dbPTM

RRBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRBP1_HUMAN
UniProt AC	Q9P2E9
Protein Name	Ribosome-binding protein 1
Gene Name	RRBP1
Organism	Homo sapiens (Human).
Sequence Length	1410
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type III membrane protein.
Protein Description	Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane..
Protein Sequence	MDIYDTQTLGVVVFGGFMVVSAIGIFLVSTFSMKETSYEEALANQRKEMAKTHHQKVEKKKKEKTVEKKGKTKKKEEKPNGKIPDHDPAPNVTVLLREPVRAPAVAVAPTPVQPPIIVAPVATVPAMPQEKLASSPKDKKKKEKKVAKVEPAVSSVVNSIQVLTSKAAILETAPKEVPMVVVPPVGAKGNTPATGTTQGKKAEGTQNQSKKAEGAPNQGRKAEGTPNQGKKTEGTPNQGKKAEGTPNQGKKAEGTPNQGKKAEGAQNQGKKVDTTPNQGKKVEGAPTQGRKAEGAQNQAKKVEGAQNQGKKAEGAQNQGKKGEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKVEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKVEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGQKGEGAQNQGKKTEGAQGKKAERSPNQGKKGEGAPIQGKKADSVANQGTKVEGITNQGKKAEGSPSEGKKAEGSPNQGKKADAAANQGKKTESASVQGRNTDVAQSPEAPKQEAPAKKKSGSKKKGEPGPPDADGPLYLPYKTLVSTVGSMVFNEGEAQRLIEILSEKAGIIQDTWHKATQKGDPVAILKRQLEEKEKLLATEQEDAAVAKSKLRELNKEMAAEKAKAAAGEAKVKKQLVAREQEITAVQARMQASYREHVKEVQQLQGKIRTLQEQLENGPNTQLARLQQENSILRDALNQATSQVESKQNAELAKLRQELSKVSKELVEKSEAVRQDEQQRKALEAKAAAFEKQVLQLQASHRESEEALQKRLDEVSRELCHTQSSHASLRADAEKAQEQQQQMAELHSKLQSSEAEVRSKCEELSGLHGQLQEARAENSQLTERIRSIEALLEAGQARDAQDVQASQAEADQQQTRLKELESQVSGLEKEAIELREAVEQQKVKNNDLREKNWKAMEALATAEQACKEKLLSLTQAKEESEKQLCLIEAQTMEALLALLPELSVLAQQNYTEWLQDLKEKGPTLLKHPPAPAEPSSDLASKLREAEETQSTLQAECDQYRSILAETEGMLRDLQKSVEEEEQVWRAKVGAAEEELQKSRVTVKHLEEIVEKLKGELESSDQVREHTSHLEAELEKHMAAASAECQNYAKEVAGLRQLLLESQSQLDAAKSEAQKQSDELALVRQQLSEMKSHVEDGDIAGAPASSPEAPPAEQDPVQLKTQLEWTEAILEDEQTQRQKLTAEFEEAQTSACRLQEELEKLRTAGPLESSETEEASQLKERLEKEKKLTSDLGRAATRLQELLKTTQEQLAREKDTVKKLQEQLEKAEDGSSSKEGTSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MDIYDTQTLGV ----CCCCCCCCCEE	25.85	24043423
6	Phosphorylation	--MDIYDTQTLGVVV --CCCCCCCCCEEEE	13.39	24043423
8	Phosphorylation	MDIYDTQTLGVVVFG CCCCCCCCCEEEEEC	27.80	24043423
21	Phosphorylation	FGGFMVVSAIGIFLV ECCCHHHHHHHHHHH	11.62	22210691
29	Phosphorylation	AIGIFLVSTFSMKET HHHHHHHHCCCCCCC	26.36	22210691
30	Phosphorylation	IGIFLVSTFSMKETS HHHHHHHCCCCCCCC	16.55	24043423
32	Phosphorylation	IFLVSTFSMKETSYE HHHHHCCCCCCCCHH	29.09	24719451
36	Phosphorylation	STFSMKETSYEEALA HCCCCCCCCHHHHHH	30.96	28796482
37	Phosphorylation	TFSMKETSYEEALAN CCCCCCCCHHHHHHH	31.47	28796482
38	Phosphorylation	FSMKETSYEEALANQ CCCCCCCHHHHHHHH	25.80	28796482
47	Ubiquitination	EALANQRKEMAKTHH HHHHHHHHHHHHHHH	41.92	29967540
