dbPTM

RB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RB_HUMAN
UniProt AC	P06400
Protein Name	Retinoblastoma-associated protein
Gene Name	RB1
Organism	Homo sapiens (Human).
Sequence Length	928
Subcellular Localization	Nucleus .
Protein Description	Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity..
Protein Sequence	MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MPPKTPRKT ------CCCCCCCHH	38.81	-
5	Phosphorylation	---MPPKTPRKTAAT ---CCCCCCCHHHHH	33.81	9139732
9	Phosphorylation	PPKTPRKTAATAAAA CCCCCCHHHHHHHHH	23.86	23927012
12	Phosphorylation	TPRKTAATAAAAAAE CCCHHHHHHHHHHCC	17.86	28464451
37	Phosphorylation	EEDPEQDSGPEDLPL CCCCCCCCCCCCCCE	56.81	29255136
52	Phosphorylation	VRLEFEETEEPDFTA EEEEEECCCCCCHHH	38.15	28464451
63	Ubiquitination	DFTALCQKLKIPDHV CHHHHHHHCCCCHHH	51.23	-
65	Ubiquitination	TALCQKLKIPDHVRE HHHHHHCCCCHHHHH	60.26	-
77	Phosphorylation	VRERAWLTWEKVSSV HHHHHHCCHHHHHCC	22.37	26074081
82	Phosphorylation	WLTWEKVSSVDGVLG HCCHHHHHCCCCCHH	35.39	26074081
83	Phosphorylation	LTWEKVSSVDGVLGG CCHHHHHCCCCCHHH	27.50	26074081
91	Phosphorylation	VDGVLGGYIQKKKEL CCCCHHHHHHHHHHH	9.81	26074081
94	Ubiquitination	VLGGYIQKKKELWGI CHHHHHHHHHHHHCE	57.14	-
136	Ubiquitination	HKFFNLLKEIDTSTK HHHHHHHHHCCCCHH	56.65	-
140	Phosphorylation	NLLKEIDTSTKVDNA HHHHHCCCCHHHHHH	43.91	-
143	Ubiquitination	KEIDTSTKVDNAMSR HHCCCCHHHHHHHHH	47.56	21890473
149	Phosphorylation	TKVDNAMSRLLKKYD HHHHHHHHHHHHHHH	19.84	-
163	Phosphorylation	DVLFALFSKLERTCE HHHHHHHHHHHHHEE	36.86	24719451
215	Phosphorylation	MEDDLVISFQLMLCV CCCHHHHHHHHHHHH	10.24	24043423
230	Phosphorylation	LDYFIKLSPPMLLKE HHHHHHHCCCCCCCC	23.19	10207050
239	Phosphorylation	PMLLKEPYKTAVIPI CCCCCCCCCEEEEEC	23.28	28634298
241	Phosphorylation	LLKEPYKTAVIPING CCCCCCCEEEEECCC	21.95	23927012
249	Phosphorylation	AVIPINGSPRTPRRG EEEECCCCCCCCCCC	13.51	19664994
252	Phosphorylation	PINGSPRTPRRGQNR ECCCCCCCCCCCCCH	25.24	23927012
260	Phosphorylation	PRRGQNRSARIAKQL CCCCCCHHHHHHHHH	29.46	26074081
265	Acetylation	NRSARIAKQLENDTR CHHHHHHHHHCCCHH	53.71	26822725
265	Ubiquitination	NRSARIAKQLENDTR CHHHHHHHHHCCCHH	53.71	-
279	Acetylation	RIIEVLCKEHECNID HHHHHHHHHCCCCHH	58.92	25953088
279	Ubiquitination	RIIEVLCKEHECNID HHHHHHHHHCCCCHH	58.92	-
289	Acetylation	ECNIDEVKNVYFKNF CCCHHHHCCHHHHHH	38.35	25953088
289	Ubiquitination	ECNIDEVKNVYFKNF CCCHHHHCCHHHHHH	38.35	-
319	Ubiquitination	PEVENLSKRYEEIYL HHHHHHHHHHHHHHH	63.26	-
321	Phosphorylation	VENLSKRYEEIYLKN HHHHHHHHHHHHHCC	22.96	19835603
325	Phosphorylation	SKRYEEIYLKNKDLD HHHHHHHHHCCCCCC	18.20	19835603
327	Ubiquitination	RYEEIYLKNKDLDAR HHHHHHHCCCCCCHH	45.00	-
329	Ubiquitination	EEIYLKNKDLDARLF HHHHHCCCCCCHHHC	59.07	-
341	Acetylation	RLFLDHDKTLQTDSI HHCCCCCCCCCCCCC	47.95	25953088
341	Ubiquitination	RLFLDHDKTLQTDSI HHCCCCCCCCCCCCC	47.95	-
342	Phosphorylation	LFLDHDKTLQTDSID HCCCCCCCCCCCCCC	30.10	23927012
345	Phosphorylation	DHDKTLQTDSIDSFE CCCCCCCCCCCCCCC	34.52	23927012
347	Phosphorylation	DKTLQTDSIDSFETQ CCCCCCCCCCCCCCC	31.51	23927012
350	Phosphorylation	LQTDSIDSFETQRTP CCCCCCCCCCCCCCC	24.26	23927012
353	Phosphorylation	DSIDSFETQRTPRKS CCCCCCCCCCCCCCC	22.72	29255136
356	Phosphorylation	DSFETQRTPRKSNLD CCCCCCCCCCCCCCC	20.02	29255136
359	Ubiquitination	ETQRTPRKSNLDEEV CCCCCCCCCCCCCCC	44.92	-
360	Phosphorylation	TQRTPRKSNLDEEVN CCCCCCCCCCCCCCC	43.86	23927012
373	Phosphorylation	VNVIPPHTPVRTVMN CCCCCCCCHHHHHHH	29.29	29255136
414	Phosphorylation	CTVNPKESILKRVKD CCCCCHHHHHHHHHH	39.07	24719451
420	Ubiquitination	ESILKRVKDIGYIFK HHHHHHHHHHCHHHH	47.89	-
