCCCCCC		20.1119664994
374 (in isoform 2)Phosphorylation-20.1124719451
384PhosphorylationDNRERRPTWAEERRL
CCCCCCCCHHHHHHH		35.1829083192
384 (in isoform 2)Phosphorylation-35.1824719451
389MethylationRPTWAEERRLNAETF
CCCHHHHHHHCCHHH		39.63-
395 (in isoform 2)Phosphorylation-25.4224719451
395PhosphorylationERRLNAETFGIPLRP
HHHHCCHHHCCCCCC		25.4224719451
401Asymmetric dimethylarginineETFGIPLRPNRGRGG
HHHCCCCCCCCCCCC		22.54-
401MethylationETFGIPLRPNRGRGG
HHHCCCCCCCCCCCC		22.54-
409 (in isoform 2)Phosphorylation-16.8424719451
409PhosphorylationPNRGRGGYRGRGGLG
CCCCCCCCCCCCCCC		16.8424719451
412MethylationGRGGYRGRGGLGFRG
CCCCCCCCCCCCCCC		27.32-
427MethylationGRGRGGGRGGTFTAP
CCCCCCCCCCCCCCC		43.58-
442MethylationRGFRGGFRGGRGGRE
CCCCCCCCCCCCCCC		50.35-
445MethylationRGGFRGGRGGREFAD
CCCCCCCCCCCCCCC		47.41-
455PhosphorylationREFADFEYRKTTAFG
CCCCCCEEEECCCCC		19.8729978859
459PhosphorylationDFEYRKTTAFGP---
CCEEEECCCCCC---		24.0324114839
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 LS14A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LS14A_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 LS14A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LS14A_HUMAN !!
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 LS14A_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-291, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"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-183, AND MASSSPECTROMETRY.
"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-178; SER-182; SER-183;SER-192; THR-194 AND SER-216, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"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 SER-182, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-175; SER-178; SER-183;SER-216 AND SER-227, AND MASS SPECTROMETRY.
"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 SER-178; SER-183; SER-192;THR-201; SER-203; SER-216 AND SER-219, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"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-2; TYR-7 AND SER-216,AND MASS SPECTROMETRY.

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