51	2-Hydroxyisobutyrylation	NQRKEMAKTHHQKVE HHHHHHHHHHHHHHH	47.26	-
51	Methylation	NQRKEMAKTHHQKVE HHHHHHHHHHHHHHH	47.26	-
56	2-Hydroxyisobutyrylation	MAKTHHQKVEKKKKE HHHHHHHHHHHHHHH	48.26	-
82	Ubiquitination	KEEKPNGKIPDHDPA CCCCCCCCCCCCCCC	58.67	33845483
110	Phosphorylation	PAVAVAPTPVQPPII CEEEECCCCCCCCEE	26.76	27050516
123	Phosphorylation	IIVAPVATVPAMPQE EEEEECCCCCCCCHH	27.53	26074081
131	Ubiquitination	VPAMPQEKLASSPKD CCCCCHHHHCCCCCH	44.07	22817900
131 (in isoform 1)	Ubiquitination	-	44.07	21906983
131 (in isoform 3)	Ubiquitination	-	44.07	21906983
134	Phosphorylation	MPQEKLASSPKDKKK CCHHHHCCCCCHHHH	58.57	26657352
135	Phosphorylation	PQEKLASSPKDKKKK CHHHHCCCCCHHHHH	30.29	28176443
148	Acetylation	KKEKKVAKVEPAVSS HHHHHHHCCHHHHHH	50.55	11791573
148	Sumoylation	KKEKKVAKVEPAVSS HHHHHHHCCHHHHHH	50.55	28112733
154	Phosphorylation	AKVEPAVSSVVNSIQ HCCHHHHHHHHHHHH	21.37	29255136
155	Phosphorylation	KVEPAVSSVVNSIQV CCHHHHHHHHHHHHH	24.40	26657352
159	Phosphorylation	AVSSVVNSIQVLTSK HHHHHHHHHHHHHCC	11.64	29255136
164	Phosphorylation	VNSIQVLTSKAAILE HHHHHHHHCCHHHHH	29.35	28348404
165	Phosphorylation	NSIQVLTSKAAILET HHHHHHHCCHHHHHC	19.01	28348404
166	Acetylation	SIQVLTSKAAILETA HHHHHHCCHHHHHCC	36.28	11791195
166	Ubiquitination	SIQVLTSKAAILETA HHHHHHCCHHHHHCC	36.28	16196087
166 (in isoform 2)	Ubiquitination	-	36.28	-
175	Acetylation	AILETAPKEVPMVVV HHHHCCCCCCCEEEE	69.73	11791583
175	Ubiquitination	AILETAPKEVPMVVV HHHHCCCCCCCEEEE	69.73	-
185	Phosphorylation	PMVVVPPVGAKGNTP CEEEECCCCCCCCCC	10.75	19664994
185 (in isoform 3)	Phosphorylation	-	10.75	15302935
190	Sumoylation	PPVGAKGNTPATGTT CCCCCCCCCCCCCCC	42.03	-
191	Phosphorylation	PVGAKGNTPATGTTQ CCCCCCCCCCCCCCC	23.99	25849741
194	Phosphorylation	AKGNTPATGTTQGKK CCCCCCCCCCCCCCC	35.94	29255136
196	Phosphorylation	GNTPATGTTQGKKAE CCCCCCCCCCCCCCC	16.16	29255136
197	Phosphorylation	NTPATGTTQGKKAEG CCCCCCCCCCCCCCC	36.35	29255136
205	Phosphorylation	QGKKAEGTQNQSKKA CCCCCCCCCCCCCCC	18.82	29255136
209	Phosphorylation	AEGTQNQSKKAEGAP CCCCCCCCCCCCCCC	43.61	29255136
225	Phosphorylation	QGRKAEGTPNQGKKT CCCCCCCCCCCCCCC	15.57	27461979
226	Phosphorylation	GRKAEGTPNQGKKTE CCCCCCCCCCCCCCC	41.84	27251275
230	Ubiquitination	EGTPNQGKKTEGTPN CCCCCCCCCCCCCCC	46.92	33845483
232	Phosphorylation	TPNQGKKTEGTPNQG CCCCCCCCCCCCCCC	43.03	26699800
235	Phosphorylation	QGKKTEGTPNQGKKA CCCCCCCCCCCCCCC	16.91	25849741
245	Phosphorylation	QGKKAEGTPNQGKKA CCCCCCCCCCCCCCC	15.57	27461979
251	Phosphorylation	GTPNQGKKAEGTPNQ CCCCCCCCCCCCCCC	59.50	27251275
255	Phosphorylation	QGKKAEGTPNQGKKA CCCCCCCCCCCCHHC	15.57	21601212