424	Phosphorylation	KRVKDIGYIFKEKFA HHHHHHCHHHHHHHH	11.97	28152594
427	Acetylation	KDIGYIFKEKFAKAV HHHCHHHHHHHHHHH	50.89	19608861
427	Ubiquitination	KDIGYIFKEKFAKAV HHHCHHHHHHHHHHH	50.89	19608861
432	Ubiquitination	IFKEKFAKAVGQGCV HHHHHHHHHHCCCEE	46.89	-
454	Phosphorylation	KLGVRLYYRVMESML HHHHHHHHHHHHHHH	11.00	-
534	Phosphorylation	DFYKVIESFIKAEGN HHHHHHHHHHHHCCC	22.58	24719451
537	Ubiquitination	KVIESFIKAEGNLTR HHHHHHHHHCCCCHH	38.07	-
548	Acetylation	NLTREMIKHLERCEH CCHHHHHHHHHHHHH	40.61	19608861
567	Phosphorylation	SLAWLSDSPLFDLIK HHHHHCCCCHHHHHH	21.81	22279936
574	Ubiquitination	SPLFDLIKQSKDREG CCHHHHHHHCCCCCC	56.68	-
583	Phosphorylation	SKDREGPTDHLESAC CCCCCCCCCCHHHCC	47.08	20164059
588	Phosphorylation	GPTDHLESACPLNLP CCCCCHHHCCCCCCC	41.34	22115753
601	Phosphorylation	LPLQNNHTAADMYLS CCCCCCCCHHHHHCC	26.18	23401153
606	Phosphorylation	NHTAADMYLSPVRSP CCCHHHHHCCCCCCC	12.46	23401153
608	Phosphorylation	TAADMYLSPVRSPKK CHHHHHCCCCCCCCC	12.12	29255136
612	Phosphorylation	MYLSPVRSPKKKGST HHCCCCCCCCCCCCC	41.11	29255136
618	Phosphorylation	RSPKKKGSTTRVNST CCCCCCCCCCCCCCC	35.17	26074081
619	Phosphorylation	SPKKKGSTTRVNSTA CCCCCCCCCCCCCCC	27.56	26074081
620	Phosphorylation	PKKKGSTTRVNSTAN CCCCCCCCCCCCCCC	34.03	26074081
624	Phosphorylation	GSTTRVNSTANAETQ CCCCCCCCCCCCHHH	26.49	25159151
625	Phosphorylation	STTRVNSTANAETQA CCCCCCCCCCCHHHH	20.80	25159151
630	Phosphorylation	NSTANAETQATSAFQ CCCCCCHHHHCCHHC	22.54	23312004
633	Phosphorylation	ANAETQATSAFQTQK CCCHHHHCCHHCCCC	15.69	23312004
634	Phosphorylation	NAETQATSAFQTQKP CCHHHHCCHHCCCCC	30.06	23312004
638	Phosphorylation	QATSAFQTQKPLKST HHCCHHCCCCCCCCC	31.91	23312004
640	Acetylation	TSAFQTQKPLKSTSL CCHHCCCCCCCCCCH	56.56	25953088
640	Ubiquitination	TSAFQTQKPLKSTSL CCHHCCCCCCCCCCH	56.56	19608861
644	Phosphorylation	QTQKPLKSTSLSLFY CCCCCCCCCCHHHHH	30.80	30576142
648	Phosphorylation	PLKSTSLSLFYKKVY CCCCCCHHHHHHHHH	19.05	30576142
651	Phosphorylation	STSLSLFYKKVYRLA CCCHHHHHHHHHHHH	18.39	30576142
652	Acetylation	TSLSLFYKKVYRLAY CCHHHHHHHHHHHHH	28.55	25953088
720	Sumoylation	KVKNIDLKFKIIVTA EEECCCEEEEEEEEE	40.64	-
720	Sumoylation	KVKNIDLKFKIIVTA EEECCCEEEEEEEEE	40.64	-
766	Phosphorylation	VFMQRLKTNILQYAS HHHHHHHHHHHHHHC	31.89	22199227
771	Phosphorylation	LKTNILQYASTRPPT HHHHHHHHHCCCCCC	10.08	23898821
773	Phosphorylation	TNILQYASTRPPTLS HHHHHHHCCCCCCCC	21.73	22322096
774	Phosphorylation	NILQYASTRPPTLSP HHHHHHCCCCCCCCC	38.74	22322096
775	Dimethylation	ILQYASTRPPTLSPI HHHHHCCCCCCCCCC	32.48	-
775	Methylation	ILQYASTRPPTLSPI HHHHHCCCCCCCCCC	32.48	73066607
778	Phosphorylation	YASTRPPTLSPIPHI HHCCCCCCCCCCCCC	42.42	22322096
780	Phosphorylation	STRPPTLSPIPHIPR CCCCCCCCCCCCCCC	24.22	22322096
787	Dimethylation	SPIPHIPRSPYKFPS CCCCCCCCCCCCCCC	50.05	-
787	Methylation	SPIPHIPRSPYKFPS CCCCCCCCCCCCCCC	50.05	73066609
788	Phosphorylation	PIPHIPRSPYKFPSS CCCCCCCCCCCCCCC	27.51	19664994
790	Phosphorylation	PHIPRSPYKFPSSPL CCCCCCCCCCCCCCC	26.89	30266825
791	Acetylation	HIPRSPYKFPSSPLR CCCCCCCCCCCCCCC	54.93	25953088
791	Ubiquitination	HIPRSPYKFPSSPLR CCCCCCCCCCCCCCC	54.93	-
794	Phosphorylation	RSPYKFPSSPLRIPG CCCCCCCCCCCCCCC	47.96	22322096
795	Phosphorylation	SPYKFPSSPLRIPGG CCCCCCCCCCCCCCC	28.35	19664994
798	Dimethylation	KFPSSPLRIPGGNIY CCCCCCCCCCCCCEE	36.12	-
798	Methylation	KFPSSPLRIPGGNIY CCCCCCCCCCCCCEE	36.12	73066611
805	Phosphorylation	RIPGGNIYISPLKSP CCCCCCEEECCCCCC	10.19	23927012
807	Phosphorylation	PGGNIYISPLKSPYK CCCCEEECCCCCCCC	13.75	21536668
810	"N6,N6-dimethyllysine"	NIYISPLKSPYKISE CEEECCCCCCCCCCC	53.41	-
