LC7L3_HUMAN - dbPTM
LC7L3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LC7L3_HUMAN
UniProt AC O95232
Protein Name Luc7-like protein 3
Gene Name LUC7L3
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Nucleus speckle . The subnuclear localization is affected by cisplatin.
Protein Description Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing..
Protein Sequence MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAGPTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIESFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEEPDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHSSRTSDRRCSRSRDHKRSRSRERRRSRSRDRRRSRSHDRSERKHRSRSRDRRRSKSRDRKSYKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTSEDIKSEGDTQSN
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
1Acetylation-------MISAAQLL
-------CCCHHHHH		5.0120068231
3Phosphorylation-----MISAAQLLDE
-----CCCHHHHHHH		19.0925849741
232-HydroxyisobutyrylationRNLAPDEKRSNVRWD
CCCCCCHHHCCCCCC		69.38-
23UbiquitinationRNLAPDEKRSNVRWD
CCCCCCHHHCCCCCC		69.38-
36AcetylationWDHESVCKYYLCGFC
CCHHHHHHHHHCCCC		34.477407415
38PhosphorylationHESVCKYYLCGFCPA
HHHHHHHHHCCCCCH		4.88-
60AcetylationSDLGPCEKIHDENLR
CCCCCCHHHCCHHHH		52.6525953088
67MethylationKIHDENLRKQYEKSS
HHCCHHHHHHHHHCC		35.30-
78AcetylationEKSSRFMKVGYERDF
HHCCCHHHCCHHHHH		29.7819608861
88PhosphorylationYERDFLRYLQSLLAE
HHHHHHHHHHHHHHH		15.9628152594
91PhosphorylationDFLRYLQSLLAEVER
HHHHHHHHHHHHHHH		23.8228152594
110PhosphorylationGHARLALSQNQQSSG
HHHHHHHCCCCCCCC		22.8317525332
115PhosphorylationALSQNQQSSGAAGPT
HHCCCCCCCCCCCCC		22.4521712546
116PhosphorylationLSQNQQSSGAAGPTG
HCCCCCCCCCCCCCC		28.2829507054
122PhosphorylationSSGAAGPTGKNEEKI
CCCCCCCCCCCHHHH		60.9320068231
124UbiquitinationGAAGPTGKNEEKIQV
CCCCCCCCCHHHHHH		64.762190698
124AcetylationGAAGPTGKNEEKIQV
CCCCCCCCCHHHHHH		64.7626051181
124 (in isoform 1)Ubiquitination-64.7621906983
135UbiquitinationKIQVLTDKIDVLLQQ
HHHHHHHHHHHHHHH		35.25-
148PhosphorylationQQIEELGSEGKVEEA
HHHHHHCCCCCHHHH		56.6627732954
160UbiquitinationEEAQGMMKLVEQLKE
HHHHHHHHHHHHHHH		40.25-
166AcetylationMKLVEQLKEERELLR
HHHHHHHHHHHHHHH		58.1719608861
166UbiquitinationMKLVEQLKEERELLR
HHHHHHHHHHHHHHH		58.1719608861
177PhosphorylationELLRSTTSTIESFAA
HHHHHCHHHHHHHHH		27.7228555341
181PhosphorylationSTTSTIESFAAQEKQ
HCHHHHHHHHHHHHH		19.1428555341
2152-HydroxyisobutyrylationVDDHLMGKQHMGYAK
HCHHHCCCCCCCHHH		24.06-
231UbiquitinationKATVEELKEKLRKRT
HHHHHHHHHHHHHHC		56.96-
231AcetylationKATVEELKEKLRKRT
HHHHHHHHHHHHHHC		56.9619608861
238PhosphorylationKEKLRKRTEEPDRDE
HHHHHHHCCCCCHHH		47.9727273156
293PhosphorylationDRERRKRSRSRSRHS
HHHHHHHHHHHHHHH		37.3326074081
295PhosphorylationERRKRSRSRSRHSSR
HHHHHHHHHHHHHHH		35.5426074081
297PhosphorylationRKRSRSRSRHSSRTS
HHHHHHHHHHHHHHH		35.2826074081
300PhosphorylationSRSRSRHSSRTSDRR
HHHHHHHHHHHHCCH		22.0226074081
301PhosphorylationRSRSRHSSRTSDRRC
HHHHHHHHHHHCCHH		33.1926074081
303PhosphorylationRSRHSSRTSDRRCSR
HHHHHHHHHCCHHHH		36.6126074081
304PhosphorylationSRHSSRTSDRRCSRS
HHHHHHHHCCHHHHC		28.1926074081
309PhosphorylationRTSDRRCSRSRDHKR
HHHCCHHHHCHHHHH		31.3226074081
311PhosphorylationSDRRCSRSRDHKRSR
HCCHHHHCHHHHHHH		26.2626074081
317PhosphorylationRSRDHKRSRSRERRR
HCHHHHHHHHHHHHH		39.1420068231
