dbPTM

RBM6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM6_HUMAN
UniProt AC	P78332
Protein Name	RNA-binding protein 6
Gene Name	RBM6
Organism	Homo sapiens (Human).
Sequence Length	1123
Subcellular Localization	Nucleus .
Protein Description	Specifically binds poly(G) RNA homopolymers in vitro..
Protein Sequence	MWGDSRPANRTGPFRGSQEERFAPGWNRDYPPPPLKSHAQERHSGNFPGRDSLPFDFQGHSGPPFANVEEHSFSYGARDGPHGDYRGGEGPGHDFRGGDFSSSDFQSRDSSQLDFRGRDIHSGDFRDREGPPMDYRGGDGTSMDYRGREAPHMNYRDRDAHAVDFRGRDAPPSDFRGRGTYDLDFRGRDGSHADFRGRDLSDLDFRAREQSRSDFRNRDVSDLDFRDKDGTQVDFRGRGSGTTDLDFRDRDTPHSDFRGRHRSRTDQDFRGREMGSCMEFKDREMPPVDPNILDYIQPSTQDREHSGMNVNRREESTHDHTIERPAFGIQKGEFEHSETREGETQGVAFEHESPADFQNSQSPVQDQDKSQLSGREEQSSDAGLFKEEGGLDFLGRQDTDYRSMEYRDVDHRLPGSQMFGYGQSKSFPEGKTARDAQRDLQDQDYRTGPSEEKPSRLIRLSGVPEDATKEEILNAFRTPDGMPVKNLQLKEYNTGYDYGYVCVEFSLLEDAIGCMEANQGTLMIQDKEVTLEYVSSLDFWYCKRCKANIGGHRSSCSFCKNPREVTEAKQELITYPQPQKTSIPAPLEKQPNQPLRPADKEPEPRKREEGQESRLGHQKREAERYLPPSRREGPTFRRDRERESWSGETRQDGESKTIMLKRIYRSTPPEVIVEVLEPYVRLTTANVRIIKNRTGPMGHTYGFIDLDSHAEALRVVKILQNLDPPFSIDGKMVAVNLATGKRRNDSGDHSDHMHYYQGKKYFRDRRGGGRNSDWSSDTNRQGQQSSSDCYIYDSATGYYYDPLAGTYYDPNTQQEVYVPQDPGLPEEEEIKEKKPTSQGKSSSKKEMSKRDGKEKKDRGVTRFQENASEGKAPAEDVFKKPLPPTVKKEESPPPPKVVNPLIGLLGEYGGDSDYEEEEEEEQTPPPQPRTAQPQKREEQTKKENEEDKLTDWNKLACLLCRRQFPNKEVLIKHQQLSDLHKQNLEIHRKIKQSEQELAYLERREREGKFKGRGNDRREKLQSFDSPERKRIKYSRETDSDRKLVDKEDIDTSSKGGCVQQATGWRKGTGLGYGHPGLASSEEAEGRMRGPSVGASGRTSKRQSNETYRDAVRRVMFARYKELD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	DSRPANRTGPFRGSQ CCCCCCCCCCCCCCC	49.35	23186163
15	Methylation	ANRTGPFRGSQEERF CCCCCCCCCCCCCCC	47.16	115386039
17	Phosphorylation	RTGPFRGSQEERFAP CCCCCCCCCCCCCCC	30.11	28555341
36	Methylation	DYPPPPLKSHAQERH CCCCCCCHHHCCHHC	46.07	115976471
36	Sumoylation	DYPPPPLKSHAQERH CCCCCCCHHHCCHHC	46.07	28112733
44	Phosphorylation	SHAQERHSGNFPGRD HHCCHHCCCCCCCCC	41.47	25159151
96	Methylation	EGPGHDFRGGDFSSS CCCCCCCCCCCCCCH	55.00	115490775
101	Phosphorylation	DFRGGDFSSSDFQSR CCCCCCCCCHHHCCC	33.40	28555341
102	Phosphorylation	FRGGDFSSSDFQSRD CCCCCCCCHHHCCCC	33.64	28555341
107	Phosphorylation	FSSSDFQSRDSSQLD CCCHHHCCCCHHHCC	37.74	28555341
110	Phosphorylation	SDFQSRDSSQLDFRG HHHCCCCHHHCCCCC	20.90	28555341
111	Phosphorylation	DFQSRDSSQLDFRGR HHCCCCHHHCCCCCC	38.77	28555341
