dbPTM

LAR4B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LAR4B_HUMAN
UniProt AC	Q92615
Protein Name	La-related protein 4B
Gene Name	LARP4B
Organism	Homo sapiens (Human).
Sequence Length	738
Subcellular Localization	Cytoplasm, cytosol . Localized in cytoplasmic mRNP granules containing untranslated mRNAs in response to arsenite treatment.
Protein Description	Stimulates mRNA translation..
Protein Sequence	MTSDQDAKVVAEPQTQRVQEGKDSAHLMNGPISQTTSQTSSIPPLSQVPATKVSELNPNAEVWGAPVLHLEASSAADGVSAAWEEVAGHHADRGPQGSDANGDGDQGHENAALPDPQESDPADMNALALGPSEYDSLPENSETGGNESQPDSQEDPREVLKKTLEFCLSRENLASDMYLISQMDSDQYVPITTVANLDHIKKLSTDVDLIVEVLRSLPLVQVDEKGEKVRPNQNRCIVILREISESTPVEEVEALFKGDNLPKFINCEFAYNDNWFITFETEADAQQAYKYLREEVKTFQGKPIKARIKAKAIAINTFLPKNGFRPLDVSLYAQQRYATSFYFPPMYSPQQQFPLYSLITPQTWSATHSYLDPPLVTPFPNTGFINGFTSPAFKPAASPLTSLRQYPPRSRNPSKSHLRHAIPSAERGPGLLESPSIFNFTADRLINGVRSPQTRQAGQTRTRIQNPSAYAKREAGPGRVEPGSLESSPGLGRGRKNSFGYRKKREEKFTSSQTQSPTPPKPPSPSFELGLSSFPPLPGAAGNLKTEDLFENRLSSLIIGPSKERTLSADASVNTLPVVVSREPSVPASCAVSATYERSPSPAHLPDDPKVAEKQRETHSVDRLPSALTATACKSVQVNGAATELRKPSYAEICQRTSKEPPSSPLQPQKEQKPNTVGCGKEEKKLAEPAERYREPPALKSTPGAPRDQRRPAGGRPSPSAMGKRLSREQSTPPKSPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTSDQDAK -------CCCHHHCC	7.95	22814378
2	Phosphorylation	------MTSDQDAKV ------CCCHHHCCE	40.80	23312004
3	Phosphorylation	-----MTSDQDAKVV -----CCCHHHCCEE	31.79	23312004
15	Phosphorylation	KVVAEPQTQRVQEGK CEEECCCCHHHHCCC	29.11	23312004
134	Phosphorylation	LALGPSEYDSLPENS HHCCHHHHHCCCCCC	18.37	-
135	Ubiquitination	ALGPSEYDSLPENSE HCCHHHHHCCCCCCC	39.38	21890473
136	Phosphorylation	LGPSEYDSLPENSET CCHHHHHCCCCCCCC	44.94	-
145	Ubiquitination	PENSETGGNESQPDS CCCCCCCCCCCCCCC	42.00	21890473
154	Ubiquitination	ESQPDSQEDPREVLK CCCCCCCCCHHHHHH	74.14	21890473
162	Ubiquitination	DPREVLKKTLEFCLS CHHHHHHHHHHHHHC	54.93	-
164	Ubiquitination	REVLKKTLEFCLSRE HHHHHHHHHHHHCCC	6.97	21890473
167	Glutathionylation	LKKTLEFCLSRENLA HHHHHHHHHCCCCCC	2.17	22555962
169	Phosphorylation	KTLEFCLSRENLASD HHHHHHHCCCCCCCC	38.44	27499020
188	Phosphorylation	SQMDSDQYVPITTVA ECCCCCCCCCEEEEE	17.12	27642862
188	Ubiquitination	SQMDSDQYVPITTVA ECCCCCCCCCEEEEE	17.12	21890473
198	Ubiquitination	ITTVANLDHIKKLST EEEEECHHHHHHHCC	41.07	21890473
201	Ubiquitination	VANLDHIKKLSTDVD EECHHHHHHHCCCHH	44.22	21906983
202	Ubiquitination	ANLDHIKKLSTDVDL ECHHHHHHHCCCHHH	47.25	-
225	Ubiquitination	PLVQVDEKGEKVRPN CCEEECCCCCCCCCC	68.83	33845483
228	Ubiquitination	QVDEKGEKVRPNQNR EECCCCCCCCCCCCE	52.81	29967540
236	Glutathionylation	VRPNQNRCIVILREI CCCCCCEEEEEEEEH	3.70	22555962
244	Phosphorylation	IVILREISESTPVEE EEEEEEHHCCCCHHH	22.27	28464451
246	Phosphorylation	ILREISESTPVEEVE EEEEHHCCCCHHHHH	31.08	30087585
247	Phosphorylation	LREISESTPVEEVEA EEEHHCCCCHHHHHH	27.57	20873877
257	Ubiquitination	EEVEALFKGDNLPKF HHHHHHHCCCCCCCE	67.23	21906983
296	Ubiquitination	YKYLREEVKTFQGKP HHHHHHHHHHHCCCC	6.40	27667366
297	Ubiquitination	KYLREEVKTFQGKPI HHHHHHHHHHCCCCC	47.07	29967540
