dbPTM

RBL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBL2_HUMAN
UniProt AC	Q08999
Protein Name	Retinoblastoma-like protein 2
Gene Name	RBL2
Organism	Homo sapiens (Human).
Sequence Length	1139
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	MPSGGDQSPPPPPPPPAAAASDEEEEDDGEAEDAAPPAESPTPQIQQRFDELCSRLNMDEAARAEAWDSYRSMSESYTLEGNDLHWLACALYVACRKSVPTVSKGTVEGNYVSLTRILKCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEQPRQQRGRKQRRQPCTVSEIFHFCWVLFIYAKGNFPMISDDLVNSYHLLLCALDLVYGNALQCSNRKELVNPNFKGLSEDFHAKDSKPSSDPPCIIEKLCSLHDGLVLEAKGIKEHFWKPYIRKLYEKKLLKGKEENLTGFLEPGNFGESFKAINKAYEEYVLSVGNLDERIFLGEDAEEEIGTLSRCLNAGSGTETAERVQMKNILQQHFDKSKALRISTPLTGVRYIKENSPCVTPVSTATHSLSRLHTMLTGLRNAPSEKLEQILRTCSRDPTQAIANRLKEMFEIYSQHFQPDEDFSNCAKEIASKHFRFAEMLYYKVLESVIEQEQKRLGDMDLSGILEQDAFHRSLLACCLEVVTFSYKPPGNFPFITEIFDVPLYHFYKVIEVFIRAEDGLCREVVKHLNQIEEQILDHLAWKPESPLWEKIRDNENRVPTCEEVMPPQNLERADEICIAGSPLTPRRVTEVRADTGGLGRSITSPTTLYDRYSSPPASTTRRRLFVENDSPSDGGTPGRMPPQPLVNAVPVQNVSGETVSVTPVPGQTLVTMATATVTANNGQTVTIPVQGIANENGGITFFPVQVNVGGQAQAVTGSIQPLSAQALAGSLSSQQVTGTTLQVPGQVAIQQISPGGQQQKQGQSVTSSSNRPRKTSSLSLFFRKVYHLAAVRLRDLCAKLDISDELRKKIWTCFEFSIIQCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMRCYRTQPQARSQVYRSVLIKGKRKRRNSGSSDSRSHQNSPTELNKDRTSRDSSPVMRSSSTLPVPQPSSAPPTPTRLTGANSDMEEEERGDLIQFYNNIYIKQIKTFAMKYSQANMDAPPLSPYPFVRTGSPRRIQLSQNHPVYISPHKNETMLSPREKIFYYFSNSPSKRLREINSMIRTGETPTKKRGILLEDGSESPAKRICPENHSALLRRLQDVANDRGSH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPSGGDQSPP -----CCCCCCCCCC	68.23	24211406
8	Phosphorylation	MPSGGDQSPPPPPPP CCCCCCCCCCCCCCC	44.08	24211406
21	Phosphorylation	PPPAAAASDEEEEDD CCCCCCCCCCCCCCC	40.61	24211406
40	Phosphorylation	DAAPPAESPTPQIQQ CCCCCCCCCCHHHHH	35.86	26074081
42	Phosphorylation	APPAESPTPQIQQRF CCCCCCCCHHHHHHH	36.78	24211406
72	Phosphorylation	EAWDSYRSMSESYTL HHHHHHHHCCCCEEC	20.58	28985074
74	Phosphorylation	WDSYRSMSESYTLEG HHHHHHCCCCEECCC	25.33	28985074
76	Phosphorylation	SYRSMSESYTLEGND HHHHCCCCEECCCCC	18.99	28985074
98	Phosphorylation	LYVACRKSVPTVSKG HHHHHHHCCCCCCCC	17.61	21253578
111	Phosphorylation	KGTVEGNYVSLTRIL CCEEECCEEEHHHHH	11.41	21253578
113	Phosphorylation	TVEGNYVSLTRILKC EEECCEEEHHHHHCC	17.42	21253578
115	Phosphorylation	EGNYVSLTRILKCSE ECCEEEHHHHHCCCH	14.25	21253578
149	Phosphorylation	PPHFRERTERLERNF CHHHHHHHHHHHHCE	22.24	22468782
157	Phosphorylation	ERLERNFTVSAVIFK HHHHHCEEEEEEEEE	19.66	22468782
168	Ubiquitination	VIFKKYEPIFQDIFK EEEECCCHHHHHHHC	29.60	21890473
168	Ubiquitination	VIFKKYEPIFQDIFK EEEECCCHHHHHHHC	29.60	21890473
181	Ubiquitination	FKYPQEEQPRQQRGR HCCCCHHCHHHHHCH	37.41	29967540
240	Ubiquitination	LDLVYGNALQCSNRK HHHHHCCHHHCCCCH	8.47	29967540
255	Ubiquitination	ELVNPNFKGLSEDFH HHCCCCCCCCCCCCC	66.63	29967540
310	Ubiquitination	RKLYEKKLLKGKEEN HHHHHHHHHCCCHHC	9.89	21890473
314	Ubiquitination	EKKLLKGKEENLTGF HHHHHCCCHHCCCCC	61.34	29967540
319	Ubiquitination	KGKEENLTGFLEPGN CCCHHCCCCCCCCCC	37.15	29967540