810	Acetylation	NIYISPLKSPYKISE CEEECCCCCCCCCCC	53.41	25953088
810	Methylation	NIYISPLKSPYKISE CEEECCCCCCCCCCC	53.41	22787429
810	Ubiquitination	NIYISPLKSPYKISE CEEECCCCCCCCCCC	53.41	21906983
811	Phosphorylation	IYISPLKSPYKISEG EEECCCCCCCCCCCC	40.94	21536668
813	Phosphorylation	ISPLKSPYKISEGLP ECCCCCCCCCCCCCC	28.22	23927012
814	Acetylation	SPLKSPYKISEGLPT CCCCCCCCCCCCCCC	43.04	25953088
814	Ubiquitination	SPLKSPYKISEGLPT CCCCCCCCCCCCCCC	43.04	-
816	Phosphorylation	LKSPYKISEGLPTPT CCCCCCCCCCCCCCC	22.81	29255136
821	Phosphorylation	KISEGLPTPTKMTPR CCCCCCCCCCCCCCC	48.94	19664994
823	Phosphorylation	SEGLPTPTKMTPRSR CCCCCCCCCCCCCCE	35.61	19664994
824	Acetylation	EGLPTPTKMTPRSRI CCCCCCCCCCCCCEE	41.81	25953088
824	Ubiquitination	EGLPTPTKMTPRSRI CCCCCCCCCCCCCEE	41.81	-
826	Phosphorylation	LPTPTKMTPRSRILV CCCCCCCCCCCEEEE	19.67	19664994
829	Phosphorylation	PTKMTPRSRILVSIG CCCCCCCCEEEEECC	25.52	26074081
834	Phosphorylation	PRSRILVSIGESFGT CCCEEEEECCHHCCC	22.79	26074081
838	Phosphorylation	ILVSIGESFGTSEKF EEEECCHHCCCHHHH	24.62	30266825
841	Phosphorylation	SIGESFGTSEKFQKI ECCHHCCCHHHHHHH	31.53	30266825
842	Phosphorylation	IGESFGTSEKFQKIN CCHHCCCHHHHHHHH	38.89	30266825
844	Ubiquitination	ESFGTSEKFQKINQM HHCCCHHHHHHHHHH	53.51	-
847	Acetylation	GTSEKFQKINQMVCN CCHHHHHHHHHHHHC	46.92	25953088
847	Ubiquitination	GTSEKFQKINQMVCN CCHHHHHHHHHHHHC	46.92	-
855	Phosphorylation	INQMVCNSDRVLKRS HHHHHHCCHHHHHHH	22.97	29255136
857	Methylation	QMVCNSDRVLKRSAE HHHHCCHHHHHHHCC	35.17	115490375
860	Methylation	CNSDRVLKRSAEGSN HCCHHHHHHHCCCCC	41.26	20870719
860	Ubiquitination	CNSDRVLKRSAEGSN HCCHHHHHHHCCCCC	41.26	20870719
862	Phosphorylation	SDRVLKRSAEGSNPP CHHHHHHHCCCCCCC	29.14	28111955
866	Phosphorylation	LKRSAEGSNPPKPLK HHHHCCCCCCCCCCC	37.35	29496963
870	Ubiquitination	AEGSNPPKPLKKLRF CCCCCCCCCCCCCCE	65.33	-
873	Acetylation	SNPPKPLKKLRFDIE CCCCCCCCCCCEEEE	59.28	16374512
873	Methylation	SNPPKPLKKLRFDIE CCCCCCCCCCCEEEE	59.28	20140018
874	Acetylation	NPPKPLKKLRFDIEG CCCCCCCCCCEEEEC	53.21	16374512
882	Phosphorylation	LRFDIEGSDEADGSK CCEEEECCCCCCCCC	21.35	30266825
888	Phosphorylation	GSDEADGSKHLPGES CCCCCCCCCCCCCCH	19.90	30001349
895	Phosphorylation	SKHLPGESKFQQKLA CCCCCCCHHHHHHHH	44.69	21712546
896	Acetylation	KHLPGESKFQQKLAE CCCCCCHHHHHHHHH	42.78	23749302
896	Ubiquitination	KHLPGESKFQQKLAE CCCCCCHHHHHHHHH	42.78	19608861
900	Acetylation	GESKFQQKLAEMTST CCHHHHHHHHHHHHH	38.59	25953088
900	Ubiquitination	GESKFQQKLAEMTST CCHHHHHHHHHHHHH	38.59	-
905	Phosphorylation	QQKLAEMTSTRTRMQ HHHHHHHHHHHHHHH	20.60	-
919	Phosphorylation	QKQKMNDSMDTSNKE HHHHHHHCCCCCCCC	17.35	25159151
922	Phosphorylation	KMNDSMDTSNKEEK- HHHHCCCCCCCCCC-	26.09	28111955
923	Phosphorylation	MNDSMDTSNKEEK-- HHHCCCCCCCCCC--	41.46	28111955
925	Acetylation	DSMDTSNKEEK---- HCCCCCCCCCC----	68.00	25953088

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
249	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
249	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
249	S	Phosphorylation	Kinase	CDK2	P24941	PSP
249	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
249	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
252	T	Phosphorylation	Kinase	CDK4	P11802	PSP
252	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
252	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
252	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
252	T	Phosphorylation	Kinase	CDK2	P24941	PSP
252	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
356	T	Phosphorylation	Kinase	CDK4	P11802	PSP
356	T	Phosphorylation	Kinase	CDK2	P24941	PSP
