dbPTM

RBL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBL1_HUMAN
UniProt AC	P28749
Protein Name	Retinoblastoma-like protein 1
Gene Name	RBL1
Organism	Homo sapiens (Human).
Sequence Length	1068
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	MFEDKPHAEGAAVVAAAGEALQALCQELNLDEGSAAEALDDFTAIRGNYSLEGEVTHWLACSLYVACRKSIIPTVGKGIMEGNCVSLTRILRSAKLSLIQFFSKMKKWMDMSNLPQEFRERIERLERNFEVSTVIFKKYEPIFLDIFQNPYEEPPKLPRSRKQRRIPCSVKDLFNFCWTLFVYTKGNFRMIGDDLVNSYHLLLCCLDLIFANAIMCPNRQDLLNPSFKGLPSDFHTADFTASEEPPCIIAVLCELHDGLLVEAKGIKEHYFKPYISKLFDRKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTRDTPLGKLTAQANVEYNLQQHFEKKRSFAPSTPLTGRRYLREKEAVITPVASATQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTDEQPGSHIDFAVNRLKLAEILYYKILETVMVQETRRLHGMDMSVLLEQDIFHRSLMACCLEIVLFAYSSPRTFPWIIEVLNLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLAWSHDSALWEALQVSANKVPTCEEVIFPNNFETGNGGNVQGHLPLMPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSSSITAENVSILPGQTLLTMATAPVTGTTGHKVTIPLHGVANDAGEITLIPLSMNTNQESKVKSPVSLTAHSLIGASPKQTNLTKAQEVHSTGINRPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIMKSYRNQPQANSHVYRSVLLKSIPREVVAYNKNINDDFEMIDCDLEDATKTPDCSSGPVKEERGDLIKFYNTIYVGRVKSFALKYDLANQDHMMDAPPLSPFPHIKQQPGSPRRISQQHSIYISPHKNGSGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSERANH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
70	Phosphorylation	LYVACRKSIIPTVGK HHHHHHHCCCCCCCC	13.34	21815630
88	Phosphorylation	EGNCVSLTRILRSAK HCCHHHHHHHHHHHH	14.25	-
93	Phosphorylation	SLTRILRSAKLSLIQ HHHHHHHHHHHHHHH	26.72	18491316
103	Phosphorylation	LSLIQFFSKMKKWMD HHHHHHHHHHHHHHC	32.88	18491316
274	Phosphorylation	KEHYFKPYISKLFDR CHHHCHHHHHHHHCC	20.58	26657352
300	Ubiquitination	SSFTDNSKAVNKEYE HHCCCCCHHHCHHHH	63.71	29967540
304	Ubiquitination	DNSKAVNKEYEEYVL CCCHHHCHHHHHEEE	55.89	29967540
312	Phosphorylation	EYEEYVLTVGDFDER HHHHEEEEECCCCCE	16.64	23403867
332	Phosphorylation	DAEEEIGTPRKFTRD CHHCHHCCCCCCCCC	26.11	19664994
337	Phosphorylation	IGTPRKFTRDTPLGK HCCCCCCCCCCCCCH	30.58	23312004
340	Phosphorylation	PRKFTRDTPLGKLTA CCCCCCCCCCCHHEH	19.68	23898821
364	Phosphorylation	QHFEKKRSFAPSTPL HHHHHCCCCCCCCCC	34.34	23927012
368	Phosphorylation	KKRSFAPSTPLTGRR HCCCCCCCCCCCCHH	38.95	30266825
369	Phosphorylation	KRSFAPSTPLTGRRY CCCCCCCCCCCCHHH	22.66	19664994
372	Phosphorylation	FAPSTPLTGRRYLRE CCCCCCCCCHHHHHH	29.82	30266825
385	Phosphorylation	REKEAVITPVASATQ HHHCEEEECCCHHHH	12.71	23401153
389	Phosphorylation	AVITPVASATQSVSR EEEECCCHHHHHHHH	31.89	30266825
391	Phosphorylation	ITPVASATQSVSRLQ EECCCHHHHHHHHHH	20.91	22199227
393	Phosphorylation	PVASATQSVSRLQSI CCCHHHHHHHHHHHH	20.08	22199227
395	Phosphorylation	ASATQSVSRLQSIVA CHHHHHHHHHHHHHH	32.30	22199227
468	Phosphorylation	LKLAEILYYKILETV HHHHHHHHHHHHHHH	14.36	-
469	Phosphorylation	KLAEILYYKILETVM HHHHHHHHHHHHHHH	6.52	-
480	Phosphorylation	ETVMVQETRRLHGMD HHHHHHHHHHHCCCC	12.19	23879269
599	Phosphorylation	IFPNNFETGNGGNVQ ECCCCCCCCCCCCCC	31.63	26074081
615	Phosphorylation	HLPLMPMSPLMHPRV CCCCCCCCCCCCCCE	14.71	25849741
627	Phosphorylation	PRVKEVRTDSGSLRR CCEEEEECCCCCCCC	39.43	26074081
629	Phosphorylation	VKEVRTDSGSLRRDM EEEEECCCCCCCCCC	29.66	26074081
631	Phosphorylation	EVRTDSGSLRRDMQP EEECCCCCCCCCCCC	23.74	26074081
