dbPTM

RBL2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBL2_MOUSE
UniProt AC	Q64700
Protein Name	Retinoblastoma-like protein 2
Gene Name	Rbl2
Organism	Mus musculus (Mouse).
Sequence Length	1135
Subcellular Localization	Nucleus.
Protein Description	Key regulator of entry into cell division. 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 KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor..
Protein Sequence	MASGGNQSPPPPPAAAASSEEEEEDGDAADRAQPAGSPSHQIQQRFEELCSRLNMDEAARAEAWSSYRSMSESYTLEGNDLHWLACALYVACRKSVPTVSKGTAEGNYVSLTRILRCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEQPRQQRGRKQRRQPCTTSEIFHFCWVLFIYAKGNFPMISDDLVNSYHLLLCALDLVYGNALQCSNRKELVNPNFKGLSEDCHPKDSKASSDPPCVIEKLCSLHDGLVLEAKGIKEHFWKPYIRKLFEKKLLKGKEENLTGFLEPGNFGESFKAVNKAYEEYVLAAGNLDERVFLGEDAEEEVGTLSRCLSAASGTESAERTQMRDILQQHLDKSKALRVCTPLTGVRYVQENSPCVTPVSTAAHSLSRLHTMLSGLRNAPSEKLERILRSCSRDPTQAIADRLKEMYEIYSQHFQPDENFSNCAKEIANKHFRFAEMLYYKVLESVIEQEQKRLGDMDLSGVLEHDAFHRSLLACCLEVVAFSHKPPGNFPFIAEIFDVPHYHFYKVIEVFIRAEDGLCREVVKHLNQIEEQILDHLAWKTKSPLWDRIRDNENRVPTCEEVMPPQNLERTDEIYIAGSPLTPRRVGEVRADAGGLGRSITSPTTLYDRYSSPTVSTTRRRLFENDSPSEGSTSGRIPPQPLVNAVPVQNVPGETVSVTPVPGQTLVTMATATVTANNGQTVTIPVQGIANENGGITFFPVQVNVGGQAQAVAGSIQPLSAQALAGSLSSQQVTGTTLQVPGPVAIQQISPGGQQQNPGQPLTSSSIRPRKTSSLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMRCYRTQPQARSQVYRSVLIKGKRRNSGSSESRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGASSDVEEEERGDLIQFYNNIYRKQIQAFAMKYSQANAQTDTPPLSPYPFVRTGSPRRVQLSQSHPIYISPHNNEAMPSPREKIFYYFSNSPSKRLREINSMIRTGETPTKKRGILLDDGSESPAKRICPENHSALLRRLQDVANDRGSQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASGGNQSPP -----CCCCCCCCCC	60.12	30635358
8	Phosphorylation	MASGGNQSPPPPPAA CCCCCCCCCCCCCCC	43.29	25293948
18	Phosphorylation	PPPAAAASSEEEEED CCCCCCCCCHHHHCC	33.29	25338131
19	Phosphorylation	PPAAAASSEEEEEDG CCCCCCCCHHHHCCC	44.28	25338131
37	Phosphorylation	DRAQPAGSPSHQIQQ HHCCCCCCHHHHHHH	25.90	25521595
39	Phosphorylation	AQPAGSPSHQIQQRF CCCCCCHHHHHHHHH	29.71	28833060
101	Ubiquitination	KSVPTVSKGTAEGNY HCCCCCCCCCCCCCE	56.81	22790023
128	Acetylation	SLIEFFNKMKKWEDM HHHHHHHHHHCHHHH	47.11	20676144
130	Acetylation	IEFFNKMKKWEDMAN HHHHHHHHCHHHHHC	57.24	20676144
367	Phosphorylation	GTLSRCLSAASGTES HHHHHHHHHHCCCCH	25.97	28833060
370	Phosphorylation	SRCLSAASGTESAER HHHHHHHCCCCHHHH	46.06	28833060
372	Phosphorylation	CLSAASGTESAERTQ HHHHHCCCCHHHHHH	25.03	28833060
398	Phosphorylation	SKALRVCTPLTGVRY HHHHCCCCCCCCCCE	20.62	27600695
405	Phosphorylation	TPLTGVRYVQENSPC CCCCCCCEECCCCCC	12.22	28833060