356	T	Phosphorylation	Kinase	UL97	P16788	PSP
373	T	Phosphorylation	Kinase	CDK4	P11802	PSP
373	T	Phosphorylation	Kinase	CDK2	P24941	PSP
373	T	Phosphorylation	Kinase	UL97	P16788	PSP
373	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
373	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
373	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
567	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
567	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
608	S	Phosphorylation	Kinase	CDK2	P24941	PSP
608	S	Phosphorylation	Kinase	CDK4	P11802	PSP
608	S	Phosphorylation	Kinase	UL97	P16788	PSP
612	S	Phosphorylation	Kinase	CHK1	O14757	PSP
612	S	Phosphorylation	Kinase	UL97	P16788	PSP
612	S	Phosphorylation	Kinase	CDK4	P11802	PSP
612	S	Phosphorylation	Kinase	CHK2	O96017	PSP
612	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
612	S	Phosphorylation	Kinase	CDK2	P24941	PSP
780	S	Phosphorylation	Kinase	UL97	P16788	PSP
780	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
780	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
780	S	Phosphorylation	Kinase	CDK4	P11802	PSP
780	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
788	S	Phosphorylation	Kinase	UL97	P16788	PSP
788	S	Phosphorylation	Kinase	CDK4	P11802	PSP
788	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
795	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
795	S	Phosphorylation	Kinase	UL97	P16788	PSP
795	S	Phosphorylation	Kinase	CDK4	P11802	PSP
795	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
795	S	Phosphorylation	Kinase	CDK2	P97377	PSP
795	S	Phosphorylation	Kinase	CDK9	P50750	PSP
795	S	Phosphorylation	Kinase	CDK18	Q07002	PSP
805	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
807	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
807	S	Phosphorylation	Kinase	UL97	P16788	PSP
807	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
807	S	Phosphorylation	Kinase	CDK9	P50750	PSP
807	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
807	S	Phosphorylation	Kinase	CDK18	Q07002	PSP
807	S	Phosphorylation	Kinase	CDK2	P24941	PSP
807	S	Phosphorylation	Kinase	CDK3	Q00526	Uniprot
807	S	Phosphorylation	Kinase	CDK4	P11802	PSP
807	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
807	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
811	S	Phosphorylation	Kinase	CDK2	P24941	PSP
811	S	Phosphorylation	Kinase	CDK9	P50750	PSP
811	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
811	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
811	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
811	S	Phosphorylation	Kinase	CDK18	Q07002	PSP
811	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
811	S	Phosphorylation	Kinase	UL97	P16788	PSP
811	S	Phosphorylation	Kinase	CDK3	Q00526	Uniprot
811	S	Phosphorylation	Kinase	CDK4	P11802	PSP
811	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
821	T	Phosphorylation	Kinase	CDK2	P24941	PSP
821	T	Phosphorylation	Kinase	UL97	P16788	PSP
821	T	Phosphorylation	Kinase	CDK6	Q00534	Uniprot
826	T	Phosphorylation	Kinase	UL97	P16788	PSP
826	T	Phosphorylation	Kinase	CDK6	Q00534	PSP
826	T	Phosphorylation	Kinase	CDK2	P24941	PSP
826	T	Phosphorylation	Kinase	CDK4	P11802	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:11035041
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:17907805
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:11032804

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
567	S	Phosphorylation	-
Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth.