122	Phosphorylation	FRGRDIHSGDFRDRE CCCCCCCCCCCCCCC	40.15	21712546
141	Phosphorylation	DYRGGDGTSMDYRGR CCCCCCCCCCCCCCC	26.14	-
166	Methylation	DAHAVDFRGRDAPPS CCCCCCCCCCCCCCC	34.47	115490767
176	Methylation	DAPPSDFRGRGTYDL CCCCCCCCCCCEEEC	38.60	115490783
178	Methylation	PPSDFRGRGTYDLDF CCCCCCCCCEEECCC	29.98	82954889
181	Phosphorylation	DFRGRGTYDLDFRGR CCCCCCEEECCCCCC	19.82	27642862
201	Phosphorylation	DFRGRDLSDLDFRAR CCCCCCHHHCHHHHH	40.18	20873877
211	Phosphorylation	DFRAREQSRSDFRNR HHHHHHHHHHHHHCC	29.06	21406692
213	Phosphorylation	RAREQSRSDFRNRDV HHHHHHHHHHHCCCH	46.47	21406692
221	Phosphorylation	DFRNRDVSDLDFRDK HHHCCCHHHCCCCCC	36.42	28555341
238	Methylation	TQVDFRGRGSGTTDL CEEEECCCCCCCCCC	31.67	115490791
240	Phosphorylation	VDFRGRGSGTTDLDF EEECCCCCCCCCCCC	31.44	21815630
242	Phosphorylation	FRGRGSGTTDLDFRD ECCCCCCCCCCCCCC	20.87	25159151
243	Phosphorylation	RGRGSGTTDLDFRDR CCCCCCCCCCCCCCC	37.78	29214152
252	Phosphorylation	LDFRDRDTPHSDFRG CCCCCCCCCCCCCCC	24.64	29255136
255	Phosphorylation	RDRDTPHSDFRGRHR CCCCCCCCCCCCCCC	39.38	29255136
258	Methylation	DTPHSDFRGRHRSRT CCCCCCCCCCCCCCC	46.34	30988985
263	Phosphorylation	DFRGRHRSRTDQDFR CCCCCCCCCCCCCCC	33.15	21406692
265	Phosphorylation	RGRHRSRTDQDFRGR CCCCCCCCCCCCCCC	38.98	21406692
281	Acetylation	MGSCMEFKDREMPPV CCCCCEECCCCCCCC	42.44	26051181
316	Phosphorylation	NVNRREESTHDHTIE CCCCCCHHCCCCCCC	26.70	28555341
321	Phosphorylation	EESTHDHTIERPAFG CHHCCCCCCCCCCCC	30.50	28555341
331	Sumoylation	RPAFGIQKGEFEHSE CCCCCCCCCEECCCC	59.49	28112733
344	Phosphorylation	SETREGETQGVAFEH CCCCCCCEEECEEEC	41.29	23927012
353	Phosphorylation	GVAFEHESPADFQNS ECEEECCCHHHHCCC	27.56	23927012
360	Phosphorylation	SPADFQNSQSPVQDQ CHHHHCCCCCCCCCC	22.66	22167270
362	Phosphorylation	ADFQNSQSPVQDQDK HHHCCCCCCCCCCCH	27.19	29255136
370	Phosphorylation	PVQDQDKSQLSGREE CCCCCCHHHHCCCHH	44.64	30108239
373	Phosphorylation	DQDKSQLSGREEQSS CCCHHHHCCCHHHHC	28.32	30108239
379	Phosphorylation	LSGREEQSSDAGLFK HCCCHHHHCCCCCCC	33.20	30266825
380	Phosphorylation	SGREEQSSDAGLFKE CCCHHHHCCCCCCCC	31.04	30266825
386	Sumoylation	SSDAGLFKEEGGLDF HCCCCCCCCCCCCCC	60.96	-
386	Sumoylation	SSDAGLFKEEGGLDF HCCCCCCCCCCCCCC	60.96	28112733
386	Ubiquitination	SSDAGLFKEEGGLDF HCCCCCCCCCCCCCC	60.96	-
399	Phosphorylation	DFLGRQDTDYRSMEY CCCCCCCCCCCCCCC	26.96	-