256	Phosphorylation	GKKAEGTPNQGKKAE CCCCCCCCCCCHHCC	41.84	-
258	Ubiquitination	KAEGTPNQGKKAEGA CCCCCCCCCHHCCCC	67.30	33845483
266	Methylation	GKKAEGAQNQGKKVD CHHCCCCCCCCCCCC	54.35	-
266	Ubiquitination	GKKAEGAQNQGKKVD CHHCCCCCCCCCCCC	54.35	33845483
274	Phosphorylation	NQGKKVDTTPNQGKK CCCCCCCCCCCCCCC	47.33	30266825
275	Phosphorylation	QGKKVDTTPNQGKKV CCCCCCCCCCCCCCC	18.77	30266825
278	Phosphorylation	KVDTTPNQGKKVEGA CCCCCCCCCCCCCCC	67.30	-
287	Ubiquitination	KKVEGAPTQGRKAEG CCCCCCCCCCCCCCH	43.02	33845483
310	2-Hydroxyisobutyrylation	EGAQNQGKKAEGAQN HHHHHHHHHCHHHHC	38.76	-
310	Ubiquitination	EGAQNQGKKAEGAQN HHHHHHHHHCHHHHC	38.76	33845483
338	Ubiquitination	KAEGAQNQGKKAEGA HCHHHHHHHHHHHHH	53.67	33845483
346	Ubiquitination	GKKAEGAQNQGKKAE HHHHHHHHHHHHHHH	54.35	33845483
360	Phosphorylation	EGAQNQGKKAEGAQN HHHHHHHHHHHHHHH	38.76	20068231
370	Phosphorylation	EGAQNQGKKAEGAQN HHHHHHHHHHHHHHH	38.76	-
380	Phosphorylation	EGAQNQGKKAEGAQN HHHHHHHHHCCHHHH	43.28	-
381	Phosphorylation	GAQNQGKKAEGAQNQ HHHHHHHHCCHHHHH	61.64	-
382	Phosphorylation	AQNQGKKAEGAQNQG HHHHHHHCCHHHHHC	44.76	21601212
385	Phosphorylation	QGKKAEGAQNQGKKV HHHHCCHHHHHCCCC	10.91	-
386	Ubiquitination	GKKAEGAQNQGKKVE HHHCCHHHHHCCCCC	54.35	33845483
463	Phosphorylation	QNQGKKAEGAQNQGK HHHHHHCCHHHHHCC	65.03	27251275
467	Phosphorylation	KKAEGAQNQGKKVEG HHCCHHHHHCCCCCC	52.63	-
488	Ubiquitination	KAEGAQNQGKKAEGA HCHHHHHHHHHHHHH	53.67	29967540
491	Phosphorylation	GAQNQGKKAEGAQNQ HHHHHHHHHHHHHHH	59.50	-
499	Ubiquitination	AEGAQNQGKKAEGAQ HHHHHHHHHHCCCCC	40.77	24816145
526	Phosphorylation	GKKTEGAQGKKAERS CCCCCCCCCCCCCCC	75.09	24719451
533	Phosphorylation	QGKKAERSPNQGKKG CCCCCCCCCCCCCCC	21.51	28102081
545	Phosphorylation	KKGEGAPIQGKKADS CCCCCCCCCCCCCCC	9.28	24719451
548	2-Hydroxyisobutyrylation	EGAPIQGKKADSVAN CCCCCCCCCCCCCCC	28.54	-
552	Phosphorylation	IQGKKADSVANQGTK CCCCCCCCCCCCCCE	28.17	28985074
557	Ubiquitination	ADSVANQGTKVEGIT CCCCCCCCCEEEEEC	27.58	23000965
558	Phosphorylation	DSVANQGTKVEGITN CCCCCCCCEEEEECC	23.35	23312004
559	Acetylation	SVANQGTKVEGITNQ CCCCCCCEEEEECCC	45.15	26051181
564	Phosphorylation	GTKVEGITNQGKKAE CCEEEEECCCCCCCC	32.14	23898821
568	2-Hydroxyisobutyrylation	EGITNQGKKAEGSPS EEECCCCCCCCCCCC	38.76	-
568	Ubiquitination	EGITNQGKKAEGSPS EEECCCCCCCCCCCC	38.76	33845483
573	Phosphorylation	QGKKAEGSPSEGKKA CCCCCCCCCCCCCCC	19.43	27461979
575	Phosphorylation	KKAEGSPSEGKKAEG CCCCCCCCCCCCCCC	61.76	27461979
583	Phosphorylation	EGKKAEGSPNQGKKA CCCCCCCCCCCHHHH	16.51	22617229
583	Ubiquitination	EGKKAEGSPNQGKKA CCCCCCCCCCCHHHH	16.51	24816145