795	S	Phosphorylation	-
Dephosphorylated at Ser-795 by calcineruin upon calcium stimulation.
807	S	Methylation	16360038
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression.
807	S	Phosphorylation	-
CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition.
807	S	Phosphorylation	16360038
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression.
810	K	Methylation	16360038
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression.
810	K	Phosphorylation	16360038
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression.
811	S	Methylation	16360038
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression.
811	S	Phosphorylation	-
CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition.
811	S	Phosphorylation	16360038
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression.
821	T	Phosphorylation	-
Phosphorylation at Thr-821 and Thr-826 promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes.
826	T	Phosphorylation	-
Phosphorylation at Thr-821 and Thr-826 promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes.
860	K	Methylation	16360038
Monomethylation at Lys-860 by SMYD2 promotes interaction with L3MBTL1.
873	K	Acetylation	20940255
Acetylation at Lys-873 and Lys-874 regulates subcellular localization.
874	K	Acetylation	20940255
Acetylation at Lys-873 and Lys-874 regulates subcellular localization.

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 RB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUX1_HUMAN	CUX1	physical	12891711
CASP_HUMAN	CUX1	physical	12891711
TRAP1_HUMAN	TRAP1	physical	8756626
THOC1_HUMAN	THOC1	physical	7525595
BAG1_HUMAN	BAG1	physical	12845674
CTIP_HUMAN	RBBP8	physical	10779361
HDAC1_HUMAN	HDAC1	physical	10779361
ANDR_HUMAN	AR	physical	9813067
NCOA6_HUMAN	NCOA6	physical	14645241
CBX1_HUMAN	CBX1	physical	12711675
PELP1_HUMAN	PELP1	physical	12682072
P55G_HUMAN	PIK3R3	physical	12588990
PPARG_HUMAN	PPARG	physical	12479814
RBBP4_HUMAN	RBBP4	physical	11470869
E2F1_HUMAN	E2F1	physical	11470869
MO4L1_HUMAN	MORF4L1	physical	11500496
MOFA1_HUMAN	MRFAP1	physical	11500496
E2F1_HUMAN	E2F1	physical	12397079
MO4L1_HUMAN	MORF4L1	physical	12397079
BRCA1_HUMAN	BRCA1	physical	10220405
RBBP7_HUMAN	RBBP7	physical	10220405
HDAC1_HUMAN	HDAC1	physical	10615135
HDAC1_HUMAN	HDAC1	physical	11684023
HDAC1_HUMAN	HDAC1	physical	9491888
DNMT1_HUMAN	DNMT1	physical	10888886
HDAC1_HUMAN	HDAC1	physical	10490602
HDAC2_HUMAN	HDAC2	physical	10490602
HDAC3_HUMAN	HDAC3	physical	10490602
ARI4A_HUMAN	ARID4A	physical	10490602
HDAC1_HUMAN	HDAC1	physical	9724731
SMCA4_MOUSE	Smarca4	physical	7923370
SMCA4_HUMAN	SMARCA4	physical	7923370
RBBP7_HUMAN	RBBP7	physical	7503932
RBBP4_HUMAN	RBBP4	physical	7503932
RBBP4_HUMAN	RBBP4	physical	10734134
EID1_HUMAN	EID1	physical	11073990
TF3B_HUMAN	BRF1	physical	11997511
PRDM2_HUMAN	PRDM2	physical	7538672
SUV91_HUMAN	SUV39H1	physical	11484059
SUV91_HUMAN	SUV39H1	physical	11533237
CBX4_HUMAN	CBX4	physical	11583618
VDR_HUMAN	VDR	physical	11358960
KDM5A_HUMAN	KDM5A	physical	11358960
KDM5A_HUMAN	KDM5A	physical	7935440
CCND3_HUMAN	CCND3	physical	17972097
E2F1_HUMAN	E2F1	physical	8896460
PML_HUMAN	PML	physical	9448006
CCND1_HUMAN	CCND1	genetic	11126356
TAF1_HUMAN	TAF1	physical	11126356
PA2G4_HUMAN	PA2G4	physical	11268000
CCND1_HUMAN	CCND1	physical	8490963
MYC_HUMAN	MYC	physical	7838535
AATF_HUMAN	AATF	physical	12450794
ABL1_HUMAN	ABL1	physical	8242749
ATF2_HUMAN	ATF2	physical	1641004
SNW1_HUMAN	SNW1	physical	12466551