302	Ubiquitination	EVKTFQGKPIKARIK HHHHHCCCCCCHHHH	32.55	29967540
305	Ubiquitination	TFQGKPIKARIKAKA HHCCCCCCHHHHHEE	39.89	29967540
311	Ubiquitination	IKARIKAKAIAINTF CCHHHHHEEEEEECC	35.01	21890473
311	Ubiquitination	IKARIKAKAIAINTF CCHHHHHEEEEEECC	35.01	21906983
315	Ubiquitination	IKAKAIAINTFLPKN HHHEEEEEECCCCCC	4.00	27667366
320	Ubiquitination	IAINTFLPKNGFRPL EEEECCCCCCCCCCC	24.71	27667366
321	Ubiquitination	AINTFLPKNGFRPLD EEECCCCCCCCCCCC	72.37	21890473
321	Ubiquitination	AINTFLPKNGFRPLD EEECCCCCCCCCCCC	72.37	27667366
330	Phosphorylation	GFRPLDVSLYAQQRY CCCCCCCHHHCCHHH	18.48	29978859
332	Phosphorylation	RPLDVSLYAQQRYAT CCCCCHHHCCHHHCC	8.54	29978859
339	Ubiquitination	YAQQRYATSFYFPPM HCCHHHCCCCCCCCC	15.50	27667366
349	Ubiquitination	YFPPMYSPQQQFPLY CCCCCCCCCCCCCEE	20.64	27667366
373	Ubiquitination	ATHSYLDPPLVTPFP CCCCCCCCCCCCCCC	22.87	27667366
389	Phosphorylation	TGFINGFTSPAFKPA CCCCCCCCCCCCCCC	34.89	20068231
390	Phosphorylation	GFINGFTSPAFKPAA CCCCCCCCCCCCCCC	16.39	26074081
398	Phosphorylation	PAFKPAASPLTSLRQ CCCCCCCCCCCCHHH	23.65	29255136
401	Phosphorylation	KPAASPLTSLRQYPP CCCCCCCCCHHHCCC	29.15	20068231
402	Phosphorylation	PAASPLTSLRQYPPR CCCCCCCCHHHCCCC	29.27	29978859
404	Methylation	ASPLTSLRQYPPRSR CCCCCCHHHCCCCCC	33.48	24129315
414	Phosphorylation	PPRSRNPSKSHLRHA CCCCCCCCHHHHHHH	50.79	24719451
415	Ubiquitination	PRSRNPSKSHLRHAI CCCCCCCHHHHHHHC	43.05	-
419	Dimethylation	NPSKSHLRHAIPSAE CCCHHHHHHHCCCCC	16.27	-
419	Methylation	NPSKSHLRHAIPSAE CCCHHHHHHHCCCCC	16.27	24129315
424	Phosphorylation	HLRHAIPSAERGPGL HHHHHCCCCCCCCCC	36.33	22617229
427	Methylation	HAIPSAERGPGLLES HHCCCCCCCCCCCCC	57.21	115481823
434	Phosphorylation	RGPGLLESPSIFNFT CCCCCCCCCCCEEEC	24.74	29255136
436	Phosphorylation	PGLLESPSIFNFTAD CCCCCCCCCEEECHH	49.44	29255136
441	Phosphorylation	SPSIFNFTADRLING CCCCEEECHHHHHCC	28.84	29255136
444	Methylation	IFNFTADRLINGVRS CEEECHHHHHCCCCC	34.70	80702951
451	Phosphorylation	RLINGVRSPQTRQAG HHHCCCCCCCCCCCC	20.96	25159151
454	Phosphorylation	NGVRSPQTRQAGQTR CCCCCCCCCCCCCCC	28.29	23403867
463	Methylation	QAGQTRTRIQNPSAY CCCCCCCCCCCHHHH	25.79	115481839
468	Phosphorylation	RTRIQNPSAYAKREA CCCCCCHHHHHCCCC	41.27	28555341
470	Phosphorylation	RIQNPSAYAKREAGP CCCCHHHHHCCCCCC	19.59	25839225
472	Methylation	QNPSAYAKREAGPGR CCHHHHHCCCCCCCC	37.79	115972353
472	Ubiquitination	QNPSAYAKREAGPGR CCHHHHHCCCCCCCC	37.79	27667366
484	Phosphorylation	PGRVEPGSLESSPGL CCCCCCCCCCCCCCC	39.41	22777824
487	Phosphorylation	VEPGSLESSPGLGRG CCCCCCCCCCCCCCC	47.31	22777824
488	Phosphorylation	EPGSLESSPGLGRGR CCCCCCCCCCCCCCC	17.38	21815630
493	Dimethylation	ESSPGLGRGRKNSFG CCCCCCCCCCCCCCC	46.95	-
493	Methylation	ESSPGLGRGRKNSFG CCCCCCCCCCCCCCC	46.95	16188947
495	Methylation	SPGLGRGRKNSFGYR CCCCCCCCCCCCCCC	33.35	30987767
496	Ubiquitination	PGLGRGRKNSFGYRK CCCCCCCCCCCCCCH	60.82	27667366
498	Phosphorylation	LGRGRKNSFGYRKKR CCCCCCCCCCCCHHC	24.08	22167270
