dbPTM

RB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RB_MOUSE
UniProt AC	P13405
Protein Name	Retinoblastoma-associated protein
Gene Name	Rb1
Organism	Mus musculus (Mouse).
Sequence Length	921
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)..
Protein Sequence	MPPKAPRRAAAAEPPPPPPPPPREDDPAQDSGPEELPLARLEFEEIEEPEFIALCQKLKVPDHVRERAWLTWEKVSSVDGILEGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKSIETSVYKFFDLLKEIDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSMLVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFIKFSPPALLREPYKTAAIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFINSLGIVSSNGLPEVESLSKRYEEVYLKNKDLDARLFLDHDKTLQTDPIDSFETERTPRKNNPDEEANVVTPHTPVRTVMNTIQQLMVILNSASDQPSENLISYFNNCTVNPKENILKRVKDVGHIFKEKFANAVGQGCVDIGVQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTLQHLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDGEGPDNLEPACPLSLPLQGNHTAADMYLSPLRSPKKRTSTTRVNSAANTETQAASAFHTQKPLKSTSLALFYKKVYRLAYLRLNTLCARLLSDHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGADEADGSKHLPAESKFQQKLAEMTSTRTRMQKQRMNESKDVSNKEEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MPPKAPRRA ------CCCCCCCCC	38.81	20668449
31	Phosphorylation	EDDPAQDSGPEELPL CCCCCCCCCCCCCCC	44.14	25521595
57	Ubiquitination	EFIALCQKLKVPDHV HHHHHHHHCCCCHHH	49.64	-
120	Phosphorylation	ELQKSIETSVYKFFD HHHHHHHHHHHHHHH	23.09	28576409
123	Phosphorylation	KSIETSVYKFFDLLK HHHHHHHHHHHHHHH	11.22	28576409
224	Phosphorylation	VDYFIKFSPPALLRE HHHHHHCCCHHHHCC	25.60	22817900
235	Phosphorylation	LLREPYKTAAIPING HHCCCCCCCEEECCC	18.58	27087446
243	Phosphorylation	AAIPINGSPRTPRRG CEEECCCCCCCCCCC	13.51	27087446
246	Phosphorylation	PINGSPRTPRRGQNR ECCCCCCCCCCCCCH	25.24	12417722
336	Phosphorylation	LFLDHDKTLQTDPID HCCCCCCCCCCCCCC	30.10	25777480
339	Phosphorylation	DHDKTLQTDPIDSFE CCCCCCCCCCCCCCC	47.02	25777480
344	Phosphorylation	LQTDPIDSFETERTP CCCCCCCCCCCCCCC	26.21	26745281
347	Phosphorylation	DPIDSFETERTPRKN CCCCCCCCCCCCCCC	28.85	25266776
350	Phosphorylation	DSFETERTPRKNNPD CCCCCCCCCCCCCCC	22.63	21082442
364	Phosphorylation	DEEANVVTPHTPVRT CHHCCCCCCCCHHHH	12.69	27149854
367	Phosphorylation	ANVVTPHTPVRTVMN CCCCCCCCHHHHHHH	25.36	26824392
440	Phosphorylation	VDIGVQRYKLGVRLY EECCCCCCCHHHHHH	8.09	-
561	Phosphorylation	SLAWLSDSPLFDLIK HHHHHCCCCHHHHHH	21.81	22817900
586	Phosphorylation	LEPACPLSLPLQGNH CCCCCCCCCCCCCCC	17.06	25159016
594	Phosphorylation	LPLQGNHTAADMYLS CCCCCCCCCCHHHCC	27.78	25293948
599	Phosphorylation	NHTAADMYLSPLRSP CCCCCHHHCCCCCCC	12.46	25159016
601	Phosphorylation	TAADMYLSPLRSPKK CCCHHHCCCCCCCCC	12.37	21082442
605	Phosphorylation	MYLSPLRSPKKRTST HHCCCCCCCCCCCCC	49.07	21082442
617	Phosphorylation	TSTTRVNSAANTETQ CCCCCCCCCCCCHHH	26.38	26824392
621	Phosphorylation	RVNSAANTETQAASA CCCCCCCCHHHHHHH	35.37	29550500
713	Sumoylation	KVKNIDLKFKIIVTA EEECCCEEEEEEEEE	40.64	-
719	Phosphorylation	LKFKIIVTAYKDLPH EEEEEEEEECCCCCH	17.54	21183079
721	Phosphorylation	FKIIVTAYKDLPHAA EEEEEEECCCCCHHH	8.82	21183079
764	Phosphorylation	LKTNILQYASTRPPT HHHHHHHHHCCCCCC	10.08	26643407
766	Phosphorylation	TNILQYASTRPPTLS HHHHHHHCCCCCCCC	21.73	26643407
767	Phosphorylation	NILQYASTRPPTLSP HHHHHHCCCCCCCCC	38.74	26643407
771	Phosphorylation	YASTRPPTLSPIPHI HHCCCCCCCCCCCCC	42.42	25266776
773	Phosphorylation	STRPPTLSPIPHIPR CCCCCCCCCCCCCCC	24.22	21082442
781	Phosphorylation	PIPHIPRSPYKFSSS CCCCCCCCCCCCCCC	27.51	25266776
783	Phosphorylation	PHIPRSPYKFSSSPL CCCCCCCCCCCCCCC	26.38	26643407
786	Phosphorylation	PRSPYKFSSSPLRIP CCCCCCCCCCCCCCC	26.25	26745281
787	Phosphorylation	RSPYKFSSSPLRIPG CCCCCCCCCCCCCCC	38.82	26745281
788	Phosphorylation	SPYKFSSSPLRIPGG CCCCCCCCCCCCCCC	27.10	22942356
798	Phosphorylation	RIPGGNIYISPLKSP CCCCCCEEEECCCCC	10.19	27600695
800	Phosphorylation	PGGNIYISPLKSPYK CCCCEEEECCCCCCC	13.75	17045206
803	Ubiquitination	NIYISPLKSPYKISE CEEEECCCCCCCCCC	53.41	22790023
803	Methylation	NIYISPLKSPYKISE CEEEECCCCCCCCCC	53.41	-
804	Phosphorylation	IYISPLKSPYKISEG EEEECCCCCCCCCCC	40.94	17045206
806	Phosphorylation	ISPLKSPYKISEGLP EECCCCCCCCCCCCC	28.22	26643407
809	Phosphorylation	LKSPYKISEGLPTPT CCCCCCCCCCCCCCC	22.81	22817900
814	Phosphorylation	KISEGLPTPTKMTPR CCCCCCCCCCCCCCC	48.94	12417722
816	Phosphorylation	SEGLPTPTKMTPRSR CCCCCCCCCCCCCCE	35.61	26824392
818	Oxidation	GLPTPTKMTPRSRIL CCCCCCCCCCCCEEE	7.40	17242355
819	Phosphorylation	LPTPTKMTPRSRILV CCCCCCCCCCCEEEE	19.67	26824392
834	Phosphorylation	SIGESFGTSEKFQKI ECCHHCCCHHHHHHH	31.53	27600695
835	Phosphorylation	IGESFGTSEKFQKIN CCHHCCCHHHHHHHH	38.89	26745281
848	Phosphorylation	INQMVCNSDRVLKRS HHHHHHCCHHHHHHH	22.97	25266776
853	Methylation	CNSDRVLKRSAEGGN HCCHHHHHHHCCCCC	41.26	-
866	Acetylation	GNPPKPLKKLRFDIE CCCCCCHHHCCEEEC	59.28	-
867	Acetylation	NPPKPLKKLRFDIEG CCCCCHHHCCEEECC	53.21	-