ARI3B_HUMAN	ARID3B	physical	10446990
MYOD1_HUMAN	MYOD1	physical	8381715
MCM7_HUMAN	MCM7	physical	9566894
SNPC1_HUMAN	SNAPC1	physical	11094070
SNPC3_HUMAN	SNAPC3	physical	11094070
TAF1_HUMAN	TAF1	physical	7724524
CCNT2_HUMAN	CCNT2	physical	12037672
CDK9_HUMAN	CDK9	physical	12037672
RAF1_HUMAN	RAF1	physical	9819434
E2F1_HUMAN	E2F1	physical	10869426
E2F4_HUMAN	E2F4	physical	10869426
E4F1_HUMAN	E4F1	physical	10869426
ENC1_HUMAN	ENC1	physical	9566959
RFC1_HUMAN	RFC1	physical	10353443
HMGB1_HUMAN	HMGB1	physical	11748221
RAF1_HUMAN	RAF1	physical	10523633
MDM2_HUMAN	MDM2	physical	10078201
JUN_HUMAN	JUN	physical	10026157
MAT1_HUMAN	MNAT1	physical	11113200
E2F2_HUMAN	E2F2	physical	12502741
TRIPB_HUMAN	TRIP11	physical	9256431
UBF1_HUMAN	UBTF	physical	11042686
AHR_HUMAN	AHR	physical	9712901
ARNT_HUMAN	ARNT	physical	9712901
AATF_HUMAN	AATF	physical	10783144
ANDR_HUMAN	AR	physical	9675141
CCNA1_HUMAN	CCNA1	physical	10022926
E2F1_HUMAN	E2F1	physical	7739537
TFDP1_HUMAN	TFDP1	physical	7739537
TFDP2_HUMAN	TFDP2	physical	7739537
E2F1_HUMAN	E2F1	physical	9422723
RBBP9_HUMAN	RBBP9	physical	9697699
TAF1_HUMAN	TAF1	physical	9242374
TBP_HUMAN	TBP	physical	9242374
TF3B_HUMAN	BRF1	physical	10330166
PHB_HUMAN	PHB	physical	10376528
CTIP_HUMAN	RBBP8	physical	9721205
HDAC1_HUMAN	HDAC1	physical	12473678
E2F1_HUMAN	E2F1	physical	12963846
SMCA4_HUMAN	SMARCA4	physical	19081374
ANDR_HUMAN	AR	physical	16964284
PHB_HUMAN	PHB	physical	16964284
ZBT7A_HUMAN	ZBTB7A	physical	18801742
SKP2_HUMAN	SKP2	physical	15469821
HMGA2_HUMAN	HMGA2	physical	16766265
E2F1_HUMAN	E2F1	physical	16766265
HDAC1_HUMAN	HDAC1	physical	16766265
KDM5B_HUMAN	KDM5B	physical	16645588
PAI2_HUMAN	SERPINB2	physical	16397580
DNMT1_HUMAN	DNMT1	physical	11847125
STAT3_HUMAN	STAT3	physical	15677471
E2F1_HUMAN	E2F1	physical	15670817
HDAC1_HUMAN	HDAC1	physical	11583987
HDAC2_HUMAN	HDAC2	physical	11583987
KDM1A_HUMAN	KDM1A	physical	18216119
E2F1_HUMAN	E2F1	physical	18216119
RAF1_HUMAN	RAF1	physical	15485920
ARI4A_HUMAN	ARID4A	physical	11283269
RBBP7_HUMAN	RBBP7	physical	11283269
RBBP4_HUMAN	RBBP4	physical	11283269
LIN9_HUMAN	LIN9	physical	15479636
LIN54_HUMAN	LIN54	physical	15479636
SP1_HUMAN	SP1	physical	11158299
HDAC1_HUMAN	HDAC1	physical	11158299
HDAC1_HUMAN	HDAC1	physical	10958676
HDAC3_HUMAN	HDAC3	physical	10958676
SMCA4_HUMAN	SMARCA4	physical	10778858
HDAC1_HUMAN	HDAC1	physical	10778858
SIN3A_MOUSE	Sin3a	physical	9988677
HDAC1_HUMAN	HDAC1	physical	9988677
KAT2B_HUMAN	KAT2B	physical	15044952
MDM2_HUMAN	MDM2	physical	15044952
HDAC1_HUMAN	HDAC1	physical	15044952
EID1_HUMAN	EID1	physical	15044952
FOXM1_HUMAN	FOXM1	physical	15024056
HDAC1_HUMAN	HDAC1	physical	15003538
HDAC1_HUMAN	HDAC1	physical	9468140
HDAC1_HUMAN	HDAC1	physical	9468139
HDAC1_HUMAN	HDAC1	physical	17827154
HDAC2_HUMAN	HDAC2	physical	17827154
DNJA2_HUMAN	DNAJA2	physical	17242198
PRDM2_HUMAN	PRDM2	physical	9223517
SMYD2_HUMAN	SMYD2	physical	20870719
RBBP7_HUMAN	RBBP7	physical	2005966
UHRF2_HUMAN	UHRF2	physical	21952639
TAL1_HUMAN	TAL1	physical	10866689
TFE2_HUMAN	TCF3	physical	10866689
HDAC1_HUMAN	HDAC1	physical	21900881
KAT5_HUMAN	KAT5	physical	16501607
TRI27_HUMAN	TRIM27	physical	15837424
E2F1_HUMAN	E2F1	physical	15837424
HDAC1_HUMAN	HDAC1	physical	10499802
E2F1_HUMAN	E2F1	physical	10499802
MDM2_HUMAN	MDM2	physical	16337594
PSA7_HUMAN	PSMA7	physical	16337594
PSD10_HUMAN	PSMD10	physical	10613832
CDC27_HUMAN	CDC27	physical	17187060
ANC2_HUMAN	ANAPC2	physical	17187060