588	Ubiquitination	EGSPNQGKKADAAAN CCCCCCHHHHHHHHH	34.72	-
588 (in isoform 2)	Ubiquitination	-	34.72	-
589	Ubiquitination	GSPNQGKKADAAANQ CCCCCHHHHHHHHHC	59.32	-
589 (in isoform 2)	Ubiquitination	-	59.32	-
593	Ubiquitination	QGKKADAAANQGKKT CHHHHHHHHHCCCCC	13.90	29967540
598	Ubiquitination	DAAANQGKKTESASV HHHHHCCCCCCCCCC	46.92	-
598 (in isoform 2)	Ubiquitination	-	46.92	-
600	Phosphorylation	AANQGKKTESASVQG HHHCCCCCCCCCCCC	38.36	20068231
602	Phosphorylation	NQGKKTESASVQGRN HCCCCCCCCCCCCCC	30.95	25849741
604	Phosphorylation	GKKTESASVQGRNTD CCCCCCCCCCCCCCC	25.01	25849741
610	Phosphorylation	ASVQGRNTDVAQSPE CCCCCCCCCCCCCCC	30.41	22167270
615	Phosphorylation	RNTDVAQSPEAPKQE CCCCCCCCCCCCCCC	18.25	19664994
620	Acetylation	AQSPEAPKQEAPAKK CCCCCCCCCCCCCCC	68.75	26051181
620	Sumoylation	AQSPEAPKQEAPAKK CCCCCCCCCCCCCCC	68.75	25114211
620	Ubiquitination	AQSPEAPKQEAPAKK CCCCCCCCCCCCCCC	68.75	33845483
634	Malonylation	KKSGSKKKGEPGPPD CCCCCCCCCCCCCCC	72.71	26320211
647	Phosphorylation	PDADGPLYLPYKTLV CCCCCCEECCHHHHH	14.57	27642862
652	Phosphorylation	PLYLPYKTLVSTVGS CEECCHHHHHHCHHH	26.92	28857561
655	Phosphorylation	LPYKTLVSTVGSMVF CCHHHHHHCHHHHHC	22.08	28857561
656	O-linked_Glycosylation	PYKTLVSTVGSMVFN CHHHHHHCHHHHHCC	22.77	OGP
656	Phosphorylation	PYKTLVSTVGSMVFN CHHHHHHCHHHHHCC	22.77	28857561
659	Phosphorylation	TLVSTVGSMVFNEGE HHHHCHHHHHCCCHH	13.87	28348404
659	Ubiquitination	TLVSTVGSMVFNEGE HHHHCHHHHHCCCHH	13.87	23000965
665	Ubiquitination	GSMVFNEGEAQRLIE HHHHCCCHHHHHHHH	36.32	23000965
675	Phosphorylation	QRLIEILSEKAGIIQ HHHHHHHHHHCCCCH	42.59	24719451
677	2-Hydroxyisobutyrylation	LIEILSEKAGIIQDT HHHHHHHHCCCCHHH	48.84	-
677	Ubiquitination	LIEILSEKAGIIQDT HHHHHHHHCCCCHHH	48.84	-
680	Ubiquitination	ILSEKAGIIQDTWHK HHHHHCCCCHHHHHH	2.82	33845483
684	Phosphorylation	KAGIIQDTWHKATQK HCCCCHHHHHHHHHC	17.06	23312004
687	Malonylation	IIQDTWHKATQKGDP CCHHHHHHHHHCCCH	44.69	26320211
687	Ubiquitination	IIQDTWHKATQKGDP CCHHHHHHHHHCCCH	44.69	-
689	Phosphorylation	QDTWHKATQKGDPVA HHHHHHHHHCCCHHH	35.30	28857561
691	Malonylation	TWHKATQKGDPVAIL HHHHHHHCCCHHHHH	62.01	26320211
691	Ubiquitination	TWHKATQKGDPVAIL HHHHHHHCCCHHHHH	62.01	33845483
699	Acetylation	GDPVAILKRQLEEKE CCHHHHHHHHHHHHH	31.80	26051181
699	Malonylation	GDPVAILKRQLEEKE CCHHHHHHHHHHHHH	31.80	26320211
699	Methylation	GDPVAILKRQLEEKE CCHHHHHHHHHHHHH	31.80	72642407
699	Ubiquitination	GDPVAILKRQLEEKE CCHHHHHHHHHHHHH	31.80	33845483
711	Phosphorylation	EKEKLLATEQEDAAV HHHHHHHHHHHHHHH	37.86	-
714	Ubiquitination	KLLATEQEDAAVAKS HHHHHHHHHHHHHHH	43.30	29967540
720	Ubiquitination	QEDAAVAKSKLRELN HHHHHHHHHHHHHHH	41.34	33845483