410	Phosphorylation	VRYVQENSPCVTPVS CCEECCCCCCCCCCH	20.94	21082442
414	Phosphorylation	QENSPCVTPVSTAAH CCCCCCCCCCHHHHH	25.37	21082442
417	Phosphorylation	SPCVTPVSTAAHSLS CCCCCCCHHHHHHHH	17.33	28833060
628	Phosphorylation	PPQNLERTDEIYIAG CCCCCCCCCEEEECC	28.71	25619855
632	Phosphorylation	LERTDEIYIAGSPLT CCCCCEEEECCCCCC	5.22	25619855
636	Phosphorylation	DEIYIAGSPLTPRRV CEEEECCCCCCCCCC	14.02	26824392
639	Phosphorylation	YIAGSPLTPRRVGEV EECCCCCCCCCCCEE	20.38	21082442
656	Phosphorylation	DAGGLGRSITSPTTL CCCCCCCCCCCCCCH	28.55	26643407
658	Phosphorylation	GGLGRSITSPTTLYD CCCCCCCCCCCCHHH	29.87	26643407
659	Phosphorylation	GLGRSITSPTTLYDR CCCCCCCCCCCHHHC	20.69	26824392
661	Phosphorylation	GRSITSPTTLYDRYS CCCCCCCCCHHHCCC	29.24	28066266
662	Phosphorylation	RSITSPTTLYDRYSS CCCCCCCCHHHCCCC	27.06	28066266
664	Phosphorylation	ITSPTTLYDRYSSPT CCCCCCHHHCCCCCC	9.04	26643407
667	Phosphorylation	PTTLYDRYSSPTVST CCCHHHCCCCCCCCC	15.59	28066266
668	Phosphorylation	TTLYDRYSSPTVSTT CCHHHCCCCCCCCCC	30.64	28066266
669	Phosphorylation	TLYDRYSSPTVSTTR CHHHCCCCCCCCCCC	18.69	30352176
671	Phosphorylation	YDRYSSPTVSTTRRR HHCCCCCCCCCCCCH	29.09	28066266
684	Phosphorylation	RRLFENDSPSEGSTS CHHCCCCCCCCCCCC	41.74	25521595
686	Phosphorylation	LFENDSPSEGSTSGR HCCCCCCCCCCCCCC	59.55	28066266
935	Phosphorylation	IKGKRRNSGSSESRS HCCCCCCCCCCCCCC	37.94	23684622
938	Phosphorylation	KRRNSGSSESRSHQN CCCCCCCCCCCCCCC	43.02	25195567
940	Phosphorylation	RNSGSSESRSHQNSP CCCCCCCCCCCCCCC	40.82	25195567
942	Phosphorylation	SGSSESRSHQNSPTE CCCCCCCCCCCCCCH	38.41	25521595
946	Phosphorylation	ESRSHQNSPTELNTD CCCCCCCCCCHHCCC	26.99	25521595
948	Phosphorylation	RSHQNSPTELNTDRA CCCCCCCCHHCCCCC	53.58	25521595
952	Phosphorylation	NSPTELNTDRASRDS CCCCHHCCCCCCCCC	39.21	29472430
956	Phosphorylation	ELNTDRASRDSSPVM HHCCCCCCCCCCCCC	37.20	22817900
959	Phosphorylation	TDRASRDSSPVMRSN CCCCCCCCCCCCCCC	35.12	25266776
960	Phosphorylation	DRASRDSSPVMRSNS CCCCCCCCCCCCCCC	26.29	25521595
965	Phosphorylation	DSSPVMRSNSTLPVP CCCCCCCCCCCCCCC	19.62	22817900
967	Phosphorylation	SPVMRSNSTLPVPQP CCCCCCCCCCCCCCC	32.35	19060867
968	Phosphorylation	PVMRSNSTLPVPQPS CCCCCCCCCCCCCCC	39.05	19060867
975	Phosphorylation	TLPVPQPSSAPPTPT CCCCCCCCCCCCCCC	33.61	26643407
976	Phosphorylation	LPVPQPSSAPPTPTR CCCCCCCCCCCCCCC	52.02	24723360
980	Phosphorylation	QPSSAPPTPTRLTGA CCCCCCCCCCCCCCC	35.91	24723360
982	Phosphorylation	SSAPPTPTRLTGASS CCCCCCCCCCCCCCC	40.57	26643407
988	Phosphorylation	PTRLTGASSDVEEEE CCCCCCCCCCCCHHH	28.54	28833060
