dbPTM

RBL2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBL2_RAT
UniProt AC	O55081
Protein Name	Retinoblastoma-like protein 2
Gene Name	Rbl2
Organism	Rattus norvegicus (Rat).
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 (By similarity)..
Protein Sequence	MASGGNQSSPPPPAAAASSEEEEEDGDTADRAQPAGSPSHQIQQRFEELCSRLNMDEAARAEAWSSYRSMSESYTLEGNDLHWLACALYVACRKSVPTVSKGTAEGNYVSLTRILRCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEQPRQQRGRKQRRQPCTTSEIFHFCWVLFIYAKGNFPMISDDLVNSYHLLLCALDLVYGNALQCSNRKELVNPNFKGVSEDGHPRDSHPSSDPPCVIEKLCSLHDGLVLEAKGIKQHFWKPYIRKLFEKKLLRGKEENLTGFLEPGNFAESFKAVNKAYEEYVLATGSLDERIFLGEDAEEEVGTFSRCVSAASGTESAERTQMRDILQQHLDKSKTLRVCNPLTGVRYVQENSPCVTPVSTATHSLNRLHTMLAGLRNAPSEKLEQILRSCSRDPTRAIADRLREMYEIYSQHFQPDENVSNCAKEMANKHFRFAEMLYYKVLESVIEQEQKRLGDMDLSGVLEQDAFHKSLLACCLEVVAFSYKPPGNFPFIAEIFDVPHYHFYKVIEVFIRAEDGLCREVVKHLNQIEEQILDHLAWKTKSPLWDRIRDNENRVPTCEEVTPPHNLERTDEIYIAGSPLTPRRVGEVRTDAGGLGRSVTSPTTLYDRYSSPTVSTTRRRLFESDSPSEGSTAGRIPPQPLVNAVPVQNVSGETVSVTPVPGQTLVTMATATVTANNGQTVTIPVQGIANENGGITFFPVQVNVGGQAQAVTGSIQPLSAQALAGSLSSQQVTGTTLQVPGPVAIQQISPGGQQQNQGQPLTSSSIRPRKTSSLSLFFRKVYYLAGVRLRDLCTKLDISDELRKKIWTCFEFSIVQCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMRCYRTQPQARSQVYRSVLIKGKRRNSGSCENRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGANSDIEEEERGDLIQFYNNIYRKQIQTFAMKYSQANSQMDTPPLSPYPFVRTGSPRRVQLSQSHPIYISPHKNEAMLSPREKIFYYFSNSPSKRLREINSMIRTGETPTKKRGILLDDGSESPAKRICPENHSALLRRLQDVANDRGSH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	Phosphorylation	DRAQPAGSPSHQIQQ CCCCCCCCHHHHHHH	25.90	29779826
39	Phosphorylation	AQPAGSPSHQIQQRF CCCCCCHHHHHHHHH	29.71	27097102
50	S-nitrosylation	QQRFEELCSRLNMDE HHHHHHHHHHCCCCH	2.23	22178444
50	S-nitrosocysteine	QQRFEELCSRLNMDE HHHHHHHHHHCCCCH	2.23	-
405	Phosphorylation	NPLTGVRYVQENSPC CCCCCCCEEECCCCC	12.22	27097102
410	Phosphorylation	VRYVQENSPCVTPVS CCEEECCCCCCCCCC	20.94	27097102
414	Phosphorylation	QENSPCVTPVSTATH ECCCCCCCCCCHHHH	25.37	27097102
417	Phosphorylation	SPCVTPVSTATHSLN CCCCCCCCHHHHHHH	17.33	30181290
628	Phosphorylation	PPHNLERTDEIYIAG CCCCCCCCCEEEECC	28.71	25575281
632	Phosphorylation	LERTDEIYIAGSPLT CCCCCEEEECCCCCC	5.22	22673903
636	Phosphorylation	DEIYIAGSPLTPRRV CEEEECCCCCCCCCC	14.02	27097102
639	Phosphorylation	YIAGSPLTPRRVGEV EECCCCCCCCCCCEE	20.38	22108457
656	Phosphorylation	DAGGLGRSVTSPTTL CCCCCCCCCCCCCCH	28.13	22673903
658	Phosphorylation	GGLGRSVTSPTTLYD CCCCCCCCCCCCHHH	30.18	27097102
659	Phosphorylation	GLGRSVTSPTTLYDR CCCCCCCCCCCHHHC	20.35	27097102
661	Phosphorylation	GRSVTSPTTLYDRYS CCCCCCCCCHHHCCC	29.24	27097102
662	Phosphorylation	RSVTSPTTLYDRYSS CCCCCCCCHHHCCCC	27.06	27097102
667	Phosphorylation	PTTLYDRYSSPTVST CCCHHHCCCCCCCCC	15.59	28432305
668	Phosphorylation	TTLYDRYSSPTVSTT CCHHHCCCCCCCCCC	30.64	28432305