726	Ubiquitination	AKSKLRELNKEMAAE HHHHHHHHHHHHHHH	10.04	33845483
728	Malonylation	SKLRELNKEMAAEKA HHHHHHHHHHHHHHH	62.58	26320211
742	Ubiquitination	AKAAAGEAKVKKQLV HHHHHHHHHHHHHHH	22.48	33845483
743	Ubiquitination	KAAAGEAKVKKQLVA HHHHHHHHHHHHHHH	50.73	33845483
752	Ubiquitination	KKQLVAREQEITAVQ HHHHHHHHHHHHHHH	42.71	32142685
766	Phosphorylation	QARMQASYREHVKEV HHHHHHHHHHHHHHH	24.04	27251275
771	Ubiquitination	ASYREHVKEVQQLQG HHHHHHHHHHHHHHH	54.82	33845483
779	2-Hydroxyisobutyrylation	EVQQLQGKIRTLQEQ HHHHHHHHHHHHHHH	18.96	-
779	Acetylation	EVQQLQGKIRTLQEQ HHHHHHHHHHHHHHH	18.96	25953088
779	Malonylation	EVQQLQGKIRTLQEQ HHHHHHHHHHHHHHH	18.96	26320211
779	Ubiquitination	EVQQLQGKIRTLQEQ HHHHHHHHHHHHHHH	18.96	33845483
782	Phosphorylation	QLQGKIRTLQEQLEN HHHHHHHHHHHHHHC	35.94	20068231
793	Phosphorylation	QLENGPNTQLARLQQ HHHCCCCHHHHHHHH	28.26	20068231
803	Phosphorylation	ARLQQENSILRDALN HHHHHHHHHHHHHHH	23.42	30108239
808	Ubiquitination	ENSILRDALNQATSQ HHHHHHHHHHHHHHH	11.28	32142685
813	Phosphorylation	RDALNQATSQVESKQ HHHHHHHHHHHHHHH	15.21	21406692
813	Ubiquitination	RDALNQATSQVESKQ HHHHHHHHHHHHHHH	15.21	33845483
814	Phosphorylation	DALNQATSQVESKQN HHHHHHHHHHHHHHH	34.93	21406692
818	Phosphorylation	QATSQVESKQNAELA HHHHHHHHHHHHHHH	40.46	21406692
819	Acetylation	ATSQVESKQNAELAK HHHHHHHHHHHHHHH	33.78	26051181
819	Malonylation	ATSQVESKQNAELAK HHHHHHHHHHHHHHH	33.78	26320211
819	Ubiquitination	ATSQVESKQNAELAK HHHHHHHHHHHHHHH	33.78	33845483
829	Ubiquitination	AELAKLRQELSKVSK HHHHHHHHHHHHHHH	67.43	22817900
829 (in isoform 3)	Ubiquitination	-	67.43	21906983
830	Phosphorylation	ELAKLRQELSKVSKE HHHHHHHHHHHHHHH	48.88	20068231
832	Phosphorylation	AKLRQELSKVSKELV HHHHHHHHHHHHHHH	30.20	29514088
836	Malonylation	QELSKVSKELVEKSE HHHHHHHHHHHHHHH	59.04	26320211
841	2-Hydroxyisobutyrylation	VSKELVEKSEAVRQD HHHHHHHHHHHHHHH	46.23	-
841	Acetylation	VSKELVEKSEAVRQD HHHHHHHHHHHHHHH	46.23	26051181
843	Phosphorylation	KELVEKSEAVRQDEQ HHHHHHHHHHHHHHH	63.35	20166139
844	Phosphorylation	ELVEKSEAVRQDEQQ HHHHHHHHHHHHHHH	14.64	20166139
858	2-Hydroxyisobutyrylation	QRKALEAKAAAFEKQ HHHHHHHHHHHHHHH	29.23	-
858	Malonylation	QRKALEAKAAAFEKQ HHHHHHHHHHHHHHH	29.23	26320211
864	2-Hydroxyisobutyrylation	AKAAAFEKQVLQLQA HHHHHHHHHHHHHHH	38.97	-
864	Acetylation	AKAAAFEKQVLQLQA HHHHHHHHHHHHHHH	38.97	26051181
864	Malonylation	AKAAAFEKQVLQLQA HHHHHHHHHHHHHHH	38.97	26320211
872	Phosphorylation	QVLQLQASHRESEEA HHHHHHHHHHHCHHH	15.32	28111955
887	Phosphorylation	LQKRLDEVSRELCHT HHHHHHHHHHHHHHH	6.97	27251275