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
243	S	Phosphorylation	Kinase	CDK4	P30285	PSP
243	S	Phosphorylation	Kinase	CDK6	Q64261	PSP
246	T	Phosphorylation	Kinase	CDK4	P30285	PSP
246	T	Phosphorylation	Kinase	CDK6	Q64261	PSP
561	S	Phosphorylation	Kinase	CDK2	P97377	Uniprot
800	S	Phosphorylation	Kinase	CDK4	P30285	PSP
800	S	Phosphorylation	Kinase	CDK6	Q64261	PSP
804	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
804	S	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS
804	S	Phosphorylation	Kinase	CDK4	P30285	PSP
804	S	Phosphorylation	Kinase	CDK6	Q64261	PSP
819	T	Phosphorylation	Kinase	CDK4	P30285	PSP
819	T	Phosphorylation	Kinase	CDK6	Q64261	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
561	S	Phosphorylation	8336704
Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth.
788	S	Phosphorylation	8336704
Dephosphorylated at Ser-788 by calcineruin upon calcium stimulation.
800	S	Methylation	20668449
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression.
800	S	Phosphorylation	8336704
CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition (By similarity).
800	S	Phosphorylation	20668449
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression.
803	K	Methylation	20668449
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression.
803	K	Phosphorylation	20668449
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression.
804	S	Methylation	20668449
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression.
804	S	Phosphorylation	8336704
CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition (By similarity).
804	S	Phosphorylation	20668449
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression.
853	K	Methylation	20668449
Monomethylation at Lys-853 by SMYD2 promotes interaction with L3MBTL1 (By similarity).
866	K	Acetylation	20940255
Acetylation at Lys-866 and Lys-867 regulates subcellular localization during keratinocytes differentiation (By similarity).
867	K	Acetylation	20940255
Acetylation at Lys-866 and Lys-867 regulates subcellular localization during keratinocytes differentiation (By similarity).

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_MOUSE	Hdac1	physical	11684023
SMCA4_MOUSE	Smarca4	physical	7923370
GATA1_HUMAN	GATA1	physical	19513100
HDAC1_MOUSE	Hdac1	physical	19633359
HMGA1_MOUSE	Hmga1	physical	19633359
HMGA2_MOUSE	Hmga2	physical	16766265
HDAC1_MOUSE	Hdac1	physical	10409740
PSD10_MOUSE	Psmd10	physical	17292836
RBAK_MOUSE	Rbak	physical	10702291
PP1A_BOVIN	PPP1CA	physical	12434308
NDF1_MOUSE	Neurod1	physical	15701640
CEBPB_MOUSE	Cebpb	physical	8946919
MO4L1_MOUSE	Morf4l1	physical	15367658
MOFA1_MOUSE	Mrfap1	physical	15367658
JARD2_MOUSE	Jarid2	physical	15870077
PAX2_MOUSE	Pax2	physical	12200151
KPCB_MOUSE	Prkcb	physical	11805327

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RB_MOUSE

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"NRMT is an alpha-N-methyltransferase that methylates RCC1 andretinoblastoma protein."; Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; Nature 466:1125-1128(2010). Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2.	20668449 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-819, AND MASSSPECTROMETRY.	17242355 [Abstract]

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