640	Phosphorylation	RRDMQPLSPISVHER CCCCCCCCCCCHHHC	27.20	29255136
643	Phosphorylation	MQPLSPISVHERYSS CCCCCCCCHHHCCCC	22.32	30266825
648	Phosphorylation	PISVHERYSSPTAGS CCCHHHCCCCCCCCH	15.54	28985074
649	Phosphorylation	ISVHERYSSPTAGSA CCHHHCCCCCCCCHH	35.74	30266825
650	Phosphorylation	SVHERYSSPTAGSAK CHHHCCCCCCCCHHH	19.82	30266825
652	Phosphorylation	HERYSSPTAGSAKRR HHCCCCCCCCHHHHH	45.67	30266825
655	Phosphorylation	YSSPTAGSAKRRLFG CCCCCCCHHHHHHCC	28.31	30266825
657	Ubiquitination	SPTAGSAKRRLFGED CCCCCHHHHHHCCCC	39.48	29967540
719	Phosphorylation	GTTGHKVTIPLHGVA CCCCCEEEEECCCCC	22.98	29083192
733	Phosphorylation	ANDAGEITLIPLSMN CCCCCEEEEEECCCC	17.84	29083192
738	Phosphorylation	EITLIPLSMNTNQES EEEEEECCCCCCCCC	12.48	29083192
741	Phosphorylation	LIPLSMNTNQESKVK EEECCCCCCCCCCCC	29.63	29083192
745	Phosphorylation	SMNTNQESKVKSPVS CCCCCCCCCCCCCCC	32.74	26074081
749	Phosphorylation	NQESKVKSPVSLTAH CCCCCCCCCCCHHHH	33.26	23927012
752	Phosphorylation	SKVKSPVSLTAHSLI CCCCCCCCHHHHHHH	24.32	30278072
754	Phosphorylation	VKSPVSLTAHSLIGA CCCCCCHHHHHHHCC	18.15	30278072
757	Phosphorylation	PVSLTAHSLIGASPK CCCHHHHHHHCCCCC	21.15	23401153
762	Phosphorylation	AHSLIGASPKQTNLT HHHHHCCCCCCCCCC	27.67	23927012
766	Phosphorylation	IGASPKQTNLTKAQE HCCCCCCCCCCCHHH	38.02	26074081
769	Phosphorylation	SPKQTNLTKAQEVHS CCCCCCCCCHHHHHH	26.80	26074081
776	Phosphorylation	TKAQEVHSTGINRPK CCHHHHHHCCCCCCC	33.24	25056879
792	Phosphorylation	TGSLALFYRKVYHLA CCCHHHHHHHHHHHH	15.46	-
849	Phosphorylation	QLLLCAFYIMAKVTK HHHHHHHHHHHHCCH	3.25	24043423
855	Phosphorylation	FYIMAKVTKEERTFQ HHHHHHCCHHHHHHH	31.84	28509920
913	Phosphorylation	DCDLEDATKTPDCSS ECCHHHCCCCCCCCC	48.01	30576142
915	Phosphorylation	DLEDATKTPDCSSGP CHHHCCCCCCCCCCC	21.72	30576142
919	Phosphorylation	ATKTPDCSSGPVKEE CCCCCCCCCCCCCCC	45.79	28122231
920	Phosphorylation	TKTPDCSSGPVKEER CCCCCCCCCCCCCCC	54.14	28122231
938	Phosphorylation	IKFYNTIYVGRVKSF HHEEEEEEECCCHHH	8.53	-
949	Phosphorylation	VKSFALKYDLANQDH CHHHEEECCCCCCCC	19.62	28176443
964	Phosphorylation	MMDAPPLSPFPHIKQ CCCCCCCCCCCCHHC	30.21	23401153
970	Acetylation	LSPFPHIKQQPGSPR CCCCCCHHCCCCCCC	39.59	19413330
975	Phosphorylation	HIKQQPGSPRRISQQ CHHCCCCCCCCCCCC	23.16	10069453
980	Phosphorylation	PGSPRRISQQHSIYI CCCCCCCCCCCCEEE	23.21	23927012
984	Phosphorylation	RRISQQHSIYISPHK CCCCCCCCEEECCCC	16.85	23927012
986	Phosphorylation	ISQQHSIYISPHKNG CCCCCCEEECCCCCC	9.81	30576142
988	Phosphorylation	QQHSIYISPHKNGSG CCCCEEECCCCCCCC	12.18	23401153
994	Phosphorylation	ISPHKNGSGLTPRSA ECCCCCCCCCCCHHH	39.77	23401153
997	Phosphorylation	HKNGSGLTPRSALLY CCCCCCCCCHHHEEH	21.85	28152594
1000	Phosphorylation	GSGLTPRSALLYKFN CCCCCCHHHEEHHHC	25.19	19835603
1004	Phosphorylation	TPRSALLYKFNGSPS CCHHHEEHHHCCCCC	17.87	19835603
1009 (in isoform 2)	Phosphorylation	-	27.40	12006580
1009	Phosphorylation	LLYKFNGSPSKSLKD EEHHHCCCCCCCHHH	27.40	30576142
1011	Phosphorylation	YKFNGSPSKSLKDIN HHHCCCCCCCHHHHH	36.25	19835603
1037	Phosphorylation	KRVIAIDSDAESPAK CCEEEECCCCCCHHH	32.38	23401153
1041	Phosphorylation	AIDSDAESPAKRVCQ EECCCCCCHHHHHHH	31.70	29255136
1056	Acetylation	ENDDVLLKRLQDVVS HCCHHHHHHHHHHHH	47.07	23236377