669	Phosphorylation	TLYDRYSSPTVSTTR CHHHCCCCCCCCCCH	18.69	28432305
682	Phosphorylation	TRRRLFESDSPSEGS CHHHHCCCCCCCCCC	35.73	27097102
684	Phosphorylation	RRLFESDSPSEGSTA HHHCCCCCCCCCCCC	39.34	27097102
686	Phosphorylation	LFESDSPSEGSTAGR HCCCCCCCCCCCCCC	59.55	27097102
689	Phosphorylation	SDSPSEGSTAGRIPP CCCCCCCCCCCCCCC	15.84	22673903
690	Phosphorylation	DSPSEGSTAGRIPPQ CCCCCCCCCCCCCCC	43.94	30181290
942	Phosphorylation	SGSCENRSHQNSPTE CCCCCCCCCCCCCCC	40.79	25575281
946	Phosphorylation	ENRSHQNSPTELNTD CCCCCCCCCCCCCCC	26.99	29779826
948	Phosphorylation	RSHQNSPTELNTDRA CCCCCCCCCCCCCCC	53.58	25575281
952	Phosphorylation	NSPTELNTDRASRDS CCCCCCCCCCCCCCC	39.21	27097102
956	Phosphorylation	ELNTDRASRDSSPVM CCCCCCCCCCCCCCC	37.20	27097102
959	Phosphorylation	TDRASRDSSPVMRSN CCCCCCCCCCCCCCC	35.12	25575281
960	Phosphorylation	DRASRDSSPVMRSNS CCCCCCCCCCCCCCC	26.29	25575281
965	Phosphorylation	DSSPVMRSNSTLPVP CCCCCCCCCCCCCCC	19.62	28689409
967	Phosphorylation	SPVMRSNSTLPVPQP CCCCCCCCCCCCCCC	32.35	-
968	Phosphorylation	PVMRSNSTLPVPQPS CCCCCCCCCCCCCCC	39.05	22108457
975	Phosphorylation	TLPVPQPSSAPPTPT CCCCCCCCCCCCCCC	33.61	27097102
976	Phosphorylation	LPVPQPSSAPPTPTR CCCCCCCCCCCCCCC	52.02	27097102
980	Phosphorylation	QPSSAPPTPTRLTGA CCCCCCCCCCCCCCC	35.91	27097102
982	Phosphorylation	SSAPPTPTRLTGANS CCCCCCCCCCCCCCC	40.57	27097102
985	Phosphorylation	PPTPTRLTGANSDIE CCCCCCCCCCCCCCC	30.84	28432305
989	Phosphorylation	TRLTGANSDIEEEER CCCCCCCCCCCHHHH	39.16	28432305
1031	Phosphorylation	QMDTPPLSPYPFVRT CCCCCCCCCCCCCCC	28.32	-
1047	Phosphorylation	SPRRVQLSQSHPIYI CCCEEEECCCCCEEE	16.73	27097102
1049	Phosphorylation	RRVQLSQSHPIYISP CEEEECCCCCEEECC	28.05	27097102
1053	Phosphorylation	LSQSHPIYISPHKNE ECCCCCEEECCCCCC	10.37	27097102
1055	Phosphorylation	QSHPIYISPHKNEAM CCCCEEECCCCCCCC	12.18	27097102
1064	Phosphorylation	HKNEAMLSPREKIFY CCCCCCCCCHHHHHH	14.61	27097102
1074	Phosphorylation	EKIFYYFSNSPSKRL HHHHHHHCCCHHHHH	21.92	23984901
1076	Phosphorylation	IFYYFSNSPSKRLRE HHHHHCCCHHHHHHH	29.38	23984901
1078	Phosphorylation	YYFSNSPSKRLREIN HHHCCCHHHHHHHHH	30.17	23984901
1106	Phosphorylation	GILLDDGSESPAKRI CEECCCCCCCCHHHH	41.73	27097102
1108	Phosphorylation	LLDDGSESPAKRICP ECCCCCCCCHHHHCC	31.67	27097102

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_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
636	S	Phosphorylation	22673903
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	22673903
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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DGKZ_RAT	Dgkz	physical	16286473

Drug and Disease Associations

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

Regulatory Network of RBL2_RAT

Related Literatures of Post-Translational Modification

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