401	Phosphorylation	LGRQDTDYRSMEYRD CCCCCCCCCCCCCCC	13.48	28555341
403	Phosphorylation	RQDTDYRSMEYRDVD CCCCCCCCCCCCCCC	15.10	28555341
406	Phosphorylation	TDYRSMEYRDVDHRL CCCCCCCCCCCCCCC	11.94	-
416	Phosphorylation	VDHRLPGSQMFGYGQ CCCCCCCCCCCCCCC	19.28	28555341
447	O-linked_Glycosylation	LQDQDYRTGPSEEKP HHCCCCCCCCCCCCC	47.41	30379171
450	O-linked_Glycosylation	QDYRTGPSEEKPSRL CCCCCCCCCCCCCCE	60.78	30379171
453	Sumoylation	RTGPSEEKPSRLIRL CCCCCCCCCCCEEHH	44.21	-
453	Sumoylation	RTGPSEEKPSRLIRL CCCCCCCCCCCEEHH	44.21	28112733
461	Phosphorylation	PSRLIRLSGVPEDAT CCCEEHHCCCCCCCC	28.09	25159151
468	Phosphorylation	SGVPEDATKEEILNA CCCCCCCCHHHHHHH	51.84	21712546
469	Sumoylation	GVPEDATKEEILNAF CCCCCCCHHHHHHHH	55.88	-
469	Acetylation	GVPEDATKEEILNAF CCCCCCCHHHHHHHH	55.88	26051181
469	Sumoylation	GVPEDATKEEILNAF CCCCCCCHHHHHHHH	55.88	28112733
469	Ubiquitination	GVPEDATKEEILNAF CCCCCCCHHHHHHHH	55.88	-
478	Phosphorylation	EILNAFRTPDGMPVK HHHHHHCCCCCCCCC	21.19	27135362
494	Phosphorylation	LQLKEYNTGYDYGYV CEEEEECCCCCCCCE	35.90	30576142
496	Phosphorylation	LKEYNTGYDYGYVCV EEEECCCCCCCCEEE	12.17	30576142
554	Phosphorylation	ANIGGHRSSCSFCKN CCCCCCCCCCCCCCC	29.98	25159151
555	Phosphorylation	NIGGHRSSCSFCKNP CCCCCCCCCCCCCCH	17.46	26657352
557	Phosphorylation	GGHRSSCSFCKNPRE CCCCCCCCCCCCHHH	35.31	23312004
560	Acetylation	RSSCSFCKNPREVTE CCCCCCCCCHHHHHH	68.89	26051181
569	Sumoylation	PREVTEAKQELITYP HHHHHHHHHHHHCCC	37.77	-
569	Sumoylation	PREVTEAKQELITYP HHHHHHHHHHHHCCC	37.77	28112733
574	Phosphorylation	EAKQELITYPQPQKT HHHHHHHCCCCCCCC	41.60	20049867
575	Phosphorylation	AKQELITYPQPQKTS HHHHHHCCCCCCCCC	7.90	20049867
600	Acetylation	QPLRPADKEPEPRKR CCCCCCCCCCCCCCC	76.81	25953088
644	Phosphorylation	RRDRERESWSGETRQ CCCCCCCCCCCCCCC	32.53	24144214
646	Phosphorylation	DRERESWSGETRQDG CCCCCCCCCCCCCCC	35.71	24144214
649	Phosphorylation	RESWSGETRQDGESK CCCCCCCCCCCCCCC	36.84	24144214
701	Phosphorylation	TGPMGHTYGFIDLDS CCCCCCEEEEECCCH	12.36	20090780
739	Phosphorylation	MVAVNLATGKRRNDS EEEEECCCCCCCCCC	46.53	28555341
741	Sumoylation	AVNLATGKRRNDSGD EEECCCCCCCCCCCC	43.78	-
741	Sumoylation	AVNLATGKRRNDSGD EEECCCCCCCCCCCC	43.78	-
741	Ubiquitination	AVNLATGKRRNDSGD EEECCCCCCCCCCCC	43.78	-
746	Phosphorylation	TGKRRNDSGDHSDHM CCCCCCCCCCCCCCC	50.06	30108239