343	Phosphorylation	KAYEEYVLSVGNLDE HHHHHHHHCCCCCCC	3.17	32645325
364	Phosphorylation	DAEEEIGTLSRCLNA CHHHHHHHHHHHHHC	27.50	30576142
366	Phosphorylation	EEEIGTLSRCLNAGS HHHHHHHHHHHHCCC	22.30	29978859
369	Ubiquitination	IGTLSRCLNAGSGTE HHHHHHHHHCCCCCH	4.84	29967540
373	Phosphorylation	SRCLNAGSGTETAER HHHHHCCCCCHHHHH	39.88	28450419
375	Phosphorylation	CLNAGSGTETAERVQ HHHCCCCCHHHHHHH	31.68	28450419
377	Phosphorylation	NAGSGTETAERVQMK HCCCCCHHHHHHHHH	33.39	28450419
384	Ubiquitination	TAERVQMKNILQQHF HHHHHHHHHHHHHHC	24.60	22817900
384	Ubiquitination	TAERVQMKNILQQHF HHHHHHHHHHHHHHC	24.60	21890473
393	Ubiquitination	ILQQHFDKSKALRIS HHHHHCCHHHCCEEC	53.57	29967540
400	Phosphorylation	KSKALRISTPLTGVR HHHCCEECCCCCCCE	19.96	30266825
401	Phosphorylation	SKALRISTPLTGVRY HHCCEECCCCCCCEE	21.68	23401153
404	Phosphorylation	LRISTPLTGVRYIKE CEECCCCCCCEECCC	34.53	30266825
408	Phosphorylation	TPLTGVRYIKENSPC CCCCCCEECCCCCCC	17.59	28464451
413	Phosphorylation	VRYIKENSPCVTPVS CEECCCCCCCCCCCC	22.29	23401153
417	Phosphorylation	KENSPCVTPVSTATH CCCCCCCCCCCHHHH	25.37	23927012
420	O-linked_Glycosylation	SPCVTPVSTATHSLS CCCCCCCCHHHHHHH	17.33	30379171
420	Phosphorylation	SPCVTPVSTATHSLS CCCCCCCCHHHHHHH	17.33	23927012
421	Phosphorylation	PCVTPVSTATHSLSR CCCCCCCHHHHHHHH	35.49	23403867
423	Phosphorylation	VTPVSTATHSLSRLH CCCCCHHHHHHHHHH	16.46	23403867
425	Phosphorylation	PVSTATHSLSRLHTM CCCHHHHHHHHHHHH	24.56	23403867
427	Phosphorylation	STATHSLSRLHTMLT CHHHHHHHHHHHHHH	35.49	23403867
434	Phosphorylation	SRLHTMLTGLRNAPS HHHHHHHHHHHCCCH	24.29	24719451
443	Ubiquitination	LRNAPSEKLEQILRT HHCCCHHHHHHHHHH	62.76	29967540
531	Phosphorylation	EQDAFHRSLLACCLE CCHHHHHHHHHHHHH	21.11	22461510
543	Phosphorylation	CLEVVTFSYKPPGNF HHHHHHCCCCCCCCC	23.92	22461510
544	Phosphorylation	LEVVTFSYKPPGNFP HHHHHCCCCCCCCCC	24.27	22461510
565	Phosphorylation	DVPLYHFYKVIEVFI CCCHHHHHHHHHHHH	7.34	32142685
603	Phosphorylation	HLAWKPESPLWEKIR HHCCCCCCCHHHHHC	33.54	-
639	Phosphorylation	DEICIAGSPLTPRRV CEEEECCCCCCCCEE	14.02	23401153
642	Phosphorylation	CIAGSPLTPRRVTEV EECCCCCCCCEEEEE	20.38	30266825
647	Phosphorylation	PLTPRRVTEVRADTG CCCCCEEEEEECCCC	27.27	26074081
659	Phosphorylation	DTGGLGRSITSPTTL CCCCCCCCCCCCCCH	28.55	23927012
661	Phosphorylation	GGLGRSITSPTTLYD CCCCCCCCCCCCHHH	29.87	30266825
662	Phosphorylation	GLGRSITSPTTLYDR CCCCCCCCCCCHHHC	20.69	23927012
664	Phosphorylation	GRSITSPTTLYDRYS CCCCCCCCCHHHCCC	29.24	30266825
665	Phosphorylation	RSITSPTTLYDRYSS CCCCCCCCHHHCCCC	27.06	30266825
667	Phosphorylation	ITSPTTLYDRYSSPP CCCCCCHHHCCCCCC	9.04	23927012
670	Phosphorylation	PTTLYDRYSSPPAST CCCHHHCCCCCCCCC	15.59	28450419
671	Phosphorylation	TTLYDRYSSPPASTT CCHHHCCCCCCCCCC	36.94	28450419
672	Phosphorylation	TLYDRYSSPPASTTR CHHHCCCCCCCCCCC	26.43	22617229
676	Phosphorylation	RYSSPPASTTRRRLF CCCCCCCCCCCEEEE	35.76	28450419
677	Phosphorylation	YSSPPASTTRRRLFV CCCCCCCCCCEEEEE	26.82	28450419