CDC16_HUMAN	CDC16	physical	17187060
FZR1_HUMAN	FZR1	physical	17187060
TFDP1_HUMAN	TFDP1	physical	17187060
E2F1_HUMAN	E2F1	physical	20871633
MDM2_HUMAN	MDM2	physical	20871633
P53_HUMAN	TP53	physical	20871633
EBNA4_EBVB9	EBNA3B	physical	16352731
PSD10_HUMAN	PSMD10	physical	11900540
E2F1_HUMAN	E2F1	physical	11090181
VIE2_HCMVM	UL122	physical	9671498
UHRF1_HUMAN	UHRF1	physical	16007129
BRCA1_HUMAN	BRCA1	physical	10518542
CDC27_HUMAN	CDC27	physical	7756179
MDM2_HUMAN	MDM2	physical	15485814
E2F1_HUMAN	E2F1	physical	15485814
TF3B_HUMAN	BRF1	physical	9169441
RBBP9_HUMAN	RBBP9	physical	21689726
RBBP4_HUMAN	RBBP4	physical	21689726
MDM2_HUMAN	MDM2	physical	7791904
RBAK_HUMAN	RBAK	physical	10702291
E2F1_HUMAN	E2F1	physical	22768064
RBBP4_HUMAN	RBBP4	physical	8350924
PP1A_BOVIN	PPP1CA	physical	12434308
SMCA4_HUMAN	SMARCA4	physical	12434308
PP1A_HUMAN	PPP1CA	physical	12434308
SPI1_HUMAN	SPI1	physical	8434021
E2F1_HUMAN	E2F1	physical	17380128
E2F1_HUMAN	E2F1	physical	16249186
CEBPD_HUMAN	CEBPD	physical	15674331
MDM4_HUMAN	MDM4	physical	16510145
MDM2_HUMAN	MDM2	physical	16510145
PAX2_HUMAN	PAX2	physical	12200151
E2F1_HUMAN	E2F1	physical	8657117
E2F2_HUMAN	E2F2	physical	8657117
E2F3_HUMAN	E2F3	physical	8657117
E2F4_HUMAN	E2F4	physical	8657117
AHR_HUMAN	AHR	physical	10644764
TF2H1_HUMAN	GTF2H1	physical	22939629
PURA_HUMAN	PURA	physical	7592647
ABL1_HUMAN	ABL1	physical	8626527
E2F1_HUMAN	E2F1	physical	8626527
E2F1_HUMAN	E2F1	physical	10207050
PPIA_HUMAN	PPIA	physical	12210730
E2F1_HUMAN	E2F1	physical	9632788
BRE1B_HUMAN	RNF40	physical	10944455
E2F1_HUMAN	E2F1	physical	8255752
E2F4_HUMAN	E2F4	physical	9380698
TOP2A_HUMAN	TOP2A	physical	10393912
E2F1_HUMAN	E2F1	physical	12598654
CEBPB_HUMAN	CEBPB	physical	18628207
INS_HUMAN	INS	physical	7818556
CEBPB_HUMAN	CEBPB	physical	8552662
E2F1_HUMAN	E2F1	physical	8816798
E2F1_HUMAN	E2F1	physical	16374512
MDM2_HUMAN	MDM2	physical	16374512
KAT2B_HUMAN	KAT2B	physical	19249677
E2F1_HUMAN	E2F1	physical	19249677
E2F3_HUMAN	E2F3	physical	19249677
E2F1_HUMAN	E2F1	physical	12096339
HDAC1_HUMAN	HDAC1	physical	10228159
ANM2_HUMAN	PRMT2	physical	16616919
ATF2_HUMAN	ATF2	physical	11566021
MK14_HUMAN	MAPK14	physical	11566021
MK08_HUMAN	MAPK8	physical	11566021
E2F2_HUMAN	E2F2	physical	8246996
E2F3_HUMAN	E2F3	physical	8246996
E2F1_HUMAN	E2F1	physical	9315635
CEBPE_HUMAN	CEBPE	physical	12947005
E2F1_HUMAN	E2F1	physical	12947005
E2F1_HUMAN	E2F1	physical	18391203
AP2A_HUMAN	TFAP2A	physical	9632747
E2F4_HUMAN	E2F4	physical	7958924
E2F1_HUMAN	E2F1	physical	7958924
PP1A_HUMAN	PPP1CA	physical	8384581
PAX5_HUMAN	PAX5	physical	10197586
CDN1A_HUMAN	CDKN1A	physical	10486249
CDN1C_HUMAN	CDKN1C	physical	10486249
ENC1_HUMAN	ENC1	physical	16306221
NFM_HUMAN	NEFM	physical	20195357
UBP7_HUMAN	USP7	physical	24823443
ABL1_HUMAN	ABL1	physical	7828850
E2F1_HUMAN	E2F1	physical	7828850
RAF1_HUMAN	RAF1	physical	19058874
EP300_HUMAN	EP300	physical	16878158
MDM2_HUMAN	MDM2	physical	11433299
E2F1_HUMAN	E2F1	physical	23001041
PAX8_HUMAN	PAX8	physical	21602887
PP1A_HUMAN	PPP1CA	physical	17008050
TF3C2_HUMAN	GTF3C2	physical	9169441
GRB2_HUMAN	GRB2	physical	25814554
KDM5B_HUMAN	KDM5B	physical	15803180
BAG6_HUMAN	BAG6	physical	26496610
UBL4A_HUMAN	UBL4A	physical	26496610
HERC4_HUMAN	HERC4	physical	26496610
RPR1B_HUMAN	RPRD1B	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610
PPR26_HUMAN	PPP1R26	physical	26442585
MDM2_HUMAN	MDM2	physical	25703327
MDM4_HUMAN	MDM4	physical	25703327