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
332	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
369	T	Phosphorylation	Kinase	CDK4	P11802	Uniprot
385	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
640	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
640	S	Phosphorylation	Kinase	CDK4	P11802	Uniprot
650	S	Phosphorylation	Kinase	CDK2	P24941	PSP
650	S	Phosphorylation	Kinase	CDK4	P11802	PhosphoELM
762	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
964	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
964	S	Phosphorylation	Kinase	CDK4	P11802	Uniprot
975	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
975	S	Phosphorylation	Kinase	CDK4	P11802	Uniprot
988	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
997	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
1009	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
332	T	Phosphorylation	11884610
Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4.
640	S	Phosphorylation	11884610
Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4.
964	S	Phosphorylation	11884610
Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4.
975	S	Phosphorylation	11884610
Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4.

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 RBL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BEGIN_HUMAN	BEGAIN	physical	16189514
MYBB_HUMAN	MYBL2	physical	12947099
CDN1C_HUMAN	CDKN1C	physical	12947099
HDAC1_HUMAN	HDAC1	physical	9724731
E2F5_HUMAN	E2F5	physical	7760804
KDM5A_HUMAN	KDM5A	physical	7935440
MCM7_HUMAN	MCM7	physical	9566894
CCNA2_HUMAN	CCNA2	physical	8230483
E2F1_HUMAN	E2F1	physical	8230483
CCNA1_HUMAN	CCNA1	physical	10022926
TFDP1_HUMAN	TFDP1	physical	7739537
TFDP2_HUMAN	TFDP2	physical	7739537
MYBB_HUMAN	MYBL2	physical	12439743
RBBP9_HUMAN	RBBP9	physical	9697699
TF3B_HUMAN	BRF1	physical	10330166
PHB_HUMAN	PHB	physical	10376528
CCNA2_HUMAN	CCNA2	physical	8798463
CCNA2_HUMAN	CCNA2	physical	9724724
PP1A_BOVIN	PPP1CA	physical	12434308
SMCA4_HUMAN	SMARCA4	physical	12434308
E2F1_HUMAN	E2F1	physical	8657117
E2F2_HUMAN	E2F2	physical	8657117
E2F3_HUMAN	E2F3	physical	8657117
E2F4_HUMAN	E2F4	physical	8657117
E2F1_HUMAN	E2F1	physical	12096339
SP1_HUMAN	SP1	physical	7565695
E2F4_HUMAN	E2F4	physical	7958925
E2F4_HUMAN	E2F4	physical	7958924
SMD3_HUMAN	SNRPD3	physical	21988832
E2F1_HUMAN	E2F1	physical	23853093
MARF1_HUMAN	KIAA0430	physical	27173435

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 RBL1_HUMAN

Related Literatures of Post-Translational Modification

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 THR-332; THR-385; SER-749AND SER-762, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Distinct phosphorylation events regulate p130- and p107-mediatedrepression of E2F-4."; Farkas T., Hansen K., Holm K., Lukas J., Bartek J.; J. Biol. Chem. 277:26741-26752(2002). Cited for: PHOSPHORYLATION AT THR-369 AND SER-650.	12006580 [Abstract]
"Reversal of growth suppression by p107 via direct phosphorylation bycyclin D1/cyclin-dependent kinase 4."; Leng X., Noble M., Adams P.D., Qin J., Harper J.W.; Mol. Cell. Biol. 22:2242-2254(2002). Cited for: PROTEIN SEQUENCE OF 320-334; 364-374; 635-657; 949-977 AND 1006-1012,PHOSPHORYLATION AT THR-332; THR-369; THR-385; SER-640; SER-762;SER-964; SER-975; SER-988; THR-997 AND SER-1009, MUTAGENESIS OFSER-640; SER-643; SER-650 AND 657-LYS--LEU-660, AND MASS SPECTROMETRY.	11884610 [Abstract]

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