989	Phosphorylation	TRLTGASSDVEEEER CCCCCCCCCCCHHHH	45.18	28833060
1025	Phosphorylation	YSQANAQTDTPPLSP HHHHCCCCCCCCCCC	39.16	26745281
1027	Phosphorylation	QANAQTDTPPLSPYP HHCCCCCCCCCCCCC	30.14	25266776
1031	Phosphorylation	QTDTPPLSPYPFVRT CCCCCCCCCCCCCCC	28.32	25266776
1033	Phosphorylation	DTPPLSPYPFVRTGS CCCCCCCCCCCCCCC	13.11	25266776
1038	Phosphorylation	SPYPFVRTGSPRRVQ CCCCCCCCCCCCEEE	36.39	22817900
1040	Phosphorylation	YPFVRTGSPRRVQLS CCCCCCCCCCEEEEC	18.02	22817900
1047	Phosphorylation	SPRRVQLSQSHPIYI CCCEEEECCCCCEEE	16.73	29899451
1049	Phosphorylation	RRVQLSQSHPIYISP CEEEECCCCCEEECC	28.05	29899451
1055	Phosphorylation	QSHPIYISPHNNEAM CCCCEEECCCCCCCC	11.79	25266776
1064	Phosphorylation	HNNEAMPSPREKIFY CCCCCCCCCHHHHHH	24.41	26824392
1068	Acetylation	AMPSPREKIFYYFSN CCCCCHHHHHHEECC	39.12	20676144
1074	Phosphorylation	EKIFYYFSNSPSKRL HHHHHEECCCHHHHH	21.92	25266776
1076	Phosphorylation	IFYYFSNSPSKRLRE HHHEECCCHHHHHHH	29.38	25266776
1078	Phosphorylation	YYFSNSPSKRLREIN HEECCCHHHHHHHHH	30.17	26643407
1079	Acetylation	YFSNSPSKRLREINS EECCCHHHHHHHHHH	59.86	20676144
1093	Phosphorylation	SMIRTGETPTKKRGI HHHHCCCCCCCCCCE	37.29	-
1106	Phosphorylation	GILLDDGSESPAKRI CEECCCCCCCCHHHH	41.73	28833060
1108	Phosphorylation	LLDDGSESPAKRICP ECCCCCCCCHHHHCC	31.67	25521595
1111	Acetylation	DGSESPAKRICPENH CCCCCCHHHHCCCCH	45.76	20676144
1134	Phosphorylation	DVANDRGSQ------ HHHHHCCCC------	33.34	25338131

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 RBL2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
636	S	Phosphorylation	17242355
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (By similarity).
636	S	ubiquitylation	17242355
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (By similarity).
669	S	Phosphorylation	-
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (By similarity).
669	S	ubiquitylation	-
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (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 RBL2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
EZH2_MOUSE	Ezh2	physical	15077161
HDAC1_MOUSE	Hdac1	physical	9823308

Drug and Disease Associations

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

Regulatory Network of RBL2_MOUSE

Related Literatures of Post-Translational Modification

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 SER-410; THR-414; SER-636;THR-639; SER-942 AND THR-1027, AND MASS SPECTROMETRY.	17242355 [Abstract]

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