501	Phosphorylation	GRKNSFGYRKKREEK CCCCCCCCCHHCHHH	19.76	28152594
510	Phosphorylation	KKREEKFTSSQTQSP HHCHHHCCCCCCCCC	38.24	30278072
511	Phosphorylation	KREEKFTSSQTQSPT HCHHHCCCCCCCCCC	24.47	30278072
512	Phosphorylation	REEKFTSSQTQSPTP CHHHCCCCCCCCCCC	33.90	30278072
514	Phosphorylation	EKFTSSQTQSPTPPK HHCCCCCCCCCCCCC	32.72	30278072
516	Phosphorylation	FTSSQTQSPTPPKPP CCCCCCCCCCCCCCC	33.84	30278072
518	Phosphorylation	SSQTQSPTPPKPPSP CCCCCCCCCCCCCCC	58.43	25159151
524	Phosphorylation	PTPPKPPSPSFELGL CCCCCCCCCCEECCC	41.52	25159151
526	Phosphorylation	PPKPPSPSFELGLSS CCCCCCCCEECCCCC	35.37	30278072
532	Phosphorylation	PSFELGLSSFPPLPG CCEECCCCCCCCCCC	28.30	30278072
533	Phosphorylation	SFELGLSSFPPLPGA CEECCCCCCCCCCCC	46.98	24888630
546	Phosphorylation	GAAGNLKTEDLFENR CCCCCCCHHHHHHHC	37.59	28122231
553	Methylation	TEDLFENRLSSLIIG HHHHHHHCCHHCEEC	28.84	115481831
555	Phosphorylation	DLFENRLSSLIIGPS HHHHHCCHHCEECCC	21.62	20068231
556	Phosphorylation	LFENRLSSLIIGPSK HHHHCCHHCEECCCC	28.34	23401153
562	Phosphorylation	SSLIIGPSKERTLSA HHCEECCCCCCEECC	41.77	20068231
563	Ubiquitination	SLIIGPSKERTLSAD HCEECCCCCCEECCC	55.11	33845483
566	Phosphorylation	IGPSKERTLSADASV ECCCCCCEECCCCCC	26.59	29255136
568	Phosphorylation	PSKERTLSADASVNT CCCCCEECCCCCCCC	24.40	29255136
572	Phosphorylation	RTLSADASVNTLPVV CEECCCCCCCCCCEE	19.22	28102081
575	Phosphorylation	SADASVNTLPVVVSR CCCCCCCCCCEEEEC	30.22	30576142
581	O-linked_Glycosylation	NTLPVVVSREPSVPA CCCCEEEECCCCCCC	21.22	30059200
581	Phosphorylation	NTLPVVVSREPSVPA CCCCEEEECCCCCCC	21.22	30576142
585	Phosphorylation	VVVSREPSVPASCAV EEEECCCCCCCCEEE	35.66	27696853
589	O-linked_Glycosylation	REPSVPASCAVSATY CCCCCCCCEEEEEEE	9.13	30059200
589	Phosphorylation	REPSVPASCAVSATY CCCCCCCCEEEEEEE	9.13	27696853
593	O-linked_Glycosylation	VPASCAVSATYERSP CCCCEEEEEEEECCC	9.07	30059200
593	Phosphorylation	VPASCAVSATYERSP CCCCEEEEEEEECCC	9.07	25159151
595	Phosphorylation	ASCAVSATYERSPSP CCEEEEEEEECCCCC	20.57	25159151
596	Phosphorylation	SCAVSATYERSPSPA CEEEEEEEECCCCCC	14.73	27696853
599	Phosphorylation	VSATYERSPSPAHLP EEEEEECCCCCCCCC	20.14	29255136
601	Phosphorylation	ATYERSPSPAHLPDD EEEECCCCCCCCCCC	35.65	29255136
618	Phosphorylation	VAEKQRETHSVDRLP HHHHHHHHCCCCCCC	22.95	30108239
620	Phosphorylation	EKQRETHSVDRLPSA HHHHHHCCCCCCCHH	32.88	25849741
623	Methylation	RETHSVDRLPSALTA HHHCCCCCCCHHHHH	46.47	115481815
626	Phosphorylation	HSVDRLPSALTATAC CCCCCCCHHHHHHHC	40.27	30108239
629	Phosphorylation	DRLPSALTATACKSV CCCCHHHHHHHCCEE	22.98	23312004
631	Phosphorylation	LPSALTATACKSVQV CCHHHHHHHCCEEEE	27.61	30387612
635	Phosphorylation	LTATACKSVQVNGAA HHHHHCCEEEECCCH	20.05	16674116
643	Phosphorylation	VQVNGAATELRKPSY EEECCCHHCCCCCCH	34.71	20068231
647	Ubiquitination	GAATELRKPSYAEIC CCHHCCCCCCHHHHH	51.44	29967540
649	Phosphorylation	ATELRKPSYAEICQR HHCCCCCCHHHHHHH	39.76	26657352
650	Phosphorylation	TELRKPSYAEICQRT HCCCCCCHHHHHHHC	19.44	28796482