678	Phosphorylation	SSPPASTTRRRLFVE CCCCCCCCCEEEEEE	21.49	28450419
688	Phosphorylation	RLFVENDSPSDGGTP EEEEECCCCCCCCCC	37.57	30266825
690	Phosphorylation	FVENDSPSDGGTPGR EEECCCCCCCCCCCC	53.49	30266825
694	Phosphorylation	DSPSDGGTPGRMPPQ CCCCCCCCCCCCCCC	28.26	30266825
861	Phosphorylation	LCAKLDISDELRKKI HHHHCCCCHHHHHHH	25.38	24114839
912	Phosphorylation	EDKSFQNIMRCYRTQ CCCCHHHHHHHHHCC	0.97	33259812
937	Phosphorylation	VLIKGKRKRRNSGSS HHHCCCCCCCCCCCC	60.23	33259812
948	Phosphorylation	SGSSDSRSHQNSPTE CCCCCCCCCCCCCCH	33.12	27362937
952	Phosphorylation	DSRSHQNSPTELNKD CCCCCCCCCCHHCCC	26.99	23401153
954	Phosphorylation	RSHQNSPTELNKDRT CCCCCCCCHHCCCCC	53.58	23403867
961	Phosphorylation	TELNKDRTSRDSSPV CHHCCCCCCCCCCCC	37.94	30576142
962	Phosphorylation	ELNKDRTSRDSSPVM HHCCCCCCCCCCCCC	34.68	27273156
965	Phosphorylation	KDRTSRDSSPVMRSS CCCCCCCCCCCCCCC	35.12	27273156
966	Phosphorylation	DRTSRDSSPVMRSSS CCCCCCCCCCCCCCC	26.29	29255136
971	Phosphorylation	DSSPVMRSSSTLPVP CCCCCCCCCCCCCCC	15.56	23911959
972	Phosphorylation	SSPVMRSSSTLPVPQ CCCCCCCCCCCCCCC	19.58	23911959
973	Phosphorylation	SPVMRSSSTLPVPQP CCCCCCCCCCCCCCC	34.90	23911959
974	Phosphorylation	PVMRSSSTLPVPQPS CCCCCCCCCCCCCCC	36.71	27794612
981	Phosphorylation	TLPVPQPSSAPPTPT CCCCCCCCCCCCCCC	33.61	30278072
982	Phosphorylation	LPVPQPSSAPPTPTR CCCCCCCCCCCCCCC	52.02	30278072
986	Phosphorylation	QPSSAPPTPTRLTGA CCCCCCCCCCCCCCC	35.91	30278072
988	Phosphorylation	SSAPPTPTRLTGANS CCCCCCCCCCCCCCC	40.57	30278072
995	Phosphorylation	TRLTGANSDMEEEER CCCCCCCCCCCHHHH	37.49	25850435
1019	Phosphorylation	IYIKQIKTFAMKYSQ HHHHHHHHHHHHHHH	20.46	22817900
1024	Phosphorylation	IKTFAMKYSQANMDA HHHHHHHHHHCCCCC	7.91	28111955
1025	Phosphorylation	KTFAMKYSQANMDAP HHHHHHHHHCCCCCC	19.80	29978859
1035	Phosphorylation	NMDAPPLSPYPFVRT CCCCCCCCCCCCCCC	28.32	22617229
1037	Phosphorylation	DAPPLSPYPFVRTGS CCCCCCCCCCCCCCC	13.11	25850435
1042	Phosphorylation	SPYPFVRTGSPRRIQ CCCCCCCCCCCCEEE	36.39	23090842
1044	Phosphorylation	YPFVRTGSPRRIQLS CCCCCCCCCCEEEEC	18.02	12006580
1051	Phosphorylation	SPRRIQLSQNHPVYI CCCEEEECCCCCEEE	16.74	28450419
1057	Phosphorylation	LSQNHPVYISPHKNE ECCCCCEEECCCCCC	10.51	28450419
1059	Phosphorylation	QNHPVYISPHKNETM CCCCEEECCCCCCCC	11.85	23927012
1065	Phosphorylation	ISPHKNETMLSPREK ECCCCCCCCCCCHHH	32.57	29691806
1068	Phosphorylation	HKNETMLSPREKIFY CCCCCCCCCHHHHHH	15.87	28355574
1075	Phosphorylation	SPREKIFYYFSNSPS CCHHHHHHHCCCCHH	13.69	29978859
1076	Phosphorylation	PREKIFYYFSNSPSK CHHHHHHHCCCCHHH	6.98	28450419
1078	Phosphorylation	EKIFYYFSNSPSKRL HHHHHHCCCCHHHHH	21.92	22617229
1080	Phosphorylation	IFYYFSNSPSKRLRE HHHHCCCCHHHHHHH	29.38	25159151
1082	Phosphorylation	YYFSNSPSKRLREIN HHCCCCHHHHHHHHH	30.17	22617229
1090	Phosphorylation	KRLREINSMIRTGET HHHHHHHHHHHCCCC	22.65	29449344
1094	Phosphorylation	EINSMIRTGETPTKK HHHHHHHCCCCCCCC	28.57	26029660
1097	Phosphorylation	SMIRTGETPTKKRGI HHHHCCCCCCCCCCE	37.29	29116813