750	Phosphorylation	RNDSGDHSDHMHYYQ CCCCCCCCCCCHHHC	33.67	21406692
755	Phosphorylation	DHSDHMHYYQGKKYF CCCCCCHHHCCCCCC	7.01	21406692
756	Phosphorylation	HSDHMHYYQGKKYFR CCCCCHHHCCCCCCC	8.98	21406692
836	Phosphorylation	EIKEKKPTSQGKSSS HHHHCCCCCCCCCCC	42.43	-
837	Phosphorylation	IKEKKPTSQGKSSSK HHHCCCCCCCCCCCH	45.52	-
840	Acetylation	KKPTSQGKSSSKKEM CCCCCCCCCCCHHHH	39.26	7429227
840	Ubiquitination	KKPTSQGKSSSKKEM CCCCCCCCCCCHHHH	39.26	-
844	Acetylation	SQGKSSSKKEMSKRD CCCCCCCHHHHHHCC	55.49	7306235
849	Acetylation	SSKKEMSKRDGKEKK CCHHHHHHCCCCCHH	53.88	7822257
871	Sumoylation	QENASEGKAPAEDVF HHCCCCCCCCHHHHC	47.33	-
871	Sumoylation	QENASEGKAPAEDVF HHCCCCCCCCHHHHC	47.33	28112733
879	Sumoylation	APAEDVFKKPLPPTV CCHHHHCCCCCCCCC	54.02	28112733
880	Acetylation	PAEDVFKKPLPPTVK CHHHHCCCCCCCCCC	40.08	26051181
887	Sumoylation	KPLPPTVKKEESPPP CCCCCCCCCCCCCCC	57.87	-
887	Sumoylation	KPLPPTVKKEESPPP CCCCCCCCCCCCCCC	57.87	28112733
891	Phosphorylation	PTVKKEESPPPPKVV CCCCCCCCCCCCCHH	43.74	23401153
908	Phosphorylation	LIGLLGEYGGDSDYE HHHHHHHCCCCCCCH	25.30	30175587
912	Phosphorylation	LGEYGGDSDYEEEEE HHHCCCCCCCHHHHH	45.42	26503892
914	Phosphorylation	EYGGDSDYEEEEEEE HCCCCCCCHHHHHHH	29.23	25159151
923	Phosphorylation	EEEEEEQTPPPQPRT HHHHHHCCCCCCCCC	40.83	26503892
935	Sumoylation	PRTAQPQKREEQTKK CCCCCHHHHHHHHHH	69.34	28112733
948	Sumoylation	KKENEEDKLTDWNKL HHHCHHHHHCHHHHH	57.47	-
948	Acetylation	KKENEEDKLTDWNKL HHHCHHHHHCHHHHH	57.47	26051181
948	Sumoylation	KKENEEDKLTDWNKL HHHCHHHHHCHHHHH	57.47	28112733
954	Acetylation	DKLTDWNKLACLLCR HHHCHHHHHHHHHHH	32.96	26051181
972	Acetylation	PNKEVLIKHQQLSDL CCHHHEEEHHHHHHH	31.06	24887519
977	Phosphorylation	LIKHQQLSDLHKQNL EEEHHHHHHHHHHHH	33.51	20068231
981	Acetylation	QQLSDLHKQNLEIHR HHHHHHHHHHHHHHH	48.45	24887527
991	Sumoylation	LEIHRKIKQSEQELA HHHHHHHHHHHHHHH	51.29	-
991	Sumoylation	LEIHRKIKQSEQELA HHHHHHHHHHHHHHH	51.29	28112733
1019	Sumoylation	RGNDRREKLQSFDSP CCCHHHHHHHHCCCH	50.44	28112733
1019	Ubiquitination	RGNDRREKLQSFDSP CCCHHHHHHHHCCCH	50.44	-
1022	Phosphorylation	DRREKLQSFDSPERK HHHHHHHHCCCHHHH	41.27	23401153
1025	Phosphorylation	EKLQSFDSPERKRIK HHHHHCCCHHHHHCC	27.01	19664994
1039	Phosphorylation	KYSRETDSDRKLVDK CCCCCCCCCCCCCCH	46.89	30387612