892	S-nitrosocysteine	DEVSRELCHTQSSHA HHHHHHHHHHHHCHH	2.53	-
892	S-nitrosylation	DEVSRELCHTQSSHA HHHHHHHHHHHHCHH	2.53	20140087
894	Phosphorylation	VSRELCHTQSSHASL HHHHHHHHHHCHHHH	29.20	28857561
896	Phosphorylation	RELCHTQSSHASLRA HHHHHHHHCHHHHHH	25.83	28857561
897	Phosphorylation	ELCHTQSSHASLRAD HHHHHHHCHHHHHHH	17.16	28857561
898	Ubiquitination	LCHTQSSHASLRADA HHHHHHCHHHHHHHH	25.28	24816145
900	Phosphorylation	HTQSSHASLRADAEK HHHHCHHHHHHHHHH	16.99	28857561
907	2-Hydroxyisobutyrylation	SLRADAEKAQEQQQQ HHHHHHHHHHHHHHH	58.03	-
907	Acetylation	SLRADAEKAQEQQQQ HHHHHHHHHHHHHHH	58.03	26051181
908	Phosphorylation	LRADAEKAQEQQQQM HHHHHHHHHHHHHHH	15.06	27251275
915	Sulfoxidation	AQEQQQQMAELHSKL HHHHHHHHHHHHHHH	2.45	30846556
917	Ubiquitination	EQQQQMAELHSKLQS HHHHHHHHHHHHHHC	41.49	33845483
921	Acetylation	QMAELHSKLQSSEAE HHHHHHHHHHCCHHH	39.54	26051181
922	Ubiquitination	MAELHSKLQSSEAEV HHHHHHHHHCCHHHH	7.18	23503661
924	Phosphorylation	ELHSKLQSSEAEVRS HHHHHHHCCHHHHHH	40.35	21406692
924	Ubiquitination	ELHSKLQSSEAEVRS HHHHHHHCCHHHHHH	40.35	24816145
925	Phosphorylation	LHSKLQSSEAEVRSK HHHHHHCCHHHHHHH	28.06	21406692
931	Phosphorylation	SSEAEVRSKCEELSG CCHHHHHHHHHHHHH	47.00	21406692
932	Acetylation	SEAEVRSKCEELSGL CHHHHHHHHHHHHHH	34.79	23236377
932	Malonylation	SEAEVRSKCEELSGL CHHHHHHHHHHHHHH	34.79	26320211
937	Phosphorylation	RSKCEELSGLHGQLQ HHHHHHHHHHHHHHH	42.46	21406692
942	Ubiquitination	ELSGLHGQLQEARAE HHHHHHHHHHHHHHH	29.26	23503661
959	Phosphorylation	QLTERIRSIEALLEA HHHHHHHHHHHHHHH	23.55	30266825
969	Phosphorylation	ALLEAGQARDAQDVQ HHHHHHCCCCHHHHH	15.48	-
970	Phosphorylation	LLEAGQARDAQDVQA HHHHHCCCCHHHHHH	31.73	24719451
972	Ubiquitination	EAGQARDAQDVQASQ HHHCCCCHHHHHHHH	11.26	24816145
976	Phosphorylation	ARDAQDVQASQAEAD CCCHHHHHHHHHHHH	43.52	24719451
978	Phosphorylation	DAQDVQASQAEADQQ CHHHHHHHHHHHHHH	16.90	21712546
990	Acetylation	DQQQTRLKELESQVS HHHHHHHHHHHHHHH	57.89	26051181
990	Malonylation	DQQQTRLKELESQVS HHHHHHHHHHHHHHH	57.89	26320211
994	Phosphorylation	TRLKELESQVSGLEK HHHHHHHHHHHCHHH	48.81	29514088
997	Phosphorylation	KELESQVSGLEKEAI HHHHHHHHCHHHHHH	29.98	29514088
1028	Sulfoxidation	REKNWKAMEALATAE HHHHHHHHHHHHHHH	2.48	21406390
1039	Malonylation	ATAEQACKEKLLSLT HHHHHHHHHHHHHHH	61.98	26320211
1044	Phosphorylation	ACKEKLLSLTQAKEE HHHHHHHHHHHCCHH	39.55	21406692
1046	Phosphorylation	KEKLLSLTQAKEESE HHHHHHHHHCCHHHH	24.09	21406692
1092	Ubiquitination	WLQDLKEKGPTLLKH HHHHHHHHCCCCCCC	69.47	33845483
1098	2-Hydroxyisobutyrylation	EKGPTLLKHPPAPAE HHCCCCCCCCCCCCC	58.12	-
1098	Acetylation	EKGPTLLKHPPAPAE HHCCCCCCCCCCCCC	58.12	26051181