1099	Phosphorylation	IRTGETPTKKRGILL HHCCCCCCCCCCEEC	57.53	26074081
1110	Phosphorylation	GILLEDGSESPAKRI CEECCCCCCCCHHHH	47.42	30266825
1112	Phosphorylation	LLEDGSESPAKRICP ECCCCCCCCHHHHCC	31.67	23401153
1138	Phosphorylation	DVANDRGSH------ HHHHCCCCC------	27.24	24719451

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
401	T	Phosphorylation	Kinase	CDK6	Q00534	PSP
401	T	Phosphorylation	Kinase	CDK4	P11802	PSP
413	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
413	S	Phosphorylation	Kinase	CDK2	P24941	PSP
413	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
417	T	Phosphorylation	Kinase	CDK2	P24941	PSP
417	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
417	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
639	S	Phosphorylation	Kinase	CDK2	P24941	PSP
642	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
642	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
642	T	Phosphorylation	Kinase	CDK2	P24941	PSP
659	S	Phosphorylation	Kinase	NEK6	Q9HC98	PSP
662	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
662	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
662	S	Phosphorylation	Kinase	CDK2	P24941	PSP
672	S	Phosphorylation	Kinase	CDK4	P11802	PSP
672	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
672	S	Phosphorylation	Kinase	UL97	P16788	PSP
688	S	Phosphorylation	Kinase	CDK2	P24941	PSP
688	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
688	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
694	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
694	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
694	T	Phosphorylation	Kinase	CDK2	P24941	PSP
952	S	Phosphorylation	Kinase	CDK2	P24941	PSP
1035	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
1035	S	Phosphorylation	Kinase	CDK4	P11802	PSP
1044	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
1044	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
1044	S	Phosphorylation	Kinase	CDK2	P24941	PSP
1068	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
1068	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
1068	S	Phosphorylation	Kinase	CDK2	P24941	PSP
1080	S	Phosphorylation	Kinase	CDK2	P24941	PSP
1080	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
1080	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
1097	T	Phosphorylation	Kinase	CDK2	P24941	PSP
1097	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
1097	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
1112	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
1112	S	Phosphorylation	Kinase	CDK2	P24941	PSP
1112	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:12435635

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
639	S	Phosphorylation	11042701
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-639 and on 5 sites within the domain B. Phosphorylation on Ser-672 in G1 leads to its ubiquitin-dependent proteolysis.