319PhosphorylationRDHKRSRSRERRRSR
HHHHHHHHHHHHHHH		39.4820068231
325PhosphorylationRSRERRRSRSRDRRR
HHHHHHHHHHHHHHH		32.5620068231
327PhosphorylationRERRRSRSRDRRRSR
HHHHHHHHHHHHHHH		39.5220068231
333PhosphorylationRSRDRRRSRSHDRSE
HHHHHHHHHHHCHHH		36.0030576142
335PhosphorylationRDRRRSRSHDRSERK
HHHHHHHHHCHHHHH		30.8730576142
339PhosphorylationRSRSHDRSERKHRSR
HHHHHCHHHHHHHHH		48.0520068231
345PhosphorylationRSERKHRSRSRDRRR
HHHHHHHHHHHHHHH		34.0420068231
347PhosphorylationERKHRSRSRDRRRSK
HHHHHHHHHHHHHHH		39.5220068231
365PhosphorylationRKSYKHRSKSRDREQ
HHHHHHHHHHHHHHH		34.4026074081
367PhosphorylationSYKHRSKSRDREQDR
HHHHHHHHHHHHHHH		40.4326074081
376PhosphorylationDREQDRKSKEKEKRG
HHHHHHHHHHHHHCC		47.11-
389PhosphorylationRGSDDKKSSVKSGSR
CCCCCHHHHHHHCCC		46.21-
390PhosphorylationGSDDKKSSVKSGSRE
CCCCHHHHHHHCCCH		42.30-
393PhosphorylationDKKSSVKSGSREKQS
CHHHHHHHCCCHHCC		39.5828985074
395PhosphorylationKSSVKSGSREKQSED
HHHHHHCCCHHCCCC		44.3426074081
400PhosphorylationSGSREKQSEDTNTES
HCCCHHCCCCCCCCC		48.8128985074
403PhosphorylationREKQSEDTNTESKES
CHHCCCCCCCCCCHH		39.7323312004
405PhosphorylationKQSEDTNTESKESDT
HCCCCCCCCCCHHCC		43.6728985074
407PhosphorylationSEDTNTESKESDTKN
CCCCCCCCCHHCCCC		39.4223312004
410PhosphorylationTNTESKESDTKNEVN
CCCCCCHHCCCCCCC		55.0823927012
412PhosphorylationTESKESDTKNEVNGT
CCCCHHCCCCCCCCC		45.0823927012
413AcetylationESKESDTKNEVNGTS
CCCHHCCCCCCCCCH		56.9826051181
419PhosphorylationTKNEVNGTSEDIKSE
CCCCCCCCHHHHHHC		24.6022167270
420PhosphorylationKNEVNGTSEDIKSEG
CCCCCCCHHHHHHCC		34.3722167270
424AcetylationNGTSEDIKSEGDTQS
CCCHHHHHHCCCCCC		55.5726051181
424SumoylationNGTSEDIKSEGDTQS
CCCHHHHHHCCCCCC		55.5725114211
425PhosphorylationGTSEDIKSEGDTQSN
CCHHHHHHCCCCCCC		47.3329255136
429PhosphorylationDIKSEGDTQSN----
HHHHCCCCCCC----		44.7629255136
431PhosphorylationKSEGDTQSN------
HHCCCCCCC------		46.7522167270
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 LC7L3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LC7L3_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 LC7L3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LC7L3_HUMANLUC7L3physical
12565863
SRSF1_HUMANSRSF1physical
12565863
SRSF7_HUMANSRSF7physical
22939629
SNUT1_HUMANSART1physical
22939629
SMU1_HUMANSMU1physical
22939629
NXF1_HUMANNXF1physical
22939629
VTNC_HUMANVTNphysical
22939629
TR112_HUMANTRMT112physical
22939629
NFIA_HUMANNFIAphysical
22939629
RCC1_HUMANRCC1physical
22939629
S10A9_HUMANS100A9physical
22939629
SMD2_HUMANSNRPD2physical
26344197
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 LC7L3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-115; SER-425 AND SER-431, AND MASSSPECTROMETRY.
"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-78; LYS-166 AND LYS-231, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-431, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-115; SER-425 AND SER-431, 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-425 AND SER-431, ANDMASS SPECTROMETRY.
"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 SER-110; SER-425 ANDTHR-429, AND MASS 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-333 AND SER-335, ANDMASS SPECTROMETRY.

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