1098	Malonylation	EKGPTLLKHPPAPAE HHCCCCCCCCCCCCC	58.12	26320211
1098	Ubiquitination	EKGPTLLKHPPAPAE HHCCCCCCCCCCCCC	58.12	33845483
1107	Phosphorylation	PPAPAEPSSDLASKL CCCCCCCCCHHHHHH	28.17	23312004
1108	Phosphorylation	PAPAEPSSDLASKLR CCCCCCCCHHHHHHH	47.56	23312004
1112	Phosphorylation	EPSSDLASKLREAEE CCCCHHHHHHHHHHH	39.25	23312004
1113	Ubiquitination	PSSDLASKLREAEET CCCHHHHHHHHHHHH	46.05	33845483
1128	Glutathionylation	QSTLQAECDQYRSIL HHHHHHHHHHHHHHH	4.41	22555962
1148	Phosphorylation	MLRDLQKSVEEEEQV HHHHHHHHHHHHHHH	23.07	30624053
1159	2-Hydroxyisobutyrylation	EEQVWRAKVGAAEEE HHHHHHHHCCHHHHH	32.40	-
1159	Malonylation	EEQVWRAKVGAAEEE HHHHHHHHCCHHHHH	32.40	26320211
1159	Ubiquitination	EEQVWRAKVGAAEEE HHHHHHHHCCHHHHH	32.40	33845483
1169	Malonylation	AAEEELQKSRVTVKH HHHHHHHHCCCHHHH	53.51	26320211
1169	Ubiquitination	AAEEELQKSRVTVKH HHHHHHHHCCCHHHH	53.51	-
1170	Phosphorylation	AEEELQKSRVTVKHL HHHHHHHCCCHHHHH	21.01	21601212
1173	Phosphorylation	ELQKSRVTVKHLEEI HHHHCCCHHHHHHHH	23.79	21601212
1175	Acetylation	QKSRVTVKHLEEIVE HHCCCHHHHHHHHHH	32.86	25953088
1175	Malonylation	QKSRVTVKHLEEIVE HHCCCHHHHHHHHHH	32.86	26320211
1175	Ubiquitination	QKSRVTVKHLEEIVE HHCCCHHHHHHHHHH	32.86	33845483
1185	2-Hydroxyisobutyrylation	EEIVEKLKGELESSD HHHHHHHCCCCCCCH	62.50	-
1185	Malonylation	EEIVEKLKGELESSD HHHHHHHCCCCCCCH	62.50	26320211
1185	Ubiquitination	EEIVEKLKGELESSD HHHHHHHCCCCCCCH	62.50	32142685
1191	Phosphorylation	LKGELESSDQVREHT HCCCCCCCHHHHHHH	23.76	21815630
1198	Phosphorylation	SDQVREHTSHLEAEL CHHHHHHHHHHHHHH	17.06	23312004
1199	Phosphorylation	DQVREHTSHLEAELE HHHHHHHHHHHHHHH	28.16	23312004
1216	Glutathionylation	MAAASAECQNYAKEV HHHHHHHHHHHHHHH	2.96	22555962
1216	S-nitrosylation	MAAASAECQNYAKEV HHHHHHHHHHHHHHH	2.96	2212679
1221	2-Hydroxyisobutyrylation	AECQNYAKEVAGLRQ HHHHHHHHHHHHHHH	42.22	-
1221	Acetylation	AECQNYAKEVAGLRQ HHHHHHHHHHHHHHH	42.22	26051181
1221	Malonylation	AECQNYAKEVAGLRQ HHHHHHHHHHHHHHH	42.22	26320211
1233	Phosphorylation	LRQLLLESQSQLDAA HHHHHHHHHHHHHHH	34.79	28258704
1238 (in isoform 2)	Ubiquitination	-	36.52	-
1241	Ubiquitination	QSQLDAAKSEAQKQS HHHHHHHHHHHHHHH	51.02	32142685
1246	Ubiquitination	AAKSEAQKQSDELAL HHHHHHHHHHHHHHH	59.84	33845483
1248	Phosphorylation	KSEAQKQSDELALVR HHHHHHHHHHHHHHH	39.84	28509920
1259	Phosphorylation	ALVRQQLSEMKSHVE HHHHHHHHHHHHHCC	31.16	28102081
1261	Sulfoxidation	VRQQLSEMKSHVEDG HHHHHHHHHHHCCCC	4.92	30846556
1262	Ubiquitination	RQQLSEMKSHVEDGD HHHHHHHHHHCCCCC	33.10	2190698
1262 (in isoform 1)	Ubiquitination	-	33.10	21906983
1263	Phosphorylation	QQLSEMKSHVEDGDI HHHHHHHHHCCCCCC	31.30	29255136