639	S	ubiquitylation	11042701
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-639 and on 5 sites within the domain B. Phosphorylation on Ser-672 in G1 leads to its ubiquitin-dependent proteolysis.
672	S	Phosphorylation	12435635
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-639 and on 5 sites within the domain B. Phosphorylation on Ser-672 in G1 leads to its ubiquitin-dependent proteolysis.
672	S	ubiquitylation	12435635
During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-639 and on 5 sites within the domain B. Phosphorylation on Ser-672 in G1 leads to its ubiquitin-dependent proteolysis.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_HUMAN	HDAC1	physical	9724731
HDAC1_HUMAN	HDAC1	physical	10969803
MCM7_HUMAN	MCM7	physical	9566894
RAF1_HUMAN	RAF1	physical	9819434
CCNE1_HUMAN	CCNE1	physical	8253383
CCNA2_HUMAN	CCNA2	physical	8253383
CCNA1_HUMAN	CCNA1	physical	10022926
CDK2_HUMAN	CDK2	physical	9188854
RBBP9_HUMAN	RBBP9	physical	9697699
TF3B_HUMAN	BRF1	physical	10330166
PHB_HUMAN	PHB	physical	10376528
XBP1_HUMAN	XBP1	physical	20211142
ID2_HUMAN	ID2	physical	16776654
PAI2_HUMAN	SERPINB2	physical	16397580
PP2AA_HUMAN	PPP2CA	physical	12915404
SKP2_HUMAN	SKP2	physical	12717421
SKP1_HUMAN	SKP1	physical	12717421
CUL1_HUMAN	CUL1	physical	12717421
EZH2_HUMAN	EZH2	physical	15077161
LIN54_HUMAN	LIN54	physical	17531812
LIN9_HUMAN	LIN9	physical	17531812
LIN37_HUMAN	LIN37	physical	17531812
LIN52_HUMAN	LIN52	physical	17531812
RBL1_HUMAN	RBL1	physical	17531812
E2F4_HUMAN	E2F4	physical	17531812
E2F5_HUMAN	E2F5	physical	17531812
TFDP1_HUMAN	TFDP1	physical	17531812
TFDP2_HUMAN	TFDP2	physical	17531812
RBBP4_HUMAN	RBBP4	physical	17531812
P63_HUMAN	TP63	genetic	21511729
SMCA4_HUMAN	SMARCA4	physical	12434308
E2F4_HUMAN	E2F4	physical	16600870
E2F5_HUMAN	E2F5	physical	16600870
CCND1_HUMAN	CCND1	physical	16600870
CCND3_HUMAN	CCND3	physical	16600870
RINT1_HUMAN	RINT1	physical	16600870
CTIP_HUMAN	RBBP8	physical	16600870
GRAM4_HUMAN	GRAMD4	physical	16600870
LBX1_HUMAN	LBX1	physical	16600870
DCTN1_HUMAN	DCTN1	physical	16600870
LDHC_HUMAN	LDHC	physical	16600870
RAD50_HUMAN	RAD50	physical	16600870
E2F4_HUMAN	E2F4	physical	12006580
CCNA2_HUMAN	CCNA2	physical	12006580
E2F1_HUMAN	E2F1	physical	12096339
PML_HUMAN	PML	physical	22002537
E2F4_HUMAN	E2F4	physical	22002537
CDK2_HUMAN	CDK2	physical	10825149

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 RBL2_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-401; SER-662; SER-672;SER-982 AND SER-1035, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-662; SER-671;SER-672; SER-688; SER-1110 AND SER-1112, AND MASS SPECTROMETRY.	19369195 [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 THR-401; SER-639; THR-642;SER-982 AND THR-986, AND MASS SPECTROMETRY.	19413330 [Abstract]
"The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)."; Tedesco D., Lukas J., Reed S.I.; Genes Dev. 16:2946-2957(2002). Cited for: PHOSPHORYLATION AT SER-672.	12435635 [Abstract]
"Phosphorylation of the retinoblastoma-related protein p130 in growth-arrested cells."; Canhoto A.J., Chestukhin A., Litovchick L., DeCaprio J.A.; Oncogene 19:5116-5122(2000). Cited for: PHOSPHORYLATION AT SER-639; SER-952; SER-966; SER-971; SER-972;SER-973; THR-974; SER-981; SER-982 AND THR-986, AND MASS SPECTROMETRY.	11042701 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1019, AND MASSSPECTROMETRY.	18187866 [Abstract]

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