RBL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RBL1_MOUSE
• UniProt AC: Q64701
• Protein Name: Retinoblastoma-like protein 1
• Gene Name: Rbl1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1063
• 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. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor..
• Protein Sequence: MFEDEPHAEGAAAVAAAREALQALCQELNLDEGSAAEALDDFTAIRGNYSLEGEVIHWLACSLYVACRKSIIPTVGKGVMEGNCVSLTRILRSAKLSLIQFFSKMKKWMDMSNLPQEFRERIERLERNFEVSTVIFKKFEPIFLDIFQNPYEEPPKLPRSRKQRRIPCSVKDLFNFCWTLFVYTKGNFRMIGDDLVNSYHLLLCCLDLIFANAIMCPNRRDLLNPSFKGLPSDFHAPDFKAAEEPPCIIAVLCDLHDGLLVEAKGIKEHYFKPYISKLFDKKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTADTPFGKLTSQASVECNLQQHFEKKRSFAPSTPLTGRRYLQEKEAVTTPVASATQSVSRLQSIVAGLKSAPSEQLLNIFESCMRNPMGNIIKIVKGIGETFCQHYTQSTDKQPGSHIDFAVNRLKLAEILYYKILETIMVQETRRLHGMDMSVLLEQDIFHKSLMACCLEIVLFAYSSPRTFPWIIEVLDLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLAWTNNSALWEALHASANRVPSCEEVIFPNNFEIGNGGNVQGHLPMMPMSPIIHPRVKEVRTDSGSLRQDMQPLSPISVHERYSSPAAGSAKRRLFGDDPPKDTLMDKIMAEGTKLKIAPSSVTAESLSISPGQALLTMATTTVTGTTGRKVTVPLHGIANDAGEITLVPISMNPTQESTAESPVSLTAQSLIGTSPKQTHLTKAQDAHLTGVSKPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIMKSYRNQPQANSHVYRSVLLKSIPGGVVVYNGDCEMTDGDIEDATKTPNCSSEPVKEERGDLIKFYNTVYVGRVKSFALKYDLSNQDHIMDAPPLSPFPHIKQQPGSPRRISQQHSLYVSPHKNGAGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQKTKKRVIAISGDADSPAKRLCQENDDVLLKRLQDVVSERANH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
332	Phosphorylation	DAEEEIGTPRKFTAD CCHHHHCCCCCEECC	26.11	27087446
337	Phosphorylation	IGTPRKFTADTPFGK HCCCCCEECCCCCCC	27.02	28066266
340	Phosphorylation	PRKFTADTPFGKLTS CCCEECCCCCCCCCC	20.32	24453211
346	Phosphorylation	DTPFGKLTSQASVEC CCCCCCCCCCCHHHH	23.44	30635358
347	Phosphorylation	TPFGKLTSQASVECN CCCCCCCCCCHHHHH	33.90	26643407
350	Phosphorylation	GKLTSQASVECNLQQ CCCCCCCHHHHHHHH	15.71	25266776
364	Phosphorylation	QHFEKKRSFAPSTPL HHHHHCCCCCCCCCC	34.34	25777480
368	Phosphorylation	KKRSFAPSTPLTGRR HCCCCCCCCCCCCHH	38.95	24453211
369	Phosphorylation	KRSFAPSTPLTGRRY CCCCCCCCCCCCHHH	22.66	26824392
372	Phosphorylation	FAPSTPLTGRRYLQE CCCCCCCCCHHHHHH	29.82	29472430
384	Phosphorylation	LQEKEAVTTPVASAT HHHHHCCCCCCCHHH	32.22	22942356
385	Phosphorylation	QEKEAVTTPVASATQ HHHHCCCCCCCHHHH	14.79	26824392
389	Phosphorylation	AVTTPVASATQSVSR CCCCCCCHHHHHHHH	31.89	25619855
391	Phosphorylation	TTPVASATQSVSRLQ CCCCCHHHHHHHHHH	20.91	25619855
615	Phosphorylation	HLPMMPMSPIIHPRV CCCCCCCCCCCCCCE	13.69	25293948
627	Phosphorylation	PRVKEVRTDSGSLRQ CCEEEEECCCCCCCC	39.43	25777480