1276	Phosphorylation	DIAGAPASSPEAPPA CCCCCCCCCCCCCCH	45.42	29255136
1277	O-linked_Glycosylation	IAGAPASSPEAPPAE CCCCCCCCCCCCCHH	28.94	OGP
1277	Phosphorylation	IAGAPASSPEAPPAE CCCCCCCCCCCCCHH	28.94	29255136
1292	Phosphorylation	QDPVQLKTQLEWTEA CCCCCHHHHHHHHHH	47.15	25850435
1297	Phosphorylation	LKTQLEWTEAILEDE HHHHHHHHHHHHCCH	13.23	25850435
1320	Phosphorylation	AEFEEAQTSACRLQE HHHHHHHHHHHHHHH	25.91	27251275
1321	Phosphorylation	EFEEAQTSACRLQEE HHHHHHHHHHHHHHH	17.19	27251275
1323	S-nitrosocysteine	EEAQTSACRLQEELE HHHHHHHHHHHHHHH	4.46	-
1323	S-nitrosylation	EEAQTSACRLQEELE HHHHHHHHHHHHHHH	4.46	20140087
1331	Malonylation	RLQEELEKLRTAGPL HHHHHHHHHHHCCCC	56.76	26320211
1340	Phosphorylation	RTAGPLESSETEEAS HHCCCCCCCHHHHHH	40.95	29514088
1341	Phosphorylation	TAGPLESSETEEASQ HCCCCCCCHHHHHHH	38.88	26657352
1343	Phosphorylation	GPLESSETEEASQLK CCCCCCHHHHHHHHH	40.86	29514088
1347 (in isoform 2)	Ubiquitination	-	39.05	-
1350	Acetylation	TEEASQLKERLEKEK HHHHHHHHHHHHHHH	32.90	26051181
1350	Ubiquitination	TEEASQLKERLEKEK HHHHHHHHHHHHHHH	32.90	33845483
1372 (in isoform 2)	Ubiquitination	-	61.74	-
1402	Phosphorylation	LEKAEDGSSSKEGTS HHHHCCCCCCCCCCC	43.70	23911959
1403	Phosphorylation	EKAEDGSSSKEGTSV HHHCCCCCCCCCCCC	51.46	30576142
1404	Phosphorylation	KAEDGSSSKEGTSV- HHCCCCCCCCCCCC-	36.10	30624053
1408	Phosphorylation	GSSSKEGTSV----- CCCCCCCCCC-----	27.66	30624053
1409	Phosphorylation	SSSKEGTSV------ CCCCCCCCC------	36.36	23911959

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 RRBP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RRBP1_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 RRBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DEST_HUMAN	DSTN	physical	17353931
RS19_HUMAN	RPS19	physical	22939629
SRPRB_HUMAN	SRPRB	physical	22939629
MORC2_HUMAN	MORC2	physical	26344197
RBM8A_HUMAN	RBM8A	physical	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 RRBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-615; SER-1276 ANDSER-1277, 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-615, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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 SER-615, AND MASSSPECTROMETRY.	19007248 [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-615, 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-615, 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 THR-255; THR-275; SER-533;SER-583 AND SER-615, AND MASS 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 SER-583 AND SER-615, ANDMASS SPECTROMETRY.	15302935 [Abstract]