654	Glutathionylation	KPSYAEICQRTSKEP CCCHHHHHHHCCCCC	1.36	22555962
657	Phosphorylation	YAEICQRTSKEPPSS HHHHHHHCCCCCCCC	20.48	23403867
658	Phosphorylation	AEICQRTSKEPPSSP HHHHHHCCCCCCCCC	36.89	23403867
663	Phosphorylation	RTSKEPPSSPLQPQK HCCCCCCCCCCCCCC	56.13	29255136
664	Phosphorylation	TSKEPPSSPLQPQKE CCCCCCCCCCCCCCC	35.09	29255136
676	Phosphorylation	QKEQKPNTVGCGKEE CCCCCCCCCCCCHHH	27.14	19690332
693	Phosphorylation	LAEPAERYREPPALK HHCHHHHHCCCCHHH	15.72	25159151
701	Phosphorylation	REPPALKSTPGAPRD CCCCHHHCCCCCCCC	40.46	29396449
702	Phosphorylation	EPPALKSTPGAPRDQ CCCHHHCCCCCCCCC	24.93	28985074
718	Phosphorylation	RPAGGRPSPSAMGKR CCCCCCCCHHHHHHH	30.08	29255136
720	Phosphorylation	AGGRPSPSAMGKRLS CCCCCCHHHHHHHHH	34.91	30266825
724	Acetylation	PSPSAMGKRLSREQS CCHHHHHHHHHCCCC	36.76	19608861
727	Phosphorylation	SAMGKRLSREQSTPP HHHHHHHHCCCCCCC	37.49	21712546
731	Phosphorylation	KRLSREQSTPPKSPQ HHHHCCCCCCCCCCC	37.82	23401153
732	Phosphorylation	RLSREQSTPPKSPQ- HHHCCCCCCCCCCC-	43.22	25159151
736	Phosphorylation	EQSTPPKSPQ----- CCCCCCCCCC-----	34.02	29255136
753	Phosphorylation	---------------------- ----------------------		32142685
767	Phosphorylation	------------------------------------ ------------------------------------		33259812
811	Ubiquitination	-------------------------------------------------------------------------------- --------------------------------------------------------------------------------		21890473
821	Ubiquitination	------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------		21890473
972	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27667366
996	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27667366

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 LAR4B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LAR4B_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 LAR4B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of LAR4B_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 LAR4B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-724, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-424; THR-518 ANDSER-524, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-663; SER-664; SER-727;THR-732 AND SER-736, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-424 AND SER-434;SER-451; SER-516; SER-524; SER-727; THR-732 AND SER-736, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-601, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-568, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"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-601, AND MASSSPECTROMETRY.	18187866 [Abstract]
"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-434, AND MASSSPECTROMETRY.	17924679 [Abstract]
"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 SER-434 AND THR-566, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"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-601 AND SER-718, ANDMASS SPECTROMETRY.	17081983 [Abstract]