629	Phosphorylation	VKEVRTDSGSLRQDM EEEEECCCCCCCCCC	29.66	25266776
631	Phosphorylation	EVRTDSGSLRQDMQP EEECCCCCCCCCCCC	25.08	25777480
640	Phosphorylation	RQDMQPLSPISVHER CCCCCCCCCCCHHHC	27.20	22942356
643	Phosphorylation	MQPLSPISVHERYSS CCCCCCCCHHHCCCC	22.32	25159016
649	Phosphorylation	ISVHERYSSPAAGSA CCHHHCCCCCCCCCH	35.75	26745281
650	Phosphorylation	SVHERYSSPAAGSAK CHHHCCCCCCCCCHH	15.04	24453211
692	Phosphorylation	PSSVTAESLSISPGQ CCCCCHHHCCCCCCC	25.59	27600695
694	Phosphorylation	SVTAESLSISPGQAL CCCHHHCCCCCCCEE	30.24	27600695
696	Phosphorylation	TAESLSISPGQALLT CHHHCCCCCCCEEEE	21.43	25266776
703	Phosphorylation	SPGQALLTMATTTVT CCCCEEEEEEEEEEE	12.95	25266776
748	Phosphorylation	TQESTAESPVSLTAQ CCCCCCCCCCEEEHH	28.30	-
761	Phosphorylation	AQSLIGTSPKQTHLT HHHHHCCCCCCCCCC	25.53	22817900
795	Phosphorylation	ALFYRKVYHLASVRL HHHHHHHHHHHHHHH	8.31	22817900
799	Phosphorylation	RKVYHLASVRLRDLC HHHHHHHHHHHHHHH	17.71	22817900
866	Phosphorylation	TFQEIMKSYRNQPQA HHHHHHHHHCCCCCC	16.37	25338131
910	Phosphorylation	DIEDATKTPNCSSEP CHHHCCCCCCCCCCC	18.51	24453211
959	Phosphorylation	IMDAPPLSPFPHIKQ CCCCCCCCCCCCCCC	30.21	26824392
970	Phosphorylation	HIKQQPGSPRRISQQ CCCCCCCCCCCCCCC	23.16	-
975	Phosphorylation	PGSPRRISQQHSLYV CCCCCCCCCCCCEEE	23.21	27600695
979	Phosphorylation	RRISQQHSLYVSPHK CCCCCCCCEEECCCC	19.63	28066266
981	Phosphorylation	ISQQHSLYVSPHKNG CCCCCCEEECCCCCC	11.25	25159016
983	Phosphorylation	QQHSLYVSPHKNGAG CCCCEEECCCCCCCC	14.02	26824392
992	Phosphorylation	HKNGAGLTPRSALLY CCCCCCCCCHHHHHH	18.75	25266776
1004	Phosphorylation	LLYKFNGSPSKSLKD HHHHHCCCCCCCHHH	27.40	24453211
1006	Phosphorylation	YKFNGSPSKSLKDIN HHHCCCCCCCHHHHH	36.25	25293948
1031	Phosphorylation	KKRVIAISGDADSPA CCCEEEEECCCCCHH	22.92	25619855
1036	Phosphorylation	AISGDADSPAKRLCQ EEECCCCCHHHHHHH	28.60	26824392

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RBL1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
332	T	Phosphorylation	Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4.	21183079
640	S	Phosphorylation	Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4.	-
959	S	Phosphorylation	Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4.	21183079
970	S	Phosphorylation	Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RBL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLX3_MOUSE	Tlx3	physical	20211142
NDF1_MOUSE	Neurod1	physical	15701640
RBL1_MOUSE	Rbl1	physical	15701640

Drug and Disease Associations

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