1042	Sumoylation	RETDSDRKLVDKEDI CCCCCCCCCCCHHHH	58.83	28112733
1046	Sumoylation	SDRKLVDKEDIDTSS CCCCCCCHHHHCCCC	50.21	-
1046	Sumoylation	SDRKLVDKEDIDTSS CCCCCCCHHHHCCCC	50.21	28112733
1051	Phosphorylation	VDKEDIDTSSKGGCV CCHHHHCCCCCCCCE	34.92	-
1052	Phosphorylation	DKEDIDTSSKGGCVQ CHHHHCCCCCCCCEE	26.72	-
1053	Phosphorylation	KEDIDTSSKGGCVQQ HHHHCCCCCCCCEEH	37.10	-
1054	Acetylation	EDIDTSSKGGCVQQA HHHCCCCCCCCEEHH	60.12	26051181
1062	Phosphorylation	GGCVQQATGWRKGTG CCCEEHHCCCCCCCC	32.70	-
1066	Sumoylation	QQATGWRKGTGLGYG EHHCCCCCCCCCCCC	55.08	-
1066	Sumoylation	QQATGWRKGTGLGYG EHHCCCCCCCCCCCC	55.08	28112733
1068	Phosphorylation	ATGWRKGTGLGYGHP HCCCCCCCCCCCCCC	32.06	24043423
1072	Phosphorylation	RKGTGLGYGHPGLAS CCCCCCCCCCCCCCC	19.80	24043423
1079	Phosphorylation	YGHPGLASSEEAEGR CCCCCCCCCHHHCHH	43.24	24043423
1080	Phosphorylation	GHPGLASSEEAEGRM CCCCCCCCHHHCHHC	33.57	24043423
1091	Phosphorylation	EGRMRGPSVGASGRT CHHCCCCCCCCCCCC	35.69	24043423
1095	Phosphorylation	RGPSVGASGRTSKRQ CCCCCCCCCCCCCCC	23.91	28555341
1103	Phosphorylation	GRTSKRQSNETYRDA CCCCCCCCCHHHHHH	40.44	21857030

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 RBM6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM6_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 RBM6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TAF7_HUMAN	TAF7	physical	21988832
SF3B3_HUMAN	SF3B3	physical	21988832

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 RBM6_HUMAN

Related Literatures of Post-Translational Modification

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-360; SER-362 ANDTYR-914, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-362, AND MASSSPECTROMETRY.	19369195 [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-360; SER-362 ANDSER-1025, AND MASS SPECTROMETRY.	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-362; SER-891; SER-1022AND SER-1025, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-360 AND SER-362, ANDMASS SPECTROMETRY.	17525332 [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-1025, AND MASSSPECTROMETRY.	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-891 AND SER-1025, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"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-923, AND MASSSPECTROMETRY.	15302935 [Abstract]