TASOR_HUMAN	FAM208A	physical	18726359
LT_SV40	SV40gp6	physical	10570441
PCGF3_HUMAN	PCGF3	physical	27173435
HDAC1_HUMAN	HDAC1	physical	10891495
E2F1_HUMAN	E2F1	physical	10891495
VE7_HPV16	E7	physical	10891495
CCND3_HUMAN	CCND3	physical	9003773
MDM2_HUMAN	MDM2	physical	9003773
LT_SV40	SV40gp6	physical	25056122

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
180200	Childhood cancer retinoblastoma (RB)
109800	Bladder cancer (BLC)
259500	Osteogenic sarcoma (OSRC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00030	Insulin Regular

Regulatory Network of RB_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-548 AND LYS-896, AND MASSSPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Methylation of the retinoblastoma tumor suppressor by SMYD2."; Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M.,Gozani O., Sage J.; J. Biol. Chem. 285:37733-37740(2010). Cited for: METHYLATION AT LYS-860, INTERACTION WITH L3MBTL1, AND MUTAGENESIS OFLYS-860; LYS-870 AND 873-LYS-LYS-874.	20870719 [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-37; SER-249; THR-252;THR-373; SER-807; SER-811; THR-821; THR-823; THR-826; THR-841 ANDSER-882, 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-249; THR-821 ANDTHR-823, 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-37; SER-249; THR-252;SER-807; SER-811; THR-823; THR-826 AND SER-855, AND MASS SPECTROMETRY.	18669648 [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-249; THR-252; THR-356AND THR-373, AND MASS SPECTROMETRY.	18220336 [Abstract]
"Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex betweenpRB and E2F-1 after DNA damage."; Inoue Y., Kitagawa M., Taya Y.; EMBO J. 26:2083-2093(2007). Cited for: PHOSPHORYLATION AT SER-612 BY CHEK2, AND INTERACTION WITH CHEK2.	17380128 [Abstract]
"Cyclin C/cdk3 promotes Rb-dependent G0 exit."; Ren S., Rollins B.J.; Cell 117:239-251(2004). Cited for: FUNCTION IN G0-G1 TRANSITION, AND PHOSPHORYLATION AT SER-807 ANDSER-811 BY CDK3.	15084261 [Abstract]
"Cdk phosphorylation triggers sequential intramolecular interactionsthat progressively block Rb functions as cells move through G1."; Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.; Cell 98:859-869(1999). Cited for: PHOSPHORYLATION AT SER-567 BY CDK2, AND PHOSPHORYLATION BY CDK4 ANDCDK6.	10499802 [Abstract]
"The retinoblastoma protein is phosphorylated on multiple sites byhuman cdc2."; Lees J.A., Buchkovich K.J., Marshak D.R., Anderson C.W., Harlow E.; EMBO J. 10:4279-4290(1991). Cited for: PHOSPHORYLATION AT SER-249; THR-252; THR-373; SER-807 AND SER-811.	1756735 [Abstract]
"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanismfor phosphorylation-induced E2F release."; Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.; Cell 123:1093-1106(2005). Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 829-874 IN COMPLEX WITH E2F1AND TFDP1, INTERACTION WITH HETERODIMERIC COMPLEXES CONTAINING TFDP1AND EITHER E2F1; E2F3; E2F4 OR E2F5, MUTAGENESIS OF THR-821 ANDTHR-826, AND PHOSPHORYLATION AT THR-821 AND THR-826.	16360038 [Abstract]
"Preferences for phosphorylation sites in the retinoblastoma proteinof D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro."; Takaki T., Fukasawa K., Suzuki-Takahashi I., Semba K., Kitagawa M.,Taya Y., Hirai H.; J. Biochem. 137:381-386(2005). Cited for: PHOSPHORYLATION AT THR-821 AND THR-826.	15809